(data stored in SCRATCH zone)

SWISSPROT: C5DCT4_LACTC

ID   C5DCT4_LACTC            Unreviewed;       114 AA.
AC   C5DCT4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   11-DEC-2019, entry version 54.
DE   RecName: Full=Peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277, ECO:0000256|SAAS:SAAS01166441};
DE            EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277, ECO:0000256|SAAS:SAAS01166441};
GN   OrderedLocusNames=KLTH0B05654g {ECO:0000313|EMBL:CAR21595.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21595.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21595.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA   Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA   Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA   Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA   Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA   Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA   Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA   Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA   Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
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; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00277, ECO:0000256|SAAS:SAAS01166461};
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DR   EMBL; CU928166; CAR21595.1; -; Genomic_DNA.
DR   RefSeq; XP_002552033.1; XM_002551987.1.
DR   STRING; 381046.XP_002552033.1; -.
DR   EnsemblFungi; CAR21595; CAR21595; KLTH0B05654g.
DR   GeneID; 8290872; -.
DR   KEGG; lth:KLTH0B05654g; -.
DR   HOGENOM; HOG000154887; -.
DR   InParanoid; C5DCT4; -.
DR   KO; K09568; -.
DR   OMA; RVIAGWD; -.
DR   OrthoDB; 1328688at2759; -.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR023566; PPIase_FKBP.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   PANTHER; PTHR10516; PTHR10516; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   4: Predicted;
DR   PRODOM; C5DCT4.
DR   SWISS-2DPAGE; C5DCT4.
KW   Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|SAAS:SAAS01166454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277,
KW   ECO:0000256|SAAS:SAAS01166457}.
FT   DOMAIN          26..114
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50059"
SQ   SEQUENCE   114 AA;  12173 MW;  C72522F7723280A9 CRC64;
     MSETIEGNVK IDRLSPGDGK TFPKTGDLVT IHYTGTLENG QKFDSSVDRG SPFQCNIGVG
     QVIKGWDAGI PKLSVGEKAR LTIPGPYAYG PRGFPGLIPP NATLVFDVEL LKVN
//

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