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Database: UniProt/TrEMBL
Entry: A0A0E3NE21_METTE
LinkDB: A0A0E3NE21_METTE
Original site: A0A0E3NE21_METTE 
ID   A0A0E3NE21_METTE        Unreviewed;       568 AA.
AC   A0A0E3NE21;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 14.
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   ORFNames=MSTHT_0950 {ECO:0000313|EMBL:AKB12708.1};
OS   Methanosarcina thermophila TM-1.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=523844 {ECO:0000313|EMBL:AKB12708.1, ECO:0000313|Proteomes:UP000066529};
RN   [1] {ECO:0000313|EMBL:AKB12708.1, ECO:0000313|Proteomes:UP000066529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TM-1 {ECO:0000313|EMBL:AKB12708.1,
RC   ECO:0000313|Proteomes:UP000066529};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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: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; CP009501; AKB12708.1; -; Genomic_DNA.
DR   RefSeq; WP_048166836.1; NZ_CP009501.1.
DR   EnsemblBacteria; AKB12708; AKB12708; MSTHT_0950.
DR   GeneID; 24847873; -.
DR   KEGG; mthr:MSTHT_0950; -.
DR   PATRIC; fig|523844.20.peg.1222; -.
DR   KO; K10747; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000066529; 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:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; 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; 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; 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:UP000066529};
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:AKB12708.1};
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}.
FT   DOMAIN      334    466       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    256    256       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     254    254       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     261    261       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     276    276       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     306    306       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     346    346       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     425    425       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     431    431       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   568 AA;  63355 MW;  912E9E8A5D012EEA CRC64;
     MTSFREFSET CQAIEKISST IDTTNRVADF LKKVDVEELP IATHFIMSEV FPAWSGKQLG
     IGISLLYAAL SRASGMSVKS IESLLRTTGD IGDTTLLILK EKRKNQVTFS SFFEEQPELS
     ITEVYNRFKI ASEASGKGSQ DIKIKNLQFL FNSSTPREAK YIARLALEEL RIGVGEGVVR
     DAIAKAFSVP VDVVEHAFMV TNDLGIVAAT AKEGGIEALE RLGIEINRPI RMMLSQISPD
     IAADIREMGE AAIEWKFDGA RLQIHKAGDS VTLFSRKLEN VTNSLPDLVE IIRKHVKAES
     AILDGEAVAV DKNGKPRAFQ EILKRFRRKY HVEEKALGIP IQLNLFDIMY LNGKTLIDLP
     LIERRKALES CVESSTEDSK SICVAKQVIT GDLELIEQIY KEALKAGHEG LMVKNPNSVY
     SPGKRGKNWI KKKPLMETLD LVIVGAEWGF GRRANLIGSY TVACYDPETG RFLQVGKVGT
     GLTDDQLKEL TEMLSDLMEG GEAGGVFAVR PKIVLEIAFE EIQKSPNYNS GFALRFPRFI
     RIRDDKDPEE ADTIQRIEKV YSQQLKRL
//
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