ID   O82102_VICSA            Unreviewed;       503 AA.
AC   O82102;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=Cysteine proteinase {ECO:0000313|EMBL:CAA07639.1};
OS   Vicia sativa (Spring vetch) (Tare).
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=3908 {ECO:0000313|EMBL:CAA07639.1};
RN   [1] {ECO:0000313|EMBL:CAA07639.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Cotyledons {ECO:0000313|EMBL:CAA07639.1};
RA   Fischer J., Becker C., Hillmer S., Horstmann C., Neubohn B., Senyuk V.,
RA   Muentz K.;
RT   "The family of cysteine proteinases from Vicia seeds.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family.
CC       {ECO:0000256|ARBA:ARBA00009941}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ007743; CAA07639.1; -; mRNA.
DR   PIR; T10944; T10944.
DR   AlphaFoldDB; O82102; -.
DR   MEROPS; C13.001; -.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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:SF54; VACUOLAR-PROCESSING ENZYME BETA-ISOZYME; 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};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           39..503
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004160101"
FT   DOMAIN          390..486
FT                   /note="Legumain prodomain"
FT                   /evidence="ECO:0000259|Pfam:PF20985"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   ACT_SITE        227
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
SQ   SEQUENCE   503 AA;  56326 MW;  BA54326FD2ED321D CRC64;
     MSVYRCHSVF LSKNMFSDVL ASWLVLLLFL SSLHGSVARP NRLEWEPVIR LPGEPVDADV
     EDEIGTRWAV LVAGSNGYGN YRHQADVCHA YQLLIKGGVK EENIVVFMYD DIAYSEFNPR
     PGVIINHPQG PNVYDGVPKD YTGDFVTADN LYAVILGDKS KVRGGSGKVI NSKAEDRIFI
     YYSDHGGPGV LGMPNMPYVY AMDFIDVLKK KHASRGYQQM VIYVEACESG SVFQGIMPKD
     IDVYVTTASN AEESSWGTYL VPGVYPASPP EYITCLGDLY SVAWMEDSET HNLKRETLKQ
     QFASVKERTL NNNNYGLGSH VTEYGDTNIT DEKLYLYHGF DPASVNLPPN NGRLESKMEV
     VNQRDAEILF MWQMYQRLDH QSEKKRDILK KISETVKHRN HLDGSVELIG VLLFGPTRGS
     SVLQSVRASG LPLVDDWECL KSRVRVFETH CGSLTQYGMK HMRAFANICN RGISEDLMEE
     TCMVACGGYD VGLLHPSNKG YSA
//