DNLJ_COREF
ID DNLJ_COREF Reviewed; 938 AA.
AC Q8FPZ7;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA ligase;
DE EC=6.5.1.2;
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN Name=ligA; OrderedLocusNames=CE1339;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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 DNA
CC (By similarity). {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000305}.
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DR EMBL; BA000035; BAC18148.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FPZ7; -.
DR SMR; Q8FPZ7; -.
DR STRING; 196164.23493177; -.
DR EnsemblBacteria; BAC18148; BAC18148; BAC18148.
DR KEGG; cef:CE1339; -.
DR eggNOG; COG0272; Bacteria.
DR HOGENOM; CLU_007764_2_0_11; -.
DR OMA; HDVEHEI; -.
DR Proteomes; UP000001409; Chromosome.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule.
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; cd00114; LIGANc; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.10190; -; 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; IPR018239; DNA_ligase_AS.
DR InterPro; IPR033136; DNA_ligase_CS.
DR InterPro; IPR001679; DNAligase.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
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 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 SMART; SM00292; BRCT; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR TIGRFAMs; TIGR00575; dnlj; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS01055; DNA_LIGASE_N1; 1.
DR PROSITE; PS01056; DNA_LIGASE_N2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW Metal-binding; NAD; Reference proteome; Zinc.
FT CHAIN 1..938
FT /note="DNA ligase"
FT /id="PRO_0000340396"
FT DOMAIN 857..938
FT /note="BRCT"
FT REGION 1..260
FT /note="Unknown"
FT REGION 261..938
FT /note="DNA ligase"
FT ACT_SITE 373
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 295..299
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 346..347
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 394
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 434
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 550
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 574
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 668
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 671
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 938 AA; 101223 MW; DA5757B47998209F CRC64;
MSLAGLHRPG GVHCGAVPAL ALKIVPETDL LLVISHRLHL HEFLPAHGGQ FGPDAGLLPG
DAGSGQSVGG GFVGVAQLHL IMGAQISQGA LALPVGILDP VDGVGIIDQS IDGEVTGETP
QHGQIIGSVI HDEGLIISPA LLDSPDGLSQ HLLMGLAMLP GVFRGDAMHR GGTLGDLHPG
VGEQFEWGGS GIGDSHHRGG DDAGFKGVGG GGFQVEGEHV CGVEVGGEFH RGIHGFNPNQ
RPGHRVPPPD AIRDHLESGT VTDDNAQLRR TWNELAEKVR YHRDLYYNQQ PEIPDADFDA
LFRQLQDLEE QHPELAVPDS PTKEVGAPVT EQSSFDNVEH LERMLSLDNV FDEEELRDWL
ARTPAKRYLT ELKIDGLSID LVYRNGMLER AATRGDGRVG EDITANARVI GDIPHELTAT
EEYPIPAVLE VRGEVFIPIE DFADVNAQRI EDGGKPFANP RNAAAGSLRQ KNPEDVKKRR
LRMITHGIGY SEGFQPASQH DAYLALAAWG LPTSSYTEAV ETADAVVDKV LYWADHRHDA
LHEMDGLVIK VDDIASQRAL GSTSRAPRWA IAYKYPPEEV TTKLIDIKVS VGRTGRVTPF
AMMEPVFVAG STVSMATLHN QSEVKRKGVL IGDTVVVRKA GEVIPEVLGP VVELRDGTER
EFVFPEHCPE CGSTLAPTRA EDADWRCPNT RSCPGQLSQR LTYIAGRGAF DIEALGEKGA
QDLIRNGILV DEAGLFDLTE EDLLESDVYT TKAGAVNASG RKLLANLEQR KNTDLWRVLV
ALSIRHVGPT AARALAGRYR SMQKLVDAPV DELAETDGVG MIIAQSFKDW FEVDWHRAIV
DTWAAAGVTM EDAETEQLEQ TLEGLTIVVT GGLEGFTRDS VKEAIISRGG KASGSVSKKT
DYVVVGENAG SKATKAEELG LTILDEEAFV RLLDTGAV
