A2BJX6 (DNLI_HYPBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA ligase
EC=6.5.1.1

Alternative name(s):
Polydeoxyribonucleotide synthase [ATP]

Gene names

Name:	lig
Ordered Locus Names:	Hbut_0421

Organism

Hyperthermus butylicus (strain DSM 5456 / JCM 9403) [Reference proteome] [HAMAP]

Taxonomic identifier

415426 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Pyrodictiaceae › Hyperthermus › Hyperthermus butylicus

Protein attributes

Sequence length	608 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair By similarity. HAMAP-Rule MF_00407
Catalytic activity	ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). HAMAP-Rule MF_00407
Cofactor	Divalent metal cations By similarity.
Sequence similarities	Belongs to the ATP-dependent DNA ligase family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA damage DNA recombination DNA repair DNA replication
Ligand	ATP-binding Metal-binding Nucleotide-binding
Molecular function	Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA ligation involved in DNA repair Inferred from electronic annotation. Source: InterPro DNA recombination Inferred from electronic annotation. Source: HAMAP DNA replication Inferred from electronic annotation. Source: HAMAP cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (ATP) activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 608	608	DNA ligase HAMAP-Rule MF_00407		PRO_0000365248
Sites
	Active site	268	1	N6-AMP-lysine intermediate By similarity
	Binding site	266	1	ATP By similarity
	Binding site	273	1	ATP By similarity
	Binding site	288	1	ATP By similarity
	Binding site	318	1	ATP By similarity
	Binding site	358	1	ATP By similarity
	Binding site	435	1	ATP By similarity
	Binding site	441	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	A2BJX6 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: 7D16CF4AEB60771E	FASTA	608	68,330
	10 20 30 40 50 60 MSMPFSVLAE TFEKLERVTA RTQMLLYLVE LFKKTPPEII DKVVYFIQGK LWPDWKGLPE 70 80 90 100 110 120 LGIGEKMLIK AASIALHVSE KQIEQLVKKL GDTGKAIEMI KREKQQKQKA VGLLAFMQKP 130 140 150 160 170 180 SGGESTLTVE KVYDTLARIA LVQGEGSRDI KLKLLAGLLA EASPREAKYI ARFVEGRLRL 190 200 210 220 230 240 GVGDATIMEA LAVVYGGSAA MRSVVERAYN LRADLGMVAK ILATQGIDAL KNIKPEVGVP 250 260 270 280 290 300 IRPMLAERLN DPVEIIKKLG GRALVEYKYD GERAQIHKKG DKIWIFSRRL ENITHMYPDV 310 320 330 340 350 360 VEMAKKGIKA EEAIVEGEIV AIDPETGEFR PFQVLMHRRR KKDVHAVLSE IPVAVFLFDT 370 380 390 400 410 420 LYVNGEDLTL KPLPARHEVL EKIIEQSDTW RIAEGIVTSD PQELESFFLK AIEDGAEGVM 430 440 450 460 470 480 AKAIHDRSIY QAGARGWLWI KYKRDYKSEM SDTVDLVVIG AFYGKGRRGG KFGALLMAAY 490 500 510 520 530 540 DPDTDTFKSV CKVGSGFTDE DLERLDDMLK PYISDKKPAR VDSQMKPDVW VEPTLVAEII 550 560 570 580 590 600 GAELTLSPIH TCCYGWVKSG AGISIRFPRF IRWRPDKGPE DATTTKELYE MYKRQLRRIK EEEAPTGV

References

[1]

"The genome of Hyperthermus butylicus: a sulfur-reducing, peptide fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C." Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M., She Q., Garrett R.A., Klenk H.-P. Archaea 2:127-135(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 5456 / JCM 9403.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000493 Genomic DNA. Translation: ABM80287.1.
RefSeq	YP_001012632.1. NC_008818.1.
3D structure databases
ProteinModelPortal	A2BJX6.
SMR	A2BJX6. Positions 3-598.
ModBase	Search...
Protein-protein interaction databases
STRING	415426.Hbut_0421.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABM80287; ABM80287; Hbut_0421.
GeneID	4781994.
KEGG	hbu:Hbut_0421.
Phylogenomic databases
eggNOG	COG1793.
HOGENOM	HOG000036008.
KO	K10747.
OMA	AQVACLY.
ProtClustDB	PRK01109.
Family and domain databases
Gene3D	1.10.3260.10. 1 hit. 2.40.50.140. 1 hit.
HAMAP	MF_00407. DNA_ligase.
InterPro	IPR022865. DNA_ligae_ATP-dep_bac/arc. IPR000977. DNA_ligase_ATP-dep. IPR012309. DNA_ligase_ATP-dep_C. IPR012310. DNA_ligase_ATP-dep_cent. IPR016059. DNA_ligase_ATP-dep_CS. IPR012308. DNA_ligase_ATP-dep_N. IPR012340. NA-bd_OB-fold. [Graphical view]
Pfam	PF04679. DNA_ligase_A_C. 1 hit. PF01068. DNA_ligase_A_M. 1 hit. PF04675. DNA_ligase_A_N. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF117018. SSF117018. 1 hit.
TIGRFAMs	TIGR00574. dnl1. 1 hit.
PROSITE	PS00697. DNA_LIGASE_A1. 1 hit. PS00333. DNA_LIGASE_A2. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLI_HYPBU

Accession

Primary (citable) accession number: A2BJX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 3, 2009
Last sequence update:	February 20, 2007
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program