ID   F2L2N0_THEU7            Unreviewed;       594 AA.
AC   F2L2N0;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=DNA ligase {ECO:0000256|ARBA:ARBA00013308, ECO:0000256|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407};
GN   Name=lig {ECO:0000256|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=TUZN_1611 {ECO:0000313|EMBL:AEA13078.1};
OS   Thermoproteus uzoniensis (strain 768-20).
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Thermoproteus.
OX   NCBI_TaxID=999630 {ECO:0000313|EMBL:AEA13078.1, ECO:0000313|Proteomes:UP000008138};
RN   [1] {ECO:0000313|EMBL:AEA13078.1, ECO:0000313|Proteomes:UP000008138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=768-20 {ECO:0000313|EMBL:AEA13078.1,
RC   ECO:0000313|Proteomes:UP000008138};
RX   PubMed=21478349; DOI=10.1128/JB.00409-11;
RA   Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of the thermoacidophilic crenarchaeon
RT   Thermoproteus uzoniensis 768-20.";
RL   J. Bacteriol. 193:3156-3157(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=768-20;
RA   Mardanov A.V., Gumerov V.M., Beletsky A.V., Prokofeva M.I.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of the thermoacidophilic crenarchaeon
RT   Thermoproteus uzoniensis 768-20.";
RL   Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC       replication, DNA recombination and DNA repair. {ECO:0000256|HAMAP-
CC       Rule:MF_00407}.
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|HAMAP-Rule:MF_00407};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|HAMAP-Rule:MF_00407,
CC       ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP002590; AEA13078.1; -; Genomic_DNA.
DR   RefSeq; WP_013680413.1; NC_015315.1.
DR   AlphaFoldDB; F2L2N0; -.
DR   STRING; 999630.TUZN_1611; -.
DR   GeneID; 10361131; -.
DR   KEGG; tuz:TUZN_1611; -.
DR   eggNOG; arCOG01347; Archaea.
DR   HOGENOM; CLU_005138_6_0_2; -.
DR   OrthoDB; 31274at2157; -.
DR   Proteomes; UP000008138; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1.
DR   CDD; cd07969; OBF_DNA_ligase_I; 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   HAMAP; MF_00407; DNA_ligase; 1.
DR   InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc.
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:SF9; DNA LIGASE 3; 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; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00407};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00407}.
FT   DOMAIN          333..466
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   ACT_SITE        255
FT                   /note="N6-AMP-lysine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         253
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         275
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         305
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         345
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         420
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT   BINDING         426
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
SQ   SEQUENCE   594 AA;  65973 MW;  853AA43A566CE3AD CRC64;
     MEFSELAKVL ASIESTTQRT TMVRLLVGLF KKLEPAEIDK AIYIILGDLR PPWEGLELGV
     GEKLCIRAIA RASGAKADEI EELYKKTGDM GEAARRALSR RQAQTLLAFA GGRKAGLSIS
     QVYDTLFKVA KASGEGSQDL KISLLSSLFS QLSPDEAKYV ARFVVGRLRL GVADMTVIDA
     LAEAFGVPEE ALERAYNVRP DLGFLGKLVA ERGAAGLAEV RITPGVPVMP MLAQRLSTSR
     EILAKLGGAA ICEYKYDGER AQIHVSPDGV AIYSRRLENI THAYPDVVES VRKSVSAREA
     VLEGEIVAVD PDTGDLLPFQ ELMHRKRKHE VEEAVKEYPA KLNLFDLLYL DGEDLTDKPL
     MYRRLKLSEI VEEGEDVVIA KWALFDDEEK VDVFFHEAIS MGMEGLVCKS PTSVYEMGAR
     GWNWIKYKRD YRSEMSDTVD LVVVGAFYGR GKRAGLYGAF LTAAYDPKTD TFYTVCKVGS
     GFTDADLKKM YQMLEPYKID HRHPRVSSRM EPDVWFTPGV VLEIIGAEIT LSPLHTCCLG
     AVRPDVGLAI RFPRFTGRYR TDKSPEEATT VDELLEMYKS QKKVKVEQGP EAAP
//