ID H6QYV3_NOCCG Unreviewed; 786 AA.
AC H6QYV3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
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=NOCYR_0694 {ECO:0000313|EMBL:CCF61508.1};
OS Nocardia cyriacigeorgica (strain GUH-2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF61508.1, ECO:0000313|Proteomes:UP000008190};
RN [1] {ECO:0000313|EMBL:CCF61508.1, ECO:0000313|Proteomes:UP000008190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF61508.1,
RC ECO:0000313|Proteomes:UP000008190};
RX PubMed=22461543; DOI=10.1128/JB.00161-12;
RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA Richard Y., Cournoyer B., Blaha D.;
RT "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT cyriacigeorgica GUH-2.";
RL J. Bacteriol. 194:2098-2099(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; FO082843; CCF61508.1; -; Genomic_DNA.
DR AlphaFoldDB; H6QYV3; -.
DR STRING; 1127134.NOCYR_0694; -.
DR KEGG; ncy:NOCYR_0694; -.
DR eggNOG; COG1793; Bacteria.
DR eggNOG; COG3285; Bacteria.
DR HOGENOM; CLU_008325_2_1_11; -.
DR OMA; QWLAHRM; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000008190; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006310; P:DNA recombination; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR014144; LigD_PE_domain.
DR InterPro; IPR014145; LigD_pol_dom.
DR InterPro; IPR033649; MtLigD_Pol-like.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR NCBIfam; TIGR02778; ligD_pol; 1.
DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR PANTHER; PTHR42705:SF2; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING 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:CCF61508.1};
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:UP000008190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 586..719
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 322..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 786 AA; 86871 MW; AF6D78752E514355 CRC64;
MNAGSRRRAT DNGSRRSFRD AAGEPVIRIE LSNLDKVLYP ATGTTKGEVI AYYTAIAPAM
LPHVAGRPVT RKRWPNGVEE SSFFEKNLAE HAPDWLPRRA MRHSDRTVTY PLIDSEAGLA
WIGQQASLEV HVPQWRFDGE HMGPATRLVF DLDPGPGAGL AECATVALEV RDMVDRIGLR
AFPVTSGSKG IHLYVPLDRV LSPGGASTVA KQVATNLEKM HPELVTATMA KKVRTGKVFL
DWSQNNPAKT TIAPYSMRGR AQPNVAAPRS WAEIEDRESL RHLRFDEVLA RFQADGDLLA
GLDPPISQAG ASRPDPLSVY RSMRDPARTP EPVPAHPPTP GPGNRYVVQE HHARRLHWDV
RLERDGVLVS WAVPKGPPTD TKENRLAVHT EDHPLEYLDF HGSIPKGEYG AGTMTIWDSG
TYETEKWRDD EVIVVMRGER LHGRYALIRT GGKNWLMHLM KEQPAEGDGA APSGNGRRAA
KESAEVPERS GGADLPRGLA PMLATTGEVA ELDPKEWAFE TKWDGYRLIL EFDHGTPTLR
SRAGNIVTDR YPKIAALAEE LAGHRVVLDG EAVVFDDNGV ANLALLQADT RRAELVAFDL
LYLDGTSLIR KRYSDRRRVL EALAATTSAL SVPPQLEGTG EDALNASLEV GAEGVVAKRK
DSVYLPGKRG HSWVKQRNWQ TQQVLVGGYR GSAARPFASL LVGIPDNGKL IYVGRVGTGF
SEDEMRALAT RLQRRRRKTS PFVNEMSREE TKDATWVTPE ISGTVRFMNW TDSGRLWHPA
WLGRAD
//