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Database: UniProt/SWISS-PROT
Entry: DNLI2_METBF
LinkDB: DNLI2_METBF
Original site: DNLI2_METBF 
ID   DNLI2_METBF             Reviewed;         568 AA.
AC   Q46BA3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   07-NOV-2018, entry version 96.
DE   RecName: Full=DNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_00407};
DE            EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407};
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 2 {ECO:0000255|HAMAP-Rule:MF_00407};
GN   Name=lig2 {ECO:0000255|HAMAP-Rule:MF_00407};
GN   OrderedLocusNames=Mbar_A1899;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/JB.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P.,
RA   Han C.S., Lapidus A., Metcalf W.W., Saunders E., Tapia R.,
RA   Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {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}.
DR   EMBL; CP000099; AAZ70839.1; -; Genomic_DNA.
DR   RefSeq; WP_011306885.1; NC_007355.1.
DR   ProteinModelPortal; Q46BA3; -.
DR   SMR; Q46BA3; -.
DR   STRING; 269797.Mbar_A1899; -.
DR   EnsemblBacteria; AAZ70839; AAZ70839; Mbar_A1899.
DR   GeneID; 3624300; -.
DR   KEGG; mba:Mbar_A1899; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WLFEESY; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000008156; 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; 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.
FT   CHAIN         1    568       DNA ligase 2.
FT                                /FTId=PRO_1000049868.
FT   ACT_SITE    256    256       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     261    261       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     276    276       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     306    306       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     346    346       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     425    425       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     431    431       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   568 AA;  63176 MW;  CF22D6D1E1A08B95 CRC64;
     MTSFREFAET CQAIEKISST IDTTSRVADL LKKVDVEELP IATHFIMSEV FPAWSGEQLG
     IGTSLLYVSL SKASGMPVKS IESLIRTTGD IGDTALLILK EKRKNQVTFS SFFEEQPELS
     ITEVYNRFKI ASEASGKGSQ DIKIKNLQFL FTSSTPREAK YISRLALEEL RIGVGEGVVR
     DAIAKAFSVP VDVVEHAFMV TNDLGIVAAT AKDGGVEALE SLGIEINRPI KMMLSQISPD
     IVADIKEMKE AAIEWKFDGA RVQVHKAGDS VMLFSRKLEN VTNSLPDLVE IIRKHVKAES
     AILDGEAVAV DENGRPRAFQ EILKRFRRKY DVEEKALGIP IQLNLFDIMY LNGKTLIDLP
     LIERRKALES CVESSVEDSK SISVDKQVIT GDLDLIEKIY KEALDAGHEG VMVKNPNSFY
     SPGKRGKNWL KKKPLMETLD LVVVGAEWGF GRRANLLGSY TVACYDPKTL RFLQVGKVGT
     GLTDDQLKEL TEILSGLMEG GEAGGIFAIR PKIVLEIAFE EIQKSPNYDS GFALRFPRFI
     RIRDDKDPEE ADTIQRIGKV YSQQLKRL
//
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