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Q9W1H4 (DNLI1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA ligase 1
EC=6.5.1.1
Alternative name(s):
DNA ligase I
Short name=DmDNA Lig I
Gene names
Name:DNA-ligI
ORF Names:CG5602
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair By similarity.

Catalytic activity

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).

Subcellular location

Nucleus. Note: Does not accumulate at the replication foci (RF). Ref.5

Sequence similarities

Belongs to the ATP-dependent DNA ligase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 747747DNA ligase 1
PRO_0000372657

Sites

Active site3951N6-AMP-lysine intermediate By similarity

Amino acid modifications

Modified residue181Phosphoserine Ref.7
Modified residue201Phosphoserine Ref.7
Modified residue421Phosphoserine Ref.7
Modified residue441Phosphoserine Ref.7
Modified residue461Phosphoserine Ref.7
Modified residue601Phosphoserine Ref.7
Modified residue651Phosphoserine Ref.6 Ref.7

Experimental info

Sequence conflict361 – 38727Missing in AAK93363. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9W1H4 [UniParc].

Last modified October 1, 2002. Version 2.
Checksum: 9203F51CFFE3EF1D

FASTA74784,719
        10         20         30         40         50         60 
MQKSITSFFK KKSDATDSPS PPKKVPKIDA KTELPDEPHI KSESASPETK PKVEPMSVDS 

        70         80         90        100        110        120 
EEKTSPVKNV KKEPKEVDDK TTDKKVTTIG LNSTAATKED VENYDPSADS YHPLKNAYWK 

       130        140        150        160        170        180 
DKKVTPYLAL ARTFQVIEET KGRLKMIDTL SNFFCSVMLV SPEDLVPSVY LSINQLAPAY 

       190        200        210        220        230        240 
EGLELGVAET TLMKAICKAT GRNLAHIKSQ TQLTGDLGIV AEQSRVSQRM MFQPAPLNVR 

       250        260        270        280        290        300 
DVFRKLREIA KLSGQSKMDL VYNMFVACRS SEARFFIRSL IGKLRIGIAE QSLLTALAIG 

       310        320        330        340        350        360 
LVKKNHIDDC KASKVPDVYK DEIVDTTLLL KTAYCQCPNY DIIIPAILKY DIKELQERCP 

       370        380        390        400        410        420 
MHPGMPLRPM LAQPTKGVHE VFERFGGMQI TCEWKYDGER AQIHRNEKGE ISIFSRNSEN 

       430        440        450        460        470        480 
NTAKYPDLIA RSTALLKGDV KSYIIDSEIV AWDVERKQIL PFQVLSTRKR KNVDIEEIKV 

       490        500        510        520        530        540 
QVCVYIFDLL YINGTALVTK NLSERRKLLL EHFQEVEGEW KFATALDTND IDEVQQFLEE 

       550        560        570        580        590        600 
SIKGNCEGLM VKTLDEEATY EIAKRSRNWL KLKKDYLSNV GDSLDLVVIG GYKGKGRRTG 

       610        620        630        640        650        660 
TYGGFLLACY DTENEEYQSI CKIGTGFTDE DLQTHSEFLG KHVTSAAKSY YRYDPSLEPD 

       670        680        690        700        710        720 
HWFEPVQVWE VKCADLSLSP IHRAAIGIVD GERGISLRFP RFIRIRDDKN SENATDANQV 

       730        740 
AHMYQSQDQV KNNQKSSTQM EMEDEFY

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[2]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[3]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Embryo.
[5]"Distribution of DNA replication proteins in Drosophila cells."
Easwaran H.P., Leonhardt H., Cardoso M.C.
BMC Cell Biol. 8:42-42(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[6]"An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, MASS SPECTROMETRY.
[7]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-20; SER-42; SER-44; SER-46; SER-60 AND SER-65, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013599 Genomic DNA. Translation: AAF47090.3.
AY051939 mRNA. Translation: AAK93363.1.
BT016103 mRNA. Translation: AAV36988.1.
RefSeqNP_611843.2. NM_137999.2.
UniGeneDm.19278.

3D structure databases

ProteinModelPortalQ9W1H4.
SMRQ9W1H4. Positions 100-727.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9W1H4. 1 interaction.
MINTMINT-920323.
STRING7227.FBpp0072041.

Proteomic databases

PaxDbQ9W1H4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0072132; FBpp0072041; FBgn0262619.
GeneID37791.
KEGGdme:Dmel_CG5602.
UCSCCG5602-RA. d. melanogaster.

Organism-specific databases

CTD37791.
FlyBaseFBgn0262619. DNA-ligI.

Phylogenomic databases

eggNOGCOG1793.
GeneTreeENSGT00700000104556.
InParanoidQ9W1H4.
KOK10747.
OMAAQVACLY.
OrthoDBEOG48W9H3.
PhylomeDBQ9W1H4.

Gene expression databases

BgeeQ9W1H4.

Family and domain databases

Gene3D1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProIPR000977. 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]
PfamPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF117018. SSF117018. 1 hit.
TIGRFAMsTIGR00574. dnl1. 1 hit.
PROSITEPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi37791.
NextBio805425.

Entry information

Entry nameDNLI1_DROME
AccessionPrimary (citable) accession number: Q9W1H4
Secondary accession number(s): Q960P4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 1, 2002
Last modified: May 29, 2013
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents