ID A0A0V1I193_9BILA Unreviewed; 430 AA.
AC A0A0V1I193;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Chymotrypsin-like elastase family member 1 {ECO:0000313|EMBL:KRZ16680.1};
GN Name=CELA1 {ECO:0000313|EMBL:KRZ16680.1};
GN ORFNames=T11_2583 {ECO:0000313|EMBL:KRZ16680.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ16680.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ16680.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ16680.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ16680.1}.
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DR EMBL; JYDP01000010; KRZ16680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I193; -.
DR STRING; 268475.A0A0V1I193; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..430
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006879596"
FT DOMAIN 38..282
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 287..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 47444 MW; E017A98BE09967DC CRC64;
MIAYKCIILL GYITLAFAKY ECGTTAHPFP RSLKANRISG GSVVTPNSVP YQARLLFEKL
DGKLKGCGGS LIELKPGNGS QWVLTAAHCT YYAEYRRDFT PEKVEVIFGA HRPAETEKTQ
LTVGAKRIIS HPRYDDRTLA YDISLVLLKE YVIYNNEIRS VCMPKAGEPI PLDVPCYVSG
WGKTHHGGQG SDVLKIAEMN ILKKEECRIP AEQHAIIFCA AGTSRSATCQ GDSGGPLVCL
INNKATLYGI VSAGPVMCGD LRQPGEFTRV PAMMEWIQES AQRVDSAVPA VSRFEPKPNE
KKGDDNGKQQ PSPSVSPSKV DDGQKDITKD FMNIPSRDNV KDTNDYKGAD VFNFIYRETL
PSRSRFPDFD HMVSNFMSPG IGGMKGGSFF SSSPGVYRET RTVNRLPSVS RSKSDVGRFG
FNDPAFTYFR
//
