ID   H2QCP0_PANTR            Unreviewed;      1009 AA.
AC   H2QCP0; K7BBB7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   04-NOV-2026, entry version 86.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LIG3 {ECO:0000313|Ensembl:ENSPTRP00000015364.5,
GN   ECO:0000313|VGNC:VGNC:9437};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000015364.5, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000015364.5, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000015364.5}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2026) to UniProtKB.
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:0000256|ARBA:ARBA00034003,
CC         ECO:0000256|PROSITE-ProRule:PRU10135, ECO:0000256|RuleBase:RU000617};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Isoform 3 interacts (via BRCT domain) with the nuclear DNA-
CC       repair protein XRCC1. Interacts with POLG. Interacts with POLB.
CC       {ECO:0000256|ARBA:ARBA00065554}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PROSITE-ProRule:PRU00264}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; AACZ04043904; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AACZ04043905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_009430685.4; XM_009432410.5.
DR   RefSeq; XP_511409.6; XM_511409.8.
DR   AlphaFoldDB; H2QCP0; -.
DR   Ensembl; ENSPTRT00000016599.5; ENSPTRP00000015364.5; ENSPTRG00000009008.6.
DR   GeneID; 454581; -.
DR   CTD; 3980; -.
DR   VGNC; VGNC:9437; LIG3.
DR   eggNOG; KOG4437; Eukaryota.
DR   GeneTree; ENSGT00940000156492; -.
DR   Proteomes; UP000002277; Chromosome 17.
DR   Bgee; ENSPTRG00000009008; Expressed in testis and 20 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:Ensembl.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IEA:UniProtKB-ARBA.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   GO; GO:0043504; P:mitochondrial DNA repair; IEA:Ensembl.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:UniProtKB-ARBA.
DR   GO; GO:0090298; P:negative regulation of mitochondrial DNA replication; IEA:Ensembl.
DR   CDD; cd07902; Adenylation_DNA_ligase_III; 1.
DR   CDD; cd18431; BRCT_DNA_ligase_III; 1.
DR   CDD; cd07967; OBF_DNA_ligase_III; 1.
DR   FunFam; 1.10.3260.10:FF:000002; DNA ligase; 1.
DR   FunFam; 2.40.50.140:FF:000085; DNA ligase; 1.
DR   FunFam; 3.30.1740.10:FF:000001; DNA ligase; 1.
DR   FunFam; 3.30.470.30:FF:000003; DNA ligase; 1.
DR   FunFam; 3.40.50.10190:FF:000032; DNA ligase; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 1.
DR   InterPro; IPR050191; ATP-dep_DNA_ligase.
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; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR031916; LIG3_BRCT.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001510; Znf_PARP.
DR   InterPro; IPR036957; Znf_PARP_sf.
DR   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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   Pfam; PF16759; LIG3_BRCT; 1.
DR   Pfam; PF00645; zf-PARP; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM01336; zf-PARP; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR   PROSITE; PS00347; ZF_PARP_1; 1.
DR   PROSITE; PS50064; ZF_PARP_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00264};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00264}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00264}.
FT   DOMAIN          93..185
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          583..717
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          933..1009
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          226..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..253
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..854
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..877
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..899
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        508
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10135"
SQ   SEQUENCE   1009 AA;  112940 MW;  F05FEA94143A30EE CRC64;
     MSLAFKILFP QTLRALSRKE LCLFRKRHWR DVRQFSQWSE TDLLHGHPLF LRRKPILSFQ
     GSHLRSRATY LVFLPGLHVG LCSGPCEMAE QRFCVDYAKR GTAGCKKCKE KIVKGVCRIG
     KVVPNPFSES GGDMKEWYHI KCMFEKLERA RATTKKIEDL TELEGWEELE DNEKEQITQH
     IADLSSKAAG TPKKKAVVQA KLTTTGQVTS PVKGASFVTS TNPRKFSGFS AKPNNSGEAS
     SSPTPKRSLS SSKCDPRHKD CLLREFRKLC AMVADNPSYN TKTQIIQDFL RKGSAGDGFH
     GDVYLTVKLL LPGVIKTVYN LNDKQIVKLF SRIFNCNPDD MARDLEQGDV SETIRVFFEQ
     SKSFPPAAKS LLTIQEVDEF LLRLSKLTKE DEQQQALQDI ASRCTANDLK CIIRLIKHDL
     KMNSGAKHVL DALDPNAYEA FKASRNLQDV VERVLHNAQE VEKEPGQRRA LSVQASLMTP
     VQPMLAEACK SVEYAMKKCP NGMFSEIKYD GERVQVHKNG DHFSYFSRSL KPVLPHKVAH
     FKDYIPQAFP GGHSMILDSE VLLIDNKTGK PLPFGTLGVH KKAAFQDANV CLFVFDCIYF
     NDVSLMDRPL CERRKFLHDN MVEIPNRIMF SEMKRVTKAL DLADMITRVI QEGLEGLVLK
     DVKGTYEPGK RHWLKVKKDY LNEGAMADTA DLVVLGAFYG QGSKGGMMSI FLMGCYDPGS
     QKWCTVTKCA GGHDDATLAR LQKELDMVKI SKDPSKIPSW LKVNKIYYPD FIVPDPKKAA
     VWEITGAEFS KSEAHTADGI SIRFPRCTRI RDDKDWKSAT NLPQLKELYQ LSKEKADFTV
     VAGDEGSSTT GGSSEENKGP SGSAVSRKAP SKPSASTKKA EGKLSNSNSK DGNMQTAKPS
     TMKVGEKLAT KSSPVKVGEK RKAADETLCQ TKVLLDIFTG VRLYLPPSTP DFSRLRRYFV
     AFDGDLVQEF DMTSATHVLG SRDKNPAAQQ VSPEWIWACI RKRRLVAPC
//