DEF1_LODEL
ID DEF1_LODEL Reviewed; 770 AA.
AC A5E406;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=RNA polymerase II degradation factor 1;
GN Name=DEF1; ORFNames=LELG_04345;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; CH981529; EDK46164.1; -; Genomic_DNA.
DR RefSeq; XP_001524373.1; XM_001524323.1.
DR AlphaFoldDB; A5E406; -.
DR SMR; A5E406; -.
DR STRING; 379508.A5E406; -.
DR EnsemblFungi; EDK46164; EDK46164; LELG_04345.
DR GeneID; 5231753; -.
DR KEGG; lel:LELG_04345; -.
DR VEuPathDB; FungiDB:LELG_04345; -.
DR eggNOG; ENOG502S359; Eukaryota.
DR HOGENOM; CLU_438800_0_0_1; -.
DR InParanoid; A5E406; -.
DR OMA; NPYYHQY; -.
DR OrthoDB; 1596012at2759; -.
DR Proteomes; UP000001996; Unassembled WGS sequence.
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..770
FT /note="RNA polymerase II degradation factor 1"
FT /id="PRO_0000405670"
FT DOMAIN 30..73
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 83990 MW; 9A8F531C02F633D2 CRC64;
MSTTQRKSFK NQLKRFNNET SGSTNSTNSN ASPELTSLTE MFPDWESDEL NSLLQEKRNS
LEVVIDLIVN NKVSKWEPIK KEKKEKKVKD DTDGFQANNT TSSTHLGSQS GKPFNKFKSS
NKPPRKQGNV TKKPIKSTSD NNKPTTSTSN GAEKSKESSA SGSWASALGE DTAKPATSKN
TKPTTELEKA PEQDSNKDET PLESEQKQQE PQEQAEQKPK TTASATTTSE PAPKPVLKEA
VIPSLNQGSW ASAITPKTKP KPKPKAVKTA PSPTQATEPA QQQQQQQQSE QSEQSEQPEQ
PQTSQADQNE SVSKPEEPVV SESQTSAQEK TLEIQEPVAS AAAPAAQAPA SSSSAVEAGA
QGPQVVLPTS LQGVNSVGIS FGSLSLGEEE PKDSHKDLRE QFDQTQQKYE QPQEQPQPQQ
QQQQQAQAPA PSQQQQQQQQ RYDLYEQQPQ QSTNYQQQPQ QPQQSQQSQQ PQQQGQGQFG
KHASQQSVPS QGQVPQQSQP TQQQYDYYSQ FQQQQYPQQA GQPGAQFGGY PAYDYSAFNQ
QAYAASPANA HAATTGSAAA YNQYAQQSVG AADSTQSPVS AQNVLQQQQA QQQQQQIPTP
FGYPYYNYYY NNPYFGGAGG LGNNGFASAN TGSIGQQTQQ GAQQASQQLN VPSATQPSGV
SANGFGAQQQ YYNPNQYSNR YPGYSYPPQP QQQQQPGQQQ HQQQPGQHAG QSATGSESDA
AQQGQGQGQG QQSHPQSGAP QQPVVPQYGA YQQYPQYGYQ DTTQYRGGWY
