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
//