ID H0G2N8_RHIML Unreviewed; 628 AA.
AC H0G2N8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=SM0020_18642 {ECO:0000313|EMBL:EHK76477.1};
OS Sinorhizobium meliloti CCNWSX0020.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1107881 {ECO:0000313|EMBL:EHK76477.1, ECO:0000313|Proteomes:UP000004038};
RN [1] {ECO:0000313|EMBL:EHK76477.1, ECO:0000313|Proteomes:UP000004038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNWSX0020 {ECO:0000313|EMBL:EHK76477.1,
RC ECO:0000313|Proteomes:UP000004038};
RX PubMed=22328762; DOI=10.1128/JB.06682-11;
RA Li Z., Ma Z., Hao X., Wei G.;
RT "Draft Genome Sequence of Sinorhizobium meliloti CCNWSX0020, a Nitrogen-
RT Fixing Symbiont with Copper Tolerance Capability Isolated from Lead-Zinc
RT Mine Tailings.";
RL J. Bacteriol. 194:1267-1268(2012).
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; AGVV01000037; EHK76477.1; -; Genomic_DNA.
DR RefSeq; WP_004435781.1; NZ_AGVV01000037.1.
DR AlphaFoldDB; H0G2N8; -.
DR PATRIC; fig|1107881.3.peg.3791; -.
DR Proteomes; UP000004038; 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 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; IPR014145; LigD_pol_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014143; NHEJ_ligase_prk.
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; 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:EHK76477.1};
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 142..269
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 69412 MW; 4926A981FB0D86D9 CRC64;
MRQRAKAPHP SEGVPNGAQG RKAAVGSRRT ASPVDRLADL GATQSAFPEF IEPCHPTLKK
RPPDGADWVH EIKLDGYRAQ LHINDGKITI YTRTGLDWTT EFKAIATAAE DLSAHDAVVD
GEVTVFGKTG LPDFPALRRE LAKRSSPNLT FQAFDLLYLD GYDLRPVPLI ERKRVLRELI
GDAAGTIAYV DYLELEEGEP VYRHACKMGL EGIVSKRKDA PYRSGRQEIW TKTKCTKRDA
FPIVAFVEKL GAHPRRIASL YLGRWEGDRL VYAGKAQTGY TLTAAREVRE RLNPLIIGKS
PLSHPINKPK ATWVEPQVYA EIDYGGVTDD GLLREPVFKG LQDVSPAAGK PRPTTAPASI
RVPRANILQL LPEAVVPSKE ELANYWTRVA DRALHFLGGR PLKLVRHIHG TTFYHKGPLP
PIPSEVHQLR IEKREGGAGV RLWVDDLAGL LGLVEIGAVE LHPWAATVDN IEHADALIFD
LDPGEGVSWA FVVETALRLR EFLEAEGFKT WPKLTGGKGV HLMSPLTAKM THNAAHAYAK
RLAQQFASTD PDRYVTSAQL SHRPGKLFLD YLRNGRGTTA VGTYSPRARS GFPVAAPVTW
RDIERGIRPD AFTIERPPKR RAVLASAS
//
