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Database: UniProt/TrEMBL
Entry: A0A0E3QGB4_9EURY
LinkDB: A0A0E3QGB4_9EURY
Original site: A0A0E3QGB4_9EURY 
ID   A0A0E3QGB4_9EURY        Unreviewed;       568 AA.
AC   A0A0E3QGB4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   25-OCT-2017, entry version 13.
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=MSKOL_2483 {ECO:0000313|EMBL:AKB48260.1};
OS   Methanosarcina sp. Kolksee.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434099 {ECO:0000313|EMBL:AKB48260.1, ECO:0000313|Proteomes:UP000033075};
RN   [1] {ECO:0000313|EMBL:AKB48260.1, ECO:0000313|Proteomes:UP000033075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kolksee {ECO:0000313|EMBL:AKB48260.1,
RC   ECO:0000313|Proteomes:UP000033075};
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; CP009524; AKB48260.1; -; Genomic_DNA.
DR   RefSeq; WP_048156967.1; NZ_CP009524.1.
DR   EnsemblBacteria; AKB48260; AKB48260; MSKOL_2483.
DR   GeneID; 24828046; -.
DR   KEGG; mek:MSKOL_2483; -.
DR   PATRIC; fig|1434099.4.peg.3108; -.
DR   KO; K10747; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000033075; 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 {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:UP000033075};
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:AKB48260.1};
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;  63234 MW;  77E2235E9CDCAB8F CRC64;
     MTSFREFAET CQAIEKISST IDTTSRVADL LKMVDVEELP IATHFIMSEV FPAWSGEQLG
     IGTSLLYVSL SKASGMPVKS IESLIRTTGD IGDTALLILK EKRKNQVTFS SFFEEQPELS
     ITEVYNRFKI ASEASGKGSQ DIKIKNLQFL FNSSTPREAK YISRLALEEL RIGVGEGVVR
     DAIAKAFSVP AGVVEHAFMV TNDLGIVAAT AKEGGVESLE HLGIEINRPI KMMLSQISPD
     IIDDIKEMKE AAIEWKFDGA RIQVHKDGNS VTLFSRKLEN VTNSLPDLVD IVRKHVKAES
     AILDGEAVAV DENGKPRAFQ EILKRFRRKY DVEEKALGIP IQLNLFDIMY LNGKTLIDLP
     LIERRKALES CVESSVEDSK SICVDKQVIT GDLELIEKIY KEALEAGHEG VMVKNPNSIY
     SPGKRGKNWL KKKPLMETLD LVIVGAEWGF GRRANLIGSY TLACYDPENL HYLQIGKVGT
     GLTDDQLKEL TEILAGLMEG GEAGGVFAIR PKVVLEIAFE EIQKSPNYDS GFALRFPRFI
     RIRDDKDPEE ADTIQRIGKV