PAP2_YEAST
ID PAP2_YEAST Reviewed; 584 AA.
AC P53632; D6W1V2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Poly(A) RNA polymerase protein 2;
DE EC=2.7.7.19 {ECO:0000269|PubMed:20696927};
DE AltName: Full=DNA polymerase kappa;
DE AltName: Full=DNA polymerase sigma;
DE AltName: Full=Topoisomerase 1-related protein TRF4;
GN Name=PAP2; Synonyms=TRF4; OrderedLocusNames=YOL115W;
GN ORFNames=HRC584, O0716;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=8647385; DOI=10.1093/genetics/141.2.465;
RA Sadoff B.U., Heath-Pagliuso S., Castano I.B., Zhu Y., Kieff F.S.,
RA Christman M.F.;
RT "Isolation of mutants of Saccharomyces cerevisiae requiring DNA
RT topoisomerase I.";
RL Genetics 141:465-479(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7502582; DOI=10.1002/yea.320111108;
RA Vandenbol M., Durand P., Portetelle D., Hilger F.;
RT "Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including
RT the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for
RT tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.";
RL Yeast 11:1069-1075(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP FUNCTION.
RX PubMed=8895658; DOI=10.1101/gad.10.20.2564;
RA Castano I.B., Brzoska P.M., Sadoff B.U., Chen H., Christman M.F.;
RT "Mitotic chromosome condensation in the rDNA requires TRF4 and DNA
RT topoisomerase I in Saccharomyces cerevisiae.";
RL Genes Dev. 10:2564-2576(1996).
RN [7]
RP FUNCTION.
RX PubMed=8710513; DOI=10.1093/nar/24.12.2404;
RA Castano I.B., Heath-Pagliuso S., Sadoff B.U., Fitzhugh D.J.,
RA Christman M.F.;
RT "A novel family of TRF (DNA topoisomerase I-related function) genes
RT required for proper nuclear segregation.";
RL Nucleic Acids Res. 24:2404-2410(1996).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10066793; DOI=10.1074/jbc.274.11.7302;
RA Walowsky C., Fitzhugh D.J., Castano I.B., Ju J.Y., Levin N.A.,
RA Christman M.F.;
RT "The topoisomerase-related function gene TRF4 affects cellular sensitivity
RT to the antitumor agent camptothecin.";
RL J. Biol. Chem. 274:7302-7308(1999).
RN [9]
RP FUNCTION, AND MUTAGENESIS OF 236-ASP--ASP-238.
RX PubMed=10926539; DOI=10.1126/science.289.5480.774;
RA Wang Z., Castano I.B., De Las Penas A., Adams C., Christman M.F.;
RT "Pol kappa: a DNA polymerase required for sister chromatid cohesion.";
RL Science 289:774-779(2000).
RN [10]
RP NOMENCLATURE.
RX PubMed=11579108; DOI=10.1074/jbc.r100056200;
RA Burgers P.M.J., Koonin E.V., Bruford E., Blanco L., Burtis K.C.,
RA Christman M.F., Copeland W.C., Friedberg E.C., Hanaoka F., Hinkle D.C.,
RA Lawrence C.W., Nakanishi M., Ohmori H., Prakash L., Prakash S.,
RA Reynaud C.-A., Sugino A., Todo T., Wang Z., Weill J.-C., Woodgate R.;
RT "Eukaryotic DNA polymerases: proposal for a revised nomenclature.";
RL J. Biol. Chem. 276:43487-43490(2001).
RN [11]
RP FUNCTION.
RX PubMed=12062100; DOI=10.1016/s0092-8674(02)00753-5;
RA Saitoh S., Chabes A., McDonald W.H., Thelander L., Yates J.R. III,
RA Russell P.;
RT "Cid13 is a cytoplasmic poly(A) polymerase that regulates ribonucleotide
RT reductase mRNA.";
RL Cell 109:563-573(2002).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF 131-GLU--GLU-133; 140-GLU--GLU-142;
RP 182-GLU--ASP-185; 194-ARG--GLU-198; 217-ASP--ASP-219; 224-GLU-SER-225;
RP 236-ASP--ASP-238; 275-LYS--ARG-277; 282-LYS--GLU-285; 309-ARG-GLU-310;
RP 332-ARG-ARG-333; 378-GLU--GLU-381; 425-ASP--GLU-429; 444-LYS-LYS-445;
RP 467-LYS--ARG-469; 486-ARG--ASP-490; 491-GLU-ARG-492; 502-GLU--GLU-504;
RP 508-LYS--ARG-510; 559-LYS-ARG-560 AND 572-GLU--ASP-574.
