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HCMVM:AN

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Species (Taxon ID) Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5). (295027)
Gene Name(s) UL98
Protein Name(s) Alkaline nuclease
External Links
UniProt F5HF49
EMBL AY446894
RefSeq YP_081545.1
ProteinModelPortal F5HF49
GeneID 3077527
Proteomes UP000000938
GO GO:0042025
GO:0003677
GO:0004520
GO:0004529
GO:0000737
GO:0000738
Gene3D 3.90.320.10
InterPro IPR011604
IPR001616
IPR011335
Pfam PF01771
PRINTS PR00924
SUPFAM SSF52980

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004529

exodeoxyribonuclease activity

PMID:21900421[1]

ECO:0000314

F

Figure 2 shows the results demonstrating UL98's exonuclease activity. There is a wild type (WT) UL98 strain and five mutants in which alanine was used to substitute another residue within the gene. The expressed proteins were purified and labelled. They were then combined with 14C-labelled DNA. The amount of cleaved DNA was measured over time. Figure 2a shows the significantly different cleavage rates between the WT gene and the R164A mutant, whose function was greatly impaired. Figure 2b show the total cleavage done by the WT and all the mutants over the course of an hour. The WT gene product exhibited significantly more exonuclease activity than the UL98-impaired mutants.

complete
CACAO 7973

GO:0004520

endodeoxyribonuclease activity

PMID:21900421[1]

ECO:0000314

F

Figure 3 shows the results demonstrating UL98's endonuclease activity. There is a wild type (WT) UL98 strain and five mutants in which alanine was used to substitute another residue within the gene. The expressed proteins were purified and labelled. In figure 3a, the WT and mutants were incubated with closed-circular plasmid DNA to see if the gene products would convert it to open-circular and linear forms using endonuclease activity. Following incubation, gel electrophoresis measured the leftover DNA products. The WT and one of the mutants were able to degrade the entire DNA substrate by nicking the supercoiled substrate and processing the products into smaller fragments not visible on the gel. Other mutants were only able to nick the supercoiled DNA, but not digest anything else. In figure 3b, the WT and mutants were incubated with a ssDNA substrate that had a 3' quencher and a 5' fluorophore. Endonucleolytic cleavage would result in detectable fluorescence. Over time, more protein was added to the reaction in increments. The WT and one of the mutants produced significantly more fluorescence than the rest of the mutants. This indicates that those mutants suffered from impaired endonuclease function. The R164A mutant had a slightly reduced endonuclease activity compaired to the WT.

complete
CACAO 7974

enables

GO:0004529

exodeoxyribonuclease activity

PMID:21900421[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004520

endodeoxyribonuclease activity

PMID:21900421[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006259

DNA metabolic process

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004529

P

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001616

F

Seeded From UniProt

complete

enables

GO:0004527

exonuclease activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001616

F

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

P

Seeded From UniProt

complete

involved_in

GO:0090305

nucleic acid phosphodiester bond hydrolysis

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

P

Seeded From UniProt

complete

part_of

GO:0030430

host cell cytoplasm

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

C

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

F

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

F

Seeded From UniProt

complete

enables

GO:0004527

exonuclease activity

GO_REF:0000104

ECO:0000256

match to sequence model evidence used in automatic assertion

UniRule:UR000281433

F

Seeded From UniProt

complete

part_of

GO:0030430

host cell cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1035
UniProtKB-SubCell:SL-0381

C

Seeded From UniProt

complete

enables

GO:0004527

exonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0269

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0255

F

Seeded From UniProt

complete

enables

GO:0004518

nuclease activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0540

F

Seeded From UniProt

complete

involved_in

GO:0016032

viral process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0945

P

Seeded From UniProt

complete

part_of

GO:0042025

host cell nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1048
UniProtKB-SubCell:SL-0414

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 1.2 1.3 Kuchta, AL et al. (2012) Structural modelling and mutagenesis of human cytomegalovirus alkaline nuclease UL98. J. Gen. Virol. 93 130-8 PubMed GONUTS page