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Database: UniProt
Entry: A0A061DMF8_THECC
LinkDB: A0A061DMF8_THECC
Original site: A0A061DMF8_THECC 
ID   A0A061DMF8_THECC        Unreviewed;       550 AA.
AC   A0A061DMF8;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Aspartic proteinase A1 isoform 1 {ECO:0000313|EMBL:EOX93241.1};
GN   ORFNames=TCM_002083 {ECO:0000313|EMBL:EOX93241.1};
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:EOX93241.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOX93241.1, 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 A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; CM001879; EOX93241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061DMF8; -.
DR   EnsemblPlants; EOX93241; EOX93241; TCM_002083.
DR   Gramene; EOX93241; EOX93241; TCM_002083.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; A0A061DMF8; -.
DR   OMA; GVHDAAC; -.
DR   Proteomes; UP000026915; Chromosome 1.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd06098; phytepsin; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 3.
DR   Gene3D; 1.10.225.10; Saposin-like; 1.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR033869; Phytepsin.
DR   InterPro; IPR007856; SapB_1.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF39; EUKARYOTIC ASPARTYL PROTEASE FAMILY PROTEIN; 1.
DR   Pfam; PF00026; Asp; 2.
DR   Pfam; PF05184; SapB_1; 1.
DR   Pfam; PF03489; SapB_2; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF47862; Saposin; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
DR   PROSITE; PS50015; SAP_B; 2.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW   ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026915};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..550
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001596023"
FT   DOMAIN          90..547
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          356..396
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   DOMAIN          420..461
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        121..127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   550 AA;  59791 MW;  DD1088523B958DD0 CRC64;
     MGTKFNTIRV TLLLVLLLSP AVFSVPNEGM VRIGLIKKKL DQINRVAGDI DSKEGKLSRT
     PLRKYHLQGN LGASDDSEIV ALKNYMDAQY FGEIGIGTPS QTFTVIFDTG SSNLWVPSSK
     CYFSVACYFH SKYKSSQSST YQKNGTSAAI QYGTGAISGF FSQDSVKVGD LVVNNQDFIE
     ATREPGITFL AAKFDGIFGL GFQEISVGGA VPVWYNMVNQ GLVKEPVFSF WLNRKIEGEE
     GGEIVFGGID SNHYKGEHTY VPVTQKGYWQ FDMGDVLVGG ATTGFCSSGC AAIADSGTSL
     LAGPTLIYDF YALLDLLKLS IVSFLKQFYS DAERLCRSNM WTIITQINHA IGASGVVSQE
     CKAIVSQYGK MILELLVSET QPQKICSQIG FCTFDGTRGV STRIESVADE IVGKSSDGVH
     DAMCTACEMA VVWMQNKLRR NETEEQILDY VNELCERLPS PNGESVVDCS SLSSMPGVSF
     TIGGKVFDLA PEEYVLKVGE GAVAQCISGF TALDVPPPRG PLWILGDVFM GRYHTVFDYG
     NMTVGFAEAA
//
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