ID A0A0D0R4Y8_9GAMM Unreviewed; 840 AA.
AC A0A0D0R4Y8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=TI01_1643 {ECO:0000313|EMBL:KIQ96784.1};
OS Lysobacter sp. A03.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1199154 {ECO:0000313|EMBL:KIQ96784.1, ECO:0000313|Proteomes:UP000032077};
RN [1] {ECO:0000313|EMBL:KIQ96784.1, ECO:0000313|Proteomes:UP000032077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A03 {ECO:0000313|EMBL:KIQ96784.1,
RC ECO:0000313|Proteomes:UP000032077};
RA Pereira J.Q., Ambrosini A., Sant'Anna F.H., Tadra-Sfeir M., Faoro H.,
RA Pedrosa F.O., de Souza E.M., Brandelli A., Passaglia L.M.;
RT "Genome sequence of Lysobacter sp. A03.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIQ96784.1}.
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DR EMBL; JXSS01000076; KIQ96784.1; -; Genomic_DNA.
DR RefSeq; WP_043958776.1; NZ_JXSS01000076.1.
DR AlphaFoldDB; A0A0D0R4Y8; -.
DR STRING; 1199154.TI01_1643; -.
DR PATRIC; fig|1199154.3.peg.464; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000032077; Unassembled WGS sequence.
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:KIQ96784.1};
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:UP000032077};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 323..416
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 840 AA; 91304 MW; E6FA8C5017EC93BD CRC64;
MGLKEYARKR RFGDTPEPDD GARGKTGQRP IFVVQLHHAR ARHYDFRLEA DGVLKSWAVP
KGPSLRVGEK RLAVEVEDHP LDYADFAGDI PAGNYGAGHV QIFDHGVWAC DGDPLEALAK
GKLDFVLEGE KLRGGWKLIR TAKRASKPQW LLLKRDDAFA ANLEADDLLA DGAGAPVLPG
KKSGRQTRRP RPAQPGSAAK ASKPRKAKGR LDWKARARLL DGAKPLRDGT EIAPQLATLQ
AAPPDGDDWM HELKWDGYRL LATIDEGHVQ LRSRNGLDWT GEHPVIVEAL EHLGVDSASL
DGELIALDAK GHDSFSTLQH TLKGTARGEL RYVVFDLPTL AGIDLTATRL DKRKALLAEL
LDAAGTPGPL LYSEHVTGHG AEVFAASRTQ GMEGIISKAA DARYTPGRSH SWLKTKHAQS
DEFVVVGFMP PQRSRIGFAS LLLATRREGE LVYVGRVGTG FDDANLRALA ARLKPMVRKQ
PTVPLPAHVA FPIGNAIWVK PELVVEVAFR GWGKEGLLRQ ASYQRLRGDK SADEVGSAAP
ATSRSQTKKE NPNMAVISSP GRVVYPDAGI TKQEVADYYT AIANWLLPEV ADRPLSLLRC
PDGIAGECFF QKHHAEAFGE SVHAISVRAK DGGRSDYMVV RDVAGLLGLV QMGTLELHPW
GACGDDLEHP DRLVFDLDPG DGVVWKAVIA AARDVRDRLE ELGMQSFVRL TGGKGLHVVV
PIAPGPGWRQ AKTFSEGFAD AMASSAPERY VATASKALRD GVVFIDWLRN SRGATSVASW
SLRARAGAPV AVPLRWSELG RTDSGADYPL ARALRRASSL GSDPWQGWND AIKQSLVDWS
//
