ID A0A183JDT0_9TREM Unreviewed; 245 AA.
AC A0A183JDT0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Pept_C1 domain-containing protein {ECO:0000313|WBParaSite:SCUD_0000084201-mRNA-1};
GN ORFNames=SCUD_LOCUS843 {ECO:0000313|EMBL:VDO64130.1};
OS Schistosoma curassoni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6186 {ECO:0000313|Proteomes:UP000050789, ECO:0000313|WBParaSite:SCUD_0000084201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SCUD_0000084201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO64130.1, ECO:0000313|Proteomes:UP000279833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dakar {ECO:0000313|EMBL:VDO64130.1}, and Dakar, Senegal
RC {ECO:0000313|Proteomes:UP000279833};
RG Pathogen Informatics;
RL Submitted (NOV-2018) 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; UZAK01000621; VDO64130.1; -; Genomic_DNA.
DR STRING; 6186.A0A183JDT0; -.
DR WBParaSite; SCUD_0000084201-mRNA-1; SCUD_0000084201-mRNA-1; SCUD_0000084201.
DR Proteomes; UP000050789; Unplaced.
DR Proteomes; UP000279833; 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; IPR000169; Pept_cys_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:SF741; CATHEPSIN K; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 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:UP000279833};
KW Signal {ECO:0000256|SAM:SignalP};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..245
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041048912"
FT DOMAIN 53..113
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 148..245
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 245 AA; 28666 MW; 115D83D48A6264CA CRC64;
MIRLLFYLHL IVNVYPNHTY IHNNSSYGVI DQNINHTTND NDNDHDDDDD LLWLQWKSLH
HKNYSTHKEY NEHRENWLYN LHSMKQHNLM YDKGLVLYTI GLNQFSDLNW SHITTIYLTN
LSQYLNKHKQ KSQMLLKQSL NETILKEIPD SWDWRKVGAV SKVKIQGKCG ACWAFSAAGA
LEGQLKNRTG TFVELSPQQL IDCSHSFGNH GCLGGDMNNA FRYVEKDGIQ SEESYPYLTK
VYDYM
//
