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Database: UniProt
Entry: A0A0Q8BLD8_9BURK
LinkDB: A0A0Q8BLD8_9BURK
Original site: A0A0Q8BLD8_9BURK 
ID   A0A0Q8BLD8_9BURK        Unreviewed;       534 AA.
AC   A0A0Q8BLD8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=ASD71_12440 {ECO:0000313|EMBL:KRA02771.1};
OS   Achromobacter sp. Root565.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1736564 {ECO:0000313|EMBL:KRA02771.1, ECO:0000313|Proteomes:UP000052040};
RN   [1] {ECO:0000313|EMBL:KRA02771.1, ECO:0000313|Proteomes:UP000052040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root565 {ECO:0000313|EMBL:KRA02771.1,
RC   ECO:0000313|Proteomes:UP000052040};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA02771.1, ECO:0000313|Proteomes:UP000052040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root565 {ECO:0000313|EMBL:KRA02771.1,
RC   ECO:0000313|Proteomes:UP000052040};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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   -!- 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:KRA02771.1}.
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DR   EMBL; LMGO01000001; KRA02771.1; -; Genomic_DNA.
DR   RefSeq; WP_056563998.1; NZ_LMGO01000001.1.
DR   AlphaFoldDB; A0A0Q8BLD8; -.
DR   Proteomes; UP000052040; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd07897; Adenylation_DNA_ligase_Bac1; 1.
DR   CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1.
DR   Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR026333; ATP_dep_DNA_lig_pp_1105_fam.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR04120; DNA_lig_bact; 1.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR   PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KRA02771.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          315..441
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   534 AA;  60274 MW;  DD87BE2EE8FAD878 CRC64;
     MKRFAALYQE LDRSTATLDK RAALVAYFRD APPRDAVWAL YLLAGGKITS TRKKIAGVGE
     LRAWAADASR TAPWLLDACY DQVGDLAETL ALLVPDPEVA APDRGLADWI EEILLPIANR
     DESERREVVV SAWLGLPYAE RLVFNKLLTG ALRVGVSQRM VQQALAEMSG VPIARIAQRM
     LGVWSPSPAF LRDLLSTEEL PGDRQQPYPF FLASPLEGDP AVLGPIDEWL LEWKWDGIRA
     QLIRRRGEVS IWSRGEERLD GRFPEVEAAA AALDVDCVID GELLAWQDGN TDPMPFSALQ
     TRIQRLKPGP KWLAEAPVQL LAYDLLELEG ADLRELPQAE RRARLEALLR RHPDPRLRMS
     PAVAPSSWDE AHALRGESRE RGVEGFMLKR RSAPYQSGRR RGDWWKWKID PLTIDAVLLY
     AQSGHGRRST LYTDYTFGLW EGDALVPIAK AYSGLDDKEI LELDRWLRAH TRERFGPVRS
     VEPVQVFELG FEGVNVSKRH KSGIAVRFPR ILRWRHDKPA DQADQLDTLK ALAR
//
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