ID A0A370QJ47_9FLAO Unreviewed; 552 AA.
AC A0A370QJ47;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN ORFNames=C8D94_101237 {ECO:0000313|EMBL:RDK88366.1};
OS Marinirhabdus gelatinilytica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1703343 {ECO:0000313|EMBL:RDK88366.1, ECO:0000313|Proteomes:UP000255317};
RN [1] {ECO:0000313|EMBL:RDK88366.1, ECO:0000313|Proteomes:UP000255317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 101478 {ECO:0000313|EMBL:RDK88366.1,
RC ECO:0000313|Proteomes:UP000255317};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-2018) 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:RDK88366.1}.
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DR EMBL; QRAO01000001; RDK88366.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370QJ47; -.
DR OrthoDB; 9767858at2; -.
DR Proteomes; UP000255317; 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; 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; 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:RDK88366.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000255317}.
FT DOMAIN 326..458
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 552 AA; 63912 MW; DD991ACBAE3ACF17 CRC64;
MKEFAALIKT LDSTNKTNLK VAALAEYFNQ ASDDDKLWTI AILSHRRPKR PVNTTLLRLW
ATEISGIPSW LFEESYHIVG DLAETIALIL PKTENTLTAA LEGEVRSVSQ SVTQLNTQNE
KSLSTYIQEI ITLRTLAEEE KKNYLQENWL AMSYFERFVF NKIITGGFRI GVSQKLMTRA
LSKSTGIDED ILAYKLMGDW TPEKTTYQKL ILEENPEDYL SKPYPFYLAY AVEDNFKEEL
GDIGNWSFEH KWDGIRSQVI IRNDDVFVWS RGEELVTDKY PEFQRFLSKI PNGTVLDGEI
LPFGNNEIGN FNDLQTRIGR KNLTKKLLEK TPVILNAYDL LEWEGKDIRK RPFSERRKIL
DTLISECDCD EIGLYLSATM EFQNWEAAAK ERKMAREKRS EGLMIKRKDS PYLVGRKKGD
WWKWKTDPFT IDGVLTYAMR GHGRRANLYT DYTFGLWDKG ELVTFAKAYS GLTDAEFRQV
DAWIKKNTLE RFGPVRSVTP HHVFEIAFEG IAESSRHKSG VATRFPRILR WRKDKPIEEA
NTLDDLRALI PK
//
