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Database: UniProt
Entry: F0VDF5_NEOCL
LinkDB: F0VDF5_NEOCL
Original site: F0VDF5_NEOCL 
ID   F0VDF5_NEOCL            Unreviewed;       290 AA.
AC   F0VDF5;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 62.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase {ECO:0000256|RuleBase:RU363019};
DE            Short=PPIase {ECO:0000256|RuleBase:RU363019};
DE            EC=5.2.1.8 {ECO:0000256|RuleBase:RU363019};
GN   ORFNames=BN1204_015405 {ECO:0000313|EMBL:CEL65703.1}, NCLIV_015405
GN   {ECO:0000313|EMBL:CBZ51748.1};
OS   Neospora caninum (strain Liverpool).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=572307 {ECO:0000313|EMBL:CBZ51748.1, ECO:0000313|Proteomes:UP000007494};
RN   [1] {ECO:0000313|EMBL:CBZ51748.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CBZ51748.1};
RA   Aslett M.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBZ51748.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CBZ51748.1};
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:CEL65703.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Liverpool {ECO:0000313|EMBL:CEL65703.1};
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   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. {ECO:0000256|RuleBase:RU363019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC         Evidence={ECO:0000256|RuleBase:RU363019};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family.
CC       {ECO:0000256|RuleBase:RU363019}.
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DR   EMBL; FR823387; CBZ51748.1; -; Genomic_DNA.
DR   EMBL; LN714480; CEL65703.1; -; Genomic_DNA.
DR   RefSeq; XP_003881781.1; XM_003881732.1.
DR   AlphaFoldDB; F0VDF5; -.
DR   GeneID; 13443914; -.
DR   VEuPathDB; ToxoDB:NCLIV_015405; -.
DR   eggNOG; KOG0865; Eukaryota.
DR   InParanoid; F0VDF5; -.
DR   OrthoDB; 339082at2759; -.
DR   Proteomes; UP000007494; Chromosome VI.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   PANTHER; PTHR11071; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE; 1.
DR   PANTHER; PTHR11071:SF561; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE D-RELATED; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; Cyclophilin-like; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU363019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007494};
KW   Rotamase {ECO:0000256|ARBA:ARBA00023110, ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          67..231
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..45
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   290 AA;  32423 MW;  469F3305A5A16251 CRC64;
     MPRFRLPSIT SPSSMRTGPP PSSYMPPAAS SSPPSSSPPA SSRLPPAVAS PLSDAGRRSF
     LPNPLVHLDI SIGGRDAGRM VFQLFADTHP ITAENFRCLC TGETGLGYWM RPRWYKSTPF
     HRIVPGFMCQ GGDIHRGDGR GGESIYGQFF RDERFLYKHS KRGLLSMAKA RRQHTNNSQF
     FITFDACPWL DGEHVVFGQL QSGAEVLDQI EAQGTPGGWK KRPVEIWNCG ELLLNSLREV
     PREATAAVRH QEMLKDLIMD AAERPEKLYE PKEQVIPIPD DVYIKARRGF
//
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