ID A0A5E4FCK4_PRUDU Unreviewed; 363 AA.
AC A0A5E4FCK4;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=PREDICTED: vignain {ECO:0000313|EMBL:VVA25844.1};
GN ORFNames=ALMOND_2B029074 {ECO:0000313|EMBL:VVA25844.1};
OS Prunus dulcis (Almond) (Amygdalus dulcis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX NCBI_TaxID=3755 {ECO:0000313|EMBL:VVA25844.1, ECO:0000313|Proteomes:UP000327085};
RN [1] {ECO:0000313|Proteomes:UP000327085}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Texas {ECO:0000313|Proteomes:UP000327085};
RX PubMed=31529539; DOI=10.1111/tpj.14538;
RA Alioto T., Alexiou K.G., Bardil A., Barteri F., Castanera R., Cruz F.,
RA Dhingra A., Duval H., Fernandez I Marti A., Frias L., Galan B.,
RA Garcia J.L., Howad W., Gomez-Garrido J., Gut M., Julca I., Morata J.,
RA Puigdomenech P., Ribeca P., Rubio Cabetas M.J., Vlasova A., Wirthensohn M.,
RA Garcia-Mas J., Gabaldon T., Casacuberta J.M., Arus P.;
RT "Transposons played a major role in the diversification between the closely
RT related almond and peach genomes: results from the almond genome
RT sequence.";
RL Plant J. 101:455-472(2020).
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; CABIKO010000099; VVA25844.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5E4FCK4; -.
DR EnsemblPlants; VVA25844; VVA25844; Prudul26B029074.
DR Gramene; VVA25844; VVA25844; Prudul26B029074.
DR InParanoid; A0A5E4FCK4; -.
DR OMA; VYYDEEC; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000327085; Chromosome 5.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:SF1001; KDEL-TAILED CYSTEINE ENDOPEPTIDASE CEP1; 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:UP000327085};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..363
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023123517"
FT DOMAIN 40..95
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 128..344
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 363 AA; 40128 MW; BDF92953C130F0F5 CRC64;
MTKFIWVAIA LSLALVVGVA QSFDFHEKDL ASEDSLWDLY ERWRSHHTVS RSIDEKHKRF
NVFKENVKHV HNTNKGDKPY KLKLNKFADM TNHEFRSVYA GSKVKHHRML QGEQRSDGGF
RYANVDSVPP SVDWRKKGAV TPVKDQGQCG SCWAFSTVVA VEGINQIKTN KLVSLSEQEL
VDCDTEQNQG CNGGLMELAF EFIRRKGGLT TETNYPYRAE DSTCNVAKEN APAVSIDGHE
SVPANNEDAL LKAAANQPIS VAIDAGGSDF QFYSEGVFTG QCGTELDHGV AVVGYGATLD
GTKYWIVKNS WGPEWGEKGY IRMERGVSAK EGLCGIAVEA SYPVKNSSTN PKGSPTSYLK
DEL
//
