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Q91FW5 (VF205_IIV6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length615 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + beta-nicotinamide D-ribonucleotide + (deoxyribonucleotide)(n+m).

Sequence similarities

Belongs to the NAD-dependent DNA ligase family.

Ontologies

Keywords
   Biological processDNA replication
   LigandNAD
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: InterPro

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA ligase (NAD+) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 615615Putative DNA ligase 205R
PRO_0000376962

Sites

Active site1011N6-AMP-lysine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q91FW5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A3B98D1C37B317A8

FASTA61570,152
        10         20         30         40         50         60 
MDETQQLLYK FKNLTISENE KLKLKEKADH FYFNTEKEIL TDNEYDILAE QLQSTNVGCS 

        70         80         90        100        110        120 
PLISKTDLPL WMGSLDKVYN DKELNLWIKK VASDKYIIQC KLDGVSCLII NKDNKLKAYT 

       130        140        150        160        170        180 
RGNGKVGTDI SHLIKYFIKD KCLPNNIALR CEIIIKKETF NQKYKHAFSN PRSFVSGVVN 

       190        200        210        220        230        240 
RKQENIVISE LNDLCLIAYE LINFPVNEYQ KNILTQIEII EQLNFIQFVN FKTISNEFLT 

       250        260        270        280        290        300 
QKALSNLFKE MKNNSLFEMD GLVILANTPY IRVTEGNPKH SIAFKVRGDN VKEAKVTFIE 

       310        320        330        340        350        360 
WNVGKTGVFT PKVHIVPTEI NGTTVSCFTG FNANYLIEKG IGEGAIILVT RAGDAIPQII 

       370        380        390        400        410        420 
GVKQTGVLTF PKDYEWKGDC RIVEKIESKE RIIKQILHFV ESVDIPYIKE ATINKLYNNG 

       430        440        450        460        470        480 
CTSIELFLKL TQKDLLLFGP KLSSTIYNSI QKSFEAPIEK FLSGYNAFGD YIGEKKILLL 

       490        500        510        520        530        540 
LQKYPNLFEL ENLDAIDLVS IEGIGSKTAT QIKQHFINAK LIYNNIIQNK LFKGVLHTPS 

       550        560        570        580        590        600 
KQNTVELFKV CVSGTRDPLF IQELKNRGFV LSDNITKKVK VLIVKNSNEE TTKVKKANSV 

       610 
GITILTLEDF KQKYF 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the first complete DNA sequence of an invertebrate iridovirus: coding strategy of the genome of Chilo iridescent virus."
Jakob N.J., Mueller K., Bahr U., Darai G.
Virology 286:182-196(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Comparative genomic analysis of the family Iridoviridae: re-annotating and defining the core set of iridovirus genes."
Eaton H.E., Metcalf J., Penny E., Tcherepanov V., Upton C., Brunetti C.R.
Virol. J. 4:11-11(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF303741 Genomic DNA. Translation: AAK82067.1.
RefSeqNP_149668.1. NC_003038.1.

3D structure databases

ProteinModelPortalQ91FW5.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1733308.

Phylogenomic databases

ProtClustDBCLSP2511666.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.40.50.10190. 1 hit.
InterProIPR001357. BRCT_dom.
IPR004150. DNA_ligase_OB.
IPR001679. DNAligase.
IPR013839. DNAligase_adenylation.
IPR013840. DNAligase_N.
IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR012340. NA-bd_OB-fold.
IPR010994. RuvA_2-like.
[Graphical view]
PfamPF01653. DNA_ligase_aden. 1 hit.
PF03120. DNA_ligase_OB. 1 hit.
[Graphical view]
PIRSFPIRSF001604. LigA. 1 hit.
SMARTSM00278. HhH1. 1 hit.
SM00532. LIGANc. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF50249. SSF50249. 1 hit.
ProtoNetSearch...

Entry information

Entry nameVF205_IIV6
AccessionPrimary (citable) accession number: Q91FW5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2009
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families