DNLI4_YARLI
ID DNLI4_YARLI Reviewed; 956 AA.
AC Q6C8A3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=YALI0D21384g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382130; CAG81303.1; -; Genomic_DNA.
DR RefSeq; XP_503109.1; XM_503109.1.
DR AlphaFoldDB; Q6C8A3; -.
DR SMR; Q6C8A3; -.
DR STRING; 4952.CAG81303; -.
DR PRIDE; Q6C8A3; -.
DR EnsemblFungi; CAG81303; CAG81303; YALI0_D21384g.
DR GeneID; 2911076; -.
DR KEGG; yli:YALI0D21384g; -.
DR VEuPathDB; FungiDB:YALI0_D21384g; -.
DR HOGENOM; CLU_004844_1_1_1; -.
DR InParanoid; Q6C8A3; -.
DR OMA; EGIMIKH; -.
DR Proteomes; UP000001300; Chromosome D.
DR GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
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; IBA:GO_Central.
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; 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 Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 2.
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; 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; PF04679; DNA_ligase_A_C; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF04675; DNA_ligase_A_N; 1.
DR SMART; SM00292; BRCT; 2.
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..956
FT /note="DNA ligase 4"
FT /id="PRO_0000278386"
FT DOMAIN 700..793
FT /note="BRCT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 857..956
FT /note="BRCT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 666..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 331
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 956 AA; 108061 MW; 5169CFB807F4183B CRC64;
MSSERRPELE ETAVDPATGS AASRKFSIVQ DAVETTIVAP TNHGPSPRFS TLVRNLFEPL
VNLSAVVAAL RKKPTEAKAH IASQFIKGWV EEVGKDIYPA FRLILPDKDR ERAVYGLKEK
ALGRLWVKVL NLAKDSPDAK ALSEWKQGGN ESAGNFSKRC YEVLSKRTSL TDYGHMTVDE
VNERLDLLAD GETDQAKQIE ILTYFYKHMN ATELKWLVNI ILRQMKMNAT EKVFFEPWHP
DAESLFNVTA SLKRVCWELT DPTKRLTSAE AQVSLFACFM PQIAAFPKYS GQDIAGKHFK
GRPFYIEEKI DGERMQMHMS EYGNKFHWWS RRSKDFTETY GNSLDDASGS LTKRLRGIIN
PKVRNCVLDG EMVAYDPATK KIIPFGTLRT ANRNEQNDLN LTKPMFMVFD ILLLNDKPLV
DYTLAERKRT LRTIFARTDN ETVGQEGVLE VLPYTEATTA AEIETCMRKI IAESSEGLVI
KDPTSVYRVN TRDDSWLKMK PEYMSEFGEK LDVVIIGGYY GSGKRGSILS SYLCGLRADG
SDQFWSFFKV GGGLTAGDYQ AIRTKTEGKW KRWDKNDKPK NVLLAGPNGD LERPDVWIEP
SDSVVVEVKA ASVVASDQYK VGLCLRFPRF RALRLDKTWE DGLTISQFAE LRQTVEMEAE
NKELELEDRK RRNAGPGRGA KRLKLANVSS DEDELGTDER PTSVFKATSF AVLSDMSSPR
YMSKAAVENL IKKHGGTVFQ TVEGPHTIPV ADTRTIKVQA LTKRVHGVDV IRPNWLLDCI
NEEKLVALEP RNLLESSAET LALAKTNVDE FGDSYTRPLT YKEMQEVLRF MDQFDLDQTN
PPDLMMEVLE TNDGAVPKGM LFYGKKVYMS TSNMDTVALE TQFRAYDALR CLQFGGANLV
TDMKDLVVAV AKTEEEAKEL RRVSSEQVFP FRVVSIKWVE ESWKNGTVEI EDDYPL
