ID   DEF1_YEAS2              Reviewed;         738 AA.
AC   C7GP20;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 30.
DE   RecName: Full=RNA polymerase II degradation factor 1;
DE   AltName: Full=RRM3-interacting protein 1;
GN   Name=DEF1; Synonyms=RIP1, VID31; ORFNames=C1Q_02051;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA   Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(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   -!- SUBUNIT: Interacts with the RNA polymerase II in a DNA-damaged
CC       dependent manner. Interacts with RAD26. Binds DNA. {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; ACFL01000080; EEU07462.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7GP20; -.
DR   SMR; C7GP20; -.
DR   Proteomes; UP000008073; 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; Phosphoprotein;
KW   Telomere; Ubl conjugation pathway.
FT   CHAIN           1..738
FT                   /note="RNA polymerase II degradation factor 1"
FT                   /id="PRO_0000405671"
FT   DOMAIN          21..63
FT                   /note="CUE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT   REGION          69..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          640..688
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..129
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..223
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..242
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..295
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..331
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..394
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..455
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         260
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35732"
FT   MOD_RES         273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35732"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35732"
FT   MOD_RES         338
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P35732"
FT   MOD_RES         646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P35732"
SQ   SEQUENCE   738 AA;  83974 MW;  7894597E7FCD4E01 CRC64;
     MSTQFRKSNH NSHSSKKLNP ALKSKIDTLT ELFPDWTSDD LIDIVQEYDD LETIIDKITS
     GAVTRWDEVK KPAKKEKYEK KEQQHSYVPQ QHLPNPEDDI TYKSSNNSNS FTSTKHNSSN
     NYTQARNKKK VQTPRAHTTG KHVNLDKGKH VPSKPVSNTT SWAAAVSVDT KHDVPQDSND
     NNNEELEAQG QQAQEKNQEK EQEEQQQQEG HNNKEEHKQI EQPSLSSKKT TSRTSASQPK
     KMSWAAIATP KPKAVKKTES PLENVAELKK EISDIKKDDQ KSEASEEKVN EQETSAQEQE
     EETAEPSEEN EDRVPEVDGE EVQEEAEEKE QVKEEEQTAE ELEQEQDNVA APEEEVTVVE
     EKVEISAVIS EPPEDQANTV PQPQQQSQQP QQPQQPQQPQ QPQQPQQQQQ PQQPQQPQQQ
     LQQQQQQQQQ PVQAQAQAQE EQLSQNYYTQ QQQQQYAQQQ HQLQQQYLSQ QQQYAQQQQQ
     HPQPQSQQPQ SQQSPQSQKQ GNNVAAQQYY MYQNQFPGYS YPGMFDSQGY AYGQQYQQLA
     QNNAQTSGNA NQYNFQQGYG QAGANTAAAN LTSAAAAAAA SPATAHAQPQ QQQPYGGSFM
     PYYAHFYQQS FPYGQPQYGV AGQYPYQLPK NNYNYYQTQN GQEQQSPNQG VAQHSEDSQQ
     KQSQQQQQQQ PQGQPQPEVQ MQNGQPVNPQ QQMQFQQYYQ FQQQQQQAAA AAAAAAQQGV
     PYGYNGYDYN SKNSRGFY