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Description:
DNA polymerase alpha catalytic subunit (EC 2.7.7.7) (DNA polymeraseI).
Molecular weight: 1668
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair synthesis( GO:0000731 )
Important dates:
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
07-MAR-2006, entry version 61.
Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein DPOA_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | J03268 | AAA34888.1 | - |
| EMBL | Z50161 | CAA90524.1 | - |
| EMBL | Z71378 | CAA95978.1 | - |
| EMBL | Z12126 | CAA78111.1 | - |
| PIR | S58250 | S58250. | |
| IntAct | P13382 | -.1 | |
| GermOnline | 143108 | -.1 | |
| Ensembl | YNL102W | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13139_GR | YNL102W.1 | |
| SGD | S000005046 | POL1. | |
| BioCyc | SCER-S28-01:SCER-S28-01-004958-MONOMER | -.1 | |
| LinkHub | P13382 | -.1 | |
| GO | GO:0005658 | C:alpha DNA polymerase:primase complex | TAS. |
| GO | GO:0005657 | C:replication fork | IDA. |
| GO | GO:0003889 | F:alpha DNA polymerase activity | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006270 | P:DNA replication initiation | TAS. |
| GO | GO:0006269 | P:DNA replication, synthesis of RNA primer | TAS. |
| GO | GO:0000731 | P:DNA synthesis during DNA repair | IMP. |
| InterPro | IPR006172 | DNA_pol_B. | |
| InterPro | IPR006133 | DNA_pol_B_exo. | |
| InterPro | IPR006134 | DNA_pol_B_region. | |
| InterPro | IPR004578 | Pol2. | |
| InterPro | IPR012337 | RNaseH_fold. | |
| Pfam | PF00136 | DNA_pol_B | 1. |
| Pfam | PF03104 | DNA_pol_B_exo | 1. |
| PRINTS | PR00106 | DNAPOLB. | |
| SMART | SM00486 | POLBc | 1. |
| TIGRFAMs | TIGR00592 | pol2 | 1. |
| PROSITE | PS00116 | DNA_POLYMERASE_B | 1. |
Keywords:
Complete proteome; DNA replication; DNA-binding; DNA-directed DNA polymerase; Nuclear protein; Nucleotidyltransferase; Transferase.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ARG-493.
RX MEDLINE=88234507; PubMed=3287376;
RA Pizzagalli A., Valsasnini P., Plevani P., Lucchini G.;
RT "DNA polymerase I gene of Saccharomyces cerevisiae: nucleotide
RT sequence, mapping of a temperature-sensitive mutation, and protein
RT homology with other DNA polymerases.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:3772-3776(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=S288c / FY1679;
RX MEDLINE=96267765; PubMed=8701612;
RX DOI=10.1002/(SICI)1097-0061(19960330)12:4<403::AID-YEA923>3.3.CO;2-8;
RA Saiz J.E., Buitrago M.J., Soler A., del Rey F., Revuelta J.L.;
RT "The sequence of a 21.3 kb DNA fragment from the left arm of yeast
RT chromosome XIV reveals LEU4, MET4, POL1, RAS2, and six new open
RT reading frames.";
RL Yeast 12:403-409(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S288c / FY1679;
RX MEDLINE=97313269; PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
RA Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
RA Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
RA Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
RA Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
RA Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
RA Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
RA Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
RA Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
RA Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
RA Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
RA Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
RA Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
RA Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
RT and its evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC STRAIN=S288c;
RX MEDLINE=93188702; PubMed=8446029;
RA Mountain H.A., Bystroem A.S., Korch C.;
RT "The general amino acid control regulates MET4, which encodes a
RT methionine-pathway-specific transcriptional activator of Saccharomyces
RT cerevisiae.";
RL Mol. Microbiol. 7:215-228(1993).
RN [5]
RP FUNCTION, INTERACTION WITH CDC13, AND MUTAGENESIS OF ASP-236; GLU-238
RP AND PRO-241.
RX MEDLINE=20357110; PubMed=10898792;
RA Qi H., Zakian V.A.;
RT "The Saccharomyces telomere-binding protein Cdc13p interacts with both
RT the catalytic subunit of DNA polymerase alpha and the telomerase-
RT associated est1 protein.";
RL Genes Dev. 14:1777-1788(2000).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION.
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
Feature:
CHAIN 1 1468 DNA polymerase alpha catalytic subunit.
/FTId=PRO_0000046440.
DNA_BIND 1246 1381 Potential.
VARIANT 493 493 G -> R (in temperature sensitive mutant).
