ID U6GJT0_EIMAC Unreviewed; 829 AA.
AC U6GJT0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=EAH_00037650 {ECO:0000313|EMBL:CDI78859.1};
OS Eimeria acervulina (Coccidian parasite).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=5801 {ECO:0000313|EMBL:CDI78859.1};
RN [1] {ECO:0000313|EMBL:CDI78859.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI78859.1};
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:CDI78859.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Houghton {ECO:0000313|EMBL:CDI78859.1};
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; HG670924; CDI78859.1; -; Genomic_DNA.
DR RefSeq; XP_013250966.1; XM_013395512.1.
DR AlphaFoldDB; U6GJT0; -.
DR EnsemblProtists; CDI78859; CDI78859; EAH_00037650.
DR GeneID; 25271835; -.
DR VEuPathDB; ToxoDB:EAH_00037650; -.
DR OMA; QLMAMDY; -.
DR OrthoDB; 203101at2759; -.
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; 1.
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 PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
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:0000313|EMBL:CDI78859.1}.
FT DOMAIN 402..653
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 90..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 166..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..729
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 89663 MW; 45E48DB5C8096082 CRC64;
MCAAAAAAAA EVLKRLRNGP EAITLLLKWD FDCLAARRQQ QQQQQQQQQQ FEVYIDLDED
LTRRDAAAAA GAGEGGQLLF TQGVFYRDTA AAKGQQKPHR QQQQQQQQQD SQQEENAPEL
QQQEEEQHQQ ELQQQQQQQQ QQQDRRLGLE HLSRLLGHNL DLAAAVAEQQ QQQQQQQQEE
GETEGGLSPC VSSPVICKEV LLQKLLQQQE AVAVSQYLAF VEVDVVSFSK LKLFMQDAGD
NVEEEILSLI KNNKGDSCIK EASTDITGRL MGLPPRAAAP AAEVAAAAAA AAGATGAAEA
AAAAAAAAAA NAAAANAAAI AAGGAAGKRG AAGAAARAAA AAAETAADAA AAAAAANIKD
PNFLLQWHLR AAEGFYNLAA DKAWAQMQTK TGGAAAAQGE QKEVVVAVLD TGCGPHEDIN
NILWRNLKED ENNKKDNDDN GYINDYQGWD FVGDTNNIAD TYGHGTAVAS LIAASFDDKG
GRGVSPTGKV MCLRVGDNNG VLLSRQLMAM DYVMQQGAQV SVHPFSLETE SAVYREAFEK
LLSLNHLAVV AAGDDDCDLD LDECKSFPAS FHIPEPSGLL VVGSSTYAGS KTRTSNYGKQ
SVHLFAPGHR LYTATVVQGS PPGITCTNFG CFVAAAAAAA TAGAAGVVLL LLQIMLSLKG
SEETLGDASL ALLHSPQSFR GPRTYSYNLR DNPQRRLKQQ QQQQQQQEQQ QEQRPQRQQD
EEEDYQQHHQ QQQQELQEQE QEQQQQQQQQ QQQQQDEGAK HLLQRQPLAS KTDSVELPVF
AYFPMGSCET NGIVSLYKAL LYSEESSPPE FEPLYSDYPT IFKGRLPPF
//
