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Database: UniProt
Entry: A0A0Q8RKD3_9BURK
LinkDB: A0A0Q8RKD3_9BURK
Original site: A0A0Q8RKD3_9BURK 
ID   A0A0Q8RKD3_9BURK        Unreviewed;       544 AA.
AC   A0A0Q8RKD3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=ASE26_01310 {ECO:0000313|EMBL:KRC03504.1};
OS   Duganella sp. Root198D2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Duganella.
OX   NCBI_TaxID=1736489 {ECO:0000313|EMBL:KRC03504.1, ECO:0000313|Proteomes:UP000051728};
RN   [1] {ECO:0000313|EMBL:KRC03504.1, ECO:0000313|Proteomes:UP000051728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root198D2 {ECO:0000313|EMBL:KRC03504.1,
RC   ECO:0000313|Proteomes:UP000051728};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC03504.1, ECO:0000313|Proteomes:UP000051728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root198D2 {ECO:0000313|EMBL:KRC03504.1,
RC   ECO:0000313|Proteomes:UP000051728};
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:KRC03504.1}.
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DR   EMBL; LMIC01000001; KRC03504.1; -; Genomic_DNA.
DR   RefSeq; WP_055931123.1; NZ_LMIC01000001.1.
DR   AlphaFoldDB; A0A0Q8RKD3; -.
DR   Proteomes; UP000051728; 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; 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:KRC03504.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051728}.
FT   DOMAIN          319..442
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   544 AA;  60456 MW;  8445DFE79D3A92BE CRC64;
     MREFARLYAE LDETTSTNRK LEALQAYFSK AAPENAAWAV YFLAGGKPRQ AVPVKLLRQY
     ATAYAGLDEW LFDECYNAVG DLAETIAHIL PAPKRESDVG LAQWIEQRIA PLRGAAPDEV
     RAALFRYWDE LETRERFLLV KLIGGGFRVG VSRLLVTRAL SAIAAVDSKL VAQRLMGWTD
     GRVRPTAQGF LQLIAAPSAT EHAERGGQPY PFFLAHALQG DPAALGELAD WQVEWKYDGM
     RAQLVSRAGL NFLWSRGEDL ITERFPELVS IRLPQGTVID GEILVWPQGD APAPFAALQK
     RIGRKLLGAK LLAELPAVLV AYDLLELDGV DIRQLPQHER RALLERLVGQ AGQPQLRLSP
     LVLAEDWAQL AQVRTESRAR GVEGMMLKAR GAQYGVGRTK DVGTWWKWKI DPFSVDAVLV
     YAQAGHGRRA SLYTDYTFAV WDSDADGERK LVPFAKAYSG LTDAEIAQVD NAVRRTTIER
     FGPVRSVKPT MVFEIGFEGI ALSPRHKSGI AVRFPRILRR RDDKAVEDAD TLDTLRGLLV
     QAPP
//
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