ID F0VQR7_NEOCL Unreviewed; 498 AA.
AC F0VQR7;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=NCLIV_064900 {ECO:0000313|EMBL:CBZ56064.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ56064.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|Proteomes:UP000007494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Liverpool {ECO:0000313|Proteomes:UP000007494};
RX PubMed=22457617; DOI=10.1371/journal.ppat.1002567;
RA Reid A.J., Vermont S.J., Cotton J.A., Harris D., Hill-Cawthorne G.A.,
RA Konen-Waisman S., Latham S.M., Mourier T., Norton R., Quail M.A.,
RA Sanders M., Shanmugam D., Sohal A., Wasmuth J.D., Brunk B., Grigg M.E.,
RA Howard J.C., Parkinson J., Roos D.S., Trees A.J., Berriman M., Pain A.,
RA Wastling J.M.;
RT "Comparative genomics of the apicomplexan parasites Toxoplasma gondii and
RT Neospora caninum: Coccidia differing in host range and transmission
RT strategy.";
RL PLoS Pathog. 8:e1002567-e1002567(2012).
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, ECO:0000256|RuleBase:RU003355}.
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DR EMBL; FR823393; CBZ56064.1; -; Genomic_DNA.
DR RefSeq; XP_003886090.1; XM_003886041.1.
DR AlphaFoldDB; F0VQR7; -.
DR GeneID; 13445287; -.
DR VEuPathDB; ToxoDB:NCLIV_064900; -.
DR eggNOG; KOG1153; Eukaryota.
DR InParanoid; F0VQR7; -.
DR OrthoDB; 1330511at2759; -.
DR Proteomes; UP000007494; Chromosome XII.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
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; IPR023827; Peptidase_S8_Asp-AS.
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; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 179..431
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 103..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 184
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 239
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 399
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 498 AA; 52968 MW; A38CB1813FD90614 CRC64;
MNESANQGET IPLTARVVDE YAAYRTKVIS LDSAKHAEQA GEDDFFVPVR CSISEESLKR
VGVDVIEMRN CEMVGGDEMK AALETDPCVA SVEYDEEFSI DSLYPPEEPA ADQADGDVSE
ASDPLPGRRR LPLASSQTKP VREPVTLAAA AEPGAGYWRH KSGLSDSLYD VADCDPQRVV
AVIDTGVSYT HPALAKNMWV NQNEIPGNDI DDDMNGFVDD VYGFNFRDNR GDPMDDHGHG
THVAGIIGAV KNTNSRVKGV CGSTSIAALK FMGANGNGST SDAIKALNYA VQMGIPLSCN
SWGGPTWSEA LIAALEAAES VGHLFIAAAG NQGRNTDEIP HYPASYRLSN VVSVAATNSE
DQLAPFSNRG EATVDIAAPG VKILSTFPPD QFRELSGTSM ATPVVAGVAA ILMSLPYRDT
KQIKRALVNG VDKMPATEGF VKSGGRVNAS RSLSWLALEL NWGKDLKKLK GTDEEAAEAT
VAEEDRSAQT AAVEPVAA
//
