ID F0VKJ3_NEOCL Unreviewed; 1841 AA.
AC F0VKJ3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=subtilisin {ECO:0000256|ARBA:ARBA00023619};
DE EC=3.4.21.62 {ECO:0000256|ARBA:ARBA00023619};
GN ORFNames=BN1204_050220 {ECO:0000313|EMBL:CEL69308.1}, NCLIV_050220
GN {ECO:0000313|EMBL:CBZ54594.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ54594.1, ECO:0000313|Proteomes:UP000007494};
RN [1] {ECO:0000313|EMBL:CBZ54594.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ54594.1};
RA Aslett M.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBZ54594.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CBZ54594.1};
RA Reid A.J., Sohal A., Harris D., Quail M., Sanders M., Berriman M.,
RA Wastling J.M., Pain A.;
RT "Comparative genomics and transcriptomics of Neospora caninum and
RT Toxoplasma gondii.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {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).
RN [4] {ECO:0000313|EMBL:CEL69308.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Liverpool {ECO:0000313|EMBL:CEL69308.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
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; FR823391; CBZ54594.1; -; Genomic_DNA.
DR EMBL; LN714485; CEL69308.1; -; Genomic_DNA.
DR RefSeq; XP_003884624.1; XM_003884575.1.
DR GeneID; 13442525; -.
DR VEuPathDB; ToxoDB:NCLIV_050220; -.
DR eggNOG; KOG1153; Eukaryota.
DR InParanoid; F0VKJ3; -.
DR OrthoDB; 380531at2759; -.
DR Proteomes; UP000007494; Chromosome X.
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 1473..1737
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 46..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1118..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1362..1446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 826..848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1172..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1362..1387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1414..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1480
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1536
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 1700
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1841 AA; 197807 MW; 30C2E34B59D1FFF3 CRC64;
MLPTPPSDML PSSNHPGTFS AAISSAIPAV KTIEHVADFF PAAHEGGSSF QSSQKETYHI
PVSASQQSPQ TPSMQQSVPL PQLPPTVSIG SYVLDNVAAS SPGSRLVGAT PLSGPKVGHP
VEGSPVLNAK ADKDGWFPIE DLKLSRTHFD VTLKQGERLT LPFSLTANEK AKVFLRAAAN
FEKSARTIER TADLLFMHEI EERQSQMRRD RERQQNRPDL DCRTSDGPCL SAGAFVRDSG
SPEQVEHLSV QQSPTPVPYH AGRRLGTASS PFHVSDAAHP HYHANLGGAP AVTPSDDRRG
GTRPRRRPEL AARANGVQRA IAGAGDARPS SGGSEAPEKY AGSSSLDGLG RSTTGIPTSA
GGRIQGTPNW QYRRQVPSAP NSSTGESYSI RGTGAPSSAN PAVPDNPFHP LAYDALPVEP
WEGWSHSLKL LAAETRKVDW STSQRMLQSV RLQVGAAITS DLATSVRSDA SDLDLPSSSR
ISGRRGEARG LGLVTKDVSR DRGGAQSSST SVGSLGEERG PALPLSKLEV QEIDSTNNWQ
SHSNPESLSH NVGNLEASSP MKKLHQLVGE ATEFRVAASL LDHDKAQDSE KRDNVPVSSQ
KGAGNVNFLS ETRGAVTNAS PSTLLDSSKA DSPTANLPKR KTTKTSLSMP DRRQSQMIVV
NVEALGSPID KDTGRPLFYN DRILVGWRCS DRELLALKAL DLEEEEEEVG QDESGQWSPT
SSVVNVEGEM PSLSVPPSQA LPEDPRISTA DEEPHVSVPC AQPDLNRSSF AKEESERRVC
GYVPPDLGID IRSLRDSRRT TSASSSSSNP AFPLDLSRVS ELWPNAPRPR NNTVESSTFA
NVNRNDNSSS WESRAAGFFP YESQTQQASR PGLPELSGDT LGAPPRRLQV LDRMLKSFAS
PEVESVKTLF RRLPQKRSLR KKAHHDETWQ RAENHIDNQR AVNASAAQTK YSNFGLGTSS
RDSAEARRNP VSRAGNNTAS TGGARTSKGN SDSGGGWMYE SEHAQEPGTG GKLEGGRGAK
NNRDNGTENS KLGESVRRRL LDDDELCGMD LIKLSLQHYR ARVEGTRHDA DPANNFEDVE
ALKAFMKEFA SHDYVGDILF LAPDAPIHAQ AFSAVMESDT MSADRDESAP ASSTSKHPTK
NETKGEQAKT RPANAEQRLA LGPAGGDSRG RNNARGKSTV ARSTFPSRNA EQKSAFLNKT
FIAGNDRPFD LRGVGGPGRY ATSSVSTEER VLDETHGGRG LGSREQSDQQ NNLKRSLQRT
PQVSESGEWE SGGPVIPNDP LFTLQWALGS PPQDSHMTAE FCYMRAREEL EGRASEAIER
GTAGPPQPTP SSSQLAKVRQ LCAAAGHKDK NVTGEKIRST ALAEEAEHEQ GGETDQQIWE
DERGETTPDS ASTLQSETHK ADVQELEGDM ENGPSSPSPK TSATLHALQG SHMGTGGGPA
IGESSADTNS IDMVKAWQLS LSPQEDDKRK KPEVLVAVID TGVNYIHSDL AKSIWVNEQE
LNGVPGFDDD QNGYIDDVYG WNFLHGNNNP MDDNGHGSHV AGIIGAQRNN YQGVSGISSH
ARIIALKILN KKGEGDVSHA IPAIRYALDN GAKVITNSWG GISGPGTQIL GVLLKEAVAD
ASGSVFVIAA GNDGMDISKD PYYPASFLRD WTITVAAHAR DGALPKWSNY GHNTVHLTAP
GENITSTWMG SGYRLSSGTS MAAPMVSGVA AEILAYNPML QPQQVVDVLV QSAITDKRHA
NVSLTGARLN AYRAIVLSQL QFISLSPAEL HVGGTADPIG EVEILFQSLM LPPGVYEGNI
ELVYSRRLAS TRGLGVLSGV LKRRIVQLVQ VTLPVKLTIV Q
//
