ID A0A061F247_THECC Unreviewed; 402 AA.
AC A0A061F247;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Peptidase C13 family {ECO:0000313|EMBL:EOY10993.1};
GN ORFNames=TCM_026257 {ECO:0000313|EMBL:EOY10993.1};
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:EOY10993.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY10993.1, 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 -!- PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor
CC biosynthesis. {ECO:0000256|ARBA:ARBA00004687}.
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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DR EMBL; CM001883; EOY10993.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061F247; -.
DR STRING; 3641.A0A061F247; -.
DR EnsemblPlants; EOY10993; EOY10993; TCM_026257.
DR Gramene; EOY10993; EOY10993; TCM_026257.
DR eggNOG; KOG1349; Eukaryota.
DR HOGENOM; CLU_044656_2_0_1; -.
DR InParanoid; A0A061F247; -.
DR OMA; PGHTNNW; -.
DR UniPathway; UPA00196; -.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0042765; C:GPI-anchor transamidase complex; IBA:GO_Central.
DR GO; GO:0003923; F:GPI-anchor transamidase activity; IBA:GO_Central.
DR GO; GO:0016255; P:attachment of GPI anchor to protein; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1460; -; 1.
DR InterPro; IPR028361; GPI_transamidase.
DR InterPro; IPR001096; Peptidase_C13.
DR PANTHER; PTHR48067; GPI-ANCHOR TRANSAMIDASE; 1.
DR PANTHER; PTHR48067:SF1; GPI-ANCHOR TRANSAMIDASE; 1.
DR Pfam; PF01650; Peptidase_C13; 1.
DR PIRSF; PIRSF500138; GPI8; 1.
DR PIRSF; PIRSF019663; Legumain; 1.
DR PRINTS; PR00776; HEMOGLOBNASE.
PE 3: Inferred from homology;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
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}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..402
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001597546"
FT ACT_SITE 159
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ SEQUENCE 402 AA; 46029 MW; AFDCCE10A2E5BF16 CRC64;
MATFINSKTI FRLLVLPCLL LYSSIAHNSS SVEATMHTNN WAVLVCTSRF WFNYRHMANT
LSLYRTVKRL GIPDERIILM LADDMACNTR NKYPAQVFNN ENHRLNLYGD NVEVDYRGYE
VTVENFLRVL TGRHETSVPR SKRLLSDEGS HILLYMTGHG GDEFLKFQDS EELQSHDLAD
AVKQMKEKLR FKELLIMVDT CQAATLFNQL QSPGVLAIGS SMRGENSYSH HLDSDVGVSV
VDRFTYYTLA FFERLNIYDN ASLSSLFSSY NPSMLMSTAY CRRDLYQRRL EEVPVTNFFG
SVMETIHTDA AYKALSRKDS GRFKAQMSLD QSVHHHERRT LINVNDQDEI LNTKAEDQQG
ASTCPFTSFY EKLRKGENVD SLVNYGLVAM LPLLGVSSWL FQ
//
