GenomeNet

Database: UniProt
Entry: A0A061EQK0_THECC
LinkDB: A0A061EQK0_THECC
Original site: A0A061EQK0_THECC 
ID   A0A061EQK0_THECC        Unreviewed;       418 AA.
AC   A0A061EQK0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Aspartic proteinase, putative isoform 5 {ECO:0000313|EMBL:EOY06948.1};
GN   ORFNames=TCM_021509 {ECO:0000313|EMBL:EOY06948.1};
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:EOY06948.1, ECO:0000313|Proteomes:UP000026915};
RN   [1] {ECO:0000313|EMBL:EOY06948.1, 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; CM001882; EOY06948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A061EQK0; -.
DR   EnsemblPlants; EOY06948; EOY06948; TCM_021509.
DR   Gramene; EOY06948; EOY06948; TCM_021509.
DR   Proteomes; UP000026915; Chromosome 4.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
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; IPR007856; SapB_1.
DR   InterPro; IPR008138; SapB_2.
DR   InterPro; IPR011001; Saposin-like.
DR   InterPro; IPR008139; SaposinB_dom.
DR   PANTHER; PTHR47966:SF90; ASPARTIC PROTEINASE ORYZASIN-1-LIKE; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
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; 1.
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   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..418
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001597683"
FT   DOMAIN          83..418
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          313..353
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        288
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        114..120
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT   DISULFID        279..283
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   418 AA;  46087 MW;  86F490BC714DDE3D CRC64;
     MGDKNFLLVM CLLASTLYVA IASSDGLVRV GLKKQRFDIN SINAARIKGK DSMYAKGEGS
     TTHDSDDSTL NTVSLKNYLD VQYFGEIGIG SPPQKFTVIF DTGSSNLWIP SSHCYFSVAC
     FFHSRYNSSK SSTYTEIGKP CKIHYSSGTI LGFFSEDNIR VGDLVVKNQV FTEAIREGSA
     ILSLASFDGI LGLGFQDMSV GNVAPLWYSM MQQSLVVQKV FSFWFNKDPS ASEGGEIVFG
     GVDQKHFKGK HTYVPVAQKG YWQIDLADFL IADHSTGFCT RNCTAIVDSG TSFIAGPTAA
     VTKINHAIGA KGFVSMECKK VAAQYGDLMW ELLLSGLQPD KLCSNIGVCF NNGTRQLSNS
     IEMVVEQKRE RHTEVGQDLL CTACELILAW IRTELMENKT KGRVIEYVNK VLYLYIIT
//
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