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Database: UniProt/SWISS-PROT
Entry: DNLI4_PONAB
LinkDB: DNLI4_PONAB
Original site: DNLI4_PONAB 
ID   DNLI4_PONAB             Reviewed;         911 AA.
AC   Q5R6L3;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 70.
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=Polydeoxyribonucleotide synthase [ATP] 4;
GN   Name=DNL4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. The LIG4-XRCC4
CC       complex is responsible for the NHEJ ligation step, and XRCC4
CC       enhances the joining activity of LIG4. Binding of the LIG4-XRCC4
CC       complex to DNA ends is dependent on the assembly of the DNA-
CC       dependent protein kinase complex DNA-PK to these DNA ends.
CC       {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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10135};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Binds to XRCC4. The LIG4-XRCC4 complex has probably a 1:2
CC       stoichiometry. The LIG4-XRCC4 heteromer associates in a DNA-
CC       dependent manner with the DNA-dependent protein kinase complex
CC       DNA-PK, formed by the Ku p70/p86 dimer (G22P1/G22P2) and PRKDC.
CC       Interacts with APLF (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000305}.
DR   EMBL; CR860475; CAH92597.1; -; mRNA.
DR   RefSeq; NP_001126522.1; NM_001133050.1.
DR   ProteinModelPortal; Q5R6L3; -.
DR   SMR; Q5R6L3; -.
DR   STRING; 9601.ENSPPYP00000006314; -.
DR   PRIDE; Q5R6L3; -.
DR   GeneID; 100173511; -.
DR   KEGG; pon:100173511; -.
DR   CTD; 3981; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   HOVERGEN; HBG005516; -.
DR   InParanoid; Q5R6L3; -.
DR   KO; K10777; -.
DR   OrthoDB; 274264at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; 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   CDD; cd00027; BRCT; 2.
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; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR021536; DNA_ligase_IV_dom.
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; 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   Pfam; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF117018; SSF117018; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF52113; SSF52113; 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; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW   Repeat.
FT   CHAIN         1    911       DNA ligase 4.
FT                                /FTId=PRO_0000059578.
FT   DOMAIN      654    743       BRCT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   DOMAIN      808    911       BRCT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00033}.
FT   ACT_SITE    273    273       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|PROSITE-ProRule:PRU10135}.
FT   METAL       331    331       Magnesium 1. {ECO:0000255}.
FT   METAL       427    427       Magnesium 2. {ECO:0000255}.
FT   BINDING     271    271       ATP. {ECO:0000250}.
FT   BINDING     278    278       ATP. {ECO:0000250}.
FT   BINDING     293    293       ATP. {ECO:0000250}.
FT   BINDING     432    432       ATP. {ECO:0000250}.
FT   BINDING     443    443       ATP. {ECO:0000250}.
FT   BINDING     449    449       ATP. {ECO:0000250}.
SQ   SEQUENCE   911 AA;  104053 MW;  C6AD9817E9EC2B59 CRC64;
     MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFR EFLDSWRKFH DAFHKNQKDV
     TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP RDGKDALKLL NYRTPTGTHG
     DAGDFAMIAY FVLKPRCLQK GSLTIQQVND LLDSIASNNS AKRKDLIKKS LLQLITQSSA
     LEQKWLIRMI IKDLKLGVSQ QTIFSVFHSD AVELHNVTTD LEKVCRQLHD PSVGLSDISI
     TLFSAFKPML AAIADIEHIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYKY FSRNGYNYTD
     QFGASPTEGS LTPFIHNAFK TDIQICILDG EMMAYNPNTQ TFMQKGTKFD IKRMVEDSDL
     QTCYCVFDVL MVNNKKLGHE TLRKRYEILS SIFTPIPGRI EIVQKTQAHT KNEVIDALNE
     AIDKREEGIM IKQPLSIYKP DKRGEGWLKI KPEYVSGLMD ELDILIVGGY WGKGSRGGMM
     SHFLCAVAEK PPPGEKPSVF HTLSRVGSGC TMKELYDLGL KLAKYWKPFH KKAPPSSILC
     GTEKPEVYIE PCNSVIVQIK AAEIVPSDMY KTGCTLRFPR IEKIRDDKEW HECMTLDDLE
     QLRGKASGKL ASKHFYVGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLT NVNKISNIFE
     DVEFCVMSGT DSQPKPDLEN RIAEFGGYIV QNPGPDTYCV IAGSKNIRVK NIILSNKHDV
     VKPAWLLECF KTKSFVPWQP HFMIHMCPST KEHFAREYDC YGDSYFVDTD LNQLKEVFSG
     IKNSNEQTPE EMASLIADLE YRYSWDCSPL SMFRRHTVYL DLYAVINDLS TKNEGTRLAI
     KALELRFHGA KVVSCLAEGV SHVIIGEDHS RIADFKAFRR TFKRKFKILK ESWITDSIDK
     CELQEENQYL I
//
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