ID V9WQR9_9RHOB Unreviewed; 518 AA.
AC V9WQR9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=Gal_03773 {ECO:0000313|EMBL:AHD11482.1};
OS Phaeobacter gallaeciensis DSM 26640.
OG Plasmid pGal_A255 {ECO:0000313|EMBL:AHD11482.1,
OG ECO:0000313|Proteomes:UP000018782}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1423144 {ECO:0000313|EMBL:AHD11482.1, ECO:0000313|Proteomes:UP000018782};
RN [1] {ECO:0000313|EMBL:AHD11482.1, ECO:0000313|Proteomes:UP000018782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26640 {ECO:0000313|EMBL:AHD11482.1,
RC ECO:0000313|Proteomes:UP000018782};
RC PLASMID=pGal_A255 {ECO:0000313|EMBL:AHD11482.1,
RC ECO:0000313|Proteomes:UP000018782};
RA Frank O., Petersen J., Goeker M., Klenk H.-P., Rohde M., Scheuner C.;
RT "Complete genome sequence of the Phaeobacter gallaeciensis type strain CIP
RT 105210T.";
RL Submitted (DEC-2013) 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; CP006967; AHD11482.1; -; Genomic_DNA.
DR RefSeq; WP_024099065.1; NZ_AOQA01000012.1.
DR AlphaFoldDB; V9WQR9; -.
DR GeneID; 31848115; -.
DR KEGG; pgd:Gal_03773; -.
DR PATRIC; fig|1423144.3.peg.3775; -.
DR HOGENOM; CLU_005138_6_2_5; -.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000018782; Plasmid pGal_A255.
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; 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 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 Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AHD11482.1};
KW Plasmid {ECO:0000313|EMBL:AHD11482.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018782}.
FT DOMAIN 296..426
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 518 AA; 57700 MW; B0BD9A484595D193 CRC64;
MQAFAELLEQ LAFTPSRNGK IAHLMTAFST IPDPDRGYAL AAITGDLALR NVTPSLLRGL
VAEETDAELF RLSYDFVGDL AETVALIWPH SDRVVDLSLA DAVHELTSTA KAQLPALIAR
RLSQMTPTQR YAYLKLATGG LRVGVSARLA RSALAQFGNV DVTEIEELWH GLTAPYLPLF
AWLEGGEKPM NLAAAPFRPV MLSTGTDLED LNSLSPADFV AEWKWDGIRV QAVNDNGTRR
LYSRTGEDIS GSFPDVIEAL NFDGVLDGEL LVKREDIVAP FGDLQKRLGR KKVGKAMLAS
HPAALRVYDV LLWNGEDLRC RTLVDRQTHL QTCVTDLSDP RIDRSLPLDF ETWEDLAKLR
ADPPNSVIEG VMIKRRDSAY IAGRKRGNWF KWKRDPMLVD AVMLYAQRGH GKRSGYYSDF
TFGVWDGDQL VPVGKAYFGF TDAELKELDR FVRNNTIDRF GPVRAVKPGL VLEVAFEGLN
ESSRHKSGLA MRFPRINRIR TDKPALEAGT LAELRAFL
//