DEF1_DEBHA
ID DEF1_DEBHA Reviewed; 742 AA.
AC Q6BRB3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=RNA polymerase II degradation factor 1;
GN Name=DEF1; OrderedLocusNames=DEHA2D17732g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG87431.2; -; Genomic_DNA.
DR RefSeq; XP_459257.2; XM_459257.1.
DR AlphaFoldDB; Q6BRB3; -.
DR SMR; Q6BRB3; -.
DR STRING; 4959.XP_459257.2; -.
DR EnsemblFungi; CAG87431; CAG87431; DEHA2D17732g.
DR GeneID; 2901630; -.
DR KEGG; dha:DEHA2D17732g; -.
DR VEuPathDB; FungiDB:DEHA2D17732g; -.
DR eggNOG; ENOG502S359; Eukaryota.
DR HOGENOM; CLU_438800_0_0_1; -.
DR InParanoid; Q6BRB3; -.
DR OMA; QPEAPYF; -.
DR OrthoDB; 1596012at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
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..742
FT /note="RNA polymerase II degradation factor 1"
FT /id="PRO_0000405667"
FT DOMAIN 27..70
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 81125 MW; DBC105B3AC1B48BE CRC64;
MSTQRKAYKN HSKRFSNNSS SSSNNNSSST ELTSLLEMFP DWESDDLSSL LAEHNNILEV
VIDLIVNNKV SKWEPIKKEA KNKKKEKEND EFVNVPNTNV TSNNTTHTSS ADHGHKLNKY
HKEAHPSNSK SKFSSKGPHN KKPNPKFNGK DSSPTAPTTS TSTSTSGATS VPSSNSWAAA
LSKDGVKVNN KSHKESDSQP ETELEPEPEP EPVAQAGEEH EIIIEQTTTV IESTETPTST
TKPVLKEATV PQPKQGSWAS AITPKPKSKP RTKQALSGSQ EESFESKGQF EQAQEEPVEA
IIIEETTTTI PAESISSEET IEQPAQVVLP TSSQPLSSVG VSFGSLSLGD EEKESQPEQT
TEEISAPVGE QSQQQQQQRY GLYNNQNQNQ NQNRYNQQIY QQQQQHAQQQ HAQQQQQQQP
QQSQQSQQPQ QPQQPQQPQQ PQQPQQPQQP QQQPQQPQQP QQQYNQSKQQ QQQQQQQYDY
YNQFQQSQYP QQGSQTLPGA QFGVYPGMDY SAYNQQAAAA VVSSPAASPA ATANYAQYAQ
AASQPPSSGA QEGNVAAQSP ITSQINPNTL QQQVPAAPFG YPYYNYYYNT PFYGNGAGLG
AQGGFGNVAA AQGTPTSNSN VTPNSGVNSG FMGVGNTGAS QYYGQPNQFG NRYPGYNSYP
QPGQAQSAQS GNPSNNQSGS VPASQGEAND SSSASNQAGN PQSQIPQQSQ QPQQPGIPQY
GGYQQYPQYG GYQDNNQYRG WY
