Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9W1H4

- DNLI1_DROME

UniProt

Q9W1H4 - DNLI1_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA ligase 1

Gene

DNA-ligI

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m).PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei395 – 3951N6-AMP-lysine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: InterPro
  3. DNA ligase (ATP) activity Source: FlyBase

GO - Biological processi

  1. cell cycle Source: UniProtKB-KW
  2. cell division Source: UniProtKB-KW
  3. DNA biosynthetic process Source: InterPro
  4. DNA ligation involved in DNA repair Source: InterPro
  5. DNA recombination Source: UniProtKB-KW
  6. DNA replication Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, DNA replication

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_209581. Gap-filling DNA repair synthesis and ligation in GG-NER.
REACT_210849. Removal of DNA patch containing abasic residue.
REACT_213876. Resolution of D-loop structures through Holliday junction intermediates.
REACT_221569. Processive synthesis on the lagging strand.
REACT_224877. Gap-filling DNA repair synthesis and ligation in TC-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA ligase 1 (EC:6.5.1.1)
Alternative name(s):
DNA ligase I
Short name:
DmDNA Lig I
Gene namesi
Name:DNA-ligI
ORF Names:CG5602
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0262619. DNA-ligI.

Subcellular locationi

Nucleus 1 Publication
Note: Does not accumulate at the replication foci (RF).

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747DNA ligase 1PRO_0000372657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Phosphoserine1 Publication
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei44 – 441Phosphoserine1 Publication
Modified residuei46 – 461Phosphoserine1 Publication
Modified residuei60 – 601Phosphoserine1 Publication
Modified residuei65 – 651Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9W1H4.

Expressioni

Gene expression databases

BgeeiQ9W1H4.

Interactioni

Protein-protein interaction databases

BioGridi63384. 2 interactions.
IntActiQ9W1H4. 1 interaction.
MINTiMINT-920323.
STRINGi7227.FBpp0072041.

Structurei

3D structure databases

ProteinModelPortaliQ9W1H4.
SMRiQ9W1H4. Positions 100-727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATP-dependent DNA ligase family.Curated

Phylogenomic databases

eggNOGiCOG1793.
GeneTreeiENSGT00750000117745.
InParanoidiQ9W1H4.
KOiK10747.
OMAiMVKMLEG.
OrthoDBiEOG7RFTGN.
PhylomeDBiQ9W1H4.

Family and domain databases

Gene3Di1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProiIPR000977. 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]
PfamiPF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view]
SUPFAMiSSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00574. dnl1. 1 hit.
PROSITEiPS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9W1H4 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQKSITSFFK KKSDATDSPS PPKKVPKIDA KTELPDEPHI KSESASPETK
60 70 80 90 100
PKVEPMSVDS EEKTSPVKNV KKEPKEVDDK TTDKKVTTIG LNSTAATKED
110 120 130 140 150
VENYDPSADS YHPLKNAYWK DKKVTPYLAL ARTFQVIEET KGRLKMIDTL
160 170 180 190 200
SNFFCSVMLV SPEDLVPSVY LSINQLAPAY EGLELGVAET TLMKAICKAT
210 220 230 240 250
GRNLAHIKSQ TQLTGDLGIV AEQSRVSQRM MFQPAPLNVR DVFRKLREIA
260 270 280 290 300
KLSGQSKMDL VYNMFVACRS SEARFFIRSL IGKLRIGIAE QSLLTALAIG
310 320 330 340 350
LVKKNHIDDC KASKVPDVYK DEIVDTTLLL KTAYCQCPNY DIIIPAILKY
360 370 380 390 400
DIKELQERCP MHPGMPLRPM LAQPTKGVHE VFERFGGMQI TCEWKYDGER
410 420 430 440 450
AQIHRNEKGE ISIFSRNSEN NTAKYPDLIA RSTALLKGDV KSYIIDSEIV
460 470 480 490 500
AWDVERKQIL PFQVLSTRKR KNVDIEEIKV QVCVYIFDLL YINGTALVTK
510 520 530 540 550
NLSERRKLLL EHFQEVEGEW KFATALDTND IDEVQQFLEE SIKGNCEGLM
560 570 580 590 600
VKTLDEEATY EIAKRSRNWL KLKKDYLSNV GDSLDLVVIG GYKGKGRRTG
610 620 630 640 650
TYGGFLLACY DTENEEYQSI CKIGTGFTDE DLQTHSEFLG KHVTSAAKSY
660 670 680 690 700
YRYDPSLEPD HWFEPVQVWE VKCADLSLSP IHRAAIGIVD GERGISLRFP
710 720 730 740
RFIRIRDDKN SENATDANQV AHMYQSQDQV KNNQKSSTQM EMEDEFY
Length:747
Mass (Da):84,719
Last modified:October 1, 2002 - v2
Checksum:i9203F51CFFE3EF1D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti361 – 38727Missing in AAK93363. (PubMed:12537569)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF47090.3.
AY051939 mRNA. Translation: AAK93363.1.
BT016103 mRNA. Translation: AAV36988.1.
RefSeqiNP_611843.2. NM_137999.3.
UniGeneiDm.19278.

Genome annotation databases

EnsemblMetazoaiFBtr0072132; FBpp0072041; FBgn0262619.
GeneIDi37791.
KEGGidme:Dmel_CG5602.
UCSCiCG5602-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE013599 Genomic DNA. Translation: AAF47090.3 .
AY051939 mRNA. Translation: AAK93363.1 .
BT016103 mRNA. Translation: AAV36988.1 .
RefSeqi NP_611843.2. NM_137999.3.
UniGenei Dm.19278.

3D structure databases

ProteinModelPortali Q9W1H4.
SMRi Q9W1H4. Positions 100-727.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 63384. 2 interactions.
IntActi Q9W1H4. 1 interaction.
MINTi MINT-920323.
STRINGi 7227.FBpp0072041.

Proteomic databases

PaxDbi Q9W1H4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0072132 ; FBpp0072041 ; FBgn0262619 .
GeneIDi 37791.
KEGGi dme:Dmel_CG5602.
UCSCi CG5602-RA. d. melanogaster.

Organism-specific databases

CTDi 37791.
FlyBasei FBgn0262619. DNA-ligI.

Phylogenomic databases

eggNOGi COG1793.
GeneTreei ENSGT00750000117745.
InParanoidi Q9W1H4.
KOi K10747.
OMAi MVKMLEG.
OrthoDBi EOG7RFTGN.
PhylomeDBi Q9W1H4.

Enzyme and pathway databases

Reactomei REACT_209581. Gap-filling DNA repair synthesis and ligation in GG-NER.
REACT_210849. Removal of DNA patch containing abasic residue.
REACT_213876. Resolution of D-loop structures through Holliday junction intermediates.
REACT_221569. Processive synthesis on the lagging strand.
REACT_224877. Gap-filling DNA repair synthesis and ligation in TC-NER.

Miscellaneous databases

GenomeRNAii 37791.
NextBioi 805425.
PROi Q9W1H4.

Gene expression databases

Bgeei Q9W1H4.

Family and domain databases

Gene3Di 1.10.3260.10. 1 hit.
2.40.50.140. 1 hit.
InterProi 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 ]
Pfami PF04679. DNA_ligase_A_C. 1 hit.
PF01068. DNA_ligase_A_M. 1 hit.
PF04675. DNA_ligase_A_N. 1 hit.
[Graphical view ]
SUPFAMi SSF117018. SSF117018. 1 hit.
SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR00574. dnl1. 1 hit.
PROSITEi PS00697. DNA_LIGASE_A1. 1 hit.
PS00333. DNA_LIGASE_A2. 1 hit.
PS50160. DNA_LIGASE_A3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiDNLI1_DROME
AccessioniPrimary (citable) accession number: Q9W1H4
Secondary accession number(s): Q960P4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3