DEF1_YEAS7
ID DEF1_YEAS7 Reviewed; 733 AA.
AC A6ZZR2;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=RNA polymerase II degradation factor 1;
DE AltName: Full=RRM3-interacting protein 1;
GN Name=DEF1; Synonyms=RIP1, VID31;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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; AAFW02000152; EDN59855.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZZR2; -.
DR PRIDE; A6ZZR2; -.
DR EnsemblFungi; EDN59855; EDN59855; SCY_3322.
DR HOGENOM; CLU_023119_0_0_1; -.
DR Proteomes; UP000007060; 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..733
FT /note="RNA polymerase II degradation factor 1"
FT /id="PRO_0000405672"
FT DOMAIN 21..63
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 69..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..682
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 181..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..330
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35732"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35732"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35732"
FT MOD_RES 337
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P35732"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35732"
SQ SEQUENCE 733 AA; 83488 MW; 053B1EF6DC996F58 CRC64;
MSTQFRKSNH NSHSSKKLNP ALKSKIDTLT ELFPDWTSDD LIDIVQEYDD LETIIDKITS
GAVTRWDEVK KPAKKEKYEK KEQQHSYVPQ QHLPNPEDDI TYKSSNNSNS FTSTKHNSSN
NYTQARNKKK VQTPRAHTTG KHVNLDKGKH VPSKPVSNTT SWAAAVSVDT KHDVPQDSND
NNNEELEAQG QQAQENQEKE QEEQQQQEGH NNKEEHKQIE QPSLSSKKTT SKTSAPQPKK
MSWAAIATPK PKAVKKTESP LENVAELKKE ISDIKKDDQK SEASEEKVNE QETSAQEQEE
ETAEPSEENE DRVPEVDGEE VQEEAEEKEQ VKEEEQTAEE LEQEQDNVAA PEEEVTVVEE
KVEISAVISE PPEDQANTVP QPQQQQQQQQ QQPQQPQQQQ QQPQQQQQPQ QPQQQLQQQQ
QQQQQPVQAQ AQAQEEQLSQ NYYTQQQQQQ FAQQQHQFQQ QYLSQQQQYA QQQQQHPQPQ
SQQPQSQQSP QSQKQGNNVA AQQYYMYQNQ FPGYSYPGMF DSQGYAYGQQ YQQLAQNNAQ
TSGNANQYNF QQGYGQAGAN TAAANLTSAA AAAAASPATA HAQPQQQQPY GGSFMPYYAH
FYQQSFPYGQ PQYGVAGQYP YQLPKNNYNY YQTQNGQEQQ SPNQGVAQHS EDSQQKQSQQ
QQQQQPQGQP QPEVQMQNGQ SVNPQQQMQF QQYYQFQQQQ QQAAAAAAAA AQQGVPYGYN
GYDYNSKNSR GFY
