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Database: UniProt
Entry: Q6CBP4
LinkDB: Q6CBP4
Original site: Q6CBP4 
ID   PPID_YARLI              Reviewed;         367 AA.
AC   Q6CBP4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   19-MAR-2014, entry version 68.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase D;
DE            Short=PPIase D;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase D;
GN   Name=CPR6; OrderedLocusNames=YALI0C16775g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity).
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       D subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
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DR   EMBL; CR382129; CAG82238.1; -; Genomic_DNA.
DR   RefSeq; XP_501918.1; XM_501918.1.
DR   ProteinModelPortal; Q6CBP4; -.
DR   SMR; Q6CBP4; 3-170.
DR   STRING; 4952.Q6CBP4; -.
DR   PRIDE; Q6CBP4; -.
DR   EnsemblFungi; CAG82238; CAG82238; YALI0_C16775g.
DR   GeneID; 2909297; -.
DR   KEGG; yli:YALI0C16775g; -.
DR   eggNOG; COG0457; -.
DR   HOGENOM; HOG000065980; -.
DR   KO; K05864; -.
DR   OMA; KFEDEAF; -.
DR   OrthoDB; EOG757D7G; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IEA:GOC.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR020892; Cyclophilin-type_PPIase_CS.
DR   InterPro; IPR002130; Cyclophilin-type_PPIase_dom.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF07719; TPR_2; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Isomerase; Reference proteome; Repeat;
KW   Rotamase; TPR repeat.
FT   CHAIN         1    367       Peptidyl-prolyl cis-trans isomerase D.
FT                                /FTId=PRO_0000232952.
FT   DOMAIN        7    171       PPIase cyclophilin-type.
FT   REPEAT      213    246       TPR 1.
FT   REPEAT      264    297       TPR 2.
FT   REPEAT      302    335       TPR 3.
SQ   SEQUENCE   367 AA;  40061 MW;  34FBD2C5DC9F24F7 CRC64;
     MTNPRVFFEV AIGGKTIGKI YFELFADKVP KTAENFRALC TGEKGNTQAG IPLHFKGSSF
     HRVIKDFMVQ GGDFTAGNGT GGESIYGEKF PDEAFPYPHD QPFLLSMANA GPNTNGSQFF
     ITTTETPHLD NKHVVFGKLL SGKGIVRQIE RTETGEQDRP KQPVTIVDCG ELPADFQVPV
     GNVDDGTGDD YEDFLKDNDN VDVNDPASVL GAIEKLKSIG TKLFKEGNAE GALKKYLKAT
     TYLEDYLPDD LSEENIAKVH ALRISCYLNV ALMALKVNQP KVAIKAATSA LDDETVANKE
     KAKALFRRGS GYAALKNETD ALKDLNAALE LEPADGAIKN KIEEVKQAAQ RRREAEKKKY
     AGFFGGK
//
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