ID   DNLI4_KLULA             Reviewed;         907 AA.
AC   Q6CSH0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=DNA ligase 4;
DE            EC=6.5.1.1;
DE   AltName: Full=DNA ligase IV;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=LIG4; OrderedLocusNames=KLLA0D01089g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in ds DNA break repair. Has a role in non-homologous
CC       integration (NHI) pathways where it is required in the final step of
CC       non-homologous end-joining. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
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DR   EMBL; CR382124; CAH00215.1; -; Genomic_DNA.
DR   RefSeq; XP_453119.1; XM_453119.1.
DR   AlphaFoldDB; Q6CSH0; -.
DR   SMR; Q6CSH0; -.
DR   STRING; 28985.XP_453119.1; -.
DR   EnsemblFungi; CAH00215; CAH00215; KLLA0_D01089g.
DR   GeneID; 2892937; -.
DR   KEGG; kla:KLLA0_D01089g; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   HOGENOM; CLU_004844_1_1_1; -.
DR   InParanoid; Q6CSH0; -.
DR   OMA; FYPVLRI; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0032807; C:DNA ligase IV complex; IEA:EnsemblFungi.
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: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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   CDD; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.40.50.10190; -; 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; 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   PANTHER; PTHR45997; PTHR45997; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA replication;
KW   Ligase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..907
FT                   /note="DNA ligase 4"
FT                   /id="PRO_0000278383"
FT   DOMAIN          655..754
FT                   /note="BRCT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   DOMAIN          800..906
FT                   /note="BRCT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   ACT_SITE        275
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255"
FT   BINDING         443
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         454
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   907 AA;  104634 MW;  1CE0987C0B4ADFDE CRC64;
     MNDCENFSPS PEFKWLCDEL LGKIYETSSK KHLIGKPVTV RYLEIITNFI KLWRSTVGNY
     IYPALRLIVP FRDRRIYNVK ENTLIKALCR YLRLPKSSET ENRLLRWKQR AARGVKLSDF
     CVEEIRKRQK DYEGANRITI DELNGYLDEV SQEGNGKRMG YMALTDSRAF NYCLNHMTFM
     EMKFFFDIIL KTRVLSGLEN MFLTAWHPDA TDYLSVVSDL DVLSQRLYNP NERLRQTDLS
     ITISHAFEPQ LAKRTHLSYE RVASKLQHDF IIEEKMDGER LQIHYINYGE QIKYLSRRGV
     DFSYLYGENS SSGPISPSLK LHFNVKDCIL DGEMITYDTE KDIVLPFGLV KSSAMNQIQS
     ELAGIAPTES YKPLFVAFDL VYLNGKSLTN LALERRKDYL TKILTPVERS VEIIQYMKAI
     NAEAIKDSLE QAISMGSEGI VLKHLHSKYF VGSRNTDWIK IKPEYLEQFG ENMDLLIIGR
     EQGKKDSFFC GLSISDPNEV AEKPRFISFC TIANGLSNEE FKDIERKTWG KWHIFSEDPP
     SPNLLGFGTK VPYEWIHPED SVVLEVKARA IDTKESEKRK YRSGCTLHFG YCKQIRYDKD
     WKTVASFSEF EDMKDARNFY NKRKSHQVTD GKKRASKRAK IGIVNSSEPT ALVAPVSNTF
     SNCRFRVISD YFDSTKRRRI SQEDLCSVIL EHGGEIVYTS DENNLPQDNL YIIGEKLTRE
     CKILLNAKNL IIRPSWIFSC IEEGYKTPFT ESDIFRGELE SSMDCSQFYT DFNTASLNHL
     LETANRGIKN PDSDLLLPEV PLFLFSNLKL AVLNSENVLD TSILEVEFAI KCHGGELVHI
     ENASIIIVFN DFISREDLFS LRQKIASKAV KESTESTPRI PRMVDISWAL DSIKDNYIAE
     TEHYQCL