P13382 (DPOA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA polymerase alpha catalytic subunit A
EC=2.7.7.7

Alternative name(s):
DNA polymerase I subunit A
DNA polymerase alpha:primase complex p180 subunit
Short name=DNA polymerase-primase complex p180 subunit
Short name=Pol alpha-primase complex p180 subunit

Gene names

Name:	POL1
Synonyms:	CDC17
Ordered Locus Names:	YNL102W
ORF Names:	N2181

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	1468 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) consitutes a replicative polymerase. POL1 has a role in promoting telomere replication during interaction with CDC13. Ref.9
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
Subunit structure	DNA polymerase alpha:primase is a four subunit enzyme complex, which is assembled throughout the cell cycle, and consists of the two DNA polymerase subunits A and B, and the DNA primase large and small subunits. Subunit B binds to subunit A By similarity. POL1 interacts with CDC13, POB3, SPT16 and MCM10. Ref.8 Ref.9 Ref.11
Subcellular location	Nucleus.
Miscellaneous	In eukaryotes there are five DNA polymerases: alpha, beta, gamma, delta, and epsilon which are responsible for different reactions of DNA synthesis. Present with 1050 molecules/cell in log phase SD medium. Ref.10
Sequence similarities	Belongs to the DNA polymerase type-B family.

Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	DNA-directed DNA polymerase Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA replication checkpoint Inferred from Biological aspect of Ancestor. Source: RefGenome DNA replication, synthesis of RNA primer Inferred from Biological aspect of Ancestor. Source: RefGenome DNA-dependent DNA replication initiation Inferred by curator. Source: SGD RNA-dependent DNA replication Inferred from direct assay. Source: SGD S phase of mitotic cell cycle Inferred from Biological aspect of Ancestor. Source: RefGenome gene conversion at mating-type locus, DNA repair synthesis Inferred from Biological aspect of Ancestor. Source: RefGenome lagging strand elongation Inferred by curator. Source: SGD premeiotic DNA replication Inferred from mutant phenotype. Source: SGD
Cellular component	alpha DNA polymerase:primase complex Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from direct assay. Source: SGD nucleoside binding Inferred from electronic annotation. Source: InterPro nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.9. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC13	P32797	4	EBI-6128,EBI-4187
POL12	P38121	5	EBI-6128,EBI-6111

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1468

1468

DNA polymerase alpha catalytic subunit A

PRO_0000046440

Regions

DNA binding

1246 – 1381

136

Potential

Amino acid modifications

Modified residue

31

1

Phosphoserine Ref.14 Ref.15

Modified residue

169

1

Phosphoserine Ref.14 Ref.15

Modified residue

170

1

Phosphoserine Ref.12 Ref.13 Ref.14 Ref.15

Modified residue

172

1

Phosphothreonine Ref.15

Modified residue

204

1

Phosphoserine Ref.14

Modified residue

205

1

Phosphoserine Ref.15

Modified residue

209

1

Phosphotyrosine Ref.15

Modified residue

214

1

Phosphoserine Ref.15

Modified residue

215

1

Phosphoserine Ref.14 Ref.15

Modified residue

240

1

Phosphoserine Ref.14 Ref.15

Modified residue

274

1

Phosphoserine Ref.15

Modified residue

300

1

Phosphoserine Ref.15

Modified residue

313

1

Phosphothreonine Ref.12

Modified residue

1231

1

Phosphoserine Ref.15

Natural variations

Natural variant

493

1

G → R in temperature sensitive mutant. Ref.1

Experimental info

Mutagenesis

236

1

D → N: Increase in length of X' and Y' telomeres. No effect on telomere position effect. Reduced interaction with CDC13. Ref.9

Mutagenesis

238

1

E → K: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. Ref.9

Mutagenesis

241

1

P → T: Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. Ref.9

Sequence conflict

759 – 760

2

MI → IV in AAA34888. Ref.1

Secondary structure

1

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1468

Helix Strand Turn

Details...

