ID A0A093C775_TAUER Unreviewed; 924 AA.
AC A0A093C775;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
DE Flags: Fragment;
GN ORFNames=N340_04820 {ECO:0000313|EMBL:KFV08112.1};
OS Tauraco erythrolophus (Red-crested turaco).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV08112.1, ECO:0000313|Proteomes:UP000053661};
RN [1] {ECO:0000313|EMBL:KFV08112.1, ECO:0000313|Proteomes:UP000053661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV08112.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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 -!- 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 EMBL; KL454344; KFV08112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093C775; -.
DR Proteomes; UP000053661; Unassembled WGS sequence.
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: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; 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; 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 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 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:UP000053661};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..98
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 501..644
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 849..924
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 767..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 924
FT /evidence="ECO:0000313|EMBL:KFV08112.1"
SQ SEQUENCE 924 AA; 103781 MW; CF5EE682159415A7 CRC64;
MAEQRYCVDY AKRGTAGCKK CKEKIVKGMV RIGKIVPNPF TESGGDMKEW YHVKCMFEKL
EKARATTKKI EDITDLEGWE ELQDEEKELI NKHISEANSK AASTPKKKVI VQAKLTATGQ
ITTKDPLALI APSPKKFSGF TATYVFDAAK PKNSEDVSAN ASHKSSLSAA KCDPKHKDCL
LREFRKLCAM VAEKPSYNVK TQIIQDFLKK GSGGDGFHGD VYLTIKLLLP GVIKIVYNLN
DKQIVKLFSR IFNCSQEEMV RDLEQGDVSE TIRLFFEQSK SCPPAAKSLL TIQEVDEFLI
QLSKLTKEDD QQSVLHHITR RCTGNDLKCI IRLIKHDLKM NAGAKHVLDA LDPNAYEAFK
ASRNLQDVVE RVLKNQQEAE KMPGVKRTLS VQASLMTPVQ PMLAEACKSI EYAMKKCPNG
MYAEIKYDGE RVQVHKNGDH FSYFSRSLKP VLPHKVAHFK DFIPQAFPGG QSMILDSEVL
LIDNKTGKPL PFGTLGVHKK AAFQDANVCL FVFDCIYFND VSLMDRPLCE RRKFLHDNMV
EIPNRILFSE MKHVTKASDL ADMITRVIRE GLEGLVLKDT KASSQLLFTG GNYEPGKRHW
LKVKKDYLNE GAMADTADLV VLGAFYGQGS KGGMMSIFLM GCYDPKSEKW CTVTKCSGGH
DDATLARLQK ELDMVKISKD PSKIPKWLKI NKIYYPDFIV PDPKKAPVWE ITGAEFSKAE
AHTADGISIR FPRCTRIRDD KDWKTATNLQ QLKELYQLSK EKADFSVVAG EEDESTAGSS
GENEGNSRSS TPHSTIKTPP SKSPAKAQKP EDKFFFLESK AVIGSPQKSE EKRGEKRKAS
EMDDNGKKPL LDIFTGVKLY LSPSVKDFDK IRRYFIAYDG DLVPEFDTAS ATHVIGDIDE
NPGAKRVSPD WIWKCIRKRR LVAP
//
