GenomeNet

Database: UniProt
Entry: A8AB20
LinkDB: A8AB20
Original site: A8AB20 
ID   DNLI_IGNH4              Reviewed;         594 AA.
AC   A8AB20;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   23-MAY-2018, entry version 71.
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=Igni_0942;
OS   Ignicoccus hospitalis (strain KIN4/I / DSM 18386 / JCM 14125).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Ignicoccus.
OX   NCBI_TaxID=453591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIN4/I / DSM 18386 / JCM 14125;
RX   PubMed=19000309; DOI=10.1186/gb-2008-9-11-r158;
RA   Podar M., Anderson I., Makarova K.S., Elkins J.G., Ivanova N.,
RA   Wall M.A., Lykidis A., Mavromatis K., Sun H., Hudson M.E., Chen W.,
RA   Deciu C., Hutchison D., Eads J.R., Anderson A., Fernandes F.,
RA   Szeto E., Lapidus A., Kyrpides N.C., Saier M.H. Jr., Richardson P.M.,
RA   Rachel R., Huber H., Eisen J.A., Koonin E.V., Keller M., Stetter K.O.;
RT   "A genomic analysis of the archaeal system Ignicoccus hospitalis-
RT   Nanoarchaeum equitans.";
RL   Genome Biol. 9:R158.1-R158.18(2008).
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; CP000816; ABU82122.1; -; Genomic_DNA.
DR   RefSeq; WP_012123086.1; NC_009776.1.
DR   ProteinModelPortal; A8AB20; -.
DR   SMR; A8AB20; -.
DR   STRING; 453591.Igni_0942; -.
DR   PRIDE; A8AB20; -.
DR   EnsemblBacteria; ABU82122; ABU82122; Igni_0942.
DR   GeneID; 5562329; -.
DR   KEGG; iho:Igni_0942; -.
DR   eggNOG; arCOG01347; Archaea.
DR   eggNOG; COG1793; LUCA.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; IHOS453591:G1G9W-974-MONOMER; -.
DR   Proteomes; UP000000262; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
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-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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    594       DNA ligase.
FT                                /FTId=PRO_1000049867.
FT   ACT_SITE    258    258       N6-AMP-lysine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     256    256       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     263    263       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     279    279       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     309    309       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     349    349       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     426    426       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
FT   BINDING     432    432       ATP. {ECO:0000255|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   594 AA;  66459 MW;  2AB8030EEC27B803 CRC64;
     MKFSDVVDAL ERLERTTSRT QIVAILTNLF KKVIEENKDI IDKVVYFIQG KLWPDWYGYP
     EIGIGEKGII KAISLAANVK EKEVEGLYKQ LGDLGLVAER LMAKAPKGGL MMFVKKKEEL
     TFEKVYETLK RIAFMQGEGS RDLKIKTLAG LLKEASPKEA KYIVRFVQGK LRLGVGDASI
     IEALAHVAGT TKDVVERAYN LRADLGAVAK IAVTEGPEAL KRVRPKPGVP VRPMLAERLN
     DPKEILKKLG GKGLAEYKYD GERAQIHLLP DGKVVIFSRR LENITRSYPD VVQYAKSGLK
     AKEAIVEGEI IAVNPETGEP RPFQELMRRR RKHDVALAMS EIPVNVKLFD IIYVDGEDMT
     NKPLPLRRKR LEEVVEESEE FSLSTAKLVS TPEELEQFFH QSISEGHEGL VVKAVHDKSV
     YQAGARGWLW IKYKKDYKSE MVEPVDLVVV GAFYGRGRRG GTFGALLVAG YDEKRDAFAT
     VCKVGSGFSD EELARLPELL KPYISETKPP RVISNVKPDV WVRPALVAEI IGAEITLSPI
     HTCAKDEVSA GSGLAIRFPR FIRWRPDKGP EDATTCGEIV EMYKSRLKKV EEPT
//
DBGET integrated database retrieval system