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Database: UniProt
Entry: U3IN79_ANAPP
LinkDB: U3IN79_ANAPP
Original site: U3IN79_ANAPP 
ID   U3IN79_ANAPP            Unreviewed;       980 AA.
AC   U3IN79;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 2.
DT   24-JAN-2024, entry version 54.
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:ENSAPLP00000008702.2};
OS   Anas platyrhynchos platyrhynchos (Northern mallard).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC   Anatinae; Anas.
OX   NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000008702.2, ECO:0000313|Proteomes:UP000016666};
RN   [1] {ECO:0000313|Ensembl:ENSAPLP00000008702.2, ECO:0000313|Proteomes:UP000016666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT   "A new Pekin duck reference genome.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPLP00000008702.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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; U3IN79; -.
DR   STRING; 8840.ENSAPLP00000008702; -.
DR   Ensembl; ENSAPLT00000009386.2; ENSAPLP00000008702.2; ENSAPLG00000008964.2.
DR   GeneTree; ENSGT00940000156492; -.
DR   HOGENOM; CLU_011787_0_0_1; -.
DR   OMA; TQRVYNL; -.
DR   Proteomes; UP000016666; Chromosome 20.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0006288; P:base-excision repair, DNA ligation; IEA:Ensembl.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; IEA:Ensembl.
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   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; 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; PS50064; ZF_PARP_2; 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   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU000617};
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   Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          83..175
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          571..705
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   DOMAIN          904..980
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          175..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        840..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..898
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   980 AA;  108549 MW;  8EA59A8747F02351 CRC64;
     MPVGGRALAQ AARLLARGAA LGVCRPPLSS AGSPRGWLAA SAASGGLPGA ERGGGARGGI
     PEVTAGPAGG WPAPGGGMAE QRYCVDYAKR GTAGCKKCKE KLVKGTVRIG KIVPNPFTES
     GGEMKEWYHV RCMFEKLEKA RATTKKIEDI TDLEGWEELQ DEEKELIQKH IAEATSKAAS
     TPKKKATVQA KLTPTGQITS PSKDPLAAVN PKKFSGFTAK PKNSEDVPAN SSHKSSLSAK
     KSDPKHKDCL LREFRKLCAM VADKPSYNVK TQIIQDFLQK GTGGDGFHGD VYLTIKLLLP
     GVIKIVYNLN DKQIVKLFSR IFNCSQEEMI RDLEQGDVSE TIRLFFEQSK SCPPAAKSLL
     TIQEVDEFLI QLSKLTKEDD QQSVLHNITR RCTGNDLKCI IRLIKHDLKM NAGAKHVLDA
     LDPNAYEAFK ASRNLQDVVE RVLKNQQEAE KMPGLKRTLS VQASLMTPVQ PMLAEACKSI
     EYAMKKCPNG MYAEIKYDGE RVQVHKNGDH FSYFSRSLKP VLPHKVAHFK DFIPQAFPGG
     HSMILDSEVL LIDNKTGKPL PFGTLGVHKK AAFQDANVCL FVFDCIYFND ISLMDRPLRE
     RRKFLHDNMV EIPNRILFSE MKHVTKASDL ADMITRVIRE GLEGLVLKDI KGNYEPGKRH
     WLKVKKDYLN EGAMADTADL VVLGAFYGQG SKGGMMSIFL MGCYDPKSEK WCTVTKCAGG
     HDDATLARLQ TELDMVKISK DPSKIPSWLK INKIYYPDFI VPDPKKAPVW EITGAEFSKA
     EAHTADGISI RFPRCTRIRD DKDWKTATNL PQLKELYQLS KEKADFSVVA GEEEESTAGS
     SGENEGNSRS STPHKTTKTP PSKSPAKAKK PEGTKAITES PQKPEEKRGE KRKASEMDDN
     GKKTLLDIFT GVKLYLSPSV KDFNKIRRYF IAYDGDLVPE FDTASATHVI GDIDENPGAK
     RVSPKWIWEC IRKRRLVAPC
//
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