(data stored in ACNUC7421 zone)

SWISSPROT: Q750W6_ASHGO

ID   Q750W6_ASHGO            Unreviewed;       162 AA.
AC   Q750W6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 119.
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=AGOS_AGL177C {ECO:0000313|EMBL:AAS54314.1};
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811 {ECO:0000313|EMBL:AAS54314.1, ECO:0000313|Proteomes:UP000000591};
RN   [1] {ECO:0000313|EMBL:AAS54314.1, ECO:0000313|Proteomes:UP000000591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Pohlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2] {ECO:0000313|Proteomes:UP000000591}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056
RC   {ECO:0000313|Proteomes:UP000000591};
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016820; AAS54314.1; -; Genomic_DNA.
DR   RefSeq; NP_986490.1; NM_211552.1.
DR   STRING; 33169.AAS54314; -.
DR   EnsemblFungi; AAS54314; AAS54314; AGOS_AGL177C.
DR   GeneID; 4622783; -.
DR   KEGG; ago:AGOS_AGL177C; -.
DR   HOGENOM; HOG000065981; -.
DR   InParanoid; Q750W6; -.
DR   KO; K01802; -.
DR   OMA; SETFNPG; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:EnsemblFungi.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0034967; C:Set3 complex; IEA:EnsemblFungi.
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:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR   GO; GO:0016575; P:histone deacetylation; IEA:EnsemblFungi.
DR   GO; GO:0045836; P:positive regulation of meiotic nuclear division; IEA:EnsemblFungi.
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; Q750W6.
DR   SWISS-2DPAGE; Q750W6.
KW   Isomerase {ECO:0000256|RuleBase:RU363019};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000591};
KW   Rotamase {ECO:0000256|RuleBase:RU363019}.
FT   DOMAIN          5..161
FT                   /note="PPIase cyclophilin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50072"
SQ   SEQUENCE   162 AA;  17413 MW;  6B8D870381B65CEA CRC64;
     MSKVFFDVEA DGQPLGRIVF QLYNDVTPKT AENFRALCTG EKGFGYAGCP FHRVIPDFML
     QGGDFTHGTG VGGKSIYGGK FPDENFVKKH EKPGLLSMAN AGPNTNGSQF FITTVPCPWL
     NGKHVVFGEV SEGMDVVKKV ESMGSSSGAT RARIVISKSG EL
//

If you have problems or comments...

PBIL Back to PBIL home page