ID A0A565AML4_9BRAS Unreviewed; 447 AA.
AC A0A565AML4;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Granulins domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=ANE_LOCUS1102 {ECO:0000313|EMBL:VVA90657.1};
OS Arabis nemorensis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=586526 {ECO:0000313|EMBL:VVA90657.1, ECO:0000313|Proteomes:UP000489600};
RN [1] {ECO:0000313|EMBL:VVA90657.1, ECO:0000313|Proteomes:UP000489600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Dittberner H.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR EMBL; CABITT030000001; VVA90657.1; -; Genomic_DNA.
DR Proteomes; UP000489600; 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; 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:SF414; OS05G0508300 PROTEIN; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000489600};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..447
FT /note="Granulins domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5022065482"
FT DOMAIN 43..100
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 128..343
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT DOMAIN 360..417
FT /note="Granulins"
FT /evidence="ECO:0000259|SMART:SM00277"
SQ SEQUENCE 447 AA; 49347 MW; 904863ABCB717A30 CRC64;
MSPSSSSFVS LTXXXXXXXX XLLLVSSLIP TSSSSSDDIS ELFDEWCRKH GKTYDSEEDK
QHRIEIFKDN HDFVTHHNRI TNSTYSLSLN AFADLTHHEF KASRLGLSAP SSPPVMAKEQ
SLGFSENVPD SVDWRKKGAV TNVKDQGSCG ACWSFSATGS MEGINQIVTG DLISLSEQEL
IDCDKSYNDG CNGGLMDYAF EFVIKNHGID TEKDYPYQER DGTCKKDKLK RRVVTIDSYA
GVKPNDEKAL KEAVAAQPIS VGICGSERAF QLYSSGIFSG PCSTSLDHAV LIIGYGSQNG
VDYWIVKNSW GKSWGMDGYM HMQRNTGNSE GVCGINMLAS YPIKTHPNPP PPSPSGPTKC
NLFTYCSAGE TCCCARNLFG LCFSWKCCEI DSAVCCKDGR HCCPHDYPVC DTTRSLCLKK
TGNFTAIKPF WKKDSSNKLG RFEEWVM
//
