ID DNLI4_CRYD3 Reviewed; 1065 AA. AC P0CN09; Q55JS6; Q5K9S5; DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 1. DT 02-SEP-2026, entry version 64. DE RecName: Full=DNA ligase 4; DE EC=6.5.1.1 {ECO:0000250|UniProtKB:Q08387}; DE AltName: Full=DNA ligase IV; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4; GN Name=LIG4; OrderedLocusNames=CNBK2570; OS Cryptococcus deneoformans (strain B-3501A) (Cryptococcus neoformans var. OS neoformans serotype D). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=283643; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B-3501A; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J., RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus RT neoformans."; RL Science 307:1321-1324(2005). CC -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ); CC required for double-strand break (DSB) repair. CC {ECO:0000250|UniProtKB:Q08387}. 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:0000255|PROSITE- CC ProRule:PRU10135}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P49917}; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08387}. CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=EAL18239.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AAEY01000052; EAL18239.1; ALT_SEQ; Genomic_DNA. DR RefSeq; XP_772886.1; XM_767793.1. DR AlphaFoldDB; P0CN09; -. DR SMR; P0CN09; -. DR EnsemblFungi; AAW46139; AAW46139; CNK00930. DR GeneID; 4938955; -. DR KEGG; cnb:CNBK2570; -. DR HOGENOM; CLU_004844_1_0_1; -. DR OrthoDB; 5230at5206; -. DR GO; GO:0032807; C:DNA ligase IV complex; IEA:TreeGrafter. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; ISS:UniProtKB. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0097680; P:double-strand break repair via classical nonhomologous end joining; ISS:UniProtKB. DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:TreeGrafter. DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1. DR CDD; cd18435; BRCT_BRC1_like_rpt1; 1. DR CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1. DR FunFam; 1.10.3260.10:FF:000012; DNA ligase; 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; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. 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; PF16589; BRCT_2; 2. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SMART; SM00292; BRCT; 2. 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 3: Inferred from homology; KW ATP-binding; DNA damage; DNA recombination; DNA repair; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Nucleus; Repeat. FT CHAIN 1..1065 FT /note="DNA ligase 4" FT /id="PRO_0000410058" FT DOMAIN 696..775 FT /note="BRCT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 954..1064 FT /note="BRCT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 825..928 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 834..864 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 886..900 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 297 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135" FT BINDING 295 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 297 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 298 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 302 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 357 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 357 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000255" FT BINDING 387 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 452 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 452 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000255" FT BINDING 457 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 474 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" FT BINDING 476 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:P49917" SQ SEQUENCE 1065 AA; 122466 MW; 7E0AC640AB2D6236 CRC64; MAVHAPYNHA PPPTQEINGQ KPTLAPAITL ERPADCINRG QYPAFYIICG YLNRLRADAP HKKYELLTRI FGNWREKVGP DLYPLIRLLL PDKDRERPVY NLKESMLARC YIDILSLEKH SEAAQRLIKW KQPAGNSPNP TGDFAKVCYN EIKARSTVEE GQLSVEAVNM LLDKLAVGKM KQKDYVPILK AINMQCTAEE QEWIIRIILK DLHISIRERG VLSAFHPDAI DLYNVCSDLK RVCWTLYDPG FRLNKNETHL ELFHSFLPQL CGRMNDASLE NIAKAIGAPK EFIMEEKLDG ERIQLHMRGN GAQWFYCSRK AKDYTYLYGA HPGEGSLTRY IATAFQDNVR NVILDGEMMV WDPVVERYLA FGTLKSAALA FSLVKVFDIL FLNDHCLSRK RLSERKRLLR SGKIFKNIEN YKGRLEFVDE KRGKNAKDIR EYLERVVETK GEGLVVKKTD VIYQTNSRGY DWIKVKPEYS DQMGENLEVL VLGGWWGKGG RSGKISRLLC GLREQAFDDG TLQDFLFNRF WNELLGLRVD FVSHLMHLRS MRCSPTHLSQ CRNKHKKHWR PFDRSNPPPF MKLGPVGLDD KPDVYIEPEN SFVIEVKASE IVPAGYGIGF TLRFPRCKYI YYDKNSRDYA LDDECLWTVG QGFFYKTRKL IKRTDFMDLF SRPKRSYDDS QGPGNFRGQK LSDADVETSI FSDMTFSDLE ALVHKHGADF TQAQLSDLSA IVISPDQKNP LVRAQIRHGV NVIKPEWVFE SIARRTALPF LKEFLVFASE EAQDGRYYNK TLEQYDKVSF VRDRTGGALV DEDGDADVED EIMDGEDKDE IDVEESRESK NRRMAREDLK EKESNRTLEQ KKLQEAWGLR SRASPGDSDS EPEEEMSLKE ESDTDSERSR GLRAIYEDEE DGENDSHESD VGVNGDDYRA VPLSGLNDKE EGLMGESPEA MHYDEDRIFY HLAFYIDTAK NAAVNGLESS SPSFDTQERL VKVEKLLIEN GGRVARSISD PKLTHIIMDD EDSRRYVELT RKTAMPKRKH IVTPKWVEDC VDEETLLDED LYKPK //