MUTAGEN 236 236 D->N: Increase in length of X' and Y'
telomeres. No effect on telomere position
effect. Reduced interaction with CDC13.
MUTAGEN 238 238 E->K: Increase in length of X' and Y'
telomeres. Reduced interaction with
CDC13.
MUTAGEN 241 241 P->T: Increase in length of X' and Y'
telomeres. Reduced interaction with
CDC13.
CONFLICT 759 760 MI -> IV (in Ref. 1).
Comments:
-!- FUNCTION: Polymerase alpha in a complex with DNA primase is a
replicative polymerase. Has a role in promoting telomere
replication during interaction with CDC13.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: Interacts with CDC13.
-!- INTERACTION:
P32797:CDC13; NbExp=3; IntAct=EBI-6128, EBI-4187;
-!- 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.
-!- MISCELLANEOUS: Present with 1050 molecules/cell.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
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Sequence length: 1468
MSSKSEKLEK LRKLQAARNG TSIDDYEGDE SDGDRIYDEI DEKEYRARKR QELLHDDFVV
DDDGVGYVDR GVEEDWREVD NSSSDEDTGN LASKDSKRKK NIKREKDHQI TDMLRTQHSK
STLLAHAKKS QKKSIPIDNF DDILGEFESG EVEKPNILLP SKLRENLNSS PTSEFKSSIK
RVNGNDESSH DAGISKKVKI DPDSSTDKYL EIESSPLKLQ SRKLRYANDV QDLLDDVENS
PVVATKRQNV LQDTLLANPP SAQSLADEED DEDSDEDIIL KRRTMRSVTT TRRVNIDSRS
NPSTSPFVTA PGTPIGIKGL TPSKSLQSNT DVATLAVNVK KEDVVDPETD TFQMFWLDYC
EVNNTLILFG KVKLKDDNCV SAMVQINGLC RELFFLPREG KTPTDIHEEI IPLLMDKYGL
DNIRAKPQKM KYSFELPDIP SESDYLKVLL PYQTPKSSRD TIPSDLSSDT FYHVFGGNSN
IFESFVIQNR IMGPCWLDIK GADFNSIRNA SHCAVEVSVD KPQNITPTTT KTMPNLRCLS
LSIQTLMNPK ENKQEIVSIT LSAYRNISLD SPIPENIKPD DLCTLVRPPQ STSFPLGLAA
LAKQKLPGRV RLFNNEKAML SCFCAMLKVE DPDVIIGHRL QNVYLDVLAH RMHDLNIPTF
SSIGRRLRRT WPEKFGRGNS NMNHFFISDI CSGRLICDIA NEMGQSLTPK CQSWDLSEMY
QVTCEKEHKP LDIDYQNPQY QNDVNSMTMA LQENITNCMI SAEVSYRIQL LTLTKQLTNL
AGNAWAQTLG GTRAGRNEYI LLHEFSRNGF IVPDKEGNRS RAQKQRQNEE NADAPVNSKK
AKYQGGLVFE PEKGLHKNYV LVMDFNSLYP SIIQEFNICF TTVDRNKEDI DELPSVPPSE
VDQGVLPRLL ANLVDRRREV KKVMKTETDP HKRVQCDIRQ QALKLTANSM YGCLGYVNSR
FYAKPLAMLV TNKGREILMN TRQLAESMNL LVVYGDTDSV MIDTGCDNYA DAIKIGLGFK
RLVNERYRLL EIDIDNVFKK LLLHAKKKYA ALTVNLDKNG NGTTVLEVKG LDMKRREFCP
LSRDVSIHVL NTILSDKDPE EALQEVYDYL EDIRIKVETN NIRIDKYKIN MKLSKDPKAY
PGGKNMPAVQ VALRMRKAGR VVKAGSVITF VITKQDEIDN AADTPALSVA ERAHALNEVM
IKSNNLIPDP QYYLEKQIFA PVERLLERID SFNVVRLSEA LGLDSKKYFR REGGNNNGED
INNLQPLETT ITDVERFKDT VTLELSCPSC DKRFPFGGIV SSNYYRVSYN GLQCKHCEQL
FTPLQLTSQI EHSIRAHISL YYAGWLQCDD STCGIVTRQV SVFGKRCLND GCTGVMRYKY
SDKQLYNQLL YFDSLFDCEK NKKQELKPIY LPDDLDYPKE QLTESSIKAL TEQNRELMET
GRSVVQKYLN DCGRRYVDMT SIFDFMLN