NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Delta H;
PubMed=9006048 [NCBI, ExPASy, EBI, Israel, Japan]
Noelling J., Reeve J.N.;
"Growth- and substrate-dependent transcription of the formate dehydrogenase (fdhCAB) operon in Methanobacterium thermoformicicum Z-245.";
J. Bacteriol. 179:899-908(1997).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Delta H;
PubMed=9371463 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R., Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D., Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A., Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J., Reeve J.N.;
"Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics.";
J. Bacteriol. 179:7135-7155(1997).

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

U51624; AAC44812.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000666; AAB86053.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H69077; H69077.

RefSeq

NP_276692.1; -.

3D structure databases

ModBase

Q50566.

Enzyme and pathway databases

BioCyc

MTHE187420:MTH1580-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; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q50566.

Genome annotation databases

GeneID

1471849; -.

GenomeReviews

AE000666_GR; MTH_1580.

KEGG

mth:MTH1580; -.

NMPDR

fig|187420.1.peg.1547; -.

Phylogenomic databases

HOGENOM

Q50566; -.

Genome annotation databases

CMR

Q50566; MTH_1580.

Other

ProtoNet

Q50566.

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`	`1 561`	`561`	`DNA ligase.`	`PRO_0000059609`
`ACT_SITE`	`251 251`		`N6-AMP-lysine intermediate (By similarity).`

Sequence information

Length: 561 AA [This is the length of the unprocessed precursor]

Molecular weight: 63089 Da [This is the MW of the unprocessed precursor]

CRC64: 0E05CE1E361E5907 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKELLYMELA EVYHRLESTT KRLEKTEILA ELLRSVDKEL LPDVTILMLG RVFPIWSEEE 

        70         80         90        100        110        120 
LGVGIKLLMK AISLVVGVSM DEIEDEIREQ GDIGLASEKL FSRKTQTTFF SQPLTVEFVY 

       130        140        150        160        170        180 
SRLKALASAS GDRAQSKKIN ILVEVLSQAK PLEARYITRT VLEELRVGVA EGIIRDAIAR 

       190        200        210        220        230        240 
AFEVDPALVE RAHMLTNDLG MVAAVAREEG EPGLGRLNLE PGRPVKPMLA QLASSIESAI 

       250        260        270        280        290        300 
TELGRAFCET KYDGIRVQIH RCGDEISIFT RRLENITAAV PEILEGVEEA LPADDYIVEG 

       310        320        330        340        350        360 
EIIVTMDGRP ASFQYILQRV RRKYDVERLT REVPLSLFLF DVLYHREPLI DEPLRHRREV 

       370        380        390        400        410        420 
LESILSEIPG RVEASRMVDV GPDNLNDALW LFEESIREGH EGIMIKDTEA PYIPGIRGKK 

       430        440        450        460        470        480 
MLKFKAEPET LDLIVVGGTY GRGKRAHLVG SYLLAARDED SGDLVTVAHV ATGLDDETLQ 

       490        500        510        520        530        540 
QLSERMEKLA IERKGRKLLV RPEIILEVAY SEIVKSPEYE SGYSLRFPVV KRIRDDLCLD 

       550        560 
DVDTVGRIES LFQSGQPDQP G

Q50566 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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