ID W1SET3_9BACI Unreviewed; 615 AA.
AC W1SET3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ligD {ECO:0000313|EMBL:ETI67901.1};
GN ORFNames=BAVI_15471 {ECO:0000313|EMBL:ETI67901.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI67901.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI67901.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI67901.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(2014).
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:ETI67901.1}.
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DR EMBL; ALAN01000084; ETI67901.1; -; Genomic_DNA.
DR AlphaFoldDB; W1SET3; -.
DR STRING; 220686.AA980_15725; -.
DR PATRIC; fig|1131730.3.peg.3239; -.
DR eggNOG; COG1793; Bacteria.
DR eggNOG; COG3285; Bacteria.
DR Proteomes; UP000018877; 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; cd04866; LigD_Pol_like_3; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR014146; LigD_ligase_dom.
DR InterPro; IPR033652; LigD_Pol-like_3.
DR InterPro; IPR014145; LigD_pol_dom.
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; 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; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 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:ETI67901.1};
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:UP000018877};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 107..246
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 615 AA; 71936 MW; D6BD2C245F454DFC CRC64;
MMKPMLPSLT FELPVRPDWL YEVKYDGFRA LLEWTINGIT LTSRNGKPLS PQFPEIEEFL
RTYEEQFKAY LPLQFDGELV SLENAYKANF SAIQVRGRLK AVKKISEQAM KSPCRLMVFD
LLMIKGKPLL NQPYHKRKDK LINLFQQLEL EVDSNPYNRQ ILQLVFPYED FNDLWEKVVL
YDGEGIIAKS RTSLWEEGKR TLQWLKYKNW KYVSCFVTSF DKTNGYFYVS VYKENDIHVV
GQVLFGFKPE EKQALRQTIK QNIIREDGSL IFVNPAICLE VKYLELYDNQ LREPHFDHFR
FDLEPAECTY EQFMIQQKNL PADLAITHPN KPLWENQHIE KIDYIFYLRE VSPFMLPFLE
NRLLTVIRYP HGMFGEAFYQ KNCPDYAPEF IRTHSADGID YILCNNLKTL VWLGNQLAIE
FHVPFQTIHS KGPSEIVFDL DPPDQDSFHL AVKAALLIKE VLDQLNLIGF IKTSGNKGLQ
VYLPLPEGKF SYDDTRLFTS FMAEYLIAKD PDSFTIERMK KKRGKRLYVD YVQHGEGKTI
VAPYSLRGNE AAGVATPLYW EEVDEKISPA AFNMENALKR LQKQGNPFRN YFQTKQIQPF
GPILEILKKG QRKKG
//
