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Database: UniProt/TrEMBL
Entry: L0AEL7_NATGS
LinkDB: L0AEL7_NATGS
Original site: L0AEL7_NATGS 
ID   L0AEL7_NATGS            Unreviewed;       573 AA.
AC   L0AEL7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   25-OCT-2017, entry version 36.
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   OrderedLocusNames=Natgr_0319 {ECO:0000313|EMBL:AFZ71577.1};
GN   ORFNames=C490_12717 {ECO:0000313|EMBL:ELY66634.1};
OS   Natronobacterium gregoryi (strain ATCC 43098 / DSM 3393 / CCM 3738 /
OS   CIP 104747 / JCM 8860 / NBRC 102187 / NCIMB 2189 / SP2).
OC   Archaea; Euryarchaeota; Halobacteria; Natrialbales; Natrialbaceae;
OC   Natronobacterium.
OX   NCBI_TaxID=797304 {ECO:0000313|EMBL:AFZ71577.1, ECO:0000313|Proteomes:UP000010468};
RN   [1] {ECO:0000313|EMBL:AFZ71577.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SP2 {ECO:0000313|EMBL:AFZ71577.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000010468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43098 / CCM 3738 / NCIMB 2189 / SP2
RC   {ECO:0000313|Proteomes:UP000010468};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sproer C.,
RA   Anderson I., Woyke T.;
RT   "Complete sequence of Natronobacterium gregoryi SP2.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000011613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP2 {ECO:0000313|Proteomes:UP000011613};
RA   Becker E.A., Seitzer P., Tritt A., Larsen D., Yao A., Wu D.,
RA   Darling A., Eisen J.A., Facciotti M.T.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:ELY66634.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SP2 {ECO:0000313|EMBL:ELY66634.1};
RX   PubMed=25393412;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I.,
RA   Wu D., Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea
RT   reveals strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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; CP003377; AFZ71577.1; -; Genomic_DNA.
DR   EMBL; AOIC01000089; ELY66634.1; -; Genomic_DNA.
DR   RefSeq; WP_005580165.1; NZ_AOIC01000089.1.
DR   EnsemblBacteria; AFZ71577; AFZ71577; Natgr_0319.
DR   EnsemblBacteria; ELY66634; ELY66634; C490_12717.
DR   GeneID; 14207483; -.
DR   KEGG; nge:Natgr_0319; -.
DR   PATRIC; fig|797304.7.peg.2585; -.
DR   KO; K10747; -.
DR   OMA; ETVCNIG; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000010468; Chromosome.
DR   Proteomes; UP000011613; Unassembled WGS sequence.
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 {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:UP000010468,
KW   ECO:0000313|Proteomes:UP000011613};
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:AFZ71577.1};
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:UP000010468}.
FT   DOMAIN      346    478       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    262    262       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     260    260       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     267    267       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     289    289       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     318    318       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     358    358       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     437    437       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     443    443       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   573 AA;  62387 MW;  AAC23933100CFAD7 CRC64;
     MEFATFADRA AAIEAEPADL AIIEHVQDLL ADTDGDAESG EPRTIEIVAR FVQGRVFPAW
     DSTTLDIGPS ACYEAISRAA GRNVDTNDVE DRLADVGEIG EVAASYEFGG QQGLDAFGAG
     NGSGALTVRE VYDDLVALAA AEGEGSEDRK IDALFGLFNR CSSDEARYLA RLVLSEMRIG
     VGEGTVRDAI AAAFDIPQEH VERALQVSND YGEVARVARD EGLDGLDAMA LEVGRPVQAM
     LAQTGTVTDA LEAWEEAAVE WKYDGARIQL HYDPDGLEEG DGTTRVFSRN MEDVTAALPE
     VVEFAEKTLA VPVILDGEVV AVDDAGDPLP FQEVLKRFRR KHDVAKARED VAVRPVCFDC
     LHADGVDLLE EPLTTRHERL EVVLTGDGRP EDVAGLSLLW LTDDPDEIES IDAEALESGH
     EGIMLKNPES AYSPGRRGKN WRKRKPDVET LDCVVTGAEW GEGRRATFLG TFELSVRNET
     TGELETVGKV ATGITDEQLA ELTELLEPHI ATEEGQEVEI EPAVVFEVGY EEIQSSPTYS
     SGYALRFPRF QAVRDDKAIE GADTLERVER LRS
//
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