DPO5_YEAST
ID DPO5_YEAST Reviewed; 1022 AA.
AC P39985; D3DLJ5; Q9Y737;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=rDNA transcriptional regulator POL5;
DE EC=2.7.7.7;
DE AltName: Full=DNA polymerase V;
DE Short=POL V;
DE AltName: Full=DNA polymerase phi {ECO:0000303|PubMed:12093911};
GN Name=POL5 {ECO:0000303|PubMed:12093911}; OrderedLocusNames=YEL055C;
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], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-623 AND
RP ASP-625.
RX PubMed=12093911; DOI=10.1073/pnas.142277999;
RA Shimizu K., Kawasaki Y., Hiraga S., Tawaramoto M., Nakashima N., Sugino A.;
RT "The fifth essential DNA polymerase phi in Saccharomyces cerevisiae is
RT localized to the nucleolus and plays an important role in synthesis of
RT rRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9133-9138(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [3]
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 [4]
RP IDENTIFICATION.
RX PubMed=7667891; DOI=10.1016/s0968-0004(00)89059-3;
RA Sugino A.;
RT "Yeast DNA polymerases and their role at the replication fork.";
RL Trends Biochem. Sci. 20:319-323(1995).
RN [5]
RP PROTEIN FAMILY.
RX PubMed=12695662; DOI=10.4161/cc.2.2.329;
RA Yang W., Rogozin I.B., Koonin E.V.;
RT "Yeast POL5 is an evolutionarily conserved regulator of rDNA transcription
RT unrelated to any known DNA polymerases.";
RL Cell Cycle 2:120-122(2003).
RN [6]
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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-789, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH FRK1.
RX PubMed=20489023; DOI=10.1126/science.1176495;
RA Breitkreutz A., Choi H., Sharom J.R., Boucher L., Neduva V., Larsen B.,
RA Lin Z.Y., Breitkreutz B.J., Stark C., Liu G., Ahn J., Dewar-Darch D.,
RA Reguly T., Tang X., Almeida R., Qin Z.S., Pawson T., Gingras A.C.,
RA Nesvizhskii A.I., Tyers M.;
RT "A global protein kinase and phosphatase interaction network in yeast.";
RL Science 328:1043-1046(2010).
CC -!- FUNCTION: Plays an important role in the regulation of rRNA
CC transcription. Binds near or at the enhancer region of rRNA repeating
CC units. May have DNA polymerase activity, but it is not required for in
CC vivo function. {ECO:0000269|PubMed:12093911}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC Evidence={ECO:0000269|PubMed:12093911};
CC -!- ACTIVITY REGULATION: Stimulated by PCNA and inhibited by aphidicolin.
CC {ECO:0000269|PubMed:12093911}.
CC -!- SUBUNIT: Interacts with FRK1. {ECO:0000269|PubMed:20489023}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12093911,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MYBBP1A family.
CC {ECO:0000305|PubMed:12695662}.
CC -!- CAUTION: Was originally thought to belong to the DNA polymerase type-B
CC family based on conserved motifs (PubMed:12093911). Has later been
CC shown to be unrelated to B class DNA polymerases. The observation of a
CC low level of polymerase activity in vitro, which is not required for
CC its essential cellular function, may require further validation
CC (PubMed:12695662). {ECO:0000305|PubMed:12093911,
CC ECO:0000305|PubMed:12695662}.
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DR EMBL; AB027253; BAA77722.1; -; Genomic_DNA.
DR EMBL; U18795; AAB65032.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07599.1; -; Genomic_DNA.
DR PIR; S50534; S50534.
DR RefSeq; NP_010859.1; NM_001178870.1.
DR AlphaFoldDB; P39985; -.
DR BioGRID; 36674; 411.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-6314N; -.
DR IntAct; P39985; 20.
DR MINT; P39985; -.
DR STRING; 4932.YEL055C; -.
DR iPTMnet; P39985; -.
DR MaxQB; P39985; -.
DR PaxDb; P39985; -.
DR PRIDE; P39985; -.
DR EnsemblFungi; YEL055C_mRNA; YEL055C; YEL055C.
DR GeneID; 856655; -.
DR KEGG; sce:YEL055C; -.
DR SGD; S000000781; POL5.
DR VEuPathDB; FungiDB:YEL055C; -.
DR eggNOG; KOG1926; Eukaryota.
DR GeneTree; ENSGT00390000017457; -.
DR HOGENOM; CLU_005212_1_0_1; -.
DR InParanoid; P39985; -.
DR OMA; PWVEVMV; -.
DR BioCyc; YEAST:G3O-30173-MON; -.
DR PRO; PR:P39985; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P39985; protein.
DR GO; GO:0030685; C:nucleolar preribosome; IMP:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0090070; P:positive regulation of ribosome biogenesis; IDA:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IDA:SGD.
DR GO; GO:0006364; P:rRNA processing; IDA:SGD.
DR GO; GO:0009303; P:rRNA transcription; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR007015; DNA_pol_V/MYBBP1A.
DR PANTHER; PTHR13213; PTHR13213; 1.
DR Pfam; PF04931; DNA_pol_phi; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..1022
FT /note="rDNA transcriptional regulator POL5"
FT /id="PRO_0000046472"
FT REGION 706..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..748
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..805
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 623
FT /note="D->N: In POL5dn; has no DNA synthesis activity, but
FT complements the lethality of a pol5 null mutant; when
FT associated with N-625."
FT /evidence="ECO:0000269|PubMed:12093911"
FT MUTAGEN 625
FT /note="D->N: In POL5dn; has no DNA synthesis activity, but
FT complements the lethality of a pol5 null mutant; when
FT associated with N-623."
FT /evidence="ECO:0000269|PubMed:12093911"
SQ SEQUENCE 1022 AA; 115894 MW; A9F32B1D15039D18 CRC64;
MTGKVNRDLF FKLASDLREE RLHAAVALIK DLSALDLPDD AEEWSYVLNR LIKGLSSDRN
SARLGFSLCL TEVINLAVNM PPGQRPKGLE STNEFLSTLS TILNVNVNEG TKKSMKGKDE
RGILFGKLFG LKSLLNEPLF SEIFVKDLEK GNTEFFIRFT EQLIDLALKK NWIKEPCFFT
LFQTMKMLLP FMDESSAEKI LLIYDKYDLT LTNEGLSTYL LLKYEGDESL IPSVLDLKNP
GWKDNDPLAR GNLPLLTKVL RNSSVIPDAN GGLKETKKQK NTNWNPRLHF VWSVLLPLFG
NGKLENTSHI SKKRKKTNNK KVQNSIQFPE FWKMAVDESF FNEKASSERK YLGFLIIDAA
FKAVPGSYIG FCFSQNVMRT LINQSIDSQR VLNKISQLTL DSIVKACEED SANRLVPCLN
AMLFGPHGSI NFDKLTKSGT VSKLIAIKEL PSTVLAQLLD VFFLQLQDKK GVLSHTLFAL
DSILHIVRAH KVEINDMDIM KPVLRPIVYM AFFKHTSDDL KLEQLHELAK ERLYSILGEL
TINKEIRCKD PEINSWQYLT LKLILDIENS HVGDLINPLD ENLENIKNEA ISCLSKVCRS
RTAQSWGLST LLSMCLVQLY AGDTDSISVI EELCEFSKHE NNSMVGITEI LLSLLAQKKA
LLRKLSLIIW QQFIEEVGLE ELQILLDILK ARENKQGFAQ LFEGEEEFEE IKEENDASED
ESKTGSESES ESESDSDDAD EKDEEDEANE DILNIDKEAT SALVKALNLP DNIVNDKGEV
DLDQLEGLSD DGGDDEDEES MDDEKMMELD DQLSEIFKRR KEALSSISTG NQRKFEVKQS
RENVISFKHR VVDMLAVYVK YCEKLTLANK SEHSNNLGGS LSKLVYFIIP MLKCVNETLD
RPLADKISKL LKGKIFKIKV TAFKDMNKDI ELMDLLKKTH KLMLTSKPGQ HAAVFYSMCS
TSSLFLSKLY VEIGGNDKLD ELIDLYTATT KEWMQKGKCG PNIFIDFINW LSSKKQTVMD
KE
