ID A0A3Q0KPV9_SCHMA Unreviewed; 359 AA.
AC A0A3Q0KPV9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=SmCL2-like peptidase (C01 family) {ECO:0000313|WBParaSite:Smp_149730.1};
OS Schistosoma mansoni (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6183 {ECO:0000313|Proteomes:UP000008854, ECO:0000313|WBParaSite:Smp_149730.1};
RN [1] {ECO:0000313|Proteomes:UP000008854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Puerto Rican {ECO:0000313|Proteomes:UP000008854};
RX PubMed=22253936; DOI=10.1371/journal.pntd.0001455;
RA Protasio A.V., Tsai I.J., Babbage A., Nichol S., Hunt M., Aslett M.A.,
RA De Silva N., Velarde G.S., Anderson T.J., Clark R.C., Davidson C.,
RA Dillon G.P., Holroyd N.E., LoVerde P.T., Lloyd C., McQuillan J.,
RA Oliveira G., Otto T.D., Parker-Manuel S.J., Quail M.A., Wilson R.A.,
RA Zerlotini A., Dunne D.W., Berriman M.;
RT "A systematically improved high quality genome and transcriptome of the
RT human blood fluke Schistosoma mansoni.";
RL PLoS Negl. Trop. Dis. 6:E1455-E1455(2012).
RN [2] {ECO:0000313|WBParaSite:Smp_149730.1}
RP IDENTIFICATION.
RC STRAIN=Puerto Rican {ECO:0000313|WBParaSite:Smp_149730.1};
RG WormBaseParasite;
RL Submitted (DEC-2018) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase C1 family.
CC {ECO:0000256|ARBA:ARBA00008455}.
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DR AlphaFoldDB; A0A3Q0KPV9; -.
DR STRING; 6183.A0A3Q0KPV9; -.
DR EnsemblMetazoa; Smp_149730.1; Smp_149730.1; Smp_149730.
DR WBParaSite; Smp_149730.1; Smp_149730.1; Smp_149730.
DR InParanoid; A0A3Q0KPV9; -.
DR Proteomes; UP000008854; 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: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 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:UP000008854};
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..359
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018749487"
FT DOMAIN 49..109
FT /note="Cathepsin propeptide inhibitor"
FT /evidence="ECO:0000259|SMART:SM00848"
FT DOMAIN 145..358
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 359 AA; 41586 MW; 7F1F1A6D328E2A0A CRC64;
MITLLFYLHL IVHVYPNHTH THNSNNNSYD VTDQQVNHTT IIDNDDLLWL QWKHLHQKNY
STYKEYNEHR KNWLYNLHSI KQHNLMHDKG LELYTIGLNQ FSDLNWSHIS TIYLTNLSQY
FLNRHKKQSQ ILLKQSLNET RLKEIPDSWD WRKVGVVSKV KVQGECGACW AFSAAGALEG
QLKNRNGPFV ELSSQQLIDC SHSFGNHGCL GGDMNNAFRY VEKDGIQSEE SYPYLTKEGK
CQHIKSTSLT YSKSIIEIKL NDEEQLKYVL YEHGPVSAGI NVEQQFMRYK SGIYQSQSCS
STEVNHAVLI VGYGEENGVQ YWTIKNSWGT SWGEEGYVRM RRNYNNMCGI ATMASVPKL
//
