(data stored in ACNUC9543 zone)

SWISSPROT: Q8I6S4_PLAF7

ID   Q8I6S4_PLAF7            Unreviewed;       217 AA.
AC   Q8I6S4;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAY-2019, entry version 116.
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=PF3D7_0804800 {ECO:0000313|EMBL:CAD51318.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD51318.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S.,
RA   Chan M.S., Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S.,
RA   Pertea M., Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B.,
RA   Martin D.M., Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A.,
RA   McFadden G.I., Cummings L.M., Subramanian G.M., Mungall C.,
RA   Venter J.C., Carucci D.J., Hoffman S.L., Newbold C., Davis R.W.,
RA   Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium
RT   falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA   Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C.,
RA   Chillingworth T., Christodoulou Z., Clark L., Clark R., Corton C.,
RA   Cronin A., Davies R.M., Davis P., Dear P., Dearden F., Doggett J.,
RA   Feltwell T., Goble A., Goodhead I., Gwilliam R., Hamlin N., Hance Z.,
RA   Harper D., Hauser H., Hornsby T., Holroyd S., Horrocks P.,
RA   Humphray S., Jagels K., James K.D., Johnson D., Kerhornou A.,
RA   Knights A., Konfortov B., Kyes S., Larke N., Lawson D., Lennard N.,
RA   Line A., Maddison M., Mclean J., Mooney P., Moule S., Murphy L.,
RA   Oliver K., Ormond D., Price C., Quail M.A., Rabbinowitsch E.,
RA   Rajandream M.A., Rutter S., Rutherford K.M., Sanders M., Simmonds M.,
RA   Seeger K., Sharp S., Smith R., Squares R., Squares S., Stevens K.,
RA   Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the 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; AL844507; CAD51318.1; -; Genomic_DNA.
DR   RefSeq; XP_001349469.1; XM_001349433.1.
DR   SMR; Q8I6S4; -.
DR   PRIDE; Q8I6S4; -.
DR   EnsemblProtists; CAD51318; CAD51318; PF3D7_0804800.
DR   GeneDB; PF3D7_0804800.1:pep; -.
DR   GeneID; 2655320; -.
DR   KEGG; pfa:PF3D7_0804800; -.
DR   EuPathDB; PlasmoDB:PF3D7_0804800; -.
DR   HOGENOM; HOG000065981; -.
DR   InParanoid; Q8I6S4; -.
DR   KO; K09567; -.
DR   OMA; ELKHTGS; -.
DR   PhylomeDB; Q8I6S4; -.
DR   BioCyc; PLASMO:PF08_0121-MONOMER; -.
DR   Proteomes; UP000001450; Chromosome 8.
DR   GO; GO:0016018; F:cyclosporin A binding; IBA:GO_Central.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0006457; P:protein folding; TAS:GeneDB.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
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   3: Inferred from homology;
DR   PRODOM; Q8I6S4.
DR   SWISS-2DPAGE; Q8I6S4.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001450};
KW   Isomerase {ECO:0000256|RuleBase:RU363019,
KW   ECO:0000313|EMBL:CAD51318.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN       51    216       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
FT   COILED        5     25       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   217 AA;  24892 MW;  3EFDA7E9C5D01FDA CRC64;
     MKNLNQNMKN NDNKKNEKIS GLEENEEHNN NNIVPYYLSN LLTNPSNPVV FMDINLGNHF
     LGKFKFELFQ NIVPRTSENF RKFCTGEHKI NNLPVGYKNT TFHRVIKDFM IQGGDFVNYN
     GSGCISIYGE HFDDENFDIK HDKEGLLSMA NTGPNTNGCQ FFIITKKCEW LDGKNVVFGR
     IIDNDSLILL KKIENVSVTP YIYKPKIAIN IVECGEL
//

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