DNLI_HALVD
ID DNLI_HALVD Reviewed; 585 AA.
AC D4GYZ4;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407};
DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407};
GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407};
GN Synonyms=ligA {ECO:0000303|PubMed:16420348};
GN OrderedLocusNames=HVO_1565 {ECO:0000312|EMBL:ADE02689.1};
GN ORFNames=C498_03180 {ECO:0000312|EMBL:ELY35790.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP DISRUPTION PHENOTYPE, AND GENE NAME.
RX PubMed=16420348; DOI=10.1111/j.1365-2958.2005.04975.x;
RA Zhao A., Gray F.C., MacNeill S.A.;
RT "ATP- and NAD+-dependent DNA ligases share an essential function in the
RT halophilic archaeon Haloferax volcanii.";
RL Mol. Microbiol. 59:743-752(2006).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00407};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00407};
CC -!- DISRUPTION PHENOTYPE: Inactivation renders cells sensitive to DNA
CC damage. Deletion of both ligA and ligN is lethal.
CC {ECO:0000269|PubMed:16420348}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407}.
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DR EMBL; CP001956; ADE02689.1; -; Genomic_DNA.
DR EMBL; AOHU01000028; ELY35790.1; -; Genomic_DNA.
DR RefSeq; WP_004041443.1; NZ_AOHU01000028.1.
DR AlphaFoldDB; D4GYZ4; -.
DR SMR; D4GYZ4; -.
DR STRING; 309800.C498_03180; -.
DR EnsemblBacteria; ADE02689; ADE02689; HVO_1565.
DR EnsemblBacteria; ELY35790; ELY35790; C498_03180.
DR GeneID; 8925424; -.
DR KEGG; hvo:HVO_1565; -.
DR PATRIC; fig|309800.29.peg.615; -.
DR eggNOG; arCOG01347; Archaea.
DR HOGENOM; CLU_005138_6_0_2; -.
DR OMA; WLFEESY; -.
DR OrthoDB; 52275at2157; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
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 Gene3D; 1.10.3260.10; -; 1.
DR Gene3D; 2.40.50.140; -; 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 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; SSF117018; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00574; dnl1; 1.
DR PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..585
FT /note="DNA ligase"
FT /id="PRO_0000430564"
FT ACT_SITE 280
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 285
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 301
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 330
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 370
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
SQ SEQUENCE 585 AA; 62738 MW; 15585C4B5106426F CRC64;
MQFAEFAARA AEIEAEPADL AVVSLLSDLF SDAGDDLPTV ARFVQGRVFP AWDSTTLDIG
PRLCHEAIAR AAGPNVSADD VEDRLADRGE IGAVAASYDF GGQRGLAAFG SGEQDGLTVA
EVDSELRALA AASGSGSEET KLKTLYGLFN RTDPDEARFL ARLVLSEMRI GVGEGTVRDA
VAEAFLVAPA DAAAIRDDDA DAETEAAARE RRNEAIAAVA RALQVSNDYG MVAGLARDEG
EAGLDGVRLE VGRPVQAMLA QAGTAADALG EWGTAAVETK FDGARVQVHR DADGEVSLFS
RNMEDVTDAL PEVVEFVAGA VDDPVILDGE VVAMDDGGEP LPFQEILRRF RRKHDVDRMR
EEVRVELRAF DCLHAAGDDL LADPLAARHD RLTALLGDDS PAVSDLLLSD DPDEIAAYEA
DALDAGHEGI MLKNPDAPYS PGDRGKNWLK RKPDVETLDL VVTGAEWGEG RRAEFLGTFL
LSARVEAESG DDAFETIGKV ATGITDEELA ELTDLLEPEI EREAGKEVDI RPSVVFEVGY
EEIQTSPTYS SGYALRFPRF VTVREDKTAE TADSLDRVER LADSQ
