ID A0A5A7VMC5_CUCME Unreviewed; 325 AA.
AC A0A5A7VMC5;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Vignain-like {ECO:0000313|EMBL:KAA0066925.1};
GN ORFNames=E6C27_scaffold550G00530 {ECO:0000313|EMBL:KAA0066925.1};
OS Cucumis melo var. makuwa.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=1194695 {ECO:0000313|EMBL:KAA0066925.1, ECO:0000313|Proteomes:UP000321393};
RN [1] {ECO:0000313|EMBL:KAA0066925.1, ECO:0000313|Proteomes:UP000321393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SW 3 {ECO:0000313|Proteomes:UP000321393};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAA0066925.1};
RA Kwon S.-Y.;
RT "Draft genome sequences of two oriental melons (Cucumis melo L. var
RT makuwa).";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA0066925.1}.
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DR EMBL; SSTE01000742; KAA0066925.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5A7VMC5; -.
DR STRING; 1194695.A0A5A7VMC5; -.
DR Proteomes; UP000321393; Unassembled WGS sequence.
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; IPR000169; Pept_cys_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; 2.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 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:UP000321393};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023145043"
FT DOMAIN 41..96
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 133..323
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 325 AA; 37111 MW; 7A1497DCC0E9D459 CRC64;
MTIMKFLIVP LVLIAFTSHL CEGFKLEGKD FESEKSLMQL YKKWSSHHRI SRNANEMHKR
FKVFKDNARY VFRKNQMGRS LKLQLNQFAD MFDDEFSSIH SSNITYYKNL HAKTIKAAGS
RVGGFMYERA KEIPSSIDWR KKGAVNAIKN QGGCGSCWAF AAVAAVESIH QIKTNELVSL
SEQEVVDCDY RDGGCRGGHY NSAFEFIMEN GGITIEDNYP YYEGDGYCRR RRGYNERVRI
DGYENVPRNN EYALMKAVAH QPIAVAIASV VVVGYGTDED GDYWIIRNQY GTQWGMNGYM
KMQRGARNPE GVCGMAMQPA YPVKY
//
