ID   E8V3M5_TERSS            Unreviewed;       630 AA.
AC   E8V3M5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   OrderedLocusNames=AciPR4_3963 {ECO:0000313|EMBL:ADV84712.1};
OS   Terriglobus saanensis (strain ATCC BAA-1853 / DSM 23119 / SP1PR4).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=401053 {ECO:0000313|EMBL:ADV84712.1, ECO:0000313|Proteomes:UP000006844};
RN   [1] {ECO:0000313|EMBL:ADV84712.1, ECO:0000313|Proteomes:UP000006844}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-1853 / DSM 23119 / SP1PR4
RC   {ECO:0000313|Proteomes:UP000006844};
RX   PubMed=23450133; DOI=10.4056/sigs.3036810;
RA   Rawat S.R., Mannisto M.K., Starovoytov V., Goodwin L., Nolan M., Hauser L.,
RA   Land M., Davenport K.W., Woyke T., Haggblom M.M.;
RT   "Complete genome sequence of Terriglobus saanensis type strain SP1PR4(T),
RT   an Acidobacteria from tundra soil.";
RL   Stand. Genomic Sci. 7:59-69(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         ECO:0000256|RuleBase:RU000617};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP002467; ADV84712.1; -; Genomic_DNA.
DR   RefSeq; WP_013570442.1; NC_014963.1.
DR   AlphaFoldDB; E8V3M5; -.
DR   STRING; 401053.AciPR4_3963; -.
DR   KEGG; tsa:AciPR4_3963; -.
DR   eggNOG; COG1793; Bacteria.
DR   HOGENOM; CLU_005138_6_0_0; -.
DR   OrthoDB; 9767858at2; -.
DR   Proteomes; UP000006844; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; IPR000977; DNA_ligase_ATP-dep.
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; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR036599; DNA_ligase_N_sf.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   NCBIfam; TIGR00574; dnl1; 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   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 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; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617};
KW   DNA damage {ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006844}.
FT   DOMAIN          369..527
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          240..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  68879 MW;  6931CDA56D387B40 CRC64;
     MALFLQLAEL ADVLAATSSR LKKRAAIAEG ITAVHAQSPE EAGLFALYLA GQTFPEADPR
     KLNAGGAVLS RIIASISHAA DTAMTEAYRR HGDLGAATHD LFLDAGHNPP PTLTFTDLHD
     AFAQASIART TVIRQIVLTD LLTRAIPVEA KYLIKLMLGD MRIGVKQSLV EEAIAVAAEA
     SLSDVRNAVM LQADLACATE MAFAKTLREA RMRLFHPLGF MLASPVETPE EAVERFAKIP
     VESDASTPPP THVEPDPPSV SEDAYTVTAQ EEISPEAIHI HAQIEDKYDG MRVQLHCGDP
     AQPGRVALYS RNREDVTESY PEIAEAFAHA ESGAMILDGE LLAWDVQQER ALPFAVLSPR
     IGRKRVSNEV RTATPVVFMA FDVLYASDSL LLDLPLRERR NRLEAIAERL LAVTHSPLAL
     PATADTGLFA HDNGAAQTGV QRLLLSPISL AYSAEDLDRA YNAARERGNE GVMIKAADSI
     YQPGRRGISW VKLKRQLGTL DVVITGAEYG HGKRSQFLSD YTFAIRAPEG DLLNVGKAYS
     GVTDAEIVKL TAWLKDHTLE DQGHFRTVEP GIVLEVAFNN VMRSSRHASG FALRFPRILR
     IRTDKPLEEI DTLERVEEIY QSQPDKPAEA
//