ID A0A3L7JWL1_9BACI Unreviewed; 609 AA.
AC A0A3L7JWL1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=D9X91_12165 {ECO:0000313|EMBL:RLQ95237.1};
OS Falsibacillus albus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Falsibacillus.
OX NCBI_TaxID=2478915 {ECO:0000313|EMBL:RLQ95237.1, ECO:0000313|Proteomes:UP000276770};
RN [1] {ECO:0000313|EMBL:RLQ95237.1, ECO:0000313|Proteomes:UP000276770}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GY 10110 {ECO:0000313|EMBL:RLQ95237.1,
RC ECO:0000313|Proteomes:UP000276770};
RA Shi S.;
RT "Falsibacillus sp. genome draft.";
RL Submitted (OCT-2018) 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:RLQ95237.1}.
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DR EMBL; RCVZ01000007; RLQ95237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L7JWL1; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000276770; 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 Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 3.90.920.10; DNA primase, PRIM domain; 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; IPR014145; LigD_pol_dom.
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 PROSITE; PS00697; DNA_LIGASE_A1; 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:RLQ95237.1};
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:UP000276770};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 115..245
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 609 AA; 71201 MW; 24D1A33207862A54 CRC64;
MKPMLPKLKM DIPPIGEWMF EVKYDGFRAI LEWDHEEIHL WSRNEKDLLP QFPEIKEYLL
QNLERIEGCF PLKLDGELTL LENPYKSNFN GLQVRGRMRS QKDIKDAAGK RPCTYLVFDL
LELGGKTYMK TPYSIRKDRL EKFLKESEFS LSPCHDPQRL MQMVNSFRSF QDVWKEVFLN
HSEGVVAKNK NSIWSPGKRT DAWIKIKNWK EASCFIVGYN KNNGYFDVAV FRDGDIFSIG
QFLSGLNPMD KKVLIQTIIQ NGTQTGDYIE VPPGICIQLQ YLELYEGRLR EPRFKEFLFN
ASVSECTYEK FRIDSFAFPK KVELTHLDKP LWKDPFINKL EYVSYLRRIA PHLLPFLKDR
LLTVIRLPHG MFGDSFFQKN CPEYAPSYIE TYQEDEIDYI LCNHLDALIW LGNQLAIEFH
VPFQKAGSPF VSEIVFDLDP PDRNHFHMAV AAAQQLKILF DSMNLISFVK TSGNKGLQVY
LPLPENIYSW SDTRLFTEFI AHYLVSQSPD LFTVERLKKN RGNRLYFDYI QHAQGKTIIA
PYSMRGNEDA LVAAPLFWDE IKSGLMIETF TTETVLERLN KRGCPFSTYH ESKDRQPFAP
IVKYLKENK
//
