DEF1_CANGA
ID DEF1_CANGA Reviewed; 592 AA.
AC Q6FIN4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=RNA polymerase II degradation factor 1;
GN Name=DEF1; OrderedLocusNames=CAGL0M13035g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380959; CAG62890.1; -; Genomic_DNA.
DR RefSeq; XP_449910.1; XM_449910.1.
DR AlphaFoldDB; Q6FIN4; -.
DR STRING; 5478.XP_449910.1; -.
DR EnsemblFungi; CAG62890; CAG62890; CAGL0M13035g.
DR GeneID; 2891200; -.
DR KEGG; cgr:CAGL0M13035g; -.
DR CGD; CAL0136877; CAGL0M13035g.
DR VEuPathDB; FungiDB:CAGL0M13035g; -.
DR eggNOG; ENOG502S359; Eukaryota.
DR HOGENOM; CLU_023119_0_0_1; -.
DR InParanoid; Q6FIN4; -.
DR OMA; QPEAPYF; -.
DR Proteomes; UP000002428; Chromosome M.
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..592
FT /note="RNA polymerase II degradation factor 1"
FT /id="PRO_0000405664"
FT DOMAIN 3..47
FT /note="CUE"
FT REGION 53..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 65520 MW; 3A02FFA9317117EB CRC64;
MSSVQNKVET LVELFPDWKR EDLLELVQEE KDTELEIIVE KITTGKVTKW DEVKKPKRER
HAPEASSVRT YSSSTHSHSA ASGGAAAPRY KKSGRFAGNS GVSNTATGSS TSTSSGTSTS
ASSHGAAQSA SSGKNATAAA QAAVKKTGVP AGTKEEKIAQ RLNSTHTQEE RKKMSWAAIA
TPKPKPKPVQ KKKEEEPAQE SQEDTKASES SKESALENVE DLKNEVDNIE KEQEKKEEPA
QETEKETVEK EQEPQPQPQE QEQPQEQAQE QAANEQQQQE QQQPQQPQQE QQEQQLAQEA
AAPAEAAPAS KQGSVSEAAQ QQQQQQQQQT APQQTAQQQQ PAQQLTDAQL QAQAQAQAQA
QAQAQQYYMY QNQFPGYSYP GMYDMQGYAY GQQYQQPTPM GGHPAMVNAQ FSMQQGYMNA
GTPVSAGVDL NTATAAPNTA QSPVAPHTQQ QSQQQPYGAG SFMPYYAHFY QQYPYGQPQY
GVAANQYPYQ TTKSSGQNLY GGEYGQQAQQ DAQAKGVQRN DSHSEQQTSD SAQQQLTPQQ
IQLQQYYQYQ QQQQQQQQQQ QQQAPQQQQQ PNAQQYGYSG YDYNTKSTNG FY
