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Database: UniProt/SWISS-PROT
Entry: DNLI_NITMS
LinkDB: DNLI_NITMS
Original site: DNLI_NITMS 
ID   DNLI_NITMS              Reviewed;         588 AA.
AC   A9A3K1;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   05-DEC-2018, entry version 76.
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   OrderedLocusNames=Nmar_1037;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Stahl D., Richardson P.;
RT   "Complete sequence of Nitrosopumilus maritimus SCM1.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA
CC       during DNA replication, DNA recombination and DNA repair.
CC       {ECO:0000255|HAMAP-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-
CC         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}.
DR   EMBL; CP000866; ABX12933.1; -; Genomic_DNA.
DR   ProteinModelPortal; A9A3K1; -.
DR   SMR; A9A3K1; -.
DR   STRING; 436308.Nmar_1037; -.
DR   EnsemblBacteria; ABX12933; ABX12933; Nmar_1037.
DR   KEGG; nmr:Nmar_1037; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   Proteomes; UP000000792; 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   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA replication; Ligase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    588       DNA ligase.
FT                                /FTId=PRO_0000365263.
FT   ACT_SITE    252    252       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     250    250       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     257    257       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     272    272       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     302    302       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     342    342       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     417    417       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     423    423       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   588 AA;  66661 MW;  60A94750BF81C85B CRC64;
     MEFSILADSF NKMESTRKRL ELTQYLVELF KKTPQEVISK IVYLLQGKLR PDFEGVELGV
     AEKLAIRAIS KSSGIPIKKI EEEYRKGGDL GHAATTILEQ KTQTTFLVED ITVERVYETL
     FKIAKLEGNR SQDMKMKYIS SLLNDASPLE ASFILKILLG TLRLGIAENT VMDALALAFS
     GNKENRKILE HAYNVSSDLG KVAEVLATEG LAEVEKFKII LFNPIRPMLA DRVKSEQEAI
     EKMGNEFAAE YKLDGERVQL HIEGDKVVLF SRSLENISSY YPDIIEKIPK TIQAENIVLE
     AEAVAINENT GEFLPFQELM HRRRKYKIEK AVTQYPITVN LFDILYCNGK SCLELDYKER
     REKMEKVVKE DDFVKHIPMA IVKNENDIED FFENSINAGS EGLMLKTLVS PYQAGSRGSH
     WLKLKREYQN ELGDSLDLVV IGGFFGKGRR TGNYGTLLLA TYEEDEDTFT SICKVGTGFS
     DEDLDQLYQI LNPKVTIKKN PRINSEMEAD VWFEPELVIE VVASEITLSP IHKAARDKIR
     KGAGLALRFP KFTGKMRVEK MAEDASTNEE VITLYQGQKK VAHDKSLM
//
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