ID   Q9XGB9_VICNA            Unreviewed;       380 AA.
AC   Q9XGB9;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Putative preprolegumain {ECO:0000313|EMBL:CAB42655.1};
DE            EC=3.4.22.34 {ECO:0000313|EMBL:CAB42655.1};
DE   Flags: Fragment;
OS   Vicia narbonensis (Narbonne vetch).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Vicia.
OX   NCBI_TaxID=3912 {ECO:0000313|EMBL:CAB42655.1};
RN   [1] {ECO:0000313|EMBL:CAB42655.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cotyledons {ECO:0000313|EMBL:CAB42655.1};
RX   PubMed=10949376; DOI=10.1023/A:1006456615373;
RA   Fischer J., Becker C., Hillmer S., Horstmann C., Neubohn B., Schlereth A.,
RA   Senyuk V., Shutov A., Muntz K.;
RT   "The families of papain- and legumain-like cysteine proteinases from
RT   embryonic axes and cotyledons of Vicia seeds: developmental patterns,
RT   intracellular localization and functions in globulin proteolysis.";
RL   Plant Mol. Biol. 43:83-101(2000).
CC   -!- SIMILARITY: Belongs to the peptidase C13 family.
CC       {ECO:0000256|ARBA:ARBA00009941}.
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DR   EMBL; AJ238882; CAB42655.1; -; mRNA.
DR   AlphaFoldDB; Q9XGB9; -.
DR   MEROPS; C13.002; -.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IEA:InterPro.
DR   CDD; cd21115; legumain_C; 1.
DR   Gene3D; 1.10.132.130; -; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR043577; AE.
DR   InterPro; IPR048501; Legum_prodom.
DR   InterPro; IPR046427; Legumain_prodom_sf.
DR   InterPro; IPR001096; Peptidase_C13.
DR   PANTHER; PTHR12000; HEMOGLOBINASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR12000:SF42; LEGUMAIN; 1.
DR   Pfam; PF20985; Legum_prodom; 1.
DR   Pfam; PF01650; Peptidase_C13; 1.
DR   PIRSF; PIRSF500139; AE; 1.
DR   PIRSF; PIRSF019663; Legumain; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CAB42655.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          304..380
FT                   /note="Legumain prodomain"
FT                   /evidence="ECO:0000259|Pfam:PF20985"
FT   ACT_SITE        100
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   ACT_SITE        142
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAB42655.1"
FT   NON_TER         380
FT                   /evidence="ECO:0000313|EMBL:CAB42655.1"
SQ   SEQUENCE   380 AA;  42003 MW;  AFCC55BFA0526937 CRC64;
     DVCHAYQLLR KGGLKEENII VFMYDDIAYS EENPRPGVII NSPHGENVYE GVPKDYTGED
     VTVGNFFAAL LGNKSALSGG SGKVVDSGPN DRIFVFYSDH GGPGVLGMPT SPYMYASDLV
     EVLKIKHAAG TYKSLVFYLE ACESGSIFEG LLPEGLNIYA TTAANAEESS WGTYCPGENP
     SPPPEYETCL ADLYSVAWME DSDIHNLQTE TLHQQYELVK ERTSNGNSNY GSHVMQYGDI
     ELSKDSLFLY LGSNPSNENF TFVGRNSLVP PSKAINQRDA DLIHFWDKFR KAPQGSPRKA
     AAQKEVLEAM SHRMHIDDSI KLVGKLLFGM KKGPEVLTSV RPAGQPLVDD WDCLKTLVRT
     FETYCGSLSQ YGMKHMRSFA
//