NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 43049 / DSM 3752 / JCM 8966;
DOI=10.1101/gr.2700304; PubMed=15520287 [NCBI, ExPASy, EBI, Israel, Japan]
Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W., Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E., Hood L., Ng W.V.;
"Genome sequence of Haloarcula marismortui: a halophilic archaeon from the Dead Sea.";
Genome Res. 14:2221-2234(2004).

Comments

FUNCTION: This protein seals, during DNA replication, DNA recombination and DNA repair, nicks in double-stranded DNA (By similarity).
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

AY596297; AAV45492.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_135198.1; -.

3D structure databases

ModBase

Q5V4R0.

Enzyme and pathway databases

BioCyc

HMAR272569:RRNAC0463-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003910;	Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from HAMAP).
GO:0006310;	Biological process: DNA recombination (inferred from electronic annotation from HAMAP).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from HAMAP).
GO:0006260;	Biological process: DNA replication (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00407; -; 1.
PBIL [Tree]

InterPro

IPR000977; DNA_ligase.
IPR012309; DNA_ligase_A_C.
IPR012310; DNA_ligase_A_M.
IPR012308; DNA_ligase_A_N.
IPR016059; DNA_ligase_CS.
IPR012340; NA-bd_OB-fold.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.50.140; OB_NA_bd_sub; 1.

Pfam

PF04679; DNA_ligase_A_C; 1.
PF01068; DNA_ligase_A_M; 1.
PF04675; DNA_ligase_A_N; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR00574; dnl1; 1.

PROSITE

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

BLOCKS

Q5V4R0.

Genome annotation databases

GeneID

3130622; -.

GenomeReviews

AY596297_GR; rrnAC0463.

KEGG

hma:rrnAC0463; -.

NMPDR

fig|272569.1.peg.457; -.

Phylogenomic databases

HOGENOM

Q5V4R0; -.

Genome annotation databases

CMR

Q5V4R0; rrnAC0463.

Other

ProtoNet

Q5V4R0.

UniRef

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

Keywords

ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA replication; Ligase; Nucleotide-binding.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 554`	`554`	`DNA ligase.`	`PRO_1000049866`
`ACT_SITE`	`255 255`		`N6-AMP-lysine intermediate (By similarity).`

Sequence information

Length: 554 AA [This is the length of the unprocessed precursor]

Molecular weight: 59594 Da [This is the MW of the unprocessed precursor]

CRC64: 6DA9C5DCA84BCF3C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MEFAAFADRA EAIESESADT AITEAVTDLF RASGSDLSTL ARFVQGRVFP AYESRTLDIG 

        70         80         90        100        110        120 
PRLCYEAIAR AAGQNVSADD VEQRLADLGE IGAVAASYDL GGQQGLAAFG AGGGGDDALT 

       130        140        150        160        170        180 
VAELDDELRN LAAVDGSGSQ GTKVDILFGL FSRCSSTEAG YLARLVLSEM RIGVGEGTVR 

       190        200        210        220        230        240 
DAAAAAFDVP VEAVERAVQV SNDYGMVAEV ARDEGESGLA TVTLEIGRPV QAMLAQAGTV 

       250        260        270        280        290        300 
AGALEDWDRA AVEWKYDGAR VQVHFDGEDA RLFSRNMEEV TDPLPEVVET VESTLDAPAI 

       310        320        330        340        350        360 
LDGEVVAVDD GGDPLPFQEV LRRFRRKHDV AAAREDVAVR LHAFDCLHAA GEDLLDAALE 

       370        380        390        400        410        420 
TRHDRLESLF PADSDVFSQM WLSDDAEEIE SLEAEALAAG QEGIMLKDPT AAYSPGKRGK 

       430        440        450        460        470        480 
HWRKRKPDVE TLDCVVTGAE WGEGRRANVL GSFELSVRTD DGYATVGNVA TGITDEELDD 

       490        500        510        520        530        540 
LTERFEPYIR SEDGRDVVLD PAVVFEVGYE EIQASQSYAS GYALRFPRFL SVREDKTPDS 

       550 
ADSLARVERL AESQ

Q5V4R0 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