ID I3TMB5_TISMK Unreviewed; 538 AA.
AC I3TMB5;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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; Rhodospirillales;
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 OMA; WLFEESY; -.
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 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
//