ID   A9H268_GLUDA            Unreviewed;       856 AA.
AC   A9H268;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943};
GN   OrderedLocusNames=GDI0169 {ECO:0000313|EMBL:CAP54112.1};
OS   Gluconacetobacter diazotrophicus (strain ATCC 49037 / DSM 5601 / CCUG 37298
OS   / CIP 103539 / LMG 7603 / PAl5).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=272568 {ECO:0000313|EMBL:CAP54112.1, ECO:0000313|Proteomes:UP000001176};
RN   [1] {ECO:0000313|EMBL:CAP54112.1, ECO:0000313|Proteomes:UP000001176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49037 / DSM 5601 / CCUG 37298 / CIP 103539 / LMG 7603 /
RC   PAl5 {ECO:0000313|Proteomes:UP000001176};
RX   PubMed=19775431; DOI=10.1186/1471-2164-10-450;
RA   Bertalan M., Albano R., Padua V., Rouws L., Rojas C., Hemerly A.,
RA   Teixeira K., Schwab S., Araujo J., Oliveira A., Franca L., Magalhaes V.,
RA   Alqueres S., Cardoso A., Almeida W., Loureiro M.M., Nogueira E., Cidade D.,
RA   Oliveira D., Simao T., Macedo J., Valadao A., Dreschsel M., Freitas F.,
RA   Vidal M., Guedes H., Rodrigues E., Meneses C., Brioso P., Pozzer L.,
RA   Figueiredo D., Montano H., Junior J., Filho G., Flores V., Ferreira B.,
RA   Branco A., Gonzalez P., Guillobel H., Lemos M., Seibel L., Macedo J.,
RA   Alves-Ferreira M., Sachetto-Martins G., Coelho A., Santos E., Amaral G.,
RA   Neves A., Pacheco A.B., Carvalho D., Lery L., Bisch P., Rossle S.C.,
RA   Urmenyi T., Kruger W.V., Martins O., Baldani J.I., Ferreira P.C.;
RT   "Complete genome sequence of the sugarcane nitrogen-fixing endophyte
RT   Gluconacetobacter diazotrophicus Pal5.";
RL   BMC Genomics 10:450-450(2009).
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; AM889285; CAP54112.1; -; Genomic_DNA.
DR   RefSeq; WP_012222408.1; NC_010125.1.
DR   AlphaFoldDB; A9H268; -.
DR   KEGG; gdi:GDI0169; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000001176; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   CDD; cd04862; PaeLigD_Pol_like; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014143; NHEJ_ligase_prk.
DR   InterPro; IPR033651; PaeLigD_Pol-like.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; TIGR02776; NHEJ_ligase_prk; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF13298; LigD_N; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAP54112.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001176};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          345..427
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   856 AA;  92556 MW;  C1CDD9863C029CAF CRC64;
     MALDTYRNKR DFEATPEPEG AEAAEKPDTG AGHLFVIQKH AARRLHYDLR LEMDGVLKSW
     AVTRGPSLNP GDKRLAVQVE DHPLDYGTFE GTIPKGQYGG GTVMLWDKGT WTPLHDPVRG
     LAKGHLDFEL RGEKLHGRWN LVRMDGHREG THENWLLIKA ADSDARSKND ADILEERPES
     VKTGRAMDDI AAGAPGKDKV GKAAAQKAVT KKAAIPKDAP QADAAATGAA PCAGAKPGPL
     PSFVEPELAT LVRAAPTGPQ WLHEVKFDGY RLLARIEAGR VVLLTRTGLD WTARFGDQIS
     AALASLPVRA ALIDGELVVE TAGGTSDFSA LQADLSAGRT DRFIFYVFDL LHLDGYDLRD
     ATLEARKGAL HDLVPDDAAR LRFSGHFDEA GGQVLRHACR LGLEGIVSKQ RDAPYRSGRG
     RDWVKSKCVA RQEFVIGGYV PSTANRGAVG SLVLGVQENG RLVHVGRVGT GFTAATAADL
     FRRLQPLDVP DSPFAAALTA RERKGVRYVR PDCVAEVEFR AWTADGHLRH AAFLGQREDK
     PAADIVREVE APDPVSSGPS SKPVKPVSPE PAPARPARTL THPDRSYWPD AGVTKQDLAD
     YYAAIWPRMA PFITDRALAL LRCPNGIAGP RFFQKNLWKG AGGHLVPLQD PEGEAGTPLI
     GLHDRDGLID LVQAAALEIH PWGASVQAWS QPDMIVMDLD PGDGVPWSMV IEAAREIRAR
     LERSGLASFV KTTGGKGLHV VAPLKPGADW AVVKAFTRSM AQAMVSDSPQ RYVATITKSR
     RQGRILVDYL RNQRGATAVA PYSPRARPGA PVAMPLAWNE LGPDIGPAHF TIGTIGARLA
     VADPWAEIRD AARPLR
//