[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1016/S0022-2836(83)80282-4; PubMed=6864790 [NCBI, ExPASy, EBI, Israel, Japan] Dunn J.J., Studier F.W.; "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements."; J. Mol. Biol. 166:477-535(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0022-2836(81)90178-9; PubMed=7310871 [NCBI, ExPASy, EBI, Israel, Japan] Dunn J.J., Studier F.W.; "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to the beginning of gene 4."; J. Mol. Biol. 148:303-330(1981).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-359. DOI=10.1093/nar/8.10.2119; PubMed=7001354 [NCBI, ExPASy, EBI, Israel, Japan] Dunn J.J., Studier F.W.; "The transcription termination site at the end of the early region of bacteriophage T7 DNA."; Nucleic Acids Res. 8:2119-2132(1980).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5. PubMed=6254001 [NCBI, ExPASy, EBI, Israel, Japan] Saito H., Tabor S., Tamanoi F., Richardson C.C.; "Nucleotide sequence of the primary origin of bacteriophage T7 DNA replication: relationship to adjacent genes and regulatory elements."; Proc. Natl. Acad. Sci. U.S.A. 77:3917-3921(1980).
[5]	X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). DOI=10.1016/S0092-8674(00)81260-X; PubMed=8653795 [NCBI, ExPASy, EBI, Israel, Japan] Subramanya H.S., Doherty A.J., Ashford S.R., Wigley D.B.; "Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7."; Cell 85:607-615(1996).

Comments

FUNCTION: DNA ligase, which is expressed in the early stage of lytic development, has been implicated in T7 DNA synthesis and genetic recombination. It may also play a role in T7 DNA repair.
CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).
SIMILARITY: Belongs to the ATP-dependent DNA ligase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

V01124; CAA24322.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V01126; CAA24326.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V01127; CAA24336.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
V01146; CAA24393.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

E94615; LQBP37.

RefSeq

NP_041963.1; -.

3D structure databases

PDB

1A0I; X-ray; 2.60 A; A=3-349.

[ExPASy / RCSB / EBI]

PDBsum

1A0I; -.

ModBase

P00969.

Family and domain databases

InterPro

IPR012310; DNA_ligase_A_M.
IPR016059; DNA_ligase_CS.
IPR016306; DNA_ligase_phage.
IPR012340; NA-bd_OB-fold.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.50.140; OB_NA_bd_sub; 1.

Pfam

PF01068; DNA_ligase_A_M; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001600; DNA_ligase_phage_T3; 1.

PROSITE

PS00697; DNA_LIGASE_A1; 1.
PS00333; DNA_LIGASE_A2; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P00969.

Genome annotation databases

GeneID

1261055; -.

GenomeReviews

V01146_GR; 1.3.

Other

P00969; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nucleotide-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 359`	`359`	`DNA ligase.`	`PRO_0000059598`
`ACT_SITE`	`34 34`		`N6-AMP-lysine intermediate (By similarity).`
`STRAND`	`9 13`	`5`
`HELIX`	`16 26`	`11`
`STRAND`	`27 33`	`7`
`STRAND`	`37 45`	`9`
`STRAND`	`48 53`	`6`
`HELIX`	`61 66`	`6`
`HELIX`	`71 78`	`8`
`STRAND`	`87 99`	`13`
`TURN`	`101 103`	`3`
`HELIX`	`104 109`	`6`
`STRAND`	`115 119`	`5`
`TURN`	`141 143`	`3`
`STRAND`	`144 153`	`10`
`HELIX`	`154 159`	`6`
`STRAND`	`163 166`	`4`
`HELIX`	`167 184`	`18`
`STRAND`	`188 192`	`5`
`STRAND`	`195 200`	`6`
`HELIX`	`201 212`	`12`
`TURN`	`213 215`	`3`
`STRAND`	`219 222`	`4`
`STRAND`	`230 240`	`11`
`STRAND`	`243 253`	`11`
`TURN`	`257 259`	`3`
`STRAND`	`267 271`	`5`
`STRAND`	`277 281`	`5`
`HELIX`	`286 299`	`14`
`TURN`	`300 302`	`3`
`TURN`	`321 324`	`4`
`STRAND`	`326 334`	`9`
`STRAND`	`340 342`	`3`
`STRAND`	`344 348`	`5`

Sequence information

Length: 359 AA [This is the length of the unprocessed precursor]

Molecular weight: 41133 Da [This is the MW of the unprocessed precursor]

CRC64: 43DA453B71BDF8DC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMNIKTNPFK AVSFVESAIK KALDNAGYLI AEIKYDGVRG NICVDNTANS YWLSRVSKTI 

        70         80         90        100        110        120 
PALEHLNGFD VRWKRLLNDD RCFYKDGFML DGELMVKGVD FNTGSGLLRT KWTDTKNQEF 

       130        140        150        160        170        180 
HEELFVEPIR KKDKVPFKLH TGHLHIKLYA ILPLHIVESG EDCDVMTLLM QEHVKNMLPL 

       190        200        210        220        230        240 
LQEYFPEIEW QAAESYEVYD MVELQQLYEQ KRAEGHEGLI VKDPMCIYKR GKKSGWWKMK 

       250        260        270        280        290        300 
PENEADGIIQ GLVWGTKGLA NEGKVIGFEV LLESGRLVNA TNISRALMDE FTETVKEATL 

       310        320        330        340        350 
SQWGFFSPYG IGDNDACTIN PYDGWACQIS YMEETPDGSL RHPSFVMFRG TEDNPQEKM

P00969 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools