ID B9D382_CAMRE Unreviewed; 325 AA.
AC B9D382;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=ATP-dependent DNA ligase domain protein {ECO:0000313|EMBL:EEF13546.1};
DE EC=6.5.1.1 {ECO:0000313|EMBL:EEF13546.1};
GN ORFNames=CAMRE0001_2243 {ECO:0000313|EMBL:EEF13546.1};
OS Campylobacter rectus RM3267.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=553218 {ECO:0000313|EMBL:EEF13546.1, ECO:0000313|Proteomes:UP000003082};
RN [1] {ECO:0000313|EMBL:EEF13546.1, ECO:0000313|Proteomes:UP000003082}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM3267 {ECO:0000313|EMBL:EEF13546.1,
RC ECO:0000313|Proteomes:UP000003082};
RA Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (AUG-2008) 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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|ARBA:ARBA00001968};
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:EEF13546.1}.
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DR EMBL; ACFU01000018; EEF13546.1; -; Genomic_DNA.
DR RefSeq; WP_004320189.1; NZ_ACFU01000018.1.
DR AlphaFoldDB; B9D382; -.
DR STRING; 553218.CAMRE0001_2243; -.
DR eggNOG; COG1793; Bacteria.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000003082; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd07896; Adenylation_kDNA_ligase_like; 1.
DR CDD; cd08041; OBF_kDNA_ligase_like; 1.
DR Gene3D; 3.30.1490.70; -; 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; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR InterPro; IPR029319; DNA_ligase_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR47810; DNA LIGASE; 1.
DR PANTHER; PTHR47810:SF1; DNA LIGASE B; 1.
DR Pfam; PF01068; DNA_ligase_A_M; 1.
DR Pfam; PF14743; DNA_ligase_OB_2; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00333; DNA_LIGASE_A2; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000313|EMBL:EEF13546.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..325
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002882760"
FT DOMAIN 74..230
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|Pfam:PF01068"
FT DOMAIN 245..323
FT /note="DNA ligase OB-like"
FT /evidence="ECO:0000259|Pfam:PF14743"
SQ SEQUENCE 325 AA; 35346 MW; 77EF90D7CE3B6878 CRC64;
MRFFALLLAA FLNFALAAQD LASQPKKFSA AQGENLSSAV GVDTISAVAV ADKNAKFKLL
KLSEYKGQNV GGWLASEKLD GVRAYWDGRN LLSRNGKILA APGGWSAHFP PFALDGELYT
SRGEFEKIQS IVMDKTPSVA AWSEVKFYVF DVPEAVGGLL ERLSELEKFI AKNPQAGQNL
KIIKQVKVKD NAEFEAFAKH IVAKGGEGAV VREPNVPYER KRSKNALKYK KFKDAECEVT
AINAGAGKYA GLMGSVTCKA IGNEGLNPGS GEKTKDGVKF KVGSGFSDRD RANPPKIGSI
ITYKYQNLTA KGLPRFPVFL RVRED
//
