ID   Q2T9Y5_BOVIN            Unreviewed;       943 AA.
AC   Q2T9Y5;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LIG3 {ECO:0000313|EMBL:AAI11208.1};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI11208.1};
RN   [1] {ECO:0000313|EMBL:AAI11208.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Crossbred x Angus {ECO:0000313|EMBL:AAI11208.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:AAI11208.1};
RA   Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA   Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA   Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA   Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA   Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA   Holt R., Jones S.J., Marra M.A.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000617};
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; BC111207; AAI11208.1; -; mRNA.
DR   RefSeq; NP_001033196.1; NM_001038107.2.
DR   AlphaFoldDB; Q2T9Y5; -.
DR   iPTMnet; Q2T9Y5; -.
DR   GeneID; 514719; -.
DR   KEGG; bta:514719; -.
DR   CTD; 3980; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07902; Adenylation_DNA_ligase_III; 1.
DR   CDD; cd07967; OBF_DNA_ligase_III; 1.
DR   Gene3D; 3.30.1490.70; -; 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; 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; 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; PF00645; zf-PARP; 1.
DR   SMART; SM01336; zf-PARP; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding 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; 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   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          92..184
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          585..719
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          223..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..253
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..943
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   943 AA;  105101 MW;  05873FA748DA489F CRC64;
     MTLAFKILFP PTLRVLRKKE LCLFREHRRP DIRHFGRWSE TVFCGYHLLQ RRKPVPSFQE
     SNLKLRATCL VYLPGSHVGL CSGPCEMAEQ RFCVDYAKRG TAGCKKCKEK IVKGVCRIGK
     VVPNPFSESG GDMKEWYHIK CMFEKQERAP ATTKKIEDLT ELEGWEELEE NEKEQISQHI
     ADLSSKATST PKKKAVVQAK LTATGQVASP VKGASFVTNS NPRKFSGFSA KPNNSGEAHS
     SPTPKTPKTS MSSSKCDPKH KDCLLREFRK LCAMVAENPS YNTKTQIIQD FLQKGSAGDG
     FHGDVYLTVK LLLPGVIKSV YNLNDKQIVK LFSRIFNCNS DDMTRDLEQG DVSETIRVFF
     EQSKSFPPAA KSLLTIQEVD EFLLRLSKLT KEDEQQQALQ DIASRCTAND LKCIIRLIKH
     DLKMNSGAKH VLDALDPNAY EAFKASRNLQ DVVERVLRNE QEVEKEPGQR RALSVQASLM
     TPVQPMLAEA CKSIEYAMKK CPNGMFSEIK YDGERVQVHK KGDHFSYFSR SLKPVLPHKV
     AHFKDFIPRA FPGGHSMILD SEVLLVDNRT GKPLPFGTLG VHKKAAFQDA NVCQFVFDCI
     YFNDVSLMDR PLCERRKLLH DNMVEIPNRI MFSEMKQVTK ASDLVDMINR VIQEGLEGLV
     LKDVKGTYEP GKRHWLKVKK DYLNEGAMAD TADLVVLGAF YGQGSKGGMM SIFLMGCYDP
     SSQKWCTVTK CAGGHDDATL ARLQTELDMV KISKDPSKIP NWLKINKIYY PDFIVPDPKK
     AAVWEITGAE FSKSEAHTAD GISIRFPRCT RIRDDKDWKS ATTLPQLKEL YQLSKERAAF
     AITAGDEGSS ATGGSSGENE GTSGPAVPHK APRASPKQPP TSAKKAGGKP GGCTSRGGNL
     PAAEPSPVRA GVKRKAPDVT PCQAKRRPAS KRRGRRAVPT GRR
//