ID A0A0H3D331_AMYMU Unreviewed; 670 AA.
AC A0A0H3D331;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=lig {ECO:0000313|EMBL:ADJ45045.1};
GN OrderedLocusNames=AMED_3255 {ECO:0000313|EMBL:ADJ45045.1};
OS Amycolatopsis mediterranei (strain U-32).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=749927 {ECO:0000313|EMBL:ADJ45045.1, ECO:0000313|Proteomes:UP000000328};
RN [1] {ECO:0000313|EMBL:ADJ45045.1, ECO:0000313|Proteomes:UP000000328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U-32 {ECO:0000313|Proteomes:UP000000328};
RX PubMed=20567260; DOI=10.1038/cr.2010.87;
RA Zhao W., Zhong Y., Yuan H., Wang J., Zheng H., Wang Y., Cen X., Xu F.,
RA Bai J., Han X., Lu G., Zhu Y., Shao Z., Yan H., Li C., Peng N., Zhang Z.,
RA Zhang Y., Lin W., Fan Y., Qin Z., Hu Y., Zhu B., Wang S., Ding X.,
RA Zhao G.P.;
RT "Complete genome sequence of the rifamycin SV-producing Amycolatopsis
RT mediterranei U32 revealed its genetic characteristics in phylogeny and
RT metabolism.";
RL Cell Res. 20:1096-1108(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002000; ADJ45045.1; -; Genomic_DNA.
DR RefSeq; WP_013225117.1; NC_014318.1.
DR RefSeq; YP_003765447.1; NC_014318.1.
DR AlphaFoldDB; A0A0H3D331; -.
DR KEGG; amd:AMED_3255; -.
DR PATRIC; fig|749927.5.peg.3360; -.
DR eggNOG; COG1793; Bacteria.
DR eggNOG; COG3285; Bacteria.
DR HOGENOM; CLU_008325_0_2_11; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000000328; 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; cd04863; MtLigD_Pol_like; 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; IPR033649; MtLigD_Pol-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR014143; NHEJ_ligase_prk.
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; 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:ADJ45045.1};
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:UP000000328};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 119..251
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 348..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 73532 MW; D27A67A8BFE8E1AA CRC64;
MAADDASLVP AWLEPMLAKA DGGRLRTGPE WAYEYKLDGY RAAMRIAPDG TTVLTSRNNI
DFTAEFTDLE GVLAPALDGR AAYLDGEIVV YGEDGRIDFE RMQERRGRYV RHQSGPKGRE
FTDVPVRFLA FDLLRLGDES LLAMPYDERR RLLAELPMPD PYRVSVVRAV TFDELAADRR
TPADFLAHAA SAGYEGVVAK LRSSAYHPGQ RPDSWLKHPL VRTQEVIVCG WRPGQNSFTG
TLGGLLLGAH DPATGDLVYI GDVGTGFSQA TRADLRAQLE AMERRTHPFV TTPPREDTAR
ARWVEPRLVG EIVYRQFTRG GRVRHTAWRG LRHDKDPAEV LAPRAVPHEP AGAAPAPPSP
SSSASASASP SPEPAGQRIT VQAGDRRLTL SNLDKVLYPA DGFTKGEVIN YYSRVAAVLL
PHLAGRPVTF IRYPNGVDGQ KWFEKNAPKG APDWLRTVRL AGTGGTIDYP LLDDLPGLVW
AANMAALELH VPQWTVEQGT RQPPDRLVFD LDPGPGTTIV DCCRVAERLH DVLVADGLTP
YAKTSGSKGM QLYCGIRTDD PAAPSAYAKR LAQRLAKETP ESVTAVMAKA QRTGRVFIDW
SQNNPAKTTV APYSLRGRDH PTASTPVTWD EVRACRHVNR LTFTADDVLD RLEDHGDLLA
GLIEDRAPLG
//
