DNLI_ARCFU
ID DNLI_ARCFU Reviewed; 555 AA.
AC O29632;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
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}; OrderedLocusNames=AF_0623;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB90616.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000782; AAB90616.1; ALT_INIT; Genomic_DNA.
DR PIR; G69327; G69327.
DR RefSeq; WP_048064635.1; NC_000917.1.
DR PDB; 3GDE; X-ray; 2.30 A; A=1-555.
DR PDBsum; 3GDE; -.
DR AlphaFoldDB; O29632; -.
DR SMR; O29632; -.
DR STRING; 224325.AF_0623; -.
DR EnsemblBacteria; AAB90616; AAB90616; AF_0623.
DR GeneID; 24794226; -.
DR KEGG; afu:AF_0623; -.
DR eggNOG; arCOG01347; Archaea.
DR HOGENOM; CLU_005138_6_0_2; -.
DR OMA; WLFEESY; -.
DR OrthoDB; 52275at2157; -.
DR PhylomeDB; O29632; -.
DR BRENDA; 6.5.1.1; 414.
DR EvolutionaryTrace; O29632; -.
DR Proteomes; UP000002199; 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 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; PS00333; DNA_LIGASE_A2; 1.
DR PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; DNA damage;
KW DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..555
FT /note="DNA ligase"
FT /id="PRO_0000059601"
FT ACT_SITE 249
FT /note="N6-AMP-lysine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 247
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 269
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 337
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 417
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 114..126
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 279..288
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 291..303
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 310..318
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 332..345
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 373..377
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 379..391
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 411..421
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 425..434
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 442..451
FT /evidence="ECO:0007829|PDB:3GDE"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 458..464
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 470..480
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 481..483
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 484..488
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 499..503
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 505..509
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 516..521
FT /evidence="ECO:0007829|PDB:3GDE"
FT STRAND 523..527
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:3GDE"
FT HELIX 539..547
FT /evidence="ECO:0007829|PDB:3GDE"
SQ SEQUENCE 555 AA; 63553 MW; D050FE80B2341EDB CRC64;
MLFAEFAEFC ERLEKISSTL ELTARIAAFL QKIEDERDLY DVVLFITGKV YPPWDERELG
VGIGLLYEAL ENVSGVKRSE IESMIREYGD LGLVAEQLIK KKKMTTLAFE ELTVRKVRET
FDEIASLTGE GSMKRKIMLL TGLYGLATPL EARYLTRLIL NEMRLGVGEG IMRDAIARAF
RADPETVERA YMITNDLGRV AVVAKKEGEE GLRKMKIEIH IPVRMMLAQV AESLESAVRE
MRTAAVEWKF DGSRVQVHWD GSRVTIYSRR LENVTNALPD IVEEIKKSVK PGVILDGEVI
AVKEGKPMPF QHVLRRFRRK HDVAKMVEKI PLEAHFFDIL YHDGECIDLP LRERRKLLES
AVNESEKIKL AKQIVTDSVD EVRKMYDEAI SAGHEGVMIK LPSSPYIPGK RGKNWLKVKA
IMETLDLVVV GGEWGEGKRS HWLSSFELAC LDPVTGKLLK VGRVATGFTE EDLEELTEMF
RPLIVSQQGK KVEFIPKYVF EVAYQEIQKS PKYESGYALR FPRFVRLRDD KDVDEADTIE
RVENLYKLQF EVKRQ
