ID A0A093FWP3_TYTAL Unreviewed; 430 AA.
AC A0A093FWP3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Legumain {ECO:0000256|ARBA:ARBA00021147};
DE EC=3.4.22.34 {ECO:0000256|ARBA:ARBA00012628};
DE AltName: Full=Protease, cysteine 1 {ECO:0000256|ARBA:ARBA00030799};
DE Flags: Fragment;
GN ORFNames=N341_11214 {ECO:0000313|EMBL:KFV58791.1};
OS Tyto alba (Barn owl).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV58791.1, ECO:0000313|Proteomes:UP000054190};
RN [1] {ECO:0000313|EMBL:KFV58791.1, ECO:0000313|Proteomes:UP000054190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV58791.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins and small molecule substrates at
CC -Asn-|-Xaa- bonds.; EC=3.4.22.34;
CC Evidence={ECO:0000256|ARBA:ARBA00000810};
CC -!- SIMILARITY: Belongs to the peptidase C13 family.
CC {ECO:0000256|ARBA:ARBA00009941}.
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DR EMBL; KK398834; KFV58791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093FWP3; -.
DR MEROPS; C13.004; -.
DR Proteomes; UP000054190; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054190};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..430
FT /note="Legumain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001884233"
FT DOMAIN 333..428
FT /note="Legumain prodomain"
FT /evidence="ECO:0000259|Pfam:PF20985"
FT ACT_SITE 148
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT ACT_SITE 189
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR019663-1"
FT NON_TER 430
FT /evidence="ECO:0000313|EMBL:KFV58791.1"
SQ SEQUENCE 430 AA; 48804 MW; A5610B464F42453B CRC64;
MILKAVVLLG CALGISTFPM EEPEDGGKHW VVLVAGSNGW YNYRHQADVC HAYQIVHRNG
IPDEQIIVMM YDDIADNDEN PTKGIVINRP NGTDVYAGVP KDYTKEDVTS KNFLAVLRGD
VDAVKGVGSG KVLKSGPKDH VFVYFTDHGA PGLLAFPDDD LHVKDLNKTI WHMYHHKKYR
KMVFYIEACE SGSMMHHLAD NINVYATTAS NARESSYACY YDDERQTYLG DWYSVNWMED
SDMEDLRKET LHKQFQLVKK RTNTSHVMQY GNKSISSMKL MQFQGMGKKA IPISLPPVGH
YDLTPTTDMP FAIMKRKLMA ASDADEAKKI AAEMKAHLEV KEFIQESMRK IVTLVTGSIE
QTNQILSDRL IISNYDCHQA VVNNLKARCF NWHLPMYEYA LRQLYILVNL CEGGYSIDRI
CLAMDQVCLG
//
