8D96

Human DNA polymerase alpha/primase elongation complex I bound to primer/template

Functional Information from GO Data

Chain	GOid	namespace	contents
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005654	cellular_component	nucleoplasm
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	0046872	molecular_function	metal ion binding
B	0051539	molecular_function	4 iron, 4 sulfur cluster binding
B	0071667	molecular_function	DNA/RNA hybrid binding
B	1903934	biological_process	positive regulation of DNA primase activity
B	1990077	cellular_component	primosome complex
C	0000166	molecular_function	nucleotide binding
C	0000731	biological_process	DNA synthesis involved in DNA repair
C	0000785	cellular_component	chromatin
C	0003676	molecular_function	nucleic acid binding
C	0003677	molecular_function	DNA binding
C	0003682	molecular_function	chromatin binding
C	0003688	molecular_function	DNA replication origin binding
C	0003697	molecular_function	single-stranded 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	0005654	cellular_component	nucleoplasm
C	0005658	cellular_component	alpha DNA polymerase:primase complex
C	0005730	cellular_component	nucleolus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006260	biological_process	DNA replication
C	0006261	biological_process	DNA-templated DNA replication
C	0006269	biological_process	DNA replication, synthesis of primer
C	0006270	biological_process	DNA replication initiation
C	0006271	biological_process	DNA strand elongation involved in DNA replication
C	0006272	biological_process	leading strand elongation
C	0006273	biological_process	lagging strand elongation
C	0006281	biological_process	DNA repair
C	0006289	biological_process	nucleotide-excision repair
C	0006303	biological_process	double-strand break repair via nonhomologous end joining
C	0008270	molecular_function	zinc ion binding
C	0016363	cellular_component	nuclear matrix
C	0019901	molecular_function	protein kinase binding
C	0031981	cellular_component	nuclear lumen
C	0032479	biological_process	regulation of type I interferon production
C	0046872	molecular_function	metal ion binding
C	1902975	biological_process	mitotic DNA replication initiation
C	1904161	biological_process	DNA synthesis involved in UV-damage excision repair

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	TYR1000-ILE1008

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	ZN_FING: CysA-type => ECO:0000250|UniProtKB:P15436

Chain	Residue	Details
C	CYS1283-SER1318
B	CYS367
B	CYS424

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:26975377, ECO:0007744|PDB:5EXR

Chain	Residue	Details
C	CYS1283
C	CYS1286
C	CYS1310
C	CYS1315
C	CYS1348
C	CYS1353
C	CYS1371
C	CYS1374

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Cleavage

Chain	Residue	Details
C	LYS124

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231

Chain	Residue	Details
C	THR174

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	SER186

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	SER190

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	SER209

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site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P33609

Chain	Residue	Details
C	LYS224

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site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
C	THR406

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site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P33609

Chain	Residue	Details
C	LYS970

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