ID F0VAG6_NEOCL Unreviewed; 345 AA.
AC F0VAG6;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Protease Do (Precursor), related {ECO:0000313|EMBL:CBZ50655.1};
DE EC=3.4.21.107 {ECO:0000313|EMBL:CBZ50655.1};
GN ORFNames=NCLIV_011220 {ECO:0000313|EMBL:CBZ50655.1};
OS Neospora caninum (strain Liverpool).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ50655.1, 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 -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; FR823384; CBZ50655.1; -; Genomic_DNA.
DR RefSeq; XP_003880688.1; XM_003880639.1.
DR AlphaFoldDB; F0VAG6; -.
DR GeneID; 13441684; -.
DR VEuPathDB; ToxoDB:NCLIV_011220; -.
DR eggNOG; KOG1320; Eukaryota.
DR InParanoid; F0VAG6; -.
DR OrthoDB; 276064at2759; -.
DR Proteomes; UP000007494; Chromosome IV.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939:SF125; PROTEASE DO-LIKE 14-RELATED; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBZ50655.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CBZ50655.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT DOMAIN 234..325
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 18..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 36376 MW; 47351E8837FF01BE CRC64;
MHVYGCVVVT AAHLFDERSS NASSSSEAAS VAGTETVSAP LPRPREAPHL SNVSPPPKPG
DGKEEEVVYV VKMNDGQLLW GDFRGKDTRS DVAVLRLRAP HGDRPLCLPS VSLHSPVRDR
RRGEKTESPY RPRLGEFVVA VGTTYYGDEP VGACGIVSQP CQSFSALNAG TNVGFIQLGV
ITLPGMSGSL VANMRGEVVG MVVKKFQDYG LALPIHFVTA VCDQLDATGH YQAPSLGLVF
QQPASLADVA AFASSEDTPC IAPREQHLRV DSVVPGSPAE KAGIQKRDVV VAADGSAVCN
LHALFDFILS RAPGEAVVLD VLRANIKRTC KVILSPPAGP AGPPG
//
