ID A0A093IJQ4_EURHL Unreviewed; 950 AA.
AC A0A093IJQ4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN ORFNames=N326_00910 {ECO:0000313|EMBL:KFW01878.1};
OS Eurypyga helias (Sunbittern) (Ardea helias).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Eurypygiformes;
OC Eurypygidae; Eurypyga.
OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW01878.1, ECO:0000313|Proteomes:UP000054232};
RN [1] {ECO:0000313|EMBL:KFW01878.1, ECO:0000313|Proteomes:UP000054232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW01878.1};
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; KK561875; KFW01878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093IJQ4; -.
DR Proteomes; UP000054232; 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; 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 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:UP000054232};
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 520..654
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT DOMAIN 874..950
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 778..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 849..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 950 AA; 106236 MW; CEF99BD69CB32092 CRC64;
MAEQRYCVDY AKRGTAGCKK CKEKIVKGMV RIGKIVPNPF TESGGDMKEW YHVKCMFEKL
EKARATTKKI EDITDLEGWE ELQDGDKELI NKHISEANSK AASTPKKKVI VQAKLTATGQ
ITTKDPLALI TPSPKKFSGF TEVASTCTIL YLLKKQLLIF DAAKPKNSED VSANSSHKSS
LSAKNCDPKH KDCLLREFRK LCAMVAEKPS YNVKTQIIQD FLKKGSGGDG FHGDVYLTIK
LLLPGVIKIV YNLNDKQIVK LFSRIFNCSQ EEMVRDLEQG DVSETIRLFF EQSKSCPPAA
KSALTIQEVD EFLIQLSKLT KEDDQQMKCL PYLNLLLHLR CTGNDLKCII RLIKHDLKMN
AGAKHVLDAL DPNAYEAFKA SRNLQDVVER VLQNQQEAAK MPGMKRTLSV QASLMTPVQP
MLAEACKSVE YAMKKCPNGM YAEIKYDGER VQVHKNGDHF SYFSRSLKPV LPHKVAHFKD
FIPKAFPGGQ SMILDSEVLL IDNKTGKPLP FGTLGVHKKA AFQDANVCLF VFDCIYFNDI
SLMDRPLCER RKFLHDNMVE IPNRILFSEM KHVTKASDLA DMITRVIREG LEGLVLKDIK
GNYEPGKRHW LKVKKDYLNE GAMADTADLV VLGAFYGQGS KGGMMSIFLM GCYDPKSEKW
CTVTKCSGGH DDATLARLQT ELDMVKISKD PSKIPKWLKI NKIYYPDFIV PDPKKAPVWE
ITGAEFSKAE AHTADGISIR FPRCTRIRDD KDWKTATNLQ QLKELYQLSK EKADFNVVAG
EEDESTAGSS GENEGNSRSS TPHSAAKSPP SKSPAKAQKP EGKTVLLGGE RSLGACSSCK
AEESKAVAAS PQKSEEKRGE KRKASEMDDN GKKPLLDIFT GVRLYLSPAV KDFDKLRRYF
IAYDGDLVPE FDAASATHVI GDVDENPGAK RVSPNWIWEC IRKRRLVAPC
//
