ID C8TDY4_EIMTE Unreviewed; 291 AA.
AC C8TDY4;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=e1034b12.tmp1 {ECO:0000313|EMBL:CAK51470.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CAK51470.1, ECO:0000313|Proteomes:UP000243681};
RN [1] {ECO:0000313|EMBL:CAK51470.1, ECO:0000313|Proteomes:UP000243681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CAK51470.1,
RC ECO:0000313|Proteomes:UP000243681};
RX PubMed=17284678; DOI=10.1101/gr.5823007;
RA Ling K.H., Rajandream M.A., Rivailler P., Ivens A., Yap S.J.,
RA Madeira A.M.B.N., Mungall K., Billington K., Yee W.Y., Bankier A.T.,
RA Carroll F., Durham A.M., Peters N., Loo S.S., Mat-Isa M.N., Novaes J.,
RA Quail M., Rosli R., Shamsudin M.N., Sobreira T.J.P., Tivey A.R., Wai S.F.,
RA White S., Wu X., Kerhornou A.X., Blake D., Mohamed R., Shirley M.,
RA Gruber A., Berriman M., Tomley F., Dear P.H., Wan K.L.;
RT "Sequencing and analysis of chromosome 1 of Eimeria tenella reveals a
RT unique segmental organization.";
RL Genome Res. 17:311-319(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000256|ARBA:ARBA00023529};
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC ProRule:PRU01240}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AM269894; CAK51470.1; -; Genomic_DNA.
DR AlphaFoldDB; C8TDY4; -.
DR VEuPathDB; ToxoDB:ETH2_0102900; -.
DR VEuPathDB; ToxoDB:ETH_00009790; -.
DR Proteomes; UP000243681; Chromosome 1, ordered contigs.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 3.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 3.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CAK51470.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 18..163
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
SQ SEQUENCE 291 AA; 30240 MW; B49DA7F7AC463E0D CRC64;
MLRVWALGAL ESSKSAAVPV AVVDTGINYL HPELSLSMWV NRKELHGEEG VDDDGNGFVD
DLFGWNFIQD NNNPMDDNGH GSHVAGIVAA LQNNGEGISG ISERAKVMAL KILDQKGEGD
VSHAIPAIQY AVDNGAKVLT NSWGGVSDVS HAIPAIQYAV DNGAKVLTNS WGGVSDVSHA
IPAIQYAVDN GAKVLTNSWG GVSDVSHAIP AIQYAVDNGA KVLTNSWGGV SDVSHAIPAI
QYAVDNGAKV LTNSWGGVSD VSHAIPAIQY AVDNGAKVLT NSWGGVSGTK P
//
