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Database: UniProt/SWISS-PROT
Entry: DNLI_CENSY
LinkDB: DNLI_CENSY
Original site: DNLI_CENSY 
ID   DNLI_CENSY              Reviewed;         589 AA.
AC   A0RWD6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   05-DEC-2018, entry version 66.
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=CENSYa_1021;
OS   Cenarchaeum symbiosum (strain A).
OC   Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX   NCBI_TaxID=414004;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A;
RX   PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA   Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA   Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT   "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT   symbiosum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(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:
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK77653.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; DP000238; ABK77653.1; ALT_INIT; Genomic_DNA.
DR   ProteinModelPortal; A0RWD6; -.
DR   SMR; A0RWD6; -.
DR   EnsemblBacteria; ABK77653; ABK77653; CENSYa_1021.
DR   KEGG; csy:CENSYa_1021; -.
DR   PATRIC; fig|414004.10.peg.943; -.
DR   HOGENOM; HOG000036008; -.
DR   KO; K10747; -.
DR   Proteomes; UP000000758; 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; Reference proteome.
FT   CHAIN         1    589       DNA ligase.
FT                                /FTId=PRO_0000365244.
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   589 AA;  65183 MW;  862D43048CA15D39 CRC64;
     MQFSVLAGSL EKMESTAKRL ELTGILEELL RETPHEVIAQ IVYLIQGKLR PEFEGIELGV
     AEKLAVRAVS KSSGMPAARI EAAYRRDGDL GRAASSILEQ KTQTTFLAEE ITVERVYDTL
     MRIARLEGAR SQDMKMRHIS SLLNDASPRD ACYILKLILG TLRLGIAENT VMDALAAAFT
     GSKSNRPELE RAYNVSSDLG RVAEAVSSGG LEAVRGFAVA VFSPIRPMLA DRVRSESEAL
     EKMGAGLAAE YKLDGERVQV HLSGGRVELF SRSLENITAY YPDIVERIPG RLRAREAVLE
     AEAVAVNEET GEFLPFQELM HRRRKYDIDK AVMRYPITVN FFDILYLDGR DCLGISYSER
     RALLEGVVDE DSFARCVPVS TIPDESALED SLENSINAGC EGLMLKLPDA PYRAGSRGGY
     WLKLKREYRN ELGDSLDLVI IGAFFGKGRR TGRYGTLLLA TYDDSRDTFP SICKVGTGFT
     DEDLDQLYQL LSPRVTLKRN PRIDSGMEAD VWFDPEVVME VVASEITLSP VHKTALDSVR
     KGAGLALRFP KFTGKLRTEK TAEDASTDQE VIALYKSQKK VVPDGQPGV
//
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