ID   A0A0V0XJQ2_TRIPS        Unreviewed;       449 AA.
AC   A0A0V0XJQ2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Legumain {ECO:0000313|EMBL:KRX88239.1};
DE   Flags: Fragment;
GN   Name=Lgmn {ECO:0000313|EMBL:KRX88239.1};
GN   ORFNames=T4E_297 {ECO:0000313|EMBL:KRX88239.1};
OS   Trichinella pseudospiralis (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX88239.1, ECO:0000313|Proteomes:UP000054815};
RN   [1] {ECO:0000313|EMBL:KRX88239.1, ECO:0000313|Proteomes:UP000054815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS141 {ECO:0000313|EMBL:KRX88239.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase C13 family.
CC       {ECO:0000256|ARBA:ARBA00009941}.
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:KRX88239.1}.
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DR   EMBL; JYDU01000244; KRX88239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0XJQ2; -.
DR   Proteomes; UP000054815; 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; cd21115; legumain_C; 1.
DR   Gene3D; 1.10.132.130; -; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
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; PIRSF019663; Legumain; 1.
DR   PRINTS; PR00776; HEMOGLOBNASE.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..449
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006872694"
FT   DOMAIN          344..439
FT                   /note="Legumain prodomain"
FT                   /evidence="ECO:0000259|Pfam:PF20985"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   ACT_SITE        183
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRX88239.1"
SQ   SEQUENCE   449 AA;  51593 MW;  F8E18D466DC9CC90 CRC64;
     LFNMLSIWSF LLLVLFKSTT VVISDKNPSN KWALLVAGSN GWYNYRHQAD ICHAYQILHK
     HGIPDSNIVV MMYDDIAYNE ENKLSGKIIN HPDGVDVYHN DVNVKNFMNI LLGKEKEMQH
     IGSGKVIKSG PNDHIFINFV DHGGSGILCF PEGEMTIGEL NKTLTEMHRL KKYGQMLIYI
     EACESGSMFK NVLPNNIKIY ATTAANARES SYACYFSEEL ETYLGDCYSV NWMENSDKEL
     LWLETVGEQY KIVKFETNTS HVSEFGDRSV SKDYLSDFQG EEIFLKFGSF LFAQLLKPQQ
     QQHQQNRRPP NVHLDAVSSR DVPLEILKRK INKNGYESDA ARQNLHSLLL KRKYVDEFIN
     QMVGEISKHF HLNHEAMLTK RVADVMDFDC HSKLVHHFSR NCFSFSKNAY ALKYAYVLTN
     LCNTGIPVNE ILIRMEESCK TAKMYSNIV
//