ID I4EVU7_9ACTN Unreviewed; 489 AA.
AC I4EVU7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
GN OrderedLocusNames=MODMU_2075 {ECO:0000313|EMBL:CCH87510.1};
OS Modestobacter marinus.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Modestobacter.
OX NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH87510.1, ECO:0000313|Proteomes:UP000006461};
RN [1] {ECO:0000313|EMBL:CCH87510.1, ECO:0000313|Proteomes:UP000006461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BC501 {ECO:0000313|EMBL:CCH87510.1,
RC ECO:0000313|Proteomes:UP000006461};
RX PubMed=22887672; DOI=10.1128/JB.01029-12;
RA Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT a Representative Actinobacterium That Thrives on Calcareous Stone
RT Surfaces.";
RL J. Bacteriol. 194:4773-4774(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; FO203431; CCH87510.1; -; Genomic_DNA.
DR RefSeq; WP_014740105.1; NC_017955.1.
DR AlphaFoldDB; I4EVU7; -.
DR STRING; 477641.MODMU_2075; -.
DR KEGG; mmar:MODMU_2075; -.
DR PATRIC; fig|477641.3.peg.1967; -.
DR eggNOG; COG1793; Bacteria.
DR HOGENOM; CLU_008325_2_0_11; -.
DR OMA; QWLAHRM; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000006461; 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; IPR014144; LigD_PE_domain.
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 Pfam; PF13298; LigD_N; 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:CCH87510.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006461}.
FT DOMAIN 281..399
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 53431 MW; 94DF9B804D3AF243 CRC64;
MAPPDPLATY RAKRDPARTA EPVPAADQPL PVGDDDTFVV QEHHTPRGRT GQRVHWDLRL
ERDGVLKSWA VPKGPPTEPG VNRLAVPTED HPLEYASFAG TITAGEYGGG QVSIWDAGRY
ATEKWADDHV TVSFDGRRLS GRYVVFRLPD GTWNVRKLDA DPVVDAPVAA GVPEDLTPML
AAIGELPRAD DPRWGYEFKW DGVRALAHVR GGRVRLRARS GNDVTATYPE LHRLPEVLSG
HDAVVDGEVV ALDGRGRPDF GLLQGRMHRT GPEVARMAAA APVTYLVFDL LALDGENLLG
LPYTERRERL DALGLASDRW VTTPWFRGNG EQVQAASLEN GLEGVVAKRL DSVYRPGGRG
PDWRKVKNLR TQSVVVGGWR PGEGRRAGGI GSLLVGVHDD TGRLVFAGHV GTGFTARALA
DLAPLLTPRA TPPFADALPR EVTRDARWVE PLLVGEVRYG EWTREGRLRH PAWRGLRDDV
AAADVVVEP
//