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Database: UniProt/TrEMBL
Entry: N0BM06_9EURY
LinkDB: N0BM06_9EURY
Original site: N0BM06_9EURY 
ID   N0BM06_9EURY            Unreviewed;       564 AA.
AC   N0BM06;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   28-MAR-2018, entry version 29.
DE   RecName: Full=DNA ligase {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   ORFNames=Asulf_01636 {ECO:0000313|EMBL:AGK61611.1};
OS   Archaeoglobus sulfaticallidus PM70-1.
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales;
OC   Archaeoglobaceae; Archaeoglobus.
OX   NCBI_TaxID=387631 {ECO:0000313|EMBL:AGK61611.1, ECO:0000313|Proteomes:UP000013307};
RN   [1] {ECO:0000313|EMBL:AGK61611.1, ECO:0000313|Proteomes:UP000013307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PM70-1 {ECO:0000313|EMBL:AGK61611.1};
RX   PubMed=23833130;
RA   Stokke R., Hocking W.P., Steinsbu B.O., Steen I.H.;
RT   "Complete Genome Sequence of the Thermophilic and Facultatively
RT   Chemolithoautotrophic Sulfate Reducer Archaeoglobus sulfaticallidus
RT   Strain PM70-1T.";
RL   Genome Announc. 1:e00406-13(2013).
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|HAMAP-Rule:MF_00407}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00407};
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; CP005290; AGK61611.1; -; Genomic_DNA.
DR   RefSeq; WP_015591209.1; NC_021169.1.
DR   EnsemblBacteria; AGK61611; AGK61611; Asulf_01636.
DR   GeneID; 15393271; -.
DR   KEGG; ast:Asulf_01636; -.
DR   KO; K10747; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; ASUL387631:G1HH6-1610-MONOMER; -.
DR   Proteomes; UP000013307; 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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013307};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000313|EMBL:AGK61611.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013307}.
FT   DOMAIN      328    461       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    252    252       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     250    250       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     257    257       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     272    272       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     301    301       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     340    340       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     420    420       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     426    426       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   564 AA;  64154 MW;  379FFA13F09C1000 CRC64;
     MSSITFLEFS EFCDELEKIS STIELSSKIA NFLRNIESDD DIYNIALFLT GRIYPPWDER
     EVGIGVGLVY EALRLTTGLK KREIEEIVKE TGDLGLASEK VLSRKLQTIL FREELTIAYL
     REVFDAMSSL KGEKSQKKKV RMLMDLFSSA SPIEAKYITR LLLGEMRLGV GEGILRDAIA
     KAFNLSADIV ERAYMITNDF GKVAVTAKKE GEEGLKRLKI KPHIPIRMML AQVAESVESA
     VMEMGRVAVE WKFDGTRVQI HYADGRITIY SRRLENVTKA LPDVVEMVKK SVKSGVILDG
     EAIAIKDGKP LPFQNILRRF RRKHRISQAV EKIPITVQVF DILYCDNEIY SGETIDLPLH
     ERRKILENVV KDDGNGLKLA RQEITSDVRR VHEIFDEAIA AGHEGVMLKR PDSLYIPGKR
     GKNWLKIKEV METLDLVVVA GEWGEGKRSH FISSFELACV AENGDLLPVG KVATGFTEDD
     LEELTELFKN EIEYEEGKKV VFKPKYVFEV AYQEIQKSPK YESGYALRFP RFVRLREDKD
     ISEADTIERV GRLYESQFGM KGAR
//
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