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Database: UniProt/SWISS-PROT
Entry: DNLI_SULSO
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Original site: DNLI_SULSO 
ID   DNLI_SULSO              Reviewed;         601 AA.
AC   Q980T8;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   05-DEC-2018, entry version 114.
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   Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
OS   P2).
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.,
RA   Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
RA   De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
RA   Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
RA   Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
RA   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.,
RA   Classen S., Tomkinson A.E., Tainer J.A., Ellenberger T.;
RT   "A flexible interface between DNA ligase and PCNA supports
RT   conformational switching and efficient ligation of DNA.";
RL   Mol. Cell 24:279-291(2006).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       Interaction with PCNA enhances ligase activity. DNA polymerase I,
CC       DNA ligase and the flap endonuclease may be constitutively
CC       associated with the PCNA heterotrimer forming a scanning complex
CC       able to couple DNA synthesis and Okazaki fragment maturation.
CC       {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-
CC         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
CC       heterotrimer. {ECO:0000269|PubMed:12535540}.
CC   -!- SUBUNIT: Interacts with the PCNA heterotrimer, probably via
CC       subunit PCNA3. {ECO:0000269|PubMed:12535540,
CC       ECO:0000269|PubMed:17052461}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00407}.
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   PDBsum; 2HIV; -.
DR   PDBsum; 2HIX; -.
DR   ProteinModelPortal; Q980T8; -.
DR   SMR; Q980T8; -.
DR   STRING; 273057.SSO0189; -.
DR   PRIDE; Q980T8; -.
DR   EnsemblBacteria; AAK40535; AAK40535; SSO0189.
DR   GeneID; 27426483; -.
DR   KEGG; sso:SSO0189; -.
DR   PATRIC; fig|273057.12.peg.188; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   InParanoid; Q980T8; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; SSOL273057:G1FZF-196-MONOMER; -.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR   Gene3D; 1.10.3260.10; -; 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   Complete proteome; Direct protein sequencing; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    601       DNA ligase.
FT                                /FTId=PRO_0000059618.
FT   ACT_SITE    260    260       N6-AMP-lysine intermediate.
FT   BINDING     258    258       ATP.
FT   BINDING     265    265       ATP.
FT   BINDING     280    280       ATP.
FT   BINDING     310    310       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     350    350       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     427    427       ATP.
FT   BINDING     433    433       ATP.
FT   MUTAGEN       1     30       Missing: No interaction with PCNA3, no
FT                                stimulation by PCNA heterotrimer.
FT                                {ECO:0000269|PubMed:12535540}.
FT   MUTAGEN     110    111       FL->AA: Impairs interaction with PCNA.
FT                                {ECO:0000269|PubMed:17052461}.
FT   HELIX         4     15       {ECO:0000244|PDB:2HIV}.
FT   HELIX        19     31       {ECO:0000244|PDB:2HIV}.
FT   HELIX        35     37       {ECO:0000244|PDB:2HIV}.
FT   HELIX        38     44       {ECO:0000244|PDB:2HIV}.
FT   TURN         45     47       {ECO:0000244|PDB:2HIV}.
FT   HELIX        52     54       {ECO:0000244|PDB:2HIV}.
FT   HELIX        63     74       {ECO:0000244|PDB:2HIV}.
FT   HELIX        78     88       {ECO:0000244|PDB:2HIV}.
FT   HELIX        91    100       {ECO:0000244|PDB:2HIV}.
FT   HELIX       121    133       {ECO:0000244|PDB:2HIV}.
FT   HELIX       139    153       {ECO:0000244|PDB:2HIV}.
FT   HELIX       156    166       {ECO:0000244|PDB:2HIV}.
FT   HELIX       176    187       {ECO:0000244|PDB:2HIV}.
FT   STRAND      188    190       {ECO:0000244|PDB:2HIV}.
FT   HELIX       191    193       {ECO:0000244|PDB:2HIV}.
FT   HELIX       194    203       {ECO:0000244|PDB:2HIV}.
FT   HELIX       207    217       {ECO:0000244|PDB:2HIV}.
FT   HELIX       219    222       {ECO:0000244|PDB:2HIV}.
FT   STRAND      237    240       {ECO:0000244|PDB:2HIV}.
FT   HELIX       244    250       {ECO:0000244|PDB:2HIV}.
FT   TURN        251    253       {ECO:0000244|PDB:2HIV}.
FT   STRAND      255    260       {ECO:0000244|PDB:2HIV}.
FT   STRAND      262    271       {ECO:0000244|PDB:2HIV}.
FT   STRAND      274    278       {ECO:0000244|PDB:2HIV}.
FT   HELIX       286    288       {ECO:0000244|PDB:2HIV}.
FT   HELIX       290    299       {ECO:0000244|PDB:2HIV}.
FT   STRAND      303    314       {ECO:0000244|PDB:2HIV}.
FT   TURN        316    318       {ECO:0000244|PDB:2HIV}.
FT   HELIX       325    332       {ECO:0000244|PDB:2HIV}.
FT   HELIX       336    342       {ECO:0000244|PDB:2HIV}.
FT   STRAND      345    355       {ECO:0000244|PDB:2HIV}.
FT   HELIX       365    375       {ECO:0000244|PDB:2HIV}.
FT   STRAND      380    384       {ECO:0000244|PDB:2HIV}.
FT   STRAND      387    392       {ECO:0000244|PDB:2HIV}.
FT   HELIX       393    405       {ECO:0000244|PDB:2HIV}.
FT   STRAND      410    414       {ECO:0000244|PDB:2HIV}.
FT   STRAND      427    435       {ECO:0000244|PDB:2HIV}.
FT   HELIX       436    439       {ECO:0000244|PDB:2HIX}.
FT   STRAND      440    442       {ECO:0000244|PDB:2HIX}.
FT   STRAND      444    455       {ECO:0000244|PDB:2HIV}.
FT   HELIX       458    460       {ECO:0000244|PDB:2HIV}.
FT   STRAND      463    473       {ECO:0000244|PDB:2HIV}.
FT   TURN        474    477       {ECO:0000244|PDB:2HIV}.
FT   STRAND      478    485       {ECO:0000244|PDB:2HIV}.
FT   HELIX       491    502       {ECO:0000244|PDB:2HIV}.
FT   STRAND      505    508       {ECO:0000244|PDB:2HIV}.
FT   STRAND      520    523       {ECO:0000244|PDB:2HIV}.
FT   STRAND      528    539       {ECO:0000244|PDB:2HIV}.
FT   TURN        544    548       {ECO:0000244|PDB:2HIV}.
FT   STRAND      554    559       {ECO:0000244|PDB:2HIV}.
FT   STRAND      561    565       {ECO:0000244|PDB:2HIV}.
FT   HELIX       571    573       {ECO:0000244|PDB:2HIV}.
FT   HELIX       577    586       {ECO:0000244|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
//
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