NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ST 549;
Rolland J.L., Dietrich J.;
"Cloning and expression of a new thermostable DNA ligase from the hyperthermophilic Pyrococcus abyssi sp. ST 549.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=GE5 / Orsay;
DOI=10.1046/j.1365-2958.2003.03381.x; PubMed=12622808 [NCBI, ExPASy, EBI, Israel, Japan]
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.;
"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi.";
Mol. Microbiol. 47:1495-1512(2003).

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).
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Thermostable;
SUBUNIT: Monomer (By similarity).
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

AJ006532; CAC20743.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ248284; CAB49465.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

B75173; B75173.

RefSeq

NP_126234.1; -.

3D structure databases

SMR

Q9V185; 1-559.

ModBase

Q9V185.

Enzyme and pathway databases

BioCyc

PABY272844:PAB2002-MON; -.

Ontologies

GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from HAMAP).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0003910;	Molecular function: DNA ligase (ATP) activity (inferred from electronic annotation from HAMAP).
GO:0007049;	Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0051301;	Biological process: cell division (inferred from electronic annotation from UniProtKB-KW).
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; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1495445; -.

GenomeReviews

AL096836_GR; PYRAB05430.

KEGG

pab:PAB2002; -.

NMPDR

fig|272844.1.peg.569; -.

Phylogenomic databases

HOGENOM

Q9V185; -.

Genome annotation databases

CMR

Q9V185; PYRAB05430.

Other

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`	`1 559`	`559`	`DNA ligase.`	`PRO_0000059612`
`ACT_SITE`	`249 249`		`N6-AMP-lysine intermediate (By similarity).`
`VARIANT`	`100 100`	`1`	`K -> R (in strain: ST 549).`
`VARIANT`	`292 292`	`1`	`T -> A (in strain: ST 549).`
`VARIANT`	`367 367`	`1`	`T -> A (in strain: ST 549).`
`VARIANT`	`408 408`	`1`	`V -> I (in strain: ST 549).`
`VARIANT`	`484 484`	`1`	`K -> R (in strain: ST 549).`

Sequence information

Length: 559 AA [This is the length of the unprocessed precursor]

Molecular weight: 63553 Da [This is the MW of the unprocessed precursor]

CRC64: 64CDBA1BBD188433 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRYIELAQLY QKLEKTTMKL IKTRLVADFL KKVPEDHLEF IPYLILGDVF PEWDERELGV 

        70         80         90        100        110        120 
GEKLLIKAVS MATGIDSKEI ENSVKDTGDL GESIALAVKK RKQKSFFSQP LTIKRVYQTL 

       130        140        150        160        170        180 
VKVAETTGEG SQDKKMKYLA NLFMDAEPIE AKYIARTVLG TMRTGVAEGL LRDAISLAFN 

       190        200        210        220        230        240 
VKVELVERAY MLTSDFGFVA KIAKTEGNDG LAKVTIQIGK PIKPMLAQQA ANIKEALLEM 

       250        260        270        280        290        300 
GGEAEFEIKY DGARVQVHKD GEKVTIYSRR LENVTRAIPE IVEAIKEALK PTKAIVEGEL 

       310        320        330        340        350        360 
VAIGEDGRPL PFQYVLRRFR RKYNIEEMME KIPLELNLFD VLYVDGVSLI DTKFMERRKK 

       370        380        390        400        410        420 
LEEIVETNGK VKIAENLITK NVEEAEQFYK RALEMGHEGL MAKRLDAVYE PGNRGKKWLK 

       430        440        450        460        470        480 
IKPTMENLDL VIIGAEWGEG RRAHLLGSFI LGAYDPETGE FLEVGKVGSG FTDDDLVEFT 

       490        500        510        520        530        540 
KMLKPLIIKE EGKRVWIQPK VVIEVTYQEI QKSPKYRSGF ALRFPRYVAL REDKGPEDAD 

       550 
TIERIAQLYE LQERMKGKV

Q9V185 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