P13382 · DPOLA_YEAST
- ProteinDNA polymerase alpha catalytic subunit A
- GenePOL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1468 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic component of DNA polymerase alpha, which in complex with DNA primase (DNA polymerase alpha:primase) constitutes a replicative polymerase (PubMed:10898792, PubMed:22119860, PubMed:31488849).
POL1 has a role in promoting telomere replication during interaction with CDC13 (PubMed:10898792).
POL1 has a role in promoting telomere replication during interaction with CDC13 (PubMed:10898792).
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.
Catalytic activity
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 1287 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1290 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1314 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1317 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1348 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1353 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1367 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1372 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | alpha DNA polymerase:primase complex | |
Cellular Component | mitochondrion | |
Cellular Component | replication fork | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | chromatin binding | |
Molecular Function | DNA replication origin binding | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | H3-H4 histone complex chaperone activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Molecular Function | single-stranded DNA binding | |
Biological Process | DNA replication | |
Biological Process | DNA replication initiation | |
Biological Process | DNA synthesis involved in DNA repair | |
Biological Process | double-strand break repair | |
Biological Process | lagging strand elongation | |
Biological Process | leading strand elongation | |
Biological Process | mitotic DNA replication initiation | |
Biological Process | premeiotic DNA replication | |
Biological Process | RNA-templated DNA biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA polymerase alpha catalytic subunit A
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionP13382
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 236 | Increase in length of X' and Y' telomeres. No effect on telomere position effect. Reduced interaction with CDC13. | ||||
Sequence: D → N | ||||||
Mutagenesis | 238 | Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. | ||||
Sequence: E → K | ||||||
Mutagenesis | 241 | Increase in length of X' and Y' telomeres. Reduced interaction with CDC13. | ||||
Sequence: P → T | ||||||
Natural variant | 493 | in temperature sensitive mutant | ||||
Sequence: G → R | ||||||
Mutagenesis | 868 | Increases rates of C-to-A transversion substitutions. | ||||
Sequence: L → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 28 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylserine | ||||
Sequence: S | ||||||
Chain | PRO_0000046440 | 2-1468 | DNA polymerase alpha catalytic subunit A | |||
Sequence: SSKSEKLEKLRKLQAARNGTSIDDYEGDESDGDRIYDEIDEKEYRARKRQELLHDDFVVDDDGVGYVDRGVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDMLRTQHSKSTLLAHAKKSQKKSIPIDNFDDILGEFESGEVEKPNILLPSKLRENLNSSPTSEFKSSIKRVNGNDESSHDAGISKKVKIDPDSSTDKYLEIESSPLKLQSRKLRYANDVQDLLDDVENSPVVATKRQNVLQDTLLANPPSAQSLADEEDDEDSDEDIILKRRTMRSVTTTRRVNIDSRSNPSTSPFVTAPGTPIGIKGLTPSKSLQSNTDVATLAVNVKKEDVVDPETDTFQMFWLDYCEVNNTLILFGKVKLKDDNCVSAMVQINGLCRELFFLPREGKTPTDIHEEIIPLLMDKYGLDNIRAKPQKMKYSFELPDIPSESDYLKVLLPYQTPKSSRDTIPSDLSSDTFYHVFGGNSNIFESFVIQNRIMGPCWLDIKGADFNSIRNASHCAVEVSVDKPQNITPTTTKTMPNLRCLSLSIQTLMNPKENKQEIVSITLSAYRNISLDSPIPENIKPDDLCTLVRPPQSTSFPLGLAALAKQKLPGRVRLFNNEKAMLSCFCAMLKVEDPDVIIGHRLQNVYLDVLAHRMHDLNIPTFSSIGRRLRRTWPEKFGRGNSNMNHFFISDICSGRLICDIANEMGQSLTPKCQSWDLSEMYQVTCEKEHKPLDIDYQNPQYQNDVNSMTMALQENITNCMISAEVSYRIQLLTLTKQLTNLAGNAWAQTLGGTRAGRNEYILLHEFSRNGFIVPDKEGNRSRAQKQRQNEENADAPVNSKKAKYQGGLVFEPEKGLHKNYVLVMDFNSLYPSIIQEFNICFTTVDRNKEDIDELPSVPPSEVDQGVLPRLLANLVDRRREVKKVMKTETDPHKRVQCDIRQQALKLTANSMYGCLGYVNSRFYAKPLAMLVTNKGREILMNTRQLAESMNLLVVYGDTDSVMIDTGCDNYADAIKIGLGFKRLVNERYRLLEIDIDNVFKKLLLHAKKKYAALTVNLDKNGNGTTVLEVKGLDMKRREFCPLSRDVSIHVLNTILSDKDPEEALQEVYDYLEDIRIKVETNNIRIDKYKINMKLSKDPKAYPGGKNMPAVQVALRMRKAGRVVKAGSVITFVITKQDEIDNAADTPALSVAERAHALNEVMIKSNNLIPDPQYYLEKQIFAPVERLLERIDSFNVVRLSEALGLDSKKYFRREGGNNNGEDINNLQPLETTITDVERFKDTVTLELSCPSCDKRFPFGGIVSSNYYRVSYNGLQCKHCEQLFTPLQLTSQIEHSIRAHISLYYAGWLQCDDSTCGIVTRQVSVFGKRCLNDGCTGVMRYKYSDKQLYNQLLYFDSLFDCEKNKKQELKPIYLPDDLDYPKEQLTESSIKALTEQNRELMETGRSVVQKYLNDCGRRYVDMTSIFDFMLN | ||||||
Modified residue | 31 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 82 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 83 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 84 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 169 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 170 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 172 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 240 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 274 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 309 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 313 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
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 POL1 and B POL12, and the DNA primase large PRI2 and small PRI1 subunits (PubMed:3061469).
