ID A0A6A3A411_HIBSY Unreviewed; 359 AA.
AC A0A6A3A411;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 8.
DE SubName: Full=Vignain {ECO:0000313|EMBL:KAE8698938.1};
GN ORFNames=F3Y22_tig00110597pilonHSYRG01128
GN {ECO:0000313|EMBL:KAE8698938.1};
OS Hibiscus syriacus (Rose of Sharon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8698938.1, ECO:0000313|Proteomes:UP000436088};
RN [1] {ECO:0000313|EMBL:KAE8698938.1, ECO:0000313|Proteomes:UP000436088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAE8698938.1};
RA Kim Y.-M.;
RT "Draft genome information of white flower Hibiscus syriacus.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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:KAE8698938.1}.
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DR EMBL; VEPZ02001044; KAE8698938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A6A3A411; -.
DR OrthoDB; 5472443at2759; -.
DR Proteomes; UP000436088; 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 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:SF887; CYSTEINE PROTEINASE; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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:UP000436088};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..359
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025500603"
FT DOMAIN 40..95
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 126..341
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 359 AA; 40798 MW; B42D9C31FE8D8C93 CRC64;
MDMWKLFLVV FSLALAFQLA KSFDYHESDL ASEESLWDLY ERWRSHHTIS RDTKEKQKRF
NVFKENLKHI HNVNQMDRPY KLKLNKFADM TNYEFMSTRS SKVSHYRMLH GPRRMTDFQH
GEVDNLPQSI DWRRKGAVTG IKDQGKCGSC WAFSTVVAVE GINKIKTGEL VNLSEQELVD
CDKENQGCDG GLMEQAFKFI KQSNGLTTEK IYPYEAKDES CDSAKLNGPV VIIDGYEMVP
EKDEKALRNA VAQQPVSIAI DAGVKDFQFY SEGVFSGDCG TELNHGVAVV GYGATHDGTK
YWIVKNSWGE DWGEKGYIRM QRDIEAQEGL CGLTLEASYP VKLHANNDGK ASQQAKDEL
//
