ID   DNLI4_CHICK             Reviewed;         912 AA.
AC   Q90YB1; Q5ZKM3;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   16-JUN-2009, entry version 40.
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; ORFNames=RCJMB04_10b2;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21477437; PubMed=11593023; DOI=10.1073/pnas.201271098;
RA   Adachi N., Ishino T., Ishii Y., Takeda S., Koyama H.;
RT   "DNA ligase IV-deficient cells are more resistant to ionizing
RT   radiation in the absence of Ku70: implications for DNA double-strand
RT   break repair.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12109-12113(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005).
CC   -!- FUNCTION: Efficiently joins single-strand breaks in a double-
CC       stranded polydeoxynucleotide in an ATP-dependent reaction.
CC       Involved in DNA nonhomologous end joining (NHEJ) required for
CC       double-strand break repair and V(D)J recombination (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC   -!- SIMILARITY: Contains 2 BRCT domains.
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DR   EMBL; AB058600; BAB68506.1; -; Genomic_DNA.
DR   EMBL; AJ720061; CAG31720.1; -; mRNA.
DR   IPI; IPI00651271; -.
DR   RefSeq; NP_001025987.1; -.
DR   UniGene; Gga.1352; -.
DR   SMR; Q90YB1; 659-764.
DR   PRIDE; Q90YB1; -.
DR   Ensembl; ENSGALG00000016854; Gallus gallus.
DR   GeneID; 418764; -.
DR   KEGG; gga:418764; -.
DR   HOVERGEN; Q90YB1; -.
DR   BRENDA; 6.5.1.1; 4.
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:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR000977; DNA_ligase.
DR   InterPro; IPR012309; DNA_ligase_A_C.
DR   InterPro; IPR012310; DNA_ligase_A_M.
DR   InterPro; IPR012308; DNA_ligase_A_N.
DR   InterPro; IPR016059; DNA_ligase_CS.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Pfam; PF00533; BRCT; 2.
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   TIGRFAMs; TIGR00574; dnl1; 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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW   DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Repeat.
FT   CHAIN         1    912       DNA ligase 4.
FT                                /FTId=PRO_0000059579.
FT   DOMAIN      659    748       BRCT 1.
FT   DOMAIN      809    912       BRCT 2.
FT   ACT_SITE    278    278       N6-AMP-lysine intermediate (By
FT                                similarity).
FT   METAL       336    336       Magnesium 1 (Potential).
FT   METAL       432    432       Magnesium 2 (Potential).
FT   BINDING     276    276       ATP (By similarity).
FT   BINDING     283    283       ATP (By similarity).
FT   BINDING     298    298       ATP (By similarity).
FT   BINDING     437    437       ATP (By similarity).
FT   BINDING     448    448       ATP (By similarity).
FT   BINDING     454    454       ATP (By similarity).
FT   CONFLICT    492    492       V -> I (in Ref. 1; BAB68506).
SQ   SEQUENCE   912 AA;  104450 MW;  CBF2899CA76D212D CRC64;
     MASAPVLQPS PKRTVASHVP FADLCSTLER IQTCKSRPEK TKYFKDFLDS WRKFHSALHQ
     KEKDVTDSFY PAMRLILPQL ERERMAYGIK ETMLAKLYIE LLNLPKDGKD AVKLLNYRTP
     TGSRGDAGDF AMIAYFVLKP RSPKRGRLTV EQVNELLDAI ANNNAAKNKG LVKKSLLQLI
     TQSTALEQKW LIRMIIKDLK LGVSQQTIFS IFHPDAAELH NVTTDLEKVC RQLHDPSVSL
     SDVSIMLFSA FKPMLAAIAD VQQIEKQMNN QVFYIETKLD GERMQMHKDG DVYKYFSRNG
     FDYTQQFGAS PVDGSLTPFI HNVFKSDIQN CILDGEMMAY NPETQTFMQK GNKFDIKRMV
     EDSDLQTCFC VFDVLMINDQ KLAHESLSKR YKILSNVFTP LTGRIHVVHK KSARTRKEVI
     DALNEAIDNR EEGIMVKDPM STYKPDKRGE GWLKIKPEYV NGLMDELDLL IVGGYWGKGS
     RGGMMSHFLC AVAETPAPNE KPTVFHSICR VGSGYTMKEL YDLGLKLAKH WKPYNRKDPP
     CNILCGTEKP EMYIEPCNSV IVQIKAAEIV NSDMYKTDCT LRFPRIEKIR EDKEWYECMT
     LDMLEHLRSR AEGKLASKHL YIDEYDEPQE KKRRTVPKVK KVIGIAEQFK APDLSNVNKV
     SSMFEDVEFC VMTGMGRYSK SELESRIAEC GGSVVQNPGP DTYCVIVGAE NVRVKNIIAS
     NKYDVVKAEW LLQCFQSKML VPWQPAFMIH MSPETREHFA REYDCYGDSY TADTDVAQLK
     EVFSRVKDNK KMPLDLIAEL EERYSWNSCK LCIFRGNTIY VDYYAIINKP STKIHGTRLS
     IRALELRFYG AKVVPLLEEG VSHVVIGEDH SRVKEMKALR RMFGKKFKIV SELWVTESVK
     EGVPKNETQF LI
//