DEF1_ASHGO
ID DEF1_ASHGO Reviewed; 705 AA.
AC Q75DE9;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=RNA polymerase II degradation factor 1;
GN Name=DEF1; OrderedLocusNames=ABR077C;
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: RNA polymerase II degradation factor recruits the
CC ubiquitination machinery to the RNA polymerase II for
CC polyubiquitination, removal and degradation, when RAD26 fails to
CC efficiently displace stalled RNA polymerase II. Also involved in
CC telomere length regulation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEF1 family. {ECO:0000305}.
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DR EMBL; AE016815; AAS50847.2; -; Genomic_DNA.
DR RefSeq; NP_983023.2; NM_208376.2.
DR AlphaFoldDB; Q75DE9; -.
DR SMR; Q75DE9; -.
DR STRING; 33169.AAS50847; -.
DR EnsemblFungi; AAS50847; AAS50847; AGOS_ABR077C.
DR GeneID; 4619127; -.
DR KEGG; ago:AGOS_ABR077C; -.
DR eggNOG; ENOG502S359; Eukaryota.
DR HOGENOM; CLU_023119_0_0_1; -.
DR InParanoid; Q75DE9; -.
DR OMA; QPEAPYF; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:EnsemblFungi.
DR GO; GO:0061635; P:regulation of protein complex stability; IEA:EnsemblFungi.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IEA:EnsemblFungi.
DR GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IEA:EnsemblFungi.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:EnsemblFungi.
DR CDD; cd14368; CUE_DEF1_like; 1.
DR InterPro; IPR041803; DEF1_CUE.
PE 3: Inferred from homology;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome; Telomere; Ubl conjugation pathway.
FT CHAIN 1..705
FT /note="RNA polymerase II degradation factor 1"
FT /id="PRO_0000405661"
FT DOMAIN 21..63
FT /note="CUE"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..87
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 77471 MW; 231EDD53F37D9774 CRC64;
MSQQYSRRGG GKAKRTQVDA EKKFKLDTLT ELFPDWTNED LIDLVHEFED LETIIDKITT
GAVTKWDEVK KPSKKDRQQK EPAGDVEHIH AGSAAAAFGA SAQAQGAPAS LQRSHHSAGH
QNNAKPYQRQ SKYSNSPRQG KQQHQRKEKV AKENLKPAGQ PAKSTASSTS WAAMLSKKED
SKLQAPEQQL EEQPQAQSQA QQTEEPVAKE SQTEKKVGPQ PVAAPLHEEQ DSKPKKMTWA
AIASKPPKHA ENASKKPQEI LQNVQDLKKE INKIATEDTA VEHSETTVTH SEVGVNAQAE
HESFPIEDGA RSVGADDTYY AENVDATNED AAATVNGNAP AASEEAAAQE DASNANANVP
VSLPAEANHQ ASQQVSFGSE EKQQTPQQPS QQGGMHAGQH VVSQVPQSAQ HSSQAAAQTS
QQVASQAPQQ QTPQQAYYQD TYTQQLPQQQ AQAAQAQQYY MNQYQFPGYS YPGMFDSQSA
YPVYNHQQFA VPQQGQPTAQ SSQNSQQAQS QSQQQQQQQQ QQQQQQQQQQ QQQQQQQQQY
GIPPGYVQAG ELAAQSPAST HTQPQQQPQY GGYGMPYYFY QQSFPYAQPQ YGMAGQYPYQ
VPKAAYNYYQ PQQMSQAGNQ ATHQSQSSQN DDSSSASAAN PQQGQQGGAN SQQQSQAAAA
QAQAAAQAQF QQYYQFQQQA AANQQGMPYG YSGYDYTSQT SRGFY
