Probable DNA ligase - Mycobacterium tuberculosis CTRI-2

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G2N5T8 (G2N5T8_MYCTU) Unreviewed, UniProtKB/TrEMBL

Last modified May 29, 2013. Version 12. History...

Clusters with 100%, 90%, 50% identity |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info Customize order

Names and origin

Protein names

Recommended name:
Probable DNA ligase HAMAP-Rule MF_00407
EC=6.5.1.1 HAMAP-Rule MF_00407

Alternative name(s):
Polydeoxyribonucleotide synthase [ATP] HAMAP-Rule MF_00407

Gene names

Name:	ligB EMBL AEN01529.1
Synonyms:	lig HAMAP-Rule MF_00407
ORF Names:	MTCTRI2_3125 EMBL AEN01529.1

Organism

Mycobacterium tuberculosis CTRI-2 EMBL AEN01529.1

Taxonomic identifier

707235 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex ›

Protein attributes

Sequence length	507 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 RuleBase RU000617
Cofactor	Divalent metal cations By similarity. HAMAP-Rule MF_00407
Sequence similarities	Belongs to the ATP-dependent DNA ligase family. HAMAP-Rule MF_00407 RuleBase RU004196

Ontologies

Keywords
Biological process	Cell cycle Cell division HAMAP-Rule MF_00407 DNA damage DNA recombination HAMAP-Rule MF_00407 RuleBase RU000617 DNA repair HAMAP-Rule MF_00407 RuleBase RU000617 DNA replication HAMAP-Rule MF_00407 RuleBase RU000617
Ligand	ATP-binding HAMAP-Rule MF_00407 RuleBase RU000617 Metal-binding HAMAP-Rule MF_00407 Nucleotide-binding
Molecular function	Ligase HAMAP-Rule MF_00407 RuleBase RU000617 EMBL AEN01529.1
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

Sites

Active site

211

N6-AMP-lysine intermediate By similarity HAMAP-Rule MF_00407

Binding site

209

ATP By similarity HAMAP-Rule MF_00407

Binding site

216

ATP By similarity HAMAP-Rule MF_00407

Binding site

231

ATP By similarity HAMAP-Rule MF_00407

Binding site

260

ATP By similarity HAMAP-Rule MF_00407

Binding site

300

ATP By similarity HAMAP-Rule MF_00407

Binding site

372

ATP By similarity HAMAP-Rule MF_00407

Binding site

378

ATP By similarity HAMAP-Rule MF_00407

Sequences

Sequence

Length

Mass (Da)

Tools

G2N5T8 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 8D73EB4C08C7149D
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FASTA

507

53,727

        10         20         30         40         50         60 
MLLHDVAITS MDVAATSSRL TKVARIAALL HRAAPDTQLV TIIVSWLSGE LPQRHIGVGW 

        70         80         90        100        110        120 
AALRSLPPPA PQPALTVTGV DATLSKIGTL SGKGSQAQRA ALVAELFSAA TEAEQTFLLR 

       130        140        150        160        170        180 
LLGGELRQGA KGGIMADAVA QAAGLPAATV QRAAMLGGDL AAAAAAGLSG AALDTFTLRV 

       190        200        210        220        230        240 
GRPIGPMLAQ TATSVHDALE RHGGTTIFEA KLDGARVQIH RANDQVRIYT RSLDDVTARL 

       250        260        270        280        290        300 
PEVVEATLAL PVRDLVADGE AIALCPDNRP QRFQVTASRF GRSVDVAAAR ATQPLSVFFF 

       310        320        330        340        350        360 
DILHRDGTDL LEAPTTERLA ALDALVPARH RVDRLITSDP TDAANFLDAT LAAGHEGVMA 

       370        380        390        400        410        420 
KAPAARYLAG RRGAGWLKVK PVHTLDLVVL AVEWGSGRRR GKLSNIHLGA RDPATGGFVM 

       430        440        450        460        470        480 
VGKTFKGMTD AMLDWQTTRF HEIAVGPTDG YVVQLRPEQV VEVALDGVQR SSRYPGGLAL 

       490        500 
RFARVVRYRA DKDPAEADTI DAVRALY

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References

[1]

"The Complete Genome Sequence of Mycobacterium tuberculosis CTRI2."
Shitikov E., Ilina E., Ikryannikova L., Malakhova M., Parfenova T., Afanas'ev M., Kamashev D., Bazaleev N., Ischenko D., Aliper A., Alekseev D., Smirnova T., Chernousova L., Larionova E., Beletsky A., Mardanov A., Ravin N., Skryabin K., Govorun V.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CTRI-2 EMBL AEN01529.1.

[2]

"Comparative Genomic Analysis of Mycobacterium tuberculosis Drug Resistant Strains from Russia."
Ilina E.N., Shitikov E.A., Ikryannikova L.N., Alekseev D.G., Kamashev D.E., Malakhova M.V., Parfenova T.V., Afanas'ev M.V., Ischenko D.S., Bazaleev N.A., Smirnova T.G., Larionova E.E., Chernousova L.N., Beletsky A.V., Mardanov A.V., Ravin N.V., Skryabin K.G., Govorun V.M.
PLoS ONE 8:E56577-E56577(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: CTRI-2 EMBL AEN01529.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP002992 Genomic DNA. Translation: AEN01529.1.
RefSeq	YP_005918150.1. NC_017524.1.
3D structure databases
ProteinModelPortal	G2N5T8.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AEN01529; AEN01529; MTCTRI2_3125.
GeneID	12508293.
KEGG	mto:MTCTRI2_3125.
Phylogenomic databases
KO	K01971.
Enzyme and pathway databases
BioCyc	MTUB707235:GLGU-3124-MONOMER.
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. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

G2N5T8_MYCTU

Accession

Primary (citable) accession number: G2N5T8

Entry history

Integrated into UniProtKB/TrEMBL:	November 16, 2011
Last sequence update:	November 16, 2011
Last modified:	May 29, 2013
This is version 12 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information