Turn

1274 – 1279

6

Beta strand

1283 – 1286

4

Turn

1288 – 1290

3

Beta strand

1293 – 1296

4

Beta strand

1303 – 1306

4

Turn

1315 – 1317

3

Helix

1323 – 1342

20

Beta strand

1346 – 1349

4

Beta strand

1356 – 1358

3

Beta strand

1376 – 1380

5

Helix

1382 – 1395

14

Helix

1398 – 1402

5

Helix

1424 – 1433

10

Helix

1435 – 1439

5

Helix

1443 – 1449

7

Sequences

	Sequence		Length	Mass (Da)
	P13382 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 50C9032DBE95B5AE	FASTA	1,468	166,809
	10 20 30 40 50 60 MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR QELLHDDFVV 70 80 90 100 110 120 DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK NIKREKDHQI TDMLRTQHSK 130 140 150 160 170 180 STLLAHAKKS QKKSIPIDNF DDILGEFESG EVEKPNILLP SKLRENLNSS PTSEFKSSIK 190 200 210 220 230 240 RVNGNDESSH DAGISKKVKI DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS 250 260 270 280 290 300 PVVATKRQNV LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS 310 320 330 340 350 360 NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD TFQMFWLDYC 370 380 390 400 410 420 EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG KTPTDIHEEI IPLLMDKYGL 430 440 450 460 470 480 DNIRAKPQKM KYSFELPDIP SESDYLKVLL PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN 490 500 510 520 530 540 IFESFVIQNR IMGPCWLDIK GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS 550 560 570 580 590 600 LSIQTLMNPK ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA 610 620 630 640 650 660 LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH RMHDLNIPTF 670 680 690 700 710 720 SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA NEMGQSLTPK CQSWDLSEMY 730 740 750 760 770 780 QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA LQENITNCMI SAEVSYRIQL LTLTKQLTNL 790 800 810 820 830 840 AGNAWAQTLG GTRAGRNEYI LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK 850 860 870 880 890 900 AKYQGGLVFE PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE 910 920 930 940 950 960 VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM YGCLGYVNSR 970 980 990 1000 1010 1020 FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV MIDTGCDNYA DAIKIGLGFK 1030 1040 1050 1060 1070 1080 RLVNERYRLL EIDIDNVFKK LLLHAKKKYA ALTVNLDKNG NGTTVLEVKG LDMKRREFCP 1090 1100 1110 1120 1130 1140 LSRDVSIHVL NTILSDKDPE EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY 1150 1160 1170 1180 1190 1200 PGGKNMPAVQ VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM 1210 1220 1230 1240 1250 1260 IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR REGGNNNGED 1270 1280 1290 1300 1310 1320 INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV SSNYYRVSYN GLQCKHCEQL 1330 1340 1350 1360 1370 1380 FTPLQLTSQI EHSIRAHISL YYAGWLQCDD STCGIVTRQV SVFGKRCLND GCTGVMRYKY 1390 1400 1410 1420 1430 1440 SDKQLYNQLL YFDSLFDCEK NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET 1450 1460 GRSVVQKYLN DCGRRYVDMT SIFDFMLN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA polymerase I gene of Saccharomyces cerevisiae: nucleotide sequence, mapping of a temperature-sensitive mutation, and protein homology with other DNA polymerases." Pizzagalli A., Valsasnini P., Plevani P., Lucchini G. Proc. Natl. Acad. Sci. U.S.A. 85:3772-3776(1988) [PubMed: 3287376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-493.
[2]	"The sequence of a 21.3 kb DNA fragment from the left arm of yeast chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open reading frames." Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L. Yeast 12:403-409(1996) [PubMed: 8701612] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"The general amino acid control regulates MET4, which encodes a methionine-pathway-specific transcriptional activator of Saccharomyces cerevisiae." Mountain H.A., Bystroem A.S., Korch C. Mol. Microbiol. 7:215-228(1993) [PubMed: 8446029] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. Strain: ATCC 204508 / S288c.
[6]	"The yeast DNA polymerase-primase complex: genes and proteins." Plevani P., Foiani M., Muzi Falconi M., Pizzagalli A., Santocanale C., Francesconi S., Valsasnini P., Comedini A., Piatti S., Lucchini G. Biochim. Biophys. Acta 951:268-273(1988) [PubMed: 3061469] [Abstract] Cited for: COMPOSITION OF THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
[7]	"Phosphorylation of the DNA polymerase alpha-primase B subunit is dependent on its association with the p180 polypeptide." Ferrari M., Lucchini G., Plevani P., Foiani M. J. Biol. Chem. 271:8661-8666(1996) [PubMed: 8621497] [Abstract] Cited for: PHOSPHORYLATION, IDENTIFICATION IN THE DNA POLYMERASE ALPHA:PRIMASE COMPLEX.
[8]	"The Saccharomyces cerevisiae DNA polymerase alpha catalytic subunit interacts with Cdc68/Spt16 and with Pob3, a protein similar to an HMG1-like protein." Wittmeyer J., Formosa T. Mol. Cell. Biol. 17:4178-4190(1997) [PubMed: 9199353] [Abstract] Cited for: INTERACTION WITH POB3 AND SPT16.
[9]	"The Saccharomyces telomere-binding protein Cdc13p interacts with both the catalytic subunit of DNA polymerase alpha and the telomerase-associated est1 protein." Qi H., Zakian V.A. Genes Dev. 14:1777-1788(2000) [PubMed: 10898792] [Abstract] Cited for: FUNCTION, INTERACTION WITH CDC13, MUTAGENESIS OF ASP-236; GLU-238 AND PRO-241.
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"A conserved Hsp10-like domain in Mcm10 is required to stabilize the catalytic subunit of DNA polymerase-alpha in budding yeast." Ricke R.M., Bielinsky A.-K. J. Biol. Chem. 281:18414-18425(2006) [PubMed: 16675460] [Abstract] Cited for: INTERACTION WITH MCM10.
[12]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-313, MASS SPECTROMETRY. Strain: ADR376.
[13]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170, MASS SPECTROMETRY.
[14]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-169; SER-170; SER-204; SER-215 AND SER-240, MASS SPECTROMETRY.
[15]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-169; SER-170; THR-172; SER-205; TYR-209; SER-214; SER-215; SER-240; SER-274; SER-300 AND SER-1231, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J03268 Genomic DNA. Translation: AAA34888.1.
Z50161 Genomic DNA. Translation: CAA90524.1.
Z71378 Genomic DNA. Translation: CAA95978.1.
Z12126 Genomic DNA. Translation: CAA78111.1.
BK006947 Genomic DNA. Translation: DAA10443.1.

