ID A0A3L6S8D9_PANMI Unreviewed; 348 AA.
AC A0A3L6S8D9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Cysteine protease {ECO:0000313|EMBL:RLN17240.1};
GN ORFNames=C2845_PM02G22780 {ECO:0000313|EMBL:RLN17240.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN17240.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
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:RLN17240.1}.
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DR EMBL; PQIB02000005; RLN17240.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6S8D9; -.
DR STRING; 4540.A0A3L6S8D9; -.
DR Proteomes; UP000275267; Chromosome 2.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
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; 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:SF763; OS09G0381400 PROTEIN; 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; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:RLN17240.1};
KW Protease {ECO:0000313|EMBL:RLN17240.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..348
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018628451"
FT DOMAIN 44..101
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 133..347
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 348 AA; 37778 MW; B0DFEC51F3B8C7B1 CRC64;
MALSSGSASW LLALILFACG LIMSAAAGDA GGGGGDDRLM MGRFLRWLAE YNRSYPTAEE
RQRRFQVYRR NIEHIEATNR AGNLTYTLGE NQFADLTEQE FLDLYTMKGM PTGSADAGRE
QAANVSFSAV VDGPTSVDWR AQGAVTPIKN QGPSCSSCWA FVTAATIESI TKIRTGKLVS
LSEQELIDCD PYDGGCNLGY FVNGYRWVIE NGGLTTDGSY PYQARRYACN HNKAAQHAAQ
ISDYVKVPAG EGQLQQAVAK QPVAAAIEMG GSLQFYKGGV FSGQCGTRMN HAITVVGYGA
DANTGLKYWL VKNSWGQSWG ERGYLRMRRD FTHSGLCGIA LDLAYPVV
//