ID A0A0V0W8A4_9BILA Unreviewed; 447 AA.
AC A0A0V0W8A4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Legumain {ECO:0000313|EMBL:KRX71443.1};
DE Flags: Fragment;
GN Name=Lgmn {ECO:0000313|EMBL:KRX71443.1};
GN ORFNames=T06_5393 {ECO:0000313|EMBL:KRX71443.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX71443.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX71443.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX71443.1};
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:KRX71443.1}.
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DR EMBL; JYDK01000241; KRX71443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0W8A4; -.
DR STRING; 92179.A0A0V0W8A4; -.
DR Proteomes; UP000054673; 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:UP000054673};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..447
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006871570"
FT DOMAIN 341..437
FT /note="Legumain prodomain"
FT /evidence="ECO:0000259|Pfam:PF20985"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 184
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX71443.1"
SQ SEQUENCE 447 AA; 51532 MW; 6F804B902F0D50D6 CRC64;
LFNMLSIWSF LLLLVLFKST TLVISHENSS QKWALLVAGS NGWYNYRHQA DICHAYQILR
KHGIPDSNIV VMMYDDIAYN EENKLSGKII NHPHGVDVYQ NDVNVSNFMK ILLGKEKEMQ
HIGSGKVIKS GPNDHIFINF VDHGGKGILC FPEGEMTIGE LNKTLTEMHR LKKYGQMLIY
IEACESGSMF KNILPNDIKI YATTAANARE SSYACYFSEE LETYLGDCYS VNWMENSDQE
LLWMETVREQ YNIVKFETNT SHVSEFGDRS VSEDYLSDFQ GEEIFLKFGN SLFLKLLQQQ
PQNRRPPNVH LDAVSSRDVP LEILKRKVSK NGYESDAAQQ NLHSLLMKRK YVDEFINQMV
VEISKHFHLN HDAMLTKRVA DDVMDFDCHT KLVHHFSRNC FSFSKNTYAL KYAYVLTNLC
NTGIPVDKIL IRMEKSCKTA KKYSNIV
//