PIR

S58250.

RefSeq

NP_014297.1. NM_001182940.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3FLO	X-ray	2.50	B/D/F/H	1263-1468	[»]
3OIQ	X-ray	2.40	B	215-250	[»]

ProteinModelPortal

P13382.

SMR

P13382. Positions 216-245, 1273-1452.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2526N.

IntAct

P13382. 10 interactions.

MINT

MINT-421899.

STRING

P13382.

Proteomic databases

PeptideAtlas

P13382.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YNL102W; YNL102W; YNL102W.

GeneID

855621.

KEGG

sce:YNL102W.

NMPDR

fig|4932.3.peg.5368.

Organism-specific databases

CYGD

YNL102w.

SGD

S000005046. POL1.

Phylogenomic databases

eggNOG

fuNOG04132.

HOGENOM

HBG561737.

OMA

ENIERKG.

OrthoDB

EOG4K0TWK.

Gene expression databases

ArrayExpress

P13382.

Genevestigator

P13382.

GermOnline

YNL102W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR006172. DNA-dir_DNA_pol_B.
IPR017964. DNA-dir_DNA_pol_B_CS.
IPR006133. DNA-dir_DNA_pol_B_exonuc.
IPR006134. DNA-dir_DNA_pol_B_multi_dom.
IPR004578. DNA-dir_DNA_pol_B_pol2.
IPR024647. DNA_pol_a_cat_su_N.
IPR023211. DNA_pol_palm_dom.
IPR012337. RNaseH-like_dom.
IPR015088. Znf_DNA-dir_DNA_pol_B_alpha.
[Graphical view]

Gene3D

G3DSA:3.90.1600.10. DNA_pol_palm_dom. 2 hits.

KO

K02320.

Pfam

PF12254. DNA_pol_alpha_N. 1 hit.
PF00136. DNA_pol_B. 1 hit.
PF03104. DNA_pol_B_exo1. 1 hit.
PF08996. zf-DNA_Pol. 1 hit.
[Graphical view]

PRINTS

PR00106. DNAPOLB.

SMART

SM00486. POLBc. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

TIGRFAMs

TIGR00592. Pol2. 1 hit.

PROSITE

PS00116. DNA_POLYMERASE_B. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

979813.

Entry information

Entry name

DPOA_YEAST

Accession

Primary (citable) accession number: P13382
Secondary accession number(s): D6W177

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 125 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program