CWC23_ASHGO
ID CWC23_ASHGO Reviewed; 273 AA.
AC Q752B6;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Pre-mRNA-splicing factor CWC23;
GN Name=CWC23; OrderedLocusNames=AFR659W;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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., Poehlmann 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]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
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: Involved in pre-mRNA splicing. May be involved in endoplasmic
CC reticulum-associated protein degradation (ERAD) and required for growth
CC at low and high temperatures (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associated with the spliceosome. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
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; AE016819; AAS54031.1; -; Genomic_DNA.
DR RefSeq; NP_986207.1; NM_212343.1.
DR AlphaFoldDB; Q752B6; -.
DR SMR; Q752B6; -.
DR STRING; 33169.AAS54031; -.
DR EnsemblFungi; AAS54031; AAS54031; AGOS_AFR659W.
DR GeneID; 4622496; -.
DR KEGG; ago:AGOS_AFR659W; -.
DR eggNOG; KOG0716; Eukaryota.
DR HOGENOM; CLU_063717_0_0_1; -.
DR InParanoid; Q752B6; -.
DR OMA; KHFKLPY; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 3: Inferred from homology;
KW Chaperone; Cytoplasm; mRNA processing; mRNA splicing; Nucleus;
KW Reference proteome; Spliceosome.
FT CHAIN 1..273
FT /note="Pre-mRNA-splicing factor CWC23"
FT /id="PRO_0000071125"
FT DOMAIN 15..87
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
SQ SEQUENCE 273 AA; 31846 MW; 7C56619A9304FCD3 CRC64;
MSADALKDVI GGGKDLYALL EVSISSPEEL EAVDAAQLRA QFRRLALRYH PDKRRDDTQQ
NDKFVSVQKA YDILSNSSLR ATYNRWLSCR LFGDPERRRL VRELHQREQL QVRQKEPMDK
DIQNIQSYGQ LLRKMRHLRI PYGDWRPNTS ISRDSTLVET CTLRLLLRQN STTNSKSSML
QLFQRAKLHI VDLYFSSRNV DTENDLVLYA VMPDVDTMLD LLNNWAVKPP LSEHILQVQP
RVHTDYFHFK TDISLDKTIT EAIDADNQYM SSF