ID A0A091REA8_9GRUI Unreviewed; 430 AA.
AC A0A091REA8;
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=N332_04642 {ECO:0000313|EMBL:KFQ37597.1};
OS Mesitornis unicolor (brown roatelo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Mesitornithidae; Mesitornis.
OX NCBI_TaxID=54374 {ECO:0000313|EMBL:KFQ37597.1, ECO:0000313|Proteomes:UP000053369};
RN [1] {ECO:0000313|EMBL:KFQ37597.1, ECO:0000313|Proteomes:UP000053369}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N332 {ECO:0000313|EMBL:KFQ37597.1};
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; KK814151; KFQ37597.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091REA8; -.
DR MEROPS; C13.004; -.
DR Proteomes; UP000053369; 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:UP000053369};
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_5001880491"
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:KFQ37597.1"
SQ SEQUENCE 430 AA; 49043 MW; 12D97418E171E6BA CRC64;
MILKAVVLLG CALGISAFPM EDPEDGGKHW VVIVAGSNGW YNYRHQADVC HAYQIVHRNG
IPDEQIIVMM YDDIADNEEN PTKGIVINRP NGTDVYAGVP KDYTKEDVTP KNFLAVLRGD
AEAVKGVGSG KVLKSGPKDH VFVYFTDHGA PGLLAFPDDD LHVRDLNKTI WYMYRHKKYR
QMVFYIEACE SGSMMNHLAD NINVYATTAA NPRESSYACY YDDERQTYLG DWYSVNWMED
SDMEDLRKET LHKQFQLVKK RTNTSHVMQY GNRSISSMKV MQFQGMGKKA VPISLPPVDH
HDLMPSPDVP LAIMKRKLMA TNDIYEAKRI AGEMKTHLEV REFIQESMQK IITLVTGSKE
QANQILSDRL TISNYDCYQS AVNHFKARCF NWHLAMYEYA LRQLYALVNI CEGGYPIDRI
FLAMDKVCLG
//
