ID   PPIA_NEOCA              Reviewed;         178 AA.
AC   P84343;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin;
DE   AltName: Full=NcCyP;
DE   AltName: Full=Rotamase;
DE   Flags: Precursor;
OS   Neospora caninum (Coccidian parasite).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC   Eucoccidiorida; Eimeriorina; Sarcocystidae; Neospora.
OX   NCBI_TaxID=29176;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Tachyzoite;
RA   Cole R., Fogarty S., Tang K., Howe D.K., Sibley L.D., Clifton S., Marra M.,
RA   Hillier L., Pape D., Martin J., Wylie T., Theising B., Bowers Y.,
RA   Gibbons M., Ritter E., Bennet J., Ronko I., Tsagareishvili R., Fedele M.,
RA   Belaygorod L., Franklin C., Carr L.M., Grow A., Maguire L., Wadkins J.,
RA   Richey J., Waterston R., Wilson R.;
RT   "USDA-WashU Neospora EST project.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 24-38; 54-63; 70-105; 109-131 AND 145-169, AND
RP   FUNCTION.
RC   STRAIN=Nc-1 {ECO:0000269|PubMed:16041025};
RC   TISSUE=Tachyzoite {ECO:0000269|PubMed:16041025};
RX   PubMed=16041025; DOI=10.1128/iai.73.8.5093-5100.2005;
RA   Tuo W., Fetterer R., Jenkins M., Dubey J.P.;
RT   "Identification and characterization of Neospora caninum cyclophilin that
RT   elicits gamma interferon production.";
RL   Infect. Immun. 73:5093-5100(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the
CC       cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides. Up-regulates interferon gamma production by bovine T-
CC       cells. Stimulates high levels of IFN-gamma production by peripheral
CC       blood mononuclear cells and T-cells. The IFN-gamma-inducing effect is
CC       blocked by cyclosporin A (CsA). {ECO:0000269|PubMed:16041025}.
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:0000250|UniProtKB:P30405};
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CF422590; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; P84343; -.
DR   SMR; P84343; -.
DR   VEuPathDB; ToxoDB:Ncaninum_LIV_000730500; -.
DR   VEuPathDB; ToxoDB:NCLIV_004790; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:InterPro.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PIRSF; PIRSF001467; Peptidylpro_ismrse; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isomerase; Rotamase; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..178
FT                   /note="Peptidyl-prolyl cis-trans isomerase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000043374"
FT   DOMAIN          26..177
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00156"
SQ   SEQUENCE   178 AA;  19379 MW;  D67E4267B3D65D7D CRC64;
     MKLLFFFLVL AVSAAVAENA GVQKAFMDIE IDGESAGRIV LELRGDVVPK TVKNFIGLFD
     KYKGSTFHRV IADFMIQGGD FENHNGTGGH SIYGPRFEDE NFTLKHDRGV ISMANAGPNT
     NGSQFFITTV KTEWLDGRHV VFGKITNDSW PTVQAIEALG SSGGRPSKIA KITDIGLL