DEF1_KLULA
ID DEF1_KLULA Reviewed; 645 AA.
AC Q6CTH5;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=RNA polymerase II degradation factor 1;
GN Name=DEF1; OrderedLocusNames=KLLA0C12672g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382123; CAH01615.1; -; Genomic_DNA.
DR RefSeq; XP_452764.1; XM_452764.1.
DR AlphaFoldDB; Q6CTH5; -.
DR SMR; Q6CTH5; -.
DR STRING; 28985.XP_452764.1; -.
DR EnsemblFungi; CAH01615; CAH01615; KLLA0_C12672g.
DR GeneID; 2892415; -.
DR KEGG; kla:KLLA0_C12672g; -.
DR eggNOG; ENOG502S359; Eukaryota.
DR HOGENOM; CLU_023119_0_0_1; -.
DR InParanoid; Q6CTH5; -.
DR OMA; NPYYHQY; -.
DR Proteomes; UP000000598; Chromosome C.
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:0043130; F:ubiquitin binding; IEA:InterPro.
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; IPR003892; CUE.
DR InterPro; IPR041803; DEF1_CUE.
DR Pfam; PF02845; CUE; 1.
DR PROSITE; PS51140; CUE; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome; Telomere; Ubl conjugation pathway.
FT CHAIN 1..645
FT /note="RNA polymerase II degradation factor 1"
FT /id="PRO_0000405668"
FT DOMAIN 16..58
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 57..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 71618 MW; EE0B05D6C1E255F4 CRC64;
MSQFKRNASS KKLDSETKYK LETLSELFPD WTNDDLIDLV REYDDLETIV DKITTGAVTK
WDEVKKPSKK EKPASHIEHQ SHSSHQQLQQ QAASHLDPED SPSLINQHHS HQRQSRSTSK
FSNNSANGKS VQQRQQHQSN NKDNKKQPSK DSLKPAPLPS KSNAGNNAGS WAAVLAEKKK
AHEKKIDHTK SSNTIAHEST NEQSESNEHT EPTEVEVAPA QPVDSAPESV SHQHAPESES
IATTNGDSKP KSWADIASAK SRQRQLQQQN KKQQQQQKSK PLDNFDALKE EVDQLSSEQT
ENGNHAISQE PEQQQQPYAQ QSTFEEPAQQ EEEVVAETTE QQQSQQPQQE EPAQPEVSQV
QETAPVSLPE ETNAANGVSN IQFGSEDKAA QQTLASQNYY QQQPNQQYAP QQVPQSAAAA
AAAQAQAQQY YMYQNQFGYS YPGMFDNQSY LGYGQQFGAP QVPQGQVQPG QQAQPGQQPA
AGSPNAQQGQ TASAYGAPSG TGYQSQEVPQ QSPAQQHVQP QQYSGYGMPY MYYQQSFPYG
QPQYGMAGQY PYQMPKAGYN YYPPQPQSQQ QGGQAQGSTQ SQVEEEQANG QQGGANANAA
NASQQYQQYY QYQQAQTQPQ QQAQQGMPYG YSSYDYSSQT SRGFY
