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Database: UniProt
Entry: A0A3Q1MFZ7_BOVIN
LinkDB: A0A3Q1MFZ7_BOVIN
Original site: A0A3Q1MFZ7_BOVIN 
ID   A0A3Q1MFZ7_BOVIN        Unreviewed;       856 AA.
AC   A0A3Q1MFZ7;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=LIG4 {ECO:0000313|Ensembl:ENSBTAP00000069467.1,
GN   ECO:0000313|VGNC:VGNC:30884};
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|Ensembl:ENSBTAP00000069467.1, ECO:0000313|Proteomes:UP000009136};
RN   [1] {ECO:0000313|Ensembl:ENSBTAP00000069467.1, ECO:0000313|Proteomes:UP000009136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069467.1,
RC   ECO:0000313|Proteomes:UP000009136};
RA   Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA   Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA   Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT   "ARS-UCD1.2.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSBTAP00000069467.1}
RP   IDENTIFICATION.
RC   STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000069467.1};
RG   Ensembl;
RL   Submitted (NOV-2023) 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|RuleBase:RU000617};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}.
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DR   AlphaFoldDB; A0A3Q1MFZ7; -.
DR   Ensembl; ENSBTAT00000079721.1; ENSBTAP00000069467.1; ENSBTAG00000015868.5.
DR   VEuPathDB; HostDB:ENSBTAG00000015868; -.
DR   VGNC; VGNC:30884; LIG4.
DR   GeneTree; ENSGT00860000133881; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000015868; Expressed in thymus and 103 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q1MFZ7; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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: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; cd07903; Adenylation_DNA_ligase_IV; 1.
DR   CDD; cd17722; BRCT_DNA_ligase_IV_rpt1; 1.
DR   CDD; cd07968; OBF_DNA_ligase_IV; 1.
DR   Gene3D; 6.10.250.520; -; 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   InterPro; IPR044125; Adenylation_DNA_ligase_IV.
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   NCBIfam; TIGR00574; dnl1; 1.
DR   PANTHER; PTHR45997; DNA LIGASE 4; 1.
DR   PANTHER; PTHR45997:SF1; DNA LIGASE 4; 1.
DR   Pfam; PF00533; BRCT; 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; PF11411; DNA_ligase_IV; 1.
DR   SMART; SM00292; BRCT; 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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|RuleBase:RU000617}; DNA repair {ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          355..489
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          654..743
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
SQ   SEQUENCE   856 AA;  97983 MW;  ECDE265DD13F9D69 CRC64;
     MAASQTSQTV ASHVPFADLC STLERIQKSK GRAEKIRHFK AFLDSWRKFH NALHKNQKDV
     TDSFYPAMRL ILPQLERERM AYGIKETMLA KLYIELLNLP RDGKDALKLL NYRTPTGTRG
     DAGDFAMIAY FVLKPRCLQK GSLSIQQVND ILDSIASNNS AKRKDLMKKS VLQLITQSSA
     LEQKWLIRMI VKDLKLGFSQ QTIFSIFHSD AAELHNVTTD LEKVCRQLHD PSVGLSDISI
     TLFSAFKPML AAIADIERIE KDMKHQSFYI ETKLDGERMQ MHKDGDVYRY FSRNGYNYVD
     QFGASPQEGS LTPFIHNAFK TEVLNCILDG EMMAYNPNTQ TFMQKGNKFD IKRMVEDSEL
     QTCYCVFDVL MVNDKKLGHE TLRKRYEILN SVFTPVPGRI EIVQKTQAHT KKEVIDALNE
     AIDKREEGIM VKHPLSIYKP DKRGEGWLKI KPEYVNGLMD ELDILIIGGY WGKGARGGMM
     SHFLCAVSEK PPSGEKPSVF HTLCRVGSGY TMKELYDLGL KLAKHWKPFH RKAPPSNILC
     GTEKPEVYIE PCNSVIVQVK ATEIVPSDMY KTGCTLRFPR IEKIREDKEW YECTSLEDLE
     QLRGKACGKL ASRHLYLGGD DEPQEKKRKA APKMKKVIGI IEHLKAPNLS NVNRVSTVFE
     DVEFCVMSGT SSHPKPDLEN RIAELGGYIV QNPGPDTYCV IAGSENIRVK NIISSDKHDV
     VKPEWLLECF RTRSCVPWQP RFMIHMCPST KQHFAQEYDQ YGDSYFVDTD LHQLKEVFLG
     IKNAGEQTPG EMSPVIADLE HRAFNIRKKI LMYTRKTLKR KKWIVYQEIQ MVKRHPVAQC
     QERKIFSSIV SISLFL
//
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