ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9HJ26


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name DNLI_THEAC
Primary accession number Q9HJ26
Secondary accession numbers None
Integrated into Swiss-Prot on June 20, 2001
Sequence was last modified on March 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 42)
Name and origin of the protein
Protein name DNA ligase
Synonyms EC 6.5.1.1
Polydeoxyribonucleotide synthase [ATP]
Gene name
Name: lig
OrderedLocusNames: Ta1148
From
Thermoplasma acidophilum [TaxID: 2303] [HAMAP proteome]
Taxonomy Archaea; Euryarchaeota; Thermoplasmata; Thermoplasmatales; Thermoplasmataceae; Thermoplasma.
Protein existence 3: Inferred from homology;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25905 / AMRC-C165 / DSM 1728 / IFO 15155 / JCM 9062;
DOI=10.1038/35035069; PubMed=11029001 [NCBI, ExPASy, EBI, Israel, Japan]
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum.";
Nature 407:508-513(2000).
Comments
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
AL445066; CAC12273.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_394605.1; -.
3D structure databases
ModBase Q9HJ26.
Enzyme and pathway databases
BioCyc TACI273075:TA1148-MON; -.
Ontologies
GO
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; FALSE_NEG.
PS00333; DNA_LIGASE_A2; 1.
PS50160; DNA_LIGASE_A3; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9HJ26.
Genome annotation databases
GeneID 1456651; -.
GenomeReviews AL139299_GR; Ta1148.
KEGG tac:Ta1148; -.
NMPDR fig|273075.1.peg.1127; -.
Phylogenomic databases
HOGENOM Q9HJ26; -.
Genome annotation databases
CMR Q9HJ26; Ta1148.
Other
ProtoNet Q9HJ26.
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
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   588  588     DNA ligase. PRO_0000059620
ACT_SITE   250   250        N6-AMP-lysine intermediate (By similarity). 
Sequence information
Length: 588 AA [This is the length of the unprocessed precursor] Molecular weight: 66538 Da [This is the MW of the unprocessed precursor] CRC64: FFD61667871BE291 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLFSVVADAF EKMESTTKRL ELTDLLVNLL KEADDDLPLL IYLLEGKLGP DYLGIETQMS 

        70         80         90        100        110        120 
DKLIIKALSV ASNISEDEIA KEYAKAGDIG TIAKEIAEKR SLRSLVQEEM TVKYIHDTLM 

       130        140        150        160        170        180 
KMARTTGSGS TKARVDAYMD LFLNSTPKEI MYITRIITGK LRIGISDATI LDAIVKAFAD 

       190        200        210        220        230        240 
EKYSEDIENA FNFHPDLGYI ASELRKGNID AILKLGPTPM IPFKVMLAER LRSVEEILEK 

       250        260        270        280        290        300 
MGGRCAFEYK YDGMRTETHI ERGKVRLFSR GNEETTNQFP DITKAASETF KVDSAILDGE 

       310        320        330        340        350        360 
AVPYDPDTGE LYPFQVISHR RGRKYDLDKV SSEIPITVFL FDIVYLNGRD LSKTPYTERR 

       370        380        390        400        410        420 
KILESIFTES DSFRLAKRIE SGDPAEVHRF FNSAIEDGCE GLVAKSTSPD SFYKAGARGW 

       430        440        450        460        470        480 
LWIKLKRDYQ AQLWDTLDLT VVGAFYGHGR RKGTYGALLL ATYNDKNDTF ETVCKLGSGF 

       490        500        510        520        530        540 
SDDVLFSLPK KFEQYVSKEK PARVISNLEP DVWFYPAVVM EVIGAEITVS PIHTCAYGEI 

       550        560        570        580 
EKDSGLSVRF PRFTGKWRED KKPEDSTTSR EILEMYKEQK KTITEEKS 

Q9HJ26 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 logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!