ID DNLI4_NEUCR Reviewed; 1050 AA.
AC Q7SB49;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 2.
DT 27-MAR-2024, entry version 136.
DE RecName: Full=DNA ligase 4;
DE EC=6.5.1.1 {ECO:0000255|PROSITE-ProRule:PRU10135};
DE AltName: Full=DNA ligase IV;
DE AltName: Full=Mutagen-sensitive protein 53;
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN Name=mus-53; Synonyms=lig4; ORFNames=NCU06264;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=17003123; DOI=10.1073/pnas.0604477103;
RA Ishibashi K., Suzuki K., Ando Y., Takakura C., Inoue H.;
RT "Nonhomologous chromosomal integration of foreign DNA is completely
RT dependent on MUS-53 (human Lig4 homolog) in Neurospora.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14871-14876(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ);
CC required for double-strand break (DSB) repair.
CC {ECO:0000269|PubMed:17003123}.
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=BAF34364.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB261106; BAF34364.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002238; EAA33632.2; -; Genomic_DNA.
DR RefSeq; XP_962868.2; XM_957775.2.
DR AlphaFoldDB; Q7SB49; -.
DR SMR; Q7SB49; -.
DR STRING; 367110.Q7SB49; -.
DR PaxDb; 5141-EFNCRP00000006048; -.
DR EnsemblFungi; EAA33632; EAA33632; NCU06264.
DR GeneID; 3879007; -.
DR KEGG; ncr:NCU06264; -.
DR VEuPathDB; FungiDB:NCU06264; -.
DR HOGENOM; CLU_004844_1_1_1; -.
DR InParanoid; Q7SB49; -.
DR OrthoDB; 8251at2759; -.
DR Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR GO; GO:0000785; C:chromatin; IEA:EnsemblFungi.
DR GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003910; F:DNA ligase (ATP) activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0097680; P:double-strand break repair via classical nonhomologous end joining; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR CDD; cd07968; OBF_DNA_ligase_IV; 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; 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; 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 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; 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; Reference proteome; Repeat.
FT CHAIN 1..1050
FT /note="DNA ligase 4"
FT /id="PRO_0000278384"
FT DOMAIN 742..840
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 936..1049
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10135"
FT BINDING 329
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 332
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 398
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 398
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 498
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 520
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
FT BINDING 522
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P49917"
SQ SEQUENCE 1050 AA; 119433 MW; CDA8E04CF37AFA99 CRC64;
MNTNRRSRSP DEEALEEDQH QYGAGTLSLE ELDEHFPNRP RNHSKTFPFS DLFRTLFNPL
IDCKPSTSGG TVRGPKPGRG GHFSKVSYHE QRRHIIERFM SRWRSEVGND FYPAMRLILP
DKDRDRGVYG LKENTIGKLL VKVMKIDRNS EDGYNLMHWK LPGGQSGVSR SVGDFAGRCL
EVVSKRAMRA QPGDLTIADV NVLLDRLAAA SGEAEQLPIF EEFYRQMNAE EMMWLVRIIL
KDMRVGATER TFLNLWHPDA EALFSVSSSL RRVCWELFDP EFRLEQQETG IKLMQCFQPQ
LAQFQMTTTW EKLVKNLGVT EENPEFWIEE KLDGERMQMH MIEDDTVPGG FRFAFWSRKA
KDYTYLYGES LGDEQSALTR HLHKAFDDGV RNLILDGEMI TWDIDIDKMV PFGTLKTAAL
EQQKNPSKAG PRPLYRVFDI LLLNDKPLTE YTLNDRRRAL ERAVVGVHRR LEILPFERAT
SPDAIEPLLR RVVAEASEGL VLKNPRSRYS LNSRNNDWIK VKPEYMSDFG ESLDCVVVGG
YFGSGRRGGT LSSFLCGVRV SQNFIKSGNA SAEKCLSFVK VGGGFKAEDY AEIRHHTEGK
WQDWDPSSPP TEYIELGGGE KLQYEKPDVW IRPSDSVVIS VKAASITQSD QFAMGWTLRF
PRFRKLRLDR AWDSALDMDE FEVLRSKIKD QEQERKKMEM ENRKRKPATK RARKDLVIAG
MSDPSSSSAA TPVIAPKETR EASKRLFEGL DFCVLSDSLK PNKMTKPALE KLIKDHGGRI
HQQVMDHSGQ GKIIIPIADK NVIKVASLRK ANPEMDIIRP KWIFDCLVQP MPFTKQKENK
KGYLLPFEPT HLFHSGSEET SEEAEQAVDK FGDSYAGDLA DINELKAIME GMESDDYVSD
SDWDSDSGRG RGGGDGFDMN HFLDHLEEQG TSLDDLRSFM FRRCRVFFAL PSAGNGDGAA
ESKALRLKNY IRFGNGKVVD ELETATHVVV VTAPLGESSK KEEREIAAEL RYKISLREMG
SPMPRIVKGE WVEDSWKEGT VVDEEEYVAG
//
