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DNLJ_SORC5
ID   DNLJ_SORC5              Reviewed;         676 AA.
AC   A9F3W3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588};
DE            EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588};
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588};
GN   Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; OrderedLocusNames=sce4457;
OS   Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So
OS   ce56)).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; Sorangiineae;
OC   Polyangiaceae; Sorangium.
OX   NCBI_TaxID=448385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=So ce56;
RX   PubMed=17965706; DOI=10.1038/nbt1354;
RA   Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O.,
RA   Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J.,
RA   Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A.,
RA   Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C.,
RA   Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T.,
RA   Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S.,
RA   Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F.,
RA   Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G.,
RA   Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D.,
RA   Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H.,
RA   Puehler A., Mueller R.;
RT   "Complete genome sequence of the myxobacterium Sorangium cellulosum.";
RL   Nat. Biotechnol. 25:1281-1289(2007).
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; AM746676; CAN94620.1; -; Genomic_DNA.
DR   RefSeq; WP_012237089.1; NC_010162.1.
DR   AlphaFoldDB; A9F3W3; -.
DR   SMR; A9F3W3; -.
DR   STRING; 448385.sce4457; -.
DR   EnsemblBacteria; CAN94620; CAN94620; sce4457.
DR   KEGG; scl:sce4457; -.
DR   eggNOG; COG0272; Bacteria.
DR   HOGENOM; CLU_007764_2_3_7; -.
DR   OMA; HDVEHEI; -.
DR   OrthoDB; 241401at2; -.
DR   BioCyc; SCEL448385:SCE_RS22865-MON; -.
DR   Proteomes; UP000002139; 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   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; 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; 2.
DR   Pfam; PF03120; DNA_ligase_OB; 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   PROSITE; PS50172; BRCT; 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..676
FT                   /note="DNA ligase"
FT                   /id="PRO_0000340384"
FT   DOMAIN          593..676
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        148
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         52..56
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         95..96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         169
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         203
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01588"
FT   BINDING         330
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   676 AA;  72420 MW;  2DBB0885432BC799 CRC64;
     MTQAHHDDAG ARNALQGGLA TDPKHKARIE ELAERIEKYR ASYYAGHPEI SDAAFDALED
     ELRALDPAHP VLARVGSASL ITEWEKARHE IPMGSLNKVV SEDELLGWVA RCDEILVKDG
     HGDGGTGAAP PAPGSISSVA GDLFVAEKLD GISIEVIYKG GKLVDAITRG DGEWGERITA
     NVARMKGIPS RIREKGRLSV RGEIILRLSD MKRHFPGVTS PRNMAAGAAK RFDGQGAEHC
     TVLFYDVADH LEIPTCRARF AWLRELGFAT PQTAHGSVED VVKLYRRYSS ELRAGLDYEI
     DGLVVYVDSL HVQGLLGDVN RRPRGAVAFK FASPAKVTTV VAIQWDTGPS GRVTPVAIVE
     PVELAGANVR RASLHNSANV RSLGIGVGDE VLVSRRNDVI PYVEEVVEKR GPVAVPPSVC
     PVCSAPLVVE GEYLLCRNAA CRALIEGRIH NWIDAIGALE WGDKLIEQVV AAGLVREPLD
     LYKLTVKSIA DLDRRGEKSA TKCLEQLKSR LPLALPVFLA ALGIEGFAIQ TARLLVSAGY
     TTIEKLLAAG EDELAGIPGL GAIKAASIVR GLRARSDEIG RLLAAGIVPV APEAEGPLAG
     LTFCFTGAGA RPRGELTHLV ESSGGRVLNS VTKELNYLVI ADVASTSSKA VKARKYGTKL
     ITEDDLDKLI AERRGG
 
 
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