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Database: UniProt
Entry: J2JFN3_9NOCA
LinkDB: J2JFN3_9NOCA
Original site: J2JFN3_9NOCA 
ID   J2JFN3_9NOCA            Unreviewed;       318 AA.
AC   J2JFN3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   ORFNames=JVH1_3875 {ECO:0000313|EMBL:EJI98619.1};
OS   Rhodococcus sp. JVH1.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=745408 {ECO:0000313|EMBL:EJI98619.1, ECO:0000313|Proteomes:UP000009024};
RN   [1] {ECO:0000313|EMBL:EJI98619.1, ECO:0000313|Proteomes:UP000009024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JVH1 {ECO:0000313|EMBL:EJI98619.1,
RC   ECO:0000313|Proteomes:UP000009024};
RX   PubMed=22965106; DOI=10.1128/JB.01066-12;
RA   Brooks S.L., Van Hamme J.D.;
RT   "Whole-Genome Shotgun Sequence of Rhodococcus Species Strain JVH1.";
RL   J. Bacteriol. 194:5492-5493(2012).
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:EJI98619.1}.
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DR   EMBL; AKKP01000063; EJI98619.1; -; Genomic_DNA.
DR   AlphaFoldDB; J2JFN3; -.
DR   PATRIC; fig|745408.3.peg.3680; -.
DR   Proteomes; UP000009024; 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; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 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; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EJI98619.1}.
FT   DOMAIN          100..229
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   318 AA;  34626 MW;  A22E505EDE8E4BE6 CRC64;
     MLATAGTLPD NTDRPWSFEM KYDGCRILAS VGGGREPVLW TRAMNVVTSS YPEIAEALTA
     AFGGRGRIVL DGEVVVLDDH GKPSFGLLQR RMGVARATKP LQKRIPVTFL PFDVLALDGD
     DLTKASYLDR RAELAELDAV IQDVGGLPIT VPPFWENQSS KIMLNAARSA GMEGIVAKRS
     ASIYLPGQRS RSWIKHAIRT RSSVLVIGFV GSSRSVAALI LGAYDAEGRL VQVGSVSSGL
     TVSMRRQLRE DFRPLERPSS PLTDPSAAAE TFPGVQWLTP RLVVDVAYRA HTAGGLRHPS
     LKGRRFDVDF QSVRVEDL
//
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