ID Q28EB8_XENTR Unreviewed; 911 AA. AC Q28EB8; DT 04-APR-2006, integrated into UniProtKB/TrEMBL. DT 04-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 119. DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617}; DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617}; GN Name=lig4 {ECO:0000313|EMBL:CAJ82384.1, GN ECO:0000313|RefSeq:NP_001016981.1, GN ECO:0000313|Xenbase:XB-GENE-964443}; GN ORFNames=TNeu022j24.1-001 {ECO:0000313|EMBL:CAJ82384.1}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364 {ECO:0000313|EMBL:CAJ82384.1}; RN [1] {ECO:0000313|RefSeq:NP_001016981.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=12454917; DOI=10.1002/dvdy.10174; RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W., RA Richardson P.; RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus RT initiative."; RL Dev. Dyn. 225:384-391(2002). RN [2] {ECO:0000313|EMBL:CAJ82384.1} RP NUCLEOTIDE SEQUENCE. RA Amaya E., Ashurst J.L., Bonfield J.K., Croning M.D.R., Chen C-K., RA Davies R.M., Francis M.D., Garrett N., Gilchrist M.J., Grafham D.V., RA McLaren S.R., Papalopulu N., Rogers J., Smith J.C., Taylor R.G., Voigt J., RA Zorn A.M.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AAI35342.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Whole embryo {ECO:0000313|EMBL:AAI35342.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|RefSeq:NP_001016981.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (NOV-2023) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho- CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + CC diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003, CC ECO:0000256|RuleBase:RU000617}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC135341; AAI35342.1; -; mRNA. DR EMBL; CR848338; CAJ82384.1; -; mRNA. DR RefSeq; NP_001016981.1; NM_001016981.2. DR GeneID; 549735; -. DR KEGG; xtr:549735; -. DR AGR; Xenbase:XB-GENE-964443; -. DR CTD; 3981; -. DR Xenbase; XB-GENE-964443; lig4. DR OMA; EGIMIKH; -. DR OrthoDB; 8251at2759; -. DR Proteomes; UP000008143; Chromosome 2. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1. DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1. DR CDD; cd17717; BRCT_DNA_ligase_IV_rpt2; 1. DR CDD; cd07968; OBF_DNA_ligase_IV; 1. DR Gene3D; 6.10.250.520; -; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 2. DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR InterPro; IPR044125; Adenylation_DNA_ligase_IV. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR000977; DNA_ligase_ATP-dep. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR021536; DNA_ligase_IV_dom. DR InterPro; IPR036599; DNA_ligase_N_sf. DR InterPro; IPR029710; LIG4. DR InterPro; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR00574; dnl1; 1. DR PANTHER; PTHR45997; DNA LIGASE 4; 1. DR PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF16589; BRCT_2; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR Pfam; PF11411; DNA_ligase_IV; 1. DR SMART; SM00292; BRCT; 2. DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1. DR SUPFAM; SSF52113; BRCT domain; 2. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50172; BRCT; 2. DR PROSITE; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 2: Evidence at transcript level; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617}; KW DNA damage {ECO:0000256|RuleBase:RU000617}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, KW ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}. FT DOMAIN 360..494 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT DOMAIN 657..746 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT DOMAIN 808..911 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" SQ SEQUENCE 911 AA; 103871 MW; 227B0C2705291ACC CRC64; MSATKASDSA AERTVASQVP FADLCCTLEK VQKCKNRTEK SHIFKQFVDS WRKFHEALHK SQPKTTDSFY PAMRLVVPQL ERERMAYGIK ETMLAKLYIK VLGLPKEGKD AIKLLNYRSP TSSHSDAGDF AAIAYFVLKS RCRKEGSLSI QEVNYHLDSI ANNNAAKKKE LIEKSLLHLI ANTTALEQKW LIRMIIKDMK LGFSQQTVFS IFHPDAAELH NVTTDLEKVC IQLHDPNVCL SDVSISMFSA FKPMLAAIAN IQNIEKQMNH QSFYIETKLD GERMQMHKDG DVYKYFSRNG FDYTQQFGAS PLEGSLTPYI HNAFSLNIQN CILDGEMMAY NPNTQTFMQK GNKFDIKRMV DDSELQTCYC VFDVLLLNDQ KLAHETLRKR YDILQEIFIP IPGRFHIVDK TEASTKKNVV DALNEAIDKR EEGIMVKDPM SIYKPDKRGE GWLKIKPEYV NGLMDELDLI IIGGYWGKGS RGGMMSHFLC GVAEASGPGE KPSVFHSICR VGSGYTMKEL FDLGLKLAPH WKTYRKRDPP SNILCGIEKP EAYIQPCNSV IVQIKAAEIV TSDMYKTGCT LRFPRIEKIR EDKEWYDCMT LDDLEQFRDK ASGKLASKHL HIDDEPHEKK RKTAPKLKKV IGIVSHLKAP DLSNVYQESS VFAEVEFCVM SGTDTHSKDD LANIIAKCGG IGVQNPGADT YCVIAGTENV RVKNIICSNK HDVVKAAWLL ECFESKTFVP WQPHHMIHMC PSTAEHFACE YDCYGDSYIT DTSEYQLREV FHRMSNIREK IPFEMMADLE ERYSWNNSSH SFFRHCTVYV DSFATINDPT TRINTSSLNL RALELRFYGA KLVNQLEEGI SHVVVGEDLS RLEQMKTMRR AIAKKFKIVS VSWVLDSVKM RVPQMENSYL L //