(data stored in SCRATCH zone)

SWISSPROT: Q6FJ99_CANGA

ID   Q6FJ99_CANGA            Unreviewed;       387 AA.
AC   Q6FJ99;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   30-AUG-2017, entry version 103.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CAG62671.1};
GN   OrderedLocusNames=CAGL0M08030g {ECO:0000313|CGD:CAL0137319,
GN   ECO:0000313|EMBL:CAG62671.1};
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593 {ECO:0000313|Proteomes:UP000002428};
RN   [1] {ECO:0000313|EMBL:CAG62671.1, ECO:0000313|Proteomes:UP000002428}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65
RC   {ECO:0000313|Proteomes:UP000002428};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
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   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., 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   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0). {ECO:0000256|SAAS:SAAS00339244}.
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DR   EMBL; CR380959; CAG62671.1; -; Genomic_DNA.
DR   RefSeq; XP_449695.1; XM_449695.1.
DR   ProteinModelPortal; Q6FJ99; -.
DR   STRING; 284593.XP_449695.1; -.
DR   EnsemblFungi; CAG62671; CAG62671; CAGL0M08030g.
DR   KEGG; cgr:CAGL0M08030g; -.
DR   CGD; CAL0137319; CAGL0M08030g.
DR   EuPathDB; FungiDB:CAGL0M08030g; -.
DR   eggNOG; KOG0546; Eukaryota.
DR   eggNOG; COG0652; LUCA.
DR   HOGENOM; HOG000065980; -.
DR   InParanoid; Q6FJ99; -.
DR   KO; K01802; -.
DR   OMA; QFFITTY; -.
DR   OrthoDB; EOG092C3VLQ; -.
DR   Proteomes; UP000002428; Chromosome M.
DR   GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:EnsemblFungi.
DR   GO; GO:0034605; P:cellular response to heat; IEA:EnsemblFungi.
DR   GO; GO:0042026; P:protein refolding; IEA:EnsemblFungi.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR029000; Cyclophilin-like_dom.
DR   InterPro; IPR024936; Cyclophilin-type_PPIase.
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_dom.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11071; PTHR11071; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
DR   PRODOM; Q6FJ99.
DR   SWISS-2DPAGE; Q6FJ99.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002428};
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|SAAS:SAAS00495831};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002428};
KW   Repeat {ECO:0000256|SAAS:SAAS00705167};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00156,
KW   ECO:0000256|SAAS:SAAS00495895};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339,
KW   ECO:0000256|SAAS:SAAS00705174}.
FT   DOMAIN        4    190       PPIase cyclophilin-type.
FT                                {ECO:0000259|PROSITE:PS50072}.
FT   REPEAT      234    267       TPR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00339}.
FT   DOMAIN      286    357       TPR_REGION. {ECO:0000259|PROSITE:
FT                                PS50293}.
FT   REPEAT      286    319       TPR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00339}.
FT   REPEAT      324    357       TPR. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00339}.
SQ   SEQUENCE   387 AA;  44246 MW;  B08DAE7CC2352165 CRC64;
     MKVYLDIAIA GEQIGRIVCE LYNDKAPKAV ENFHRLCVGS GSVGGIHLTY KRSCFHRVIR
     NFMIQGGDLV FGKEDNLDSD KVGLGGCSIY ATEEEIKDDT KELQCHGLFE DENVGEFDEP
     FLLAMANTGS PNTNSSQFFI TTYPSPHLTG KHSIFGRVIH GKSVVRTIEY GKVDKEGTPE
     NLVVIEDCGD WDETMSIPLY NASNSTIGGD IYEEYPDDDT HFDSEDFAAA YNASNIIKDS
     GSALFKIKDY QNSYYKYMKA LKYVNTYIPE QDVDEKHCLL FIELKKKLYL NICLALFNLK
     DYDESMKYGH YLLELDSVDD KDKAKAYYRI GNSLFAKKRY DEALKNYRLC RDHNPDDNVI
     GQKIEKTENI LEKEKERTKK NISKFFR
//

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