ID A0A3N2IMV5_9MICO Unreviewed; 371 AA.
AC A0A3N2IMV5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-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=EDF38_1656 {ECO:0000313|EMBL:ROS62544.1};
OS Frigoribacterium sp. PhB160.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Frigoribacterium.
OX NCBI_TaxID=2485192 {ECO:0000313|EMBL:ROS62544.1, ECO:0000313|Proteomes:UP000280987};
RN [1] {ECO:0000313|EMBL:ROS62544.1, ECO:0000313|Proteomes:UP000280987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PhB160 {ECO:0000313|EMBL:ROS62544.1,
RC ECO:0000313|Proteomes:UP000280987};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing
RT to study the core and pangenomes of soil and plant-associated
RT prokaryotes.";
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000256|ARBA:ARBA00007572}.
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:ROS62544.1}.
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DR EMBL; RKIE01000001; ROS62544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2IMV5; -.
DR Proteomes; UP000280987; 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:InterPro.
DR CDD; cd07905; Adenylation_DNA_ligase_LigC; 1.
DR CDD; cd07970; OBF_DNA_ligase_LigC; 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; IPR044119; Adenylation_LigC-like.
DR InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR044117; OBF_LigC-like.
DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ROS62544.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000280987}.
FT DOMAIN 129..256
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
SQ SEQUENCE 371 AA; 40249 MW; 05DE3096BC26C961 CRC64;
MTPRAAATTP PTDPDRLGGV AAVSPMLAKA VARVPDADSV EGGLSYEPKW DGFRGVVSWD
GETLEISSRG SKPLTRYFPE LVEALPPLLP GPCVLDGEIV LRRGDAGNER LDWDALSQRI
HPAASRIATL STETPASFVA FDLLAEPADD GASVSLLDRP FRERRAALER LLADVAAPLH
LSRTTTDAGT ARRWLDEFEG AGLDGVVAKP LDAPYAPGKR TLLKIKHHRT ADVVVLGYRV
HKSGRGVGSL LLGLHDAAGE LRNVGGASAF SDARRLELVD ELADLVVHDA EGGVEHAETE
RSRFSSGKDV SYVPLRPERV VEVRYDQMEG DRFRHTVQVE RWRDDREAAS CGFDQLEVPA
AYDLGEVLVR S
//