RX PubMed=11861546; DOI=10.1093/genetics/160.2.381;
RA Wang Z., Castano I.B., Adams C., Vu C., Fitzhugh D.J., Christman M.F.;
RT "Structure/function analysis of the Saccharomyces cerevisiae Trf4/Pol sigma
RT DNA polymerase.";
RL Genetics 160:381-391(2002).
RN [13]
RP FUNCTION, AND INTERACTION WITH POL2.
RX PubMed=12665575; DOI=10.1128/mcb.23.8.2733-2748.2003;
RA Edwards S., Li C.M., Levy D.L., Brown J., Snow P.M., Campbell J.L.;
RT "Saccharomyces cerevisiae DNA polymerase epsilon and polymerase sigma
RT interact physically and functionally, suggesting a role for polymerase
RT epsilon in sister chromatid cohesion.";
RL Mol. Cell. Biol. 23:2733-2748(2003).
RN [14]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [15]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [16]
RP FUNCTION.
RX PubMed=15145828; DOI=10.1101/gad.1183804;
RA Kadaba S., Krueger A., Trice T., Krecic A.M., Hinnebusch A.G.,
RA Anderson J.T.;
RT "Nuclear surveillance and degradation of hypomodified initiator tRNAMet in
RT S. cerevisiae.";
RL Genes Dev. 18:1227-1240(2004).
RN [17]
RP IDENTIFICATION IN TRAMP COMPLEX, AND FUNCTION OF THE TRAMP COMPLEX.
RX PubMed=15935758; DOI=10.1016/j.cell.2005.04.029;
RA LaCava J., Houseley J., Saveanu C., Petfalski E., Thompson E., Jacquier A.,
RA Tollervey D.;
RT "RNA degradation by the exosome is promoted by a nuclear polyadenylation
RT complex.";
RL Cell 121:713-724(2005).
RN [18]
RP IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION OF THE TRF4 COMPLEX.
RX PubMed=15935759; DOI=10.1016/j.cell.2005.04.030;
RA Wyers F., Rougemaille M., Badis G., Rousselle J.-C., Dufour M.-E.,
RA Boulay J., Regnault B., Devaux F., Namane A., Seraphin B., Libri D.,
RA Jacquier A.;
RT "Cryptic pol II transcripts are degraded by a nuclear quality control
RT pathway involving a new poly(A) polymerase.";
RL Cell 121:725-737(2005).
RN [19]
RP FUNCTION.
RX PubMed=16260630; DOI=10.1128/mcb.25.22.10183-10189.2005;
RA Haracska L., Johnson R.E., Prakash L., Prakash S.;
RT "Trf4 and Trf5 proteins of Saccharomyces cerevisiae exhibit poly(A) RNA
RT polymerase activity but no DNA polymerase activity.";
RL Mol. Cell. Biol. 25:10183-10189(2005).
RN [20]
RP IDENTIFICATION IN THE TRF4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION OF THE TRF4 COMPLEX.
RX PubMed=15828860; DOI=10.1371/journal.pbio.0030189;
RA Vanacova S., Wolf J., Martin G., Blank D., Dettwiler S., Friedlein A.,
RA Langen H., Keith G., Keller W.;
RT "A new yeast poly(A) polymerase complex involved in RNA quality control.";
RL PLoS Biol. 3:986-997(2005).
RN [21]
RP FUNCTION.
RX PubMed=16373491; DOI=10.1261/rna.2207206;
RA Egecioglu D.E., Henras A.K., Chanfreau G.F.;
RT "Contributions of Trf4p- and Trf5p-dependent polyadenylation to the
RT processing and degradative functions of the yeast nuclear exosome.";
RL RNA 12:26-32(2006).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF 236-ASP--ASP-238.
RX PubMed=16431988; DOI=10.1261/rna.2305406;
RA Kadaba S., Wang X., Anderson J.T.;
RT "Nuclear RNA surveillance in Saccharomyces cerevisiae: Trf4p-dependent
RT polyadenylation of nascent hypomethylated tRNA and an aberrant form of 5S
RT rRNA.";
RL RNA 12:508-521(2006).
RN [23]
RP FUNCTION.