Subunit B POL12 binds to subunit A POL1 (PubMed:19494830).
POL1 interacts with CDC13, POB3, SPT16 and MCM10 (PubMed:10898792, PubMed:16675460, PubMed:8621497, PubMed:9199353).
Subunit B POL12 binds to subunit A POL1 (PubMed:19494830).
POL1 interacts with CDC13, POB3, SPT16 and MCM10 (PubMed:10898792, PubMed:16675460, PubMed:8621497, PubMed:9199353).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P13382 | CDC13 P32797 | 4 | EBI-6128, EBI-4187 | |
BINARY | P13382 | CTF4 Q01454 | 14 | EBI-6128, EBI-5209 | |
BINARY | P13382 | POL12 P38121 | 5 | EBI-6128, EBI-6111 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-34 | Disordered | ||||
Sequence: MSSKSEKLEKLRKLQAARNGTSIDDYEGDESDGD | ||||||
Compositional bias | 71-114 | Basic and acidic residues | ||||
Sequence: GVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDML | ||||||
Region | 71-135 | Disordered | ||||
Sequence: GVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDMLRTQHSKSTLLAHAKKSQKKSI | ||||||
Region | 166-205 | Disordered | ||||
Sequence: NLNSSPTSEFKSSIKRVNGNDESSHDAGISKKVKIDPDSS | ||||||
Compositional bias | 180-205 | Basic and acidic residues | ||||
Sequence: KRVNGNDESSHDAGISKKVKIDPDSS | ||||||
Region | 256-275 | Disordered | ||||
Sequence: LANPPSAQSLADEEDDEDSD | ||||||
Region | 813-837 | Disordered | ||||
Sequence: PDKEGNRSRAQKQRQNEENADAPVN | ||||||
Compositional bias | 817-836 | Basic and acidic residues | ||||
Sequence: GNRSRAQKQRQNEENADAPV | ||||||
Region | 1246-1381 | DNA-binding | ||||
Sequence: KKYFRREGGNNNGEDINNLQPLETTITDVERFKDTVTLELSCPSCDKRFPFGGIVSSNYYRVSYNGLQCKHCEQLFTPLQLTSQIEHSIRAHISLYYAGWLQCDDSTCGIVTRQVSVFGKRCLNDGCTGVMRYKYS | ||||||
Zinc finger | 1287-1317 | CysA-type | ||||
Sequence: CPSCDKRFPFGGIVSSNYYRVSYNGLQCKHC | ||||||
Motif | 1348-1372 | CysB motif | ||||
Sequence: CDDSTCGIVTRQVSVFGKRCLNDGC |
Domain
The CysA-type zinc finger is required for PCNA-binding.
Sequence similarities
Belongs to the DNA polymerase type-B family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,468
- Mass (Da)166,809
- Last updated1996-10-01 v2
- Checksum50C9032DBE95B5AE
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 71-114 | Basic and acidic residues | ||||
Sequence: GVEEDWREVDNSSSDEDTGNLASKDSKRKKNIKREKDHQITDML | ||||||
Compositional bias | 180-205 | Basic and acidic residues | ||||
Sequence: KRVNGNDESSHDAGISKKVKIDPDSS | ||||||
Sequence conflict | 759-760 | in Ref. 1; AAA34888 | ||||
Sequence: MI → IV | ||||||
Compositional bias | 817-836 | Basic and acidic residues | ||||
Sequence: GNRSRAQKQRQNEENADAPV |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
J03268 EMBL· GenBank· DDBJ | AAA34888.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z50161 EMBL· GenBank· DDBJ | CAA90524.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z71378 EMBL· GenBank· DDBJ | CAA95978.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z12126 EMBL· GenBank· DDBJ | CAA78111.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006947 EMBL· GenBank· DDBJ | DAA10443.1 EMBL· GenBank· DDBJ | Genomic DNA |