DNLI_SACS2
ID DNLI_SACS2 Reviewed; 601 AA.
AC Q980T8;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
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=SSO0189;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, INTERACTION WITH PCNA3, SUBUNIT, AND
RP MUTAGENESIS OF 1-MET--LEU-30.
RX PubMed=12535540; DOI=10.1016/s1097-2765(02)00824-9;
RA Dionne I., Nookala R.K., Jackson S.P., Doherty A.J., Bell S.D.;
RT "A heterotrimeric PCNA in the hyperthermophilic archaeon Sulfolobus
RT solfataricus.";
RL Mol. Cell 11:275-282(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEXES WITH ATP AND PCNA,
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, MUTAGENESIS OF 110-PHE-LEU-111, AND
RP COFACTOR.
RX PubMed=17052461; DOI=10.1016/j.molcel.2006.08.015;
RA Pascal J.M., Tsodikov O.V., Hura G.L., Song W., Cotner E.A., Classen S.,
RA Tomkinson A.E., Tainer J.A., Ellenberger T.;
RT "A flexible interface between DNA ligase and PCNA supports conformational
RT switching and efficient ligation of DNA.";
RL Mol. Cell 24:279-291(2006).
CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC replication, DNA recombination and DNA repair. Interaction with PCNA
CC enhances ligase activity. DNA polymerase I, DNA ligase and the flap
CC endonuclease may be constitutively associated with the PCNA
CC heterotrimer forming a scanning complex able to couple DNA synthesis
CC and Okazaki fragment maturation. {ECO:0000269|PubMed:12535540}.
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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:17052461};
CC -!- ACTIVITY REGULATION: Ligase activity stimulated by PCNA heterotrimer.
CC {ECO:0000269|PubMed:12535540}.
CC -!- SUBUNIT: Interacts with the PCNA heterotrimer, probably via subunit
CC PCNA3. {ECO:0000269|PubMed:12535540, ECO:0000269|PubMed:17052461}.
CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC {ECO:0000255|HAMAP-Rule:MF_00407}.
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DR EMBL; AE006641; AAK40535.1; -; Genomic_DNA.
DR PIR; H90159; H90159.
DR RefSeq; WP_009990427.1; NC_002754.1.
DR PDB; 2HIV; X-ray; 2.05 A; A=1-601.
DR PDB; 2HIX; X-ray; 2.87 A; A=1-601.
DR PDB; 7RPO; EM; 4.16 A; E=1-601.
DR PDB; 7RPW; EM; 4.38 A; E=1-601.
DR PDB; 7RPX; EM; 4.20 A; E=1-601.
DR PDBsum; 2HIV; -.
DR PDBsum; 2HIX; -.
DR PDBsum; 7RPO; -.
DR PDBsum; 7RPW; -.
DR PDBsum; 7RPX; -.
DR AlphaFoldDB; Q980T8; -.
DR SMR; Q980T8; -.
DR STRING; 273057.SSO0189; -.
DR EnsemblBacteria; AAK40535; AAK40535; SSO0189.
DR GeneID; 44129158; -.
DR KEGG; sso:SSO0189; -.
DR PATRIC; fig|273057.12.peg.188; -.
DR eggNOG; arCOG01347; Archaea.
DR HOGENOM; CLU_005138_6_0_2; -.
DR InParanoid; Q980T8; -.
DR OMA; WIKYKRD; -.
DR PhylomeDB; Q980T8; -.
DR BRENDA; 6.5.1.1; 6163.
DR EvolutionaryTrace; Q980T8; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
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:0006266; P:DNA ligation; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
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;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW DNA replication; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..601
FT /note="DNA ligase"
FT /id="PRO_0000059618"
FT ACT_SITE 260
FT /note="N6-AMP-lysine intermediate"
FT BINDING 258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 350
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407"
FT BINDING 427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MUTAGEN 1..30
FT /note="Missing: No interaction with PCNA3, no stimulation
FT by PCNA heterotrimer."
FT /evidence="ECO:0000269|PubMed:12535540"
FT MUTAGEN 110..111
FT /note="FL->AA: Impairs interaction with PCNA."
FT /evidence="ECO:0000269|PubMed:17052461"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 38..44
FT /evidence="ECO:0007829|PDB:2HIV"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 78..88
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 121..133
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 176..187
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:2HIV"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 255..260
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 262..271
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 303..314
FT /evidence="ECO:0007829|PDB:2HIV"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 325..332
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 345..355
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 365..375
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 393..405
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 410..414
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 436..439
FT /evidence="ECO:0007829|PDB:2HIX"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:2HIX"
FT STRAND 444..455
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 463..473
FT /evidence="ECO:0007829|PDB:2HIV"
FT TURN 474..477
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 478..485
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 491..502
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 505..508
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 520..523
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 528..539
FT /evidence="ECO:0007829|PDB:2HIV"
FT TURN 544..548
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 554..559
FT /evidence="ECO:0007829|PDB:2HIV"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:2HIV"
FT HELIX 577..586
FT /evidence="ECO:0007829|PDB:2HIV"
SQ SEQUENCE 601 AA; 67733 MW; DA6814F4A6F0546E CRC64;
MEFKVIAEYF DKLEKISSRL QLTALLADLL SKSDKTIIDK VVYIIQGKLW PDFLGYPELG
IGEKFLIKAI SIATNTDENS VENLYKTIGD LGEVARRLKS KQQSTGILGF LGTTSKESLT
VDEVYSTLSK VALTTGEGSR DLKIRLLAGL LKKADPLEAK FLVRFVEGRL RVGIGDATVL
DAMAIAFGGG QSASEIIERA YNLRADLGNI AKIIVEKGIE ALKTLKPQVG IPIRPMLAER
LSNPEEILKK MGGNAIVDYK YDGERAQIHK KEDKIFIFSR RLENITSQYP DVVDYVSKYI
EGKEFIIEGE IVAIDPESGE MRPFQELMHR KRKSDIYEAI KEYPVNVFLF DLMYYEDVDY
TTKPLEARRK LLESIVKPND YVKIAHHIQA NNVEDLKSFF YRAISEGGEG VMVKAIGKDA
IYQAGARGWL WIKLKRDYQS EMADTVDLVV VGGFYGKGKR GGKISSLLMA AYNPKTDSFE
SVCKVASGFS DEQLDELQKK LMEIKRDVKH PRVNSKMEPD IWVEPVYVAE IIGSEITISP
LHTCCQDVVE KDAGLSIRFP RFIRWRDDKS PEDATTTDEI LEMYNKQPKK KIESPAVDES
V
