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Database: UniProt/SWISS-PROT
Entry: DNLI4_YARLI
LinkDB: DNLI4_YARLI
Original site: 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   16-JAN-2019, entry version 98.
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
OS   lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; 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.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   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-
CC       homologous integration (NHI) pathways where it is required in the
CC       final step of 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}.
DR   EMBL; CR382130; CAG81303.1; -; Genomic_DNA.
DR   RefSeq; XP_503109.1; XM_503109.1.
DR   ProteinModelPortal; Q6C8A3; -.
DR   SMR; Q6C8A3; -.
DR   STRING; 4952.XP_503109.1; -.
DR   EnsemblFungi; CAG81303; CAG81303; YALI0_D21384g.
DR   GeneID; 2911076; -.
DR   KEGG; yli:YALI0D21384g; -.
DR   HOGENOM; HOG000176213; -.
DR   InParanoid; Q6C8A3; -.
DR   KO; K10777; -.
DR   OMA; HMCPSTK; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0032807; C:DNA ligase IV complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IBA:GO_Central.
DR   CDD; cd00027; BRCT; 1.
DR   Gene3D; 1.10.3260.10; -; 1.
DR   Gene3D; 3.40.50.10190; -; 2.
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; PTHR10459:SF7; PTHR10459:SF7; 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; Complete proteome; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat.
FT   CHAIN         1    956       DNA ligase 4.
FT                                /FTId=PRO_0000278386.
FT   DOMAIN      700    793       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      857    956       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    309    309       N6-AMP-lysine intermediate.
FT                                {ECO:0000250}.
FT   METAL       371    371       Magnesium 1. {ECO:0000255}.
FT   METAL       476    476       Magnesium 2. {ECO:0000255}.
FT   BINDING     307    307       ATP. {ECO:0000250}.
FT   BINDING     314    314       ATP. {ECO:0000250}.
FT   BINDING     331    331       ATP. {ECO:0000250}.
FT   BINDING     481    481       ATP. {ECO:0000250}.
FT   BINDING     492    492       ATP. {ECO:0000250}.
FT   BINDING     498    498       ATP. {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
//
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