ID E5GC71_CUCME Unreviewed; 412 AA.
AC E5GC71;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Aspartic proteinase nepenthesin-1 {ECO:0000313|EMBL:ADN34070.1};
OS Cucumis melo subsp. melo.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=412675 {ECO:0000313|EMBL:ADN34070.1};
RN [1] {ECO:0000313|EMBL:ADN34070.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Young leaves {ECO:0000313|EMBL:ADN34070.1};
RX PubMed=20509895; DOI=10.1186/1471-2164-11-339;
RA Gonzalez V.M., Garcia-Mas J., Arus P., Puigdomenech P.;
RT "Generation of a BAC-based physical map of the melon genome.";
RL BMC Genomics 11:339-339(2010).
RN [2] {ECO:0000313|EMBL:ADN34070.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Young leaves {ECO:0000313|EMBL:ADN34070.1};
RX PubMed=21073723; DOI=10.1186/1471-2229-10-246;
RA Gonzalez V.M., Benjak A., Henaff E.M., Mir G., Casacuberta J.M.,
RA Garcia-Mas J., Puigdomenech P.;
RT "Sequencing of 6.7 Mb of the melon genome using a BAC pooling strategy.";
RL BMC Plant Biol. 10:246-246(2010).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447}.
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DR EMBL; HM854788; ADN34070.1; -; Genomic_DNA.
DR AlphaFoldDB; E5GC71; -.
DR MEROPS; A01.A29; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd05476; pepsin_A_like_plant; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034161; Pepsin-like_plant.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR032799; TAXi_C.
DR InterPro; IPR032861; TAXi_N.
DR PANTHER; PTHR47965:SF77; ASPARTIC PROTEINASE PCS1; 1.
DR PANTHER; PTHR47965; ASPARTYL PROTEASE-RELATED; 1.
DR Pfam; PF14541; TAXi_C; 1.
DR Pfam; PF14543; TAXi_N; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022750};
KW Protease {ECO:0000256|ARBA:ARBA00022750}.
FT DOMAIN 40..397
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 58
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 267
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 412 AA; 44554 MW; A8F54749D0A0DFC2 CRC64;
MKQSLCFSAT PTTMVLPLQT QMGLISQPSN KLSFHHNVTL TVSLTVGSPP QQVTMVLDTG
SELSWLHCKK SPNLTSVFNP LSSSSYSPIP CSSPVCRTRT RDLPNPVTCD PKKLCHAIVS
YADASSLEGN LASDNFRIGS SALPGTLFGC MDSGFSSNSE EDAKTTGLMG MNRGSLSFVT
QLGLPKFSYC ISGRDSSGVL LFGDSHLSWL GNLTYTPLVQ ISTPLPYFDR VAYTVQLDGI
RVGNKILPLP KSIFAPDHTG AGQTMVDSGT QFTFLLGPVY TALRNEFLEQ TKGVLAPLGD
PNFVFQGAMD LCYRVPAGGK LPELPAVSLM FRGAEMVVGG EVLLYKVPGM MKGKEWVYCL
TFGNSDLLGI EAFVIGHHHQ QNVWMEFDLV KSRVGFVETR CDLAGQRLGL GL
//
