DNLJ2_PSECP
ID DNLJ2_PSECP Reviewed; 701 AA.
AC B8HIQ9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] 2 {ECO:0000255|HAMAP-Rule:MF_01588};
GN Name=ligA2 {ECO:0000255|HAMAP-Rule:MF_01588}; OrderedLocusNames=Achl_4355;
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OG Plasmid pACHL01.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC 13794 / A6;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of plasmid1 of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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:0000255|HAMAP-Rule:MF_01588}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01588};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01588};
CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}.
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DR EMBL; CP001342; ACL42306.1; -; Genomic_DNA.
DR RefSeq; WP_012623323.1; NC_011879.1.
DR AlphaFoldDB; B8HIQ9; -.
DR SMR; B8HIQ9; -.
DR EnsemblBacteria; ACL42306; ACL42306; Achl_4355.
DR KEGG; ach:Achl_4355; -.
DR HOGENOM; CLU_007764_2_0_11; -.
DR OMA; GRDQLDI; -.
DR OrthoDB; 241401at2; -.
DR Proteomes; UP000002505; Plasmid pACHL01.
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 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; 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 Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF12826; HHH_2; 1.
DR PIRSF; PIRSF001604; LigA; 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.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese;
KW Metal-binding; NAD; Plasmid; Zinc.
FT CHAIN 1..701
FT /note="DNA ligase 2"
FT /id="PRO_0000380294"
FT DOMAIN 615..701
FT /note="BRCT"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 64..68
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 111..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 133
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 156
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 189
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 302
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 326
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 436
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT BINDING 441
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
SQ SEQUENCE 701 AA; 74186 MW; 55DA83013F0B05AB CRC64;
MSPAPQNRQP SGVPVGGQFA ATNHAEPGIG LATFGSEEEY QAAVTTALSA AKAYETTDVE
EMNDAEFDRL LAKIASHEAA NGIEPEHDLH DTIGHGGAGG GDVEHATPMK SLEKPGEDAV
IEFAAKHPKA VIEPKIDGLA ISVRYENGKM VRAARRGDGY TGEDVTDRVR GVDGLPEMAG
DGDYEVRGEL YLNDENKAKA NAIRQAAGKA PFANARNGVA GMLNKQDGSY AGLFSFAAYS
TTIDEKADHL DSMQQLEGMG FTTARSLLPQ SVLDAEDPMA AIAALGAERK GLNFLMDGAV
LKVNTAAERA ELGEGSRAPK WAVAYKYPAV EEPTVIEDIE YNIGKTGRLS IRARLTPVEV
DGSVVEYASL HNVGHLQAAD MRIGDTVSAY KANDIIPQVH LPRADLRDES SQPWQPPSVC
PQCSEPFDKS TELWRCHTPE CSVSGRISYA ASRDAGLDIE GLGGSIGDAL IEKDLVKDVS
DLFYLGEDQL AEVELGETST GGTRTLGQKN AAKIMAEIEK AKSQPLNRVI TALSMRFTGR
TFGRRLAAEF GTMEALQAAT VSQLANVEGI GQKKAEVIHE QLKKNAPVIA KLREAGVNMG
APKAAPAAGA KAPKLTKPDG KPMNVVVTGS VKGSPLGSLS RSGVQELIEA KGGKASGSVS
KTTDLLVCGE PGSSKFLKAQ ELGIRIVTPD EFAQMVEDGE V
