ID D5U042_THEAM Unreviewed; 611 AA.
AC D5U042;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=Tagg_0212 {ECO:0000313|EMBL:ADG90492.1};
OS Thermosphaera aggregans (strain DSM 11486 / M11TL).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Thermosphaera.
OX NCBI_TaxID=633148 {ECO:0000313|EMBL:ADG90492.1, ECO:0000313|Proteomes:UP000002376};
RN [1] {ECO:0000313|EMBL:ADG90492.1, ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX PubMed=21304709;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [2] {ECO:0000313|Proteomes:UP000002376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11486 / M11TL {ECO:0000313|Proteomes:UP000002376};
RX DOI=10.4056/sigs.821804;
RA Spring S., Rachel R., Lapidus A., Davenport K., Tice H., Copeland A.,
RA Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.C., Brettin T.,
RA Detter J.C., Tapia R., Han C., Heimerl T., Weikl F., Brambilla E.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain
RT (M11TLT).";
RL Stand. Genomic Sci. 2:245-259(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 11486;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Spring S., Lapidus A., Munk C., Schroeder M., Glavina Del Rio T., Tice H.,
RA Copeland A., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.-J.,
RA Jeffries C.C., Brettin T., Detter J.C., Tapia R., Han C., Chain P.,
RA Heimerl T., Weik F., Goker M., Rachel R., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Thermosphaera aggregans type strain (M11TL).";
RL Submitted (FEB-2010) 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;
CC Evidence={ECO:0000256|HAMAP-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; CP001939; ADG90492.1; -; Genomic_DNA.
DR RefSeq; WP_013129085.1; NC_014160.1.
DR AlphaFoldDB; D5U042; -.
DR STRING; 633148.Tagg_0212; -.
DR GeneID; 9165224; -.
DR KEGG; tag:Tagg_0212; -.
DR eggNOG; arCOG01347; Archaea.
DR HOGENOM; CLU_005138_6_0_2; -.
DR OrthoDB; 31274at2157; -.
DR Proteomes; UP000002376; 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; 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|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}; Reference proteome {ECO:0000313|Proteomes:UP000002376}.
FT DOMAIN 347..482
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT ACT_SITE 269
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT BINDING 436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
FT BINDING 442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407"
SQ SEQUENCE 611 AA; 69069 MW; 08B43B1565372D8B CRC64;
MSQVQRDLPF RVIVDFFKKL ETTTARTQLT AILVNLFKQT PPDVIDKVVY LIQARLWPDW
KGLPELGIAE KLLIKAISLS TNSSEKVVEE ILKSKGDAGL AVEALKTRSL EKSKGVTLFT
FAEKKQELTV NKVYEVLTRI ALAQGEGSKD LKIRLLAGLL SDANPEEAKY IVRFVEGKLR
LGIGDATIMD ALSIVYAGGA HLRPLIERAY NLRADLGEVA KILASQGVEA IKQITPMVGI
PIRPMLAERL SDPKEILEKV EGEAFVEFKY DGERAQIHKD GNKIVIYSRR LENITHQYPD
VVEMALKNIK AEKAILEGEI VAYDPSTGEL KPFQELMHRK RKYDIHVAVK ENPVKVFLFD
LLYEEGVDYT VKRLIERRKR LEEIIVQTEE FRVAEYIRTS DPGELEKFFL QAISEGAEGV
MVKALHEGSV YQAGTRGWLW IKFKRDYRSE MVDTVDLVVV GAFYGRGRRG GKFGTLLMAS
YNPSNDTFET VCKVGSGFTD EDLDKIPELL KPFIRDRKPL RVVAEMEPDV WVEPALVAEI
IGAELTLSPI HTCAYGKIKP EAGISIRFPR FIRWRDDKKP EDATTSDELV EMYKLQLKRI
GEKVAQPGEE T
//
