ID A0A0A8J9A9_9CAUD Unreviewed; 672 AA.
AC A0A0A8J9A9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 08-NOV-2023, entry version 26.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
OS Ralstonia phage RSL2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Chiangmaivirus; Chiangmaivirus RSL2.
OX NCBI_TaxID=1585840 {ECO:0000313|EMBL:BAQ02623.2, ECO:0000313|Proteomes:UP000203794};
RN [1] {ECO:0000313|EMBL:BAQ02623.2, ECO:0000313|Proteomes:UP000203794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSL2 {ECO:0000313|EMBL:BAQ02623.2,
RC ECO:0000313|Proteomes:UP000203794};
RA Kawasaki T., Fujie M., Chatchawankanphanich O., Ogata H., Yamada T.;
RT "Genome analysis of a novel jumbo phage RSL2 infecting the phytopathogen
RT Ralstonia solanacearum.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC stranded DNA using NAD as a coenzyme and as the energy source for the
CC reaction. It is essential for DNA replication and repair of damaged
CC DNA. {ECO:0000256|ARBA:ARBA00004067}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00034005};
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DR EMBL; AP014693; BAQ02623.2; -; Genomic_DNA.
DR Proteomes; UP000203794; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; 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; cd17748; BRCT_DNA_ligase_like; 1.
DR CDD; cd00114; LIGANc; 1.
DR Gene3D; 6.20.10.30; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 1.10.287.610; Helix hairpin bin; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_01588; DNA_ligase_A; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR041663; DisA/LigA_HHH.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR NCBIfam; TIGR00575; dnlj; 1.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF9; DNA LIGASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR Pfam; PF12826; HHH_2; 1.
DR Pfam; PF14520; HHH_5; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00278; HhH1; 4.
DR SMART; SM00532; LIGANc; 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 SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000203794};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 594..672
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
SQ SEQUENCE 672 AA; 76264 MW; 574DDD70B9307E70 CRC64;
MILEYDRKYH DDDQPGITDH EYDALVRELQ ELEKKHPDHV DPESPTLRVG FKPNVKFEKV
DHKAPMLSLN NVFSEQEFRE WDSRLHLALK ANPTSRGKNF DRMIPFYICE LKFDGLSLDL
QYKRKGNKLM LDKAVTRGDG QTGEDVTHNI RHVKNVPLII TDAPGLDELE VRGEVVMPND
AFEKTNEELK AKGEKQYSNP RNAAAGALRT LDTDKAKGRG LEFMCYGYGH FEEKIVGWMP
DTHYGILELF GEWGFNTNPD YCWVANDANE AKDTYDKIKD LREKLPFGID GFVVKLNYRA
AQAIVGYVSR APRFAIAWKF PAEEAVTTLE AIEVQVGRTG AITPVGRLKP VFVGGVWVSN
ATLHNEDEIH RKGLRIGDKV IVRRAGDVVP EIVGPIEKER TGNETFFHMP VHCPDCGSAI
QKEDEEGKIY RCTGGLKCPA QKFGMFCHAV GRKALNIVGM GEKTIEELLE HRFIYELADL
FELNADHLHE LEGMGEKSIR KLLEAIEDAR DTTPQRFVYA LGIRHVGEET AKDLCRHTFN
MDLIRELTVD ELMRIEGIGE ETAKSIFTYF RENWDSIEKL LKHLRFPKKD DALTVPQTLK
GRNFSITGSF EGMSRDDIKA YIEARGGNLL PSISKKAEFL LLGKEPSGSK VEKAMKLGLK
FIDFVPSIIE NF
//
