ID A0A0N4WEG5_HAEPC Unreviewed; 353 AA.
AC A0A0N4WEG5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pept_C1 domain-containing protein {ECO:0000313|WBParaSite:HPLM_0000903001-mRNA-1};
GN ORFNames=HPLM_LOCUS9022 {ECO:0000313|EMBL:VDO36395.1};
OS Haemonchus placei (Barber's pole worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Trichostrongylidae; Haemonchus.
OX NCBI_TaxID=6290 {ECO:0000313|Proteomes:UP000038042, ECO:0000313|WBParaSite:HPLM_0000903001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:HPLM_0000903001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO36395.1, ECO:0000313|Proteomes:UP000268014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHpl1 {ECO:0000313|EMBL:VDO36395.1,
RC ECO:0000313|Proteomes:UP000268014};
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; UZAF01016979; VDO36395.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N4WEG5; -.
DR STRING; 6290.A0A0N4WEG5; -.
DR WBParaSite; HPLM_0000903001-mRNA-1; HPLM_0000903001-mRNA-1; HPLM_0000903001.
DR OMA; WPIRAWE; -.
DR Proteomes; UP000038042; Unplaced.
DR Proteomes; UP000268014; 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; cd02620; Peptidase_C1A_CathepsinB; 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 PANTHER; PTHR12411:SF895; CATHEPSIN B; 1.
DR PANTHER; PTHR12411; CYSTEINE PROTEASE FAMILY C1-RELATED; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
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:UP000268014};
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..353
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033720968"
FT DOMAIN 94..347
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
SQ SEQUENCE 353 AA; 39230 MW; 216A87902FA44363 CRC64;
MGSFLLEHLV LTLCLYLCRT LGADTDDAQE IPLHAQMLTG APLVEYLQKN QELFEVRTTP
TPGFKYKLMD VAFANANQNL NPVVNDDNDT GADLPENYDP RIVWRNCSSF HTIRDQANCG
SCWAVSTAAA ISDRICVATK GKKQVYISAT DILTCCGAPC GMGCQGGWPI RAWEFFEYDG
VVSGGPYLGK GCCSPYPLHP CGQHGNDTFY GNCRGMAPTP PCKKRCQPGF RGMYRIDKRY
GEPGRAYRLP KSEVKIRREI KERGSVTATF AVYEDFSHYK SGIYKHTAGY ITGFHAVKMI
GWGKDINGTD YWLIANSWHD DWGENGFFRM IRGINDCGIE ETVAAGIVDV ESL
//
