ID A0A1J0WIB1_9RHOB Unreviewed; 532 AA.
AC A0A1J0WIB1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=BOO69_12130 {ECO:0000313|EMBL:APE44071.1};
OS Sulfitobacter alexandrii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1917485 {ECO:0000313|EMBL:APE44071.1, ECO:0000313|Proteomes:UP000181897};
RN [1] {ECO:0000313|EMBL:APE44071.1, ECO:0000313|Proteomes:UP000181897}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM1-D1 {ECO:0000313|EMBL:APE44071.1,
RC ECO:0000313|Proteomes:UP000181897};
RA Yang Q., Zhang X., Tian X.;
RT "Complete genome sequence of Sulfitobacter sp. AM1-D1, a toxic bacteria
RT associated with marine dinoflagellate Alexandrium minutum in East China
RT Sea.";
RL Submitted (NOV-2016) 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};
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DR EMBL; CP018076; APE44071.1; -; Genomic_DNA.
DR RefSeq; WP_071972409.1; NZ_CP018076.1.
DR AlphaFoldDB; A0A1J0WIB1; -.
DR STRING; 1917485.BOO69_12130; -.
DR KEGG; suam:BOO69_12130; -.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000181897; Chromosome.
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:APE44071.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 305..436
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 532 AA; 60902 MW; C190EA46D7C930A1 CRC64;
MKRFAALFNT IDQSTKITVK VTALAEYFSV ASDEDRLWTV ALFSGRRPKR AVTTTRLREW
AAEVAEIPLW LFEDSYAIVG DLAETIALVL PPNRSTEDRS LTHWITELRS LAQLEEAERK
AFVMSAWQAL GGTERFLFNK LITGGFRVGV SQKLMTRALA QATDKPETEL AHRLMGNWHP
DDTTWHALIE AEDASADASR PYPFYLAYAL EDGPETLGEP APWRAEWKWD GIRGQLILRD
GDYYVWSRGE ELMTDRFPEL ARAIDHLPSG TVLDGELLVW LPDSDAPSTF NALQARIGRK
TVPKKLLREA PVVLHAYDLL EWQGEDIRHR PFAERRRMLE DACADLPPDA PIRLSPQIPF
DTWQELAERR ATAREAQAEG LMLKRAESPY LAGRKKGDWW KWKLDPLTID AVMIYAQSGS
GRRANLFTDF TFAVWNGNDL VPFTKAYSGL TDAEFRQITA WVRKNTLERF GPVRRVTPHH
VFEIAFEGIQ PSPRHKSGVA LRFPRMKRWR KDKPLQEANT LDDLNEMLRQ YG
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