8FOD

Cryo-EM structure of S. cerevisiae DNA polymerase alpha-primase complex in Apo state conformation II

Functional Information from GO Data

Chain	GOid	namespace	contents
1	0000166	molecular_function	nucleotide binding
1	0000510	molecular_function	H3-H4 histone complex chaperone activity
1	0000731	biological_process	DNA synthesis involved in DNA repair
1	0003676	molecular_function	nucleic acid binding
1	0003677	molecular_function	DNA binding
1	0003682	molecular_function	chromatin binding
1	0003688	molecular_function	DNA replication origin binding
1	0003697	molecular_function	single-stranded DNA binding
1	0003887	molecular_function	DNA-directed DNA polymerase activity
1	0005515	molecular_function	protein binding
1	0005634	cellular_component	nucleus
1	0005657	cellular_component	replication fork
1	0005658	cellular_component	alpha DNA polymerase:primase complex
1	0005739	cellular_component	mitochondrion
1	0006260	biological_process	DNA replication
1	0006270	biological_process	DNA replication initiation
1	0006272	biological_process	leading strand elongation
1	0006273	biological_process	lagging strand elongation
1	0006278	biological_process	RNA-templated DNA biosynthetic process
1	0006279	biological_process	premeiotic DNA replication
1	0006281	biological_process	DNA repair
1	0006302	biological_process	double-strand break repair
1	0008270	molecular_function	zinc ion binding
1	0016740	molecular_function	transferase activity
1	0016779	molecular_function	nucleotidyltransferase activity
1	0034061	molecular_function	DNA polymerase activity
1	0046872	molecular_function	metal ion binding
1	0051536	molecular_function	iron-sulfur cluster binding
1	0051539	molecular_function	4 iron, 4 sulfur cluster binding
1	1902975	biological_process	mitotic DNA replication initiation
A	0000166	molecular_function	nucleotide binding
A	0000428	cellular_component	DNA-directed RNA polymerase complex
A	0003697	molecular_function	single-stranded DNA binding
A	0003899	molecular_function	DNA-directed RNA polymerase activity
A	0005524	molecular_function	ATP binding
A	0005658	cellular_component	alpha DNA polymerase:primase complex
A	0006260	biological_process	DNA replication
A	0006269	biological_process	DNA replication, synthesis of primer
A	0006270	biological_process	DNA replication initiation
A	0008270	molecular_function	zinc ion binding
A	0016740	molecular_function	transferase activity
A	0016779	molecular_function	nucleotidyltransferase activity
A	0043596	cellular_component	nuclear replication fork
A	0046872	molecular_function	metal ion binding
B	0003677	molecular_function	DNA binding
B	0003697	molecular_function	single-stranded DNA binding
B	0003899	molecular_function	DNA-directed RNA polymerase activity
B	0005634	cellular_component	nucleus
B	0005635	cellular_component	nuclear envelope
B	0005658	cellular_component	alpha DNA polymerase:primase complex
B	0006260	biological_process	DNA replication
B	0006261	biological_process	DNA-templated DNA replication
B	0006269	biological_process	DNA replication, synthesis of primer
B	0006270	biological_process	DNA replication initiation
B	0006302	biological_process	double-strand break repair
B	0046872	molecular_function	metal ion binding
B	0051536	molecular_function	iron-sulfur cluster binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
C	0003677	molecular_function	DNA binding
C	0003887	molecular_function	DNA-directed DNA polymerase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005635	cellular_component	nuclear envelope
C	0005658	cellular_component	alpha DNA polymerase:primase complex
C	0006260	biological_process	DNA replication
C	0006270	biological_process	DNA replication initiation
C	0016233	biological_process	telomere capping
C	0071897	biological_process	DNA biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00116
Number of Residues	9
Details	DNA_POLYMERASE_B DNA polymerase family B signature. YGDTDSVMI

Chain	Residue	Details
1	TYR994-ILE1002

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	30
Details	Zinc finger: {"description":"CysA-type","evidences":[{"source":"UniProtKB","id":"P15436","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	Motif: {"description":"CysB motif","evidences":[{"source":"UniProtKB","id":"P15436","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19494830","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3FLO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	10
Details	Motif: {"description":"Zinc knuckle motif"}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	29
Details	Region: {"description":"H-T-H-like motif","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20404922","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---