RX PubMed=17179095; DOI=10.1534/genetics.106.065987;
RA Reis C.C., Campbell J.L.;
RT "Contribution of Trf4/5 and the nuclear exosome to genome stability through
RT regulation of histone mRNA levels in Saccharomyces cerevisiae.";
RL Genetics 175:993-1010(2007).
RN [24]
RP INTERACTION WITH NOP53.
RX PubMed=18631361; DOI=10.1111/j.1742-4658.2008.06565.x;
RA Granato D.C., Machado-Santelli G.M., Oliveira C.C.;
RT "Nop53p interacts with 5.8S rRNA co-transcriptionally, and regulates
RT processing of pre-rRNA by the exosome.";
RL FEBS J. 275:4164-4178(2008).
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 161-481 IN COMPLEX WITH AIR2,
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH AIR2.
RX PubMed=20696927; DOI=10.1073/pnas.1003505107;
RA Hamill S., Wolin S.L., Reinisch K.M.;
RT "Structure and function of the polymerase core of TRAMP, a RNA surveillance
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:15045-15050(2010).
CC -!- FUNCTION: Catalytic subunit of the TRAMP complex which has a poly(A)
CC RNA polymerase activity and is involved in a post-transcriptional
CC quality control mechanism limiting inappropriate expression of genetic
CC information. Polyadenylation is required for the degradative activity
CC of the exosome on several of its nuclear RNA substrates like cryptic
CC transcripts generated by RNA polymerase II and III, or hypomethylated
CC pre-tRNAi-Met. Polyadenylates RNA processing and degradation
CC intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains
CC lacking a functional exosome. TRF4 is also required for proper nuclear
CC division in mitosis, DNA damage repair and sister chromatid cohesion.
CC Involved in the regulation of histone mRNA levels. May mediate mitotic
CC chromosome condensation. {ECO:0000269|PubMed:10066793,
CC ECO:0000269|PubMed:10926539, ECO:0000269|PubMed:11861546,
CC ECO:0000269|PubMed:12062100, ECO:0000269|PubMed:12665575,
CC ECO:0000269|PubMed:15145828, ECO:0000269|PubMed:15828860,
CC ECO:0000269|PubMed:15935758, ECO:0000269|PubMed:15935759,
CC ECO:0000269|PubMed:16260630, ECO:0000269|PubMed:16373491,
CC ECO:0000269|PubMed:16431988, ECO:0000269|PubMed:17179095,
CC ECO:0000269|PubMed:20696927, ECO:0000269|PubMed:8647385,
CC ECO:0000269|PubMed:8710513, ECO:0000269|PubMed:8895658}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173115; EC=2.7.7.19;
CC Evidence={ECO:0000269|PubMed:20696927};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC composed of at least HUL4, MTR4, PAP2/TRF4 and either AIR1 or AIR2.
CC Interacts with NOP53 and POL2. Interacts directly with AIR2.
CC {ECO:0000269|PubMed:12665575, ECO:0000269|PubMed:15828860,
CC ECO:0000269|PubMed:15935758, ECO:0000269|PubMed:15935759,
CC ECO:0000269|PubMed:18631361, ECO:0000269|PubMed:20696927}.
CC -!- INTERACTION:
CC P53632; P40507: AIR1; NbExp=7; IntAct=EBI-19517, EBI-25083;
CC P53632; Q12476: AIR2; NbExp=21; IntAct=EBI-19517, EBI-31475;
CC P53632; P47047: MTR4; NbExp=11; IntAct=EBI-19517, EBI-11592;
CC P53632; P0CS90: SSC1; NbExp=2; IntAct=EBI-19517, EBI-8637;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10066793,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7550 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to have DNA polymerase activity.
CC {ECO:0000305}.
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DR EMBL; U31355; AAC49091.1; -; Genomic_DNA.
DR EMBL; Z48149; CAA88145.1; -; Genomic_DNA.
DR EMBL; Z74857; CAA99134.1; -; Genomic_DNA.
DR EMBL; AY723865; AAU09782.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10668.1; -; Genomic_DNA.
DR PIR; S51882; S51882.
DR RefSeq; NP_014526.1; NM_001183369.1.
DR PDB; 2MOW; NMR; -; B=573-584.
DR PDB; 3NYB; X-ray; 2.70 A; A=161-481.
DR PDB; 4U4C; X-ray; 2.40 A; B=111-160.
DR PDBsum; 2MOW; -.
DR PDBsum; 3NYB; -.
DR PDBsum; 4U4C; -.
DR AlphaFoldDB; P53632; -.
DR SMR; P53632; -.
DR BioGRID; 34285; 455.
DR ComplexPortal; CPX-1678; TRAMP complex variant 4-1.
DR ComplexPortal; CPX-1679; TRAMP complex variant 4-2.
DR DIP; DIP-4214N; -.
DR IntAct; P53632; 40.
DR MINT; P53632; -.
DR STRING; 4932.YOL115W; -.
DR iPTMnet; P53632; -.
DR MaxQB; P53632; -.
DR PaxDb; P53632; -.
DR PRIDE; P53632; -.
DR EnsemblFungi; YOL115W_mRNA; YOL115W; YOL115W.
DR GeneID; 854034; -.
DR KEGG; sce:YOL115W; -.
DR SGD; S000005475; PAP2.
DR VEuPathDB; FungiDB:YOL115W; -.
DR eggNOG; KOG1906; Eukaryota.
DR GeneTree; ENSGT00940000169468; -.
DR HOGENOM; CLU_013572_5_0_1; -.
DR InParanoid; P53632; -.
DR OMA; FGSCATD; -.
DR BioCyc; YEAST:G3O-33512-MON; -.
DR BRENDA; 4.2.99.B1; 984.
DR EvolutionaryTrace; P53632; -.
DR PRO; PR:P53632; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P53632; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0031499; C:TRAMP complex; IDA:SGD.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006284; P:base-excision repair; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071044; P:histone mRNA catabolic process; IGI:SGD.
DR GO; GO:0042138; P:meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0043629; P:ncRNA polyadenylation; IDA:UniProtKB.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IMP:SGD.
DR GO; GO:0071031; P:nuclear mRNA surveillance of mRNA 3'-end processing; IGI:SGD.
DR GO; GO:0071040; P:nuclear polyadenylation-dependent antisense transcript catabolic process; IMP:SGD.
DR GO; GO:0071039; P:nuclear polyadenylation-dependent CUT catabolic process; IMP:SGD.
DR GO; GO:0071042; P:nuclear polyadenylation-dependent mRNA catabolic process; IGI:SGD.
DR GO; GO:0071035; P:nuclear polyadenylation-dependent rRNA catabolic process; IMP:SGD.
DR GO; GO:0071036; P:nuclear polyadenylation-dependent snoRNA catabolic process; IMP:SGD.
DR GO; GO:0071037; P:nuclear polyadenylation-dependent snRNA catabolic process; IMP:SGD.
DR GO; GO:0071038; P:nuclear polyadenylation-dependent tRNA catabolic process; IDA:SGD.
DR GO; GO:0071047; P:polyadenylation-dependent mRNA catabolic process; IMP:SGD.
DR GO; GO:0071051; P:polyadenylation-dependent snoRNA 3'-end processing; IGI:SGD.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0000292; P:RNA fragment catabolic process; IC:ComplexPortal.
DR GO; GO:0071050; P:sno(s)RNA polyadenylation; IGI:SGD.
DR GO; GO:0006400; P:tRNA modification; IMP:SGD.
DR GO; GO:0034475; P:U4 snRNA 3'-end processing; IMP:SGD.
DR DisProt; DP01775; -.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR002058; PAP_assoc.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR045862; Trf4-like.
DR PANTHER; PTHR23092; PTHR23092; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF03828; PAP_assoc; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Magnesium; Manganese;
KW Metal-binding; Mitosis; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..584
FT /note="Poly(A) RNA polymerase protein 2"
FT /id="PRO_0000120314"
FT DOMAIN 371..431
FT /note="PAP-associated"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..34
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..584
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MUTAGEN 131..133
FT /note="EDE->AAA: In TRF4-131; slow growth."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 140..142
FT /note="ERE->AAA: In TRF4-140; slow growth."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 182..185
FT /note="EIKD->AIAA: In TRF4-182; lethal."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 194
FT /note="R->A: In TRF4-194; lethal; when associated with A-
FT 195; A-196 and A-198."
FT MUTAGEN 195..198
FT /note="EEIE->AIAA: In TRF4-194; lethal."
FT MUTAGEN 217..219
FT /note="DAD->AAA: In TRF4-217; slow growth."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 224..225
FT /note="GS->AA: In TRF4-224; lethal."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 236..238
FT /note="DID->AIA: In TRF4-236; lethal."
FT /evidence="ECO:0000269|PubMed:10926539,
FT ECO:0000269|PubMed:11861546, ECO:0000269|PubMed:16431988"
FT MUTAGEN 275..277
FT /note="KAR->AAA: In TRF4-275; temperature sensitive."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 282
FT /note="K->A: In TRF4-282; lethal; when associated with A-
FT 285."
FT MUTAGEN 285
FT /note="E->A: In TRF4-282; lethal; when associated with A-
FT 282."
FT MUTAGEN 309..310
FT /note="RE->AA: In TRF4-309; lethal."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 332..333
FT /note="RR->AA: In TRF4-332; temperature sensitive."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 378
FT /note="E->A: In TRF4-378; lethal; when associated with A-
FT 381."
FT MUTAGEN 381
FT /note="E->A: In TRF4-378; lethal; when associated with A-
FT 378."
FT MUTAGEN 425
FT /note="D->A: In TRF4-425; lethal; when associated with A-
FT 428 and A-429."
FT MUTAGEN 428..429
FT /note="DE->AA: In TRF4-425; lethal; when associated with A-
FT 425."
FT MUTAGEN 444..445
FT /note="KK->AA: In TRF4-444; lethal."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 467..469
FT /note="KDR->AAA: In TRF4-467; temperature sensitive."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 486..487
FT /note="RD->AA: In TRF4-486; lethal."
FT MUTAGEN 490..492
FT /note="DER->AAA: In TRF4-486; lethal."
FT MUTAGEN 502
FT /note="E->A: In TRF4-502; lethal; when associated with A-
FT 504."
FT MUTAGEN 504
FT /note="E->A: In TRF4-502; lethal; when associated with A-
FT 502."
FT MUTAGEN 508..510
FT /note="KKR->AAA: In TRF4-508; lethal."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 559..560
FT /note="KR->AA: In TRF4-559; slow growth."
FT /evidence="ECO:0000269|PubMed:11861546"
FT MUTAGEN 560
FT /note="R->A: In TRF4-559; slow growth; when associated with
FT A-559."
FT MUTAGEN 572..574
FT /note="EDD->AAA: In TRF4-572; slow growth."
FT /evidence="ECO:0000269|PubMed:11861546"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:4U4C"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 194..212
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:3NYB"
FT TURN 225..229
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 279..285
FT /evidence="ECO:0007829|PDB:3NYB"
FT TURN 286..289
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 290..297
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 344..356
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 359..362
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 372..385
FT /evidence="ECO:0007829|PDB:3NYB"
FT TURN 389..391
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 406..408
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:3NYB"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:3NYB"
FT TURN 433..436
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 440..462
FT /evidence="ECO:0007829|PDB:3NYB"
FT HELIX 466..469
FT /evidence="ECO:0007829|PDB:3NYB"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:3NYB"
SQ SEQUENCE 584 AA; 66031 MW; 8A58B29E4BFDC022 CRC64;
MGAKSVTASS SKKIKNRHNG KVKKSKKIKK VRKPQKSISL NDENEVEILP SRNEQETNKL
PKDHVTADGI LVLEHKSDDD EGFDVYDGHF DNPTDIPSTT EESKTPSLAV HGDEKDLANN
DDFISLSASS EDEQAEQEEE REKQELEIKK EKQKEILNTD YPWILNHDHS KQKEISDWLT
FEIKDFVAYI SPSREEIEIR NQTISTIREA VKQLWPDADL HVFGSYSTDL YLPGSDIDCV
VTSELGGKES RNNLYSLASH LKKKNLATEV EVVAKARVPI IKFVEPHSGI HIDVSFERTN
GIEAAKLIRE WLDDTPGLRE LVLIVKQFLH ARRLNNVHTG GLGGFSIICL VFSFLHMHPR
IITNEIDPKD NLGVLLIEFF ELYGKNFGYD DVALGSSDGY PVYFPKSTWS AIQPIKNPFS
LAIQDPGDES NNISRGSFNI RDIKKAFAGA FDLLTNRCFE LHSATFKDRL GKSILGNVIK
YRGKARDFKD ERGLVLNKAI IENENYHKKR SRIIHDEDFA EDTVTSTATA TTTDDDYEIT
NPPAKKAKIE EKPESEPAKR NSGETYITVS SEDDDEDGYN PYTL
