Reviewed, UniProtKB/Swiss-Prot Q9X4D0 (PRIM_BACST)

Names and origin

Protein names

Recommended name:
    DNA primase
    EC=2.7.7.-

Gene names

Name:

dnaG

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	597 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	DNA primase is the polymerase that synthesizes small RNA primers for the Okazaki fragments on both template strands at replication forks during chromosomal DNA synthesis.
Cofactor	Binds 1 zinc ion per monomer.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the DNA primase family.

Ontologies

Keywords
Biological process	DNA replication Transcription
Cellular component	DNA-directed RNA polymerase Primosome
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Nucleotidyltransferase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA replication, synthesis of RNA primer Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	alpha DNA polymerase:primase complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro DNA binding Inferred from electronic annotation. Source: InterPro DNA helicase activity Inferred from electronic annotation. Source: InterPro DNA primase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 597

597

DNA primase

PRO_0000180478

Regions

Zinc finger

40 – 64

25

CHC2-type

Secondary structure

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597

Helix Strand Turn

Details...

Helix

7 – 16

10

Helix

19 – 23

5

Turn

24 – 26

3

Beta strand

30 – 32

3

Beta strand

35 – 38

4

Beta strand

41 – 43

3

Beta strand

50 – 53

4

Turn

54 – 57

4

Beta strand

58 – 61

4

Turn

62 – 64

3

Helix

70 – 78

9

Helix

82 – 93

12

Helix

98 – 100

3

Helix

459 – 471

13

Helix

475 – 484

10

Helix

492 – 505

14

Helix

513 – 516

4

Turn

517 – 519

3

Beta strand

522 – 524

3

Helix

525 – 531

7

Helix

542 – 553

12

Helix

555 – 573

19

Helix

577 – 594

18

Sequences

	Sequence		Length	Mass (Da)
	Q9X4D0-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 02FA690CB6798447	FASTA	597	67,111
	10 20 30 40 50 60 MGHRIPEETI EAIRRGVDIV DVIGEYVQLK RQGRNYFGLC PFHGEKTPSF SVSPEKQIFH 70 80 90 100 110 120 CFGCGAGGNA FTFLMDIEGI PFVEAAKRLA AKAGVDLSVY ELDVRGRDDG QTDEAKAMTE 130 140 150 160 170 180 AHALLKRFYH HLLVHTKEGQ AALDYLQARG WTKETIDRFE IGYAPDAPDA AAKLLESHSF 190 200 210 220 230 240 SLPVMEKAGL LTKKEDGRYV GRFRNRIMFP IHDHRGETVG FSGRLLGEGH PKYVNSPETP 250 260 270 280 290 300 VFRKGAILYH FHAARVPIRK RQEALLVEGF ADVISAAQAG IDYAIATMGT SLTEEQARIL 310 320 330 340 350 360 RPCDTITICY DGDRAGIEAA WAAAEQLSAL GCRVKVASLP NGLDPDEYIR VYGGERFAGE 370 380 390 400 410 420 AGCRRPLVAF KMAYLRRGKN LQHEGERLRY IDEALREIGK LSSPVEQDYY LRQLAEEFSL 430 440 450 460 470 480 SLSALHEQLS RSQRERTKPR EAPDGETARP MLAKKLLPAF QNAERLLLAH MMRSRDVALV 490 500 510 520 530 540 VQERIGGRFN IEEHRALAAY IYAFYEEGHE ADPGALISRI PGELQPLASD VSLLLIADDV 550 560 570 580 590 SEQELEDYIR HVLNRPKWLM LKVKEQEKTE AERRKDFLTA ARIAKEMIEM KKMLSSS

References

[1]	"Cloning, expression, and purification of Bacillus stearothermophilus DNA primase and crystallization of the zinc-binding domain." Pan H., Bird L.E., Wigley D.B. Biochim. Biophys. Acta 1444:429-433(1999) [PubMed: 10095067] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CRYSTALLIZATION. Strain: ATCC 29609 / DSM 2027 / NCA 1503 / NCIB 8924.
[2]	"Structure of the zinc-binding domain of Bacillus stearothermophilus DNA primase." Pan H., Wigley D.B. Structure 8:231-239(2000) [PubMed: 10745010] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1-103.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF106033 Genomic DNA. Translation: AAD20315.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D0Q	X-ray	1.71	A/B	1-103	[»]
1Z8S	NMR	-	A	453-597	[»]
2R6A	X-ray	2.90	C	455-597	[»]
2R6C	X-ray	4.00	G/H/I	455-597	[»]

ModBase

Search...

Family and domain databases

InterPro

IPR013264. DNA_primase_core_N.
IPR006295. DNA_primase_DnaG.
IPR006171. Toprim_dom.
IPR006154. Toprim_sub.
IPR002694. Znf_CHC2.
[Graphical view]

Gene3D

G3DSA:3.90.980.10. Toprim_N. 1 hit.
G3DSA:3.90.580.10. Znf_CHC2. 1 hit.

Pfam

PF01751. Toprim. 1 hit.
PF08275. Toprim_N. 1 hit.
PF01807. zf-CHC2. 1 hit.
[Graphical view]

ProDom

PD002276. Toprim_primase. 1 hit.
PD002988. Znf_CHC2. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00493. TOPRIM. 1 hit.
SM00400. ZnF_CHCC. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01391. dnaG. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PRIM_BACST

Accession

Primary (citable) accession number: Q9X4D0

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	November 25, 2008
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)