LAMBD:TERL

Species (Taxon ID)	Escherichia phage lambda (Bacteriophage lambda). (10710)
Gene Name(s)	A
Protein Name(s)	Terminase, large subunit DNA-packaging protein A Large terminase protein gpA
External Links
UniProt	P03708
EMBL	J02459
PIR	D04333
RefSeq	NP_040581.1
IntAct	P03708
GeneID	2703524
KEGG	vg:2703524
OrthoDB	VOG0900004B
Proteomes	UP000001711
GO	GO:0030430 GO:0098009 GO:0046872 GO:0009036 GO:0019073 GO:0019076
InterPro	IPR008866
Pfam	PF05876

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
Contributes to	GO:0019073	viral DNA genome packaging	PMID:8794874	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Fig. 3 shows that a mutated gpA is unable to properly cut at the cos site, thus preventing viral DNA packaging.	complete CACAO 4629
	GO:0019073	viral DNA genome packaging	PMID:11866517	ECO:0007101	southern hybridization evidence used in manual assertion		P		Researchers wanted to show that gpA (found in the terminase large subunit) helps package phage DNA. A lambda bacteriophage was used in this experiment and various gpA mutants were cut (with a restriction endonuclease) and cloned into this phage; the amount of DNA packaged was determined experimentally by quantifying it in vivo. Table 5 shows how a normal lambda-P1 Sam7 phage with no mutated gpA was able to package 100% of its DNA. But when the same phage contained any type of mutated gpA, the percentage of DNA packaged decreased dramatically.	complete CACAO 13561
	GO:0016887	ATPase activity	PMID:17870092	ECO:0000269	experimental evidence used in manual assertion		F		Fig. 4(b) shows in a time lapse experiment that the concentration of ADP increases and the concentration of ATP decreases suggesting that gpA-ΔN179 contains an ATPase site.	complete CACAO 4634
part_of	GO:0098009	viral terminase, large subunit	PMID:11866517	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0019073	viral DNA genome packaging	PMID:11866517	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006259	DNA metabolic process	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0009036	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004519	P		Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004518	P		Seeded From UniProt	complete
enables	GO:0009036	type II site-specific deoxyribonuclease activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.21.4	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:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	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
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References

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