DNA ligase - Anaplasma phagocytophilum (strain HZ)

Preferred order of sections

Names and origin

Protein names

Recommended name:
DNA ligase
EC=6.5.1.2

Alternative name(s):
Polydeoxyribonucleotide synthase [NAD+]

Gene names

Name:	ligA
Ordered Locus Names:	APH_0138

Organism

Anaplasma phagocytophilum (strain HZ) [Complete proteome] [HAMAP]

Taxonomic identifier

212042 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma › phagocytophilum group

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA By similarity. HAMAP MF_01588
Catalytic activity	NAD⁺ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588
Cofactor	Magnesium or manganese By similarity. HAMAP MF_01588
Sequence similarities	Belongs to the NAD-dependent DNA ligase family. LigA subfamily. Contains 1 BRCT domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Ligand	Magnesium Manganese Metal-binding NAD Zinc
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	DNA ligase (NAD+) activity Inferred from electronic annotation. Source: EC 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 – 677

677

DNA ligase HAMAP MF_01588

PRO_0000313114

Regions

Domain

594 – 677

84

BRCT

Nucleotide binding

34 – 38

5

NAD By similarity

Nucleotide binding

84 – 85

2

NAD By similarity

Sites

Active site

120

1

N6-AMP-lysine intermediate By similarity

Metal binding

403

1

Zinc By similarity

Metal binding

406

1

Zinc By similarity

Metal binding

421

1

Zinc By similarity

Metal binding

427

1

Zinc By similarity

Binding site

118

1

NAD By similarity

Binding site

141

1

NAD By similarity

Binding site

176

1

NAD By similarity

Binding site

283

1

NAD By similarity

Binding site

307

1

NAD By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q2GLI8 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 413BAC9CF1B8F090
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FASTA

677

74,768

        10         20         30         40         50         60 
MSDNDSRRRL ADLNAQLKLH DVLYHEHDAP EISDAQYDAL VQEKRELLEK FPELSAYNDY 

        70         80         90        100        110        120 
EGVIGALTVD ARLPKIAHRE PMLSLENSFT IQDVEKFISR VKRSLNMDPE VSITIACEPK 

       130        140        150        160        170        180 
IDGLSFAALY EKGSLIRVAT RGNGHLGEDI TNTAKVIRKL PHKIANAPEV LEVRGEIYMH 

       190        200        210        220        230        240 
HSDFEKLKDV CNFANPRNAA AGSIRQLNPK IAEERNLRYV AYCIVNSALA SQEAILKQLA 

       250        260        270        280        290        300 
EWGFCTHTEV LFADNMDDAL SFHTRMYNTR STLGYDIDGI VYKVNDTHLQ KLLGSTSKYP 

       310        320        330        340        350        360 
RWATAHKFPS TEAITKLRDI SVQVGRTGVI TPIAELEPIN IGGTLVSRAS LHNLNEIARK 

       370        380        390        400        410        420 
DIRIGDSVIV KRAGEVIPQV VGVDHTARCN SAVPEEYVFP SHCPSCGSTL SRAPGEVAMR 

       430        440        450        460        470        480 
CTAELSCQAQ VLERVKHFVS RDGLNIVGLG EKQIEFFCNA SYISNVADIF SLREKISHMN 

       490        500        510        520        530        540 
LSAEHGWGEK SIALLINAIN ASTTVKLSNF IFALGIRFIG KGAAKLIAEH YRSYSAWVRA 

       550        560        570        580        590        600 
MTSLANGEDP DNIHGIGLKS IESLRAFFSS EDNLRVLQTL EEKLNILNEI ANTETASPIS 

       610        620        630        640        650        660 
GKTIVFTGVL EDMSRNEAAK YAETLGAKVG NTVTTKTDIL VAGSNSGSKL DTARKLGIQV 

       670 
MNESEWKDLL KTVSNSE

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References

[1]

"Comparative genomics of emerging human ehrlichiosis agents."
Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.

Tettelin H.
PLoS Genet. 2:208-222(2006) [PubMed: 16482227] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HZ.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000235 Genomic DNA. Translation: ABD43878.1.
RefSeq	YP_504763.1. NC_007797.1.
3D structure databases
ProteinModelPortal	Q2GLI8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2GLI8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3929997.
GenomeReviews	Gene locus APH_0138 in contig CP000235_GR.
KEGG	aph:APH_0138.
NMPDR	fig\|212042.5.peg.133.
PATRIC	20948848. VBIAnaPha602_0149.
TIGR	APH_0138.
Phylogenomic databases
eggNOG	COG0272.
HOGENOM	HBG620317.
OMA	TQKVGAT.
PhylomeDB	Q2GLI8.
ProtClustDB	CLSK747278.
Enzyme and pathway databases
BioCyc	APHA212042:APH_0138-MONOMER.
Family and domain databases
HAMAP	MF_01588. DNA_ligase_A. [Tree]
InterPro	IPR001357. BRCT. IPR018239. DNA_ligase_AS. IPR004150. DNA_ligase_OB. IPR001679. DNAligase. IPR013839. DNAligase_adenylation. IPR013840. DNAligase_N. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR010994. RuvA_2-like. IPR004149. Znf_DNAligase_C4. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K01972.
Pfam	PF00533. BRCT. 1 hit. PF01653. DNA_ligase_aden. 1 hit. PF03120. DNA_ligase_OB. 1 hit. PF03119. DNA_ligase_ZBD. 1 hit. [Graphical view]
PIRSF	PIRSF001604. LigA. 1 hit.
SMART	SM00292. BRCT. 1 hit. SM00532. LIGANc. 1 hit. [Graphical view]
SUPFAM	SSF52113. BRCT. 1 hit. SSF50249. Nucleic_acid_OB. 1 hit. SSF47781. RuvA_2_like. 1 hit.
TIGRFAMs	TIGR00575. Dnlj. 1 hit.
PROSITE	PS50172. BRCT. 1 hit. PS01055. DNA_LIGASE_N1. 1 hit. PS01056. DNA_LIGASE_N2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ_ANAPZ

Accession

Primary (citable) accession number: Q2GLI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 21, 2006
Last modified:	January 25, 2012
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents