P03217 (AN_EBVB9) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkaline nuclease BGLF5
EC=3.1.-.-

Gene names

ORF Names:

BGLF5

Organism

Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) [Reference proteome]

Taxonomic identifier

10377 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Gammaherpesvirinae › Lymphocryptovirus › Epstein-Barr virus (strain GD1)

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in processing non linear or branched viral DNA intermediates and in capsid egress from the host nucleus. Exhibits endonuclease and exonuclease activities and accepts both double-stranded and single-stranded DNA as substrate. Exonuclease digestion of DNA is in the 5'-> 3' direction and the products are 5'-monophosphate nucleosides. Ref.4
Subunit structure	Forms a complex with the DNA polymerase BALF5, the DNA polymerase processivity factor BMRF1, and the major DNA binding protein BALF2.
Sequence similarities	Belongs to the baculo-herpesviridae alkaline nuclease family.

Ontologies

Keywords
Molecular function	Endonuclease Exonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW exonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 470

470

Alkaline nuclease BGLF5

PRO_0000115700

Experimental info

Mutagenesis

452

1

F → A: 98% loss of nuclease activity. Ref.3

Mutagenesis

458

1

V → A: 80% loss of nuclease activity. Ref.3

Secondary structure

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470

Helix Strand Turn

Details...

Helix

12 – 14

3

Helix

19 – 23

5

Helix

26 – 33

8

Beta strand

36 – 38

3

Helix

43 – 56

14

Turn

57 – 59

3

Helix

64 – 71

8

Helix

84 – 92

9

Helix

96 – 110

15

Helix

117 – 123

7

Beta strand

127 – 129

3

Helix

132 – 138

7

Helix

141 – 144

4

Helix

158 – 175

18

Turn

176 – 180

5

Turn

193 – 195

3

Beta strand

196 – 200

5

Beta strand

203 – 211

9

Beta strand

214 – 228

15

Helix

230 – 232

3

Helix

243 – 251

9

Helix

255 – 262

8

Beta strand

265 – 267

3

Beta strand

269 – 272

4

Beta strand

284 – 287

4

Helix

290 – 292

3

Helix

307 – 316

10

Beta strand

320 – 326

7

Turn

329 – 334

6

Beta strand

338 – 345

8

Helix

353 – 370

18

Turn

371 – 373

3

Beta strand

384 – 393

10

Beta strand

397 – 399

3

Beta strand

404 – 406

3

Beta strand

413 – 415

3

Beta strand

417 – 425

9

Helix

430 – 449

20

Helix

460 – 462

3

Sequences

	Sequence		Length	Mass (Da)
	P03217 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 81C2048E8A65CE80	FASTA	470	52,667
	10 20 30 40 50 60 MADVDELEDP MEEMTSYTFA RFLRSPETEA FVRNLDRPPQ MPAMRFVYLY CLCKQIQEFS 70 80 90 100 110 120 GETGFCDFVS SLVQENDSKD GPSLKSIYWG LQEATDEQRT VLCSYVESMT RGQSENLMWD 130 140 150 160 170 180 ILRNGIISSS KLLSTIKNGP TKVFEPAPIS TNHYFGGPVA FGLRCEDTVK DIVCKLICGD 190 200 210 220 230 240 ASANRQFGFM ISPTDGIFGV SLDLCVNVES QGDFILFTDR SCIYEIKCRF KYLFSKSEFD 250 260 270 280 290 300 PIYPSYTALY KRPCKRSFIR FINSIARPTV EYVPDGRLPS EGDYLLTQDE AWNLKDVRKR 310 320 330 340 350 360 KLGPGHDLVA DSLAANRGVE SMLYVMTDPS ENAGRIGIKD RVPVNIFINP RHNYFYQVLL 370 380 390 400 410 420 QYKIVGDYVR HSGGGKPGRD CSPRVNIVTA FFRKRSPLDP ATCTLGSDLL LDASVEIPVA 430 440 450 460 470 VLVTPVVLPD SVIRKTLSTA AGSWKAYADN TFDTAPWVPS GLFADDESTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"DNA sequence and expression of the B95-8 Epstein-Barr virus genome." Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J., Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C., Tuffnell P.S., Barrell B.G. Nature 310:207-211(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"A major DNA binding protein encoded by BALF2 open reading frame of Epstein-Barr virus (EBV) forms a complex with other EBV DNA-binding proteins: DNAase, EA-D, and DNA polymerase." Zeng Y., Middeldorp J., Madjar J.J., Ooka T. Virology 239:285-295(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BALF5; BMRF1 AND BALF2.
[3]	"Distinct regions of EBV DNase are required for nuclease and DNA binding activities." Liu M.T., Hsu T.Y., Lin S.F., Seow S.V., Liu M.Y., Chen J.Y., Yang C.S. Virology 242:6-13(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF PHE-452 AND VAL-458.
[4]	"The Epstein-Barr virus alkaline exonuclease BGLF5 serves pleiotropic functions in virus replication." Feederle R., Bannert H., Lips H., Muller-Lantzsch N., Delecluse H.J. J. Virol. 83:4952-4962(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V01555 Genomic DNA. Translation: CAA24827.1.
AJ507799 Genomic DNA. Translation: CAD53437.1.

PIR

QQBE37. A03779.

RefSeq

YP_401687.1. NC_007605.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2W45	X-ray	3.00	A/B	1-470	[»]
2W4B	X-ray	3.50	A/B	1-470	[»]

ProteinModelPortal

P03217.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3783773.

Phylogenomic databases

ProtClustDB

CLSP2509676.

Family and domain databases

InterPro

IPR001616. Herpes_alk_exo.
IPR011335. Restrct_endonuc-II-like.
[Graphical view]

Pfam

PF01771. Herpes_alk_exo. 1 hit.
[Graphical view]

PRINTS

PR00924. ALKEXNUCLASE.

SUPFAM

SSF52980. Restrict_endonuc_II-like_core. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P03217.

Entry information

Entry name

AN_EBVB9

Accession

Primary (citable) accession number: P03217
Secondary accession number(s): Q777D2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program