ID A0A430QDE5_SCHBO Unreviewed; 371 AA.
AC A0A430QDE5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Cathepsin L {ECO:0000313|EMBL:RTG85715.1};
GN ORFNames=DC041_0001617 {ECO:0000313|EMBL:RTG85715.1};
OS Schistosoma bovis (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6184 {ECO:0000313|EMBL:RTG85715.1, ECO:0000313|Proteomes:UP000290809};
RN [1] {ECO:0000313|EMBL:RTG85715.1, ECO:0000313|Proteomes:UP000290809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TAN1997 {ECO:0000313|EMBL:RTG85715.1,
RC ECO:0000313|Proteomes:UP000290809};
RA Oey H., Zakrzewski M., Gobert G., Gravermann K., Stoye J., Jones M.,
RA Mcmanus D., Krause L.;
RT "Genome sequence of the bovine parasite Schistosoma bovis Tanzania.";
RL PLoS Pathog. 0:0-0(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:RTG85715.1}.
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DR EMBL; QMKO01001921; RTG85715.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430QDE5; -.
DR STRING; 6184.A0A430QDE5; -.
DR Proteomes; UP000290809; 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:SF971; CATHEPSIN L-RELATED; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 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:UP000290809};
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..371
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019238542"
FT DOMAIN 61..121
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 149..370
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 371 AA; 41057 MW; 6434F7771F831533 CRC64;
MRCLLCLSAL FVIVVGDPGY KKWSNLEPSL SLGRLLEQQV IEGGVSSSVN VDLLADIMSA
WKFFKIHFKR VYDSIHEETR RFFIFGANFV KMVEHNHAYQ EGKVTYKMGV NEFTDKTDYE
LKKLRGYKVT GGAMKHKGST FIRSEHTKLP GSVDWRREGA VTDVKNQGQC GSCWAFSTTG
AIEGQHYRKT NHLVNLSEQQ LVDCSKSYGN NGCSGGLMNS AFEYVRDNKG IDSEISYPYI
SGNGTENMKC LFNASNIVAQ VSGYVSIHEG DERALMDAVA TKGPVSVAIN AGLPSFSMYK
SGVYSDIDCK GTLDDLDHGV LVVGYGKENG HSYWLIKNSW GEDWGENGYI KILKDSHNMC
GVASAASYPL V
//
