ID   Q7RRM6_PLAYO            Unreviewed;       202 AA.
AC   Q7RRM6;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   24-JAN-2024, entry version 136.
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=PY00693 {ECO:0000313|EMBL:EAA17886.1};
OS   Plasmodium yoelii yoelii.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=73239 {ECO:0000313|EMBL:EAA17886.1, ECO:0000313|Proteomes:UP000008553};
RN   [1] {ECO:0000313|EMBL:EAA17886.1, ECO:0000313|Proteomes:UP000008553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17XNL {ECO:0000313|EMBL:EAA17886.1,
RC   ECO:0000313|Proteomes:UP000008553};
RX   PubMed=12368865; DOI=10.1038/nature01099;
RA   Carlton J.M., Angiuoli S.V., Suh B.B., Kooij T.W., Pertea M., Silva J.C.,
RA   Ermolaeva M.D., Allen J.E., Selengut J.D., Koo H.L., Peterson J.D., Pop M.,
RA   Kosack D.S., Shumway M.F., Bidwell S.L., Shallom S.J., van Aken S.E.,
RA   Riedmuller S.B., Feldblyum T.V., Cho J.K., Quackenbush J., Sedegah M.,
RA   Shoaibi A., Cummings L.M., Florens L., Yates J.R., Raine J.D., Sinden R.E.,
RA   Harris M.A., Cunningham D.A., Preiser P.R., Bergman L.W., Vaidya A.B.,
RA   van Lin L.H., Janse C.J., Waters A.P., Smith H.O., White O.R.,
RA   Salzberg S.L., Venter J.C., Fraser C.M., Hoffman S.L., Gardner M.J.,
RA   Carucci D.J.;
RT   "Genome sequence and comparative analysis of the model rodent malaria
RT   parasite Plasmodium yoelii yoelii.";
RL   Nature 419:512-519(2002).
RN   [2] {ECO:0007829|PDB:2B71}
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 7-202.
RX   PubMed=17125854; DOI=10.1016/j.molbiopara.2006.10.011;
RA   Vedadi M., Lew J., Artz J., Amani M., Zhao Y., Dong A., Wasney G.A.,
RA   Gao M., Hills T., Brokx S., Qiu W., Sharma S., Diassiti A., Alam Z.,
RA   Melone M., Mulichak A., Wernimont A., Bray J., Loppnau P., Plotnikova O.,
RA   Newberry K., Sundararajan E., Houston S., Walker J., Tempel W.,
RA   Bochkarev A., Kozieradzki I., Edwards A., Arrowsmith C., Roos D., Kain K.,
RA   Hui R.;
RT   "Genome-scale protein expression and structural biology of Plasmodium
RT   falciparum and related Apicomplexan organisms.";
RL   Mol. Biochem. Parasitol. 151:100-110(2007).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAA17886.1}.
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DR   EMBL; AABL01000189; EAA17886.1; -; Genomic_DNA.
DR   PDB; 2B71; X-ray; 2.50 A; A=7-202.
DR   PDBsum; 2B71; -.
DR   AlphaFoldDB; Q7RRM6; -.
DR   SMR; Q7RRM6; -.
DR   STRING; 73239.Q7RRM6; -.
DR   PaxDb; 73239-Q7RRM6; -.
DR   EnsemblProtists; EAA17886; EAA17886; EAA17886.
DR   VEuPathDB; PlasmoDB:Py17XNL_001205314; -.
DR   InParanoid; Q7RRM6; -.
DR   OMA; ELYNDHA; -.
DR   EvolutionaryTrace; Q7RRM6; -.
DR   Proteomes; UP000008553; Unassembled WGS sequence.
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   InterPro; IPR044666; Cyclophilin_A-like.
DR   PANTHER; PTHR45625; PEPTIDYL-PROLYL CIS-TRANS ISOMERASE-RELATED; 1.
DR   PANTHER; PTHR45625:SF4; PEPTIDYLPROLYL ISOMERASE DOMAIN AND WD REPEAT-CONTAINING PROTEIN 1; 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   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:2B71};
KW   Isomerase {ECO:0000256|RuleBase:RU363019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008553};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          51..197
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   202 AA;  22716 MW;  9C2D43E2364B5AF2 CRC64;
     MFTLCKGYSD DEEEESNAIN VVSEKTKSLE EKIAYYKMKG HTERGYITIY TNLGDFEVEL
     YWYHSPKTCL NFYTLCEMGF YDNTIFHRVI PNFVIQGGDP TGTGKGGKSI YGEYFEDEIN
     KELKHTGAGI LSMSNNGPNT NSSQFFITLA PLPHLDGKHT IFARVSKNMT CIENIASVQT
     TATNKPIFDL KILRTSTAVN AD
//