ID   I3TMB5_TISMK            Unreviewed;       538 AA.
AC   I3TMB5;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN   OrderedLocusNames=TMO_2065 {ECO:0000313|EMBL:AFK53903.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK53903.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK53903.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK53903.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(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};
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DR   EMBL; CP003236; AFK53903.1; -; Genomic_DNA.
DR   RefSeq; WP_014745581.1; NC_017956.1.
DR   AlphaFoldDB; I3TMB5; -.
DR   STRING; 1110502.TMO_2065; -.
DR   KEGG; tmo:TMO_2065; -.
DR   PATRIC; fig|1110502.3.peg.2127; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_005138_6_2_5; -.
DR   Proteomes; UP000005258; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   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; IPR016059; DNA_ligase_ATP-dep_CS.
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   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   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFK53903.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258}.
FT   DOMAIN          306..436
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   538 AA;  58625 MW;  D50C446AF476BDF8 CRC64;
     MRRFADLLDR LILTPSRTTK LRLIGDYFAH TPDPDRGWAL AALAGTLDLR AARPSAIREL
     IGSRTDPVLF ALSYDYVGDL AETAALMWPE PAATGAGRND PGVRLSEVAE TLAAAPSAAA
     AMRSLAGWLD GLDTTGRWAL LKLATGGLRV GVSAGLAKAA FAAWAKLAPE AVEEVWHGLE
     PPYEALFAWA TGTGPRPDPR GLPHFRSFML ATPAELADLA PLDPSDFRAE WKWDGIRAQM
     VAAGGEIRLY ARSGDEIGRG FPDLLDAWPF GEAAVDGELV VMGPNDQPAP FAELQKRINR
     RTVGAGLLKS LPAHLRLYDL LAKGGVDLRP RPFTERRAAL EALVAAHPSP RFDLSPLVAF
     SSWAELDRLR ADPPAATIEG VMLKRRDTPY LAGRPKGPWF KWKRAPLTLD VVLMYAQRGH
     GRRSSYFSDY TFGVWRDDDT LVPVGKAYSG FTDQELVELD RWIRRNTTER FGPVRAVAPG
     LVLEVAFDSV QPSPRHKSGL ALRFPRIARI RWDKPAAEAD RLETAAGLVA GSPAASVT
//