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
//