ID U6KY95_EIMTE Unreviewed; 1122 AA.
AC U6KY95;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=ETH_00009270 {ECO:0000313|EMBL:CDJ42911.1};
OS Eimeria tenella (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5802 {ECO:0000313|EMBL:CDJ42911.1};
RN [1] {ECO:0000313|EMBL:CDJ42911.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42911.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ42911.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ42911.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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; HG675744; CDJ42911.1; -; Genomic_DNA.
DR RefSeq; XP_013233661.1; XM_013378207.1.
DR AlphaFoldDB; U6KY95; -.
DR EnsemblProtists; CDJ42911; CDJ42911; ETH_00009270.
DR GeneID; 25251055; -.
DR VEuPathDB; ToxoDB:ETH2_1025400; -.
DR VEuPathDB; ToxoDB:ETH2_1025700; -.
DR VEuPathDB; ToxoDB:ETH_00009270; -.
DR OrthoDB; 1330511at2759; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07473; Peptidases_S8_Subtilisin_like; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034204; PfSUB1-like_cat_dom.
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; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CDJ42911.1};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 690..913
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 120..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1091
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 114301 MW; 716EF37C767E70EF CRC64;
MKNKEAAASL KWRSRGSCVV VAAATEAAVL QQHRQRHGEG AAADATATTA EADAAAAAEP
TAAVAEVDVG AAAAGGATAA AAPAATQQAV AAAAAAKSST SDSKIFLEFP CGASAGNMRA
AEAAGTGPPA PAASAASRRS PSPSAAAAAA GEAAAAATAA ANRKEKVAEA AADAAASAST
VKRAALAALR TADLSPAKRL HRETLQQQQQ QQQQQQQQQQ QQQQQQPSSP LMRAAATPLR
TGRKGQEAAA SSASLPAASG AAATDSAVAA AAAAAAAEAA EAVSPIGSPA PPRRVQQQQR
AGDLLQQAST PISSSRPRPP SSSSSSSSSS RKEPSLAAVP LPFRKGFNRV AEAGGPLRLP
QLGALFGFLG DLRAPLPLLQ VVGAAGSGKS FLLQLLLAEC SVAHGYVDAA AAAAVDGSAG
RNLLYLRLLR SLSASLKHEA EACCEPLFKH QQQQQQSQEA AEGLKDESFQ KLQGQLTVLQ
QQHKLLLQEC SKASKTRVTA PDAFIEMLGQ LLTASGGALG AAAAAAAAAA TAGWEGAAAV
QQEATDRAAR SAVLLVDGTE SLRQLLPELL QALLRLPELM YGCDLAAVTA SASSSSSSSS
RGVCVVLIGR RPLAAEALDG LPPPPLVRFE AYGRDAAAFV LQRSFFSLGL PLLQLLHLLQ
HFRTLLFPCA VPASPAAPAV CAACSACNGY VDDYHGYDFE RGSADPMDEH GHGTHVAGIV
AASANNGIGI AGANWRVKLM PLKFEKRSSA AVEAIAYSLQ MGAKISTNSW GFSFRSEALR
LALEQAEAKG QLFVAAVDNA GADNTTAKDF PPNWGYDWRT GRGFKNMLRV ANLAPTGKLS
TSSNYGKYNV DLAAPGTDII STLPARQFGD KYGYKSGTSM ATPLVAGIAA LVWAERPSLT
AAEVRDVLLS TAAPLPPLKA AVASGGTVNA HAAVELVHAL NQRDMGLEEP QAAAFAHWQQ
QQQQHQIQLL HASAPAPSAN AGDAAAAAAI ADQTLPPIPS PATAAAAAAA GQMTTDGYGY
DVAAAAAAAA PGTGYVYNVV IPPEPVGGSE SAPLPSSPDT SSISSGSNSS SSNSSSSNSS
NENIKGSTSA ASSPISFFSR LLDPFALIAR FVRIDTDLAR NN
//
