ID   F8A5P6_CELGA            Unreviewed;       310 AA.
AC   F8A5P6;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=Celgi_1690 {ECO:0000313|EMBL:AEI12201.1};
OS   Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI12201.1, ECO:0000313|Proteomes:UP000000485};
RN   [1] {ECO:0000313|Proteomes:UP000000485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA   Woyke T.;
RT   "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL   Submitted (APR-2011) 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; CP002665; AEI12201.1; -; Genomic_DNA.
DR   RefSeq; WP_013883720.1; NC_015671.1.
DR   AlphaFoldDB; F8A5P6; -.
DR   STRING; 593907.Celgi_1690; -.
DR   KEGG; cga:Celgi_1690; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_008325_4_0_11; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000000485; Chromosome.
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; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 1.
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; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AEI12201.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000485}.
FT   DOMAIN          106..186
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   310 AA;  33580 MW;  2BBAC4DAC9020656 CRC64;
     MQPMLATPAP SGVLPRGAAW AFEVKWDGVR VLAEVEGGLV RLLSRTGRPV TPAYPELAGL
     AHLPDVLLDG EVVALEGGVP SFAAIADRMH VRDPRRAAEL ARVRPVTFMV FDVLRVAGAD
     VVERPYDERR RLLEALDLPE HVLLSPVHDD GDGLWDVTRA HGLEGVVAKR RASPYRPGAR
     SGDWVKAAHR RTRTAYVAGW RPEQGGSGRL GALLLGAPDR DGALRFLGRA GSGVSGPLAT
     RLRTSALGLA RDTSPFADTV PAVDARGSHW CVPELVVDVR YLGRGREGRL RQPVVRGLRD
     DATVDPWEQE
//