ID A0A1S3VJ00_VIGRR Unreviewed; 500 AA.
AC A0A1S3VJ00;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=P34 probable thiol protease {ECO:0000313|RefSeq:XP_014518265.1};
GN Name=LOC106775638 {ECO:0000313|RefSeq:XP_014518265.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014518265.1};
RN [1] {ECO:0000313|RefSeq:XP_014518265.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014518265.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR RefSeq; XP_014518265.1; XM_014662779.2.
DR AlphaFoldDB; A0A1S3VJ00; -.
DR STRING; 3916.A0A1S3VJ00; -.
DR GeneID; 106775638; -.
DR KEGG; vra:106775638; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000087766; Chromosome 10.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 2.10.25.160; Granulin; 1.
DR InterPro; IPR000118; Granulin.
DR InterPro; IPR037277; Granulin_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR013128; Peptidase_C1A.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR PANTHER; PTHR12411:SF950; PROBABLE THIOL PROTEASE-RELATED; 1.
DR Pfam; PF00396; Granulin; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00277; GRAN; 1.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR SUPFAM; SSF57277; Granulin repeat; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670,
KW ECO:0000313|RefSeq:XP_014518265.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000087766};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..500
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018632357"
FT DOMAIN 50..109
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 137..353
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 396..453
FT /note="Granulins"
FT /evidence="ECO:0000259|SMART:SM00277"
FT REGION 355..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 56179 MW; 424D0B4580E0EF07 CRC64;
MVYQLKTQLV FLFLLWGSWA FLCYGLPSEY SILAIDLDKF PSEEGVVELF QRWKEEHRKS
YEHPEEAKLR LENFKRNLKY IVEKNAKRNY PYGHSLGLNR FADMSNEEFK HKFNSKVKKP
LGKRHDLPNK DDSCEDAPYT LDWRKKGVVT GVKDQGHCGS CWAFSSTGAM EGINAIATGD
LVSLSEQELV DCDSTNDGCY GGYMDYAFEW VMHNGGIDSE TEYPYTGVEG RCNVTKEKTK
VVSIDGYSDV GQSDNSLLCA TVKQPISVAI DGSSWDFQLY TGGIYDGHCS SDPDDINHAV
LIVGYGSEDD EDYWIVKNSW GTSWGMEGYI YIKRNTHLKY GVCAINYMAS YPTKEPTAPS
PSSPPSPTSP PPPQPLPPPP PPPPPPPPPP APPIRCGDFS YCSAHETCCC LHRFYHFCLV
YGCCEYENGV CCRGTEYCCP SDFPICVTEH RLCLKHHKDS IGVPAKKMKS GSHKLPWTKL
EQTENTFQPL VMRNVFAAVL
//
