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Database: UniProt
Entry: F0VFK9_NEOCL
LinkDB: F0VFK9_NEOCL
Original site: F0VFK9_NEOCL 
ID   F0VFK9_NEOCL            Unreviewed;       581 AA.
AC   F0VFK9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Renin, related {ECO:0000313|EMBL:CBZ52503.1};
GN   ORFNames=NCLIV_022920 {ECO:0000313|EMBL:CBZ52503.1};
OS   Neospora caninum (strain Liverpool).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ52503.1, 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 A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; FR823388; CBZ52503.1; -; Genomic_DNA.
DR   RefSeq; XP_003882535.1; XM_003882486.1.
DR   AlphaFoldDB; F0VFK9; -.
DR   MEROPS; A01.087; -.
DR   GeneID; 13444583; -.
DR   VEuPathDB; ToxoDB:NCLIV_022920; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   InParanoid; F0VFK9; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000007494; Chromosome VIIa.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR033121; PEPTIDASE_A1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007494}.
FT   DOMAIN          239..577
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        439
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        270..274
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   581 AA;  63690 MW;  DCD82AA7118C8F3E CRC64;
     MDTRIMSPSS RFRNLVNTQA SSHEVGKRSS LYASLLDSPP VSFLPGGSAV AERDVEDESW
     QDPAGSFSRG AKTIDRACAF TRLREFTSLR DPLGFFNHAK KRHGQGKAGG RLPSVLCITA
     LCRERFLLFF CSTPGVVKSR PVYSSQLFAG WSCWLFTGKW KCAVLRCPFR SGVMVMPLRK
     MKSLRQIGWE RNSITVPDLQ AHLVASLRQQ EGLSKRDGNF SGPSDGDDIS IHDYMNAQYY
     TEIYVGSPGQ KVRVVVDTGS SDLWVCSASC GMLCMLHKTY NHGKSETYQE DGTPYHVEYA
     SGPVGGFLSV DDVALASLRA AKFLLAEAVD LKGLGTAFFF GKFDGILGMG FPALATNGLK
     PFMQVAVEQN VVKNWIFAFY LGSANGVDGE LAIGGVDEER FIGDINFSKV VDSRYWMIDT
     KGLKSNGDLV APTTKMIIDS GTSLIAGPLD EVKRIANMMG AFAVPLMPEG TFFISCDKEK
     VLRDLQLEVE GQDYPIKIKD LLIPVSTAPG APCLFGMMGL KALEGDASTP KGVKGFPTPR
     LLASEKGPIG RTWILGDLFM RNVYTVFDYD NKQIGFARLR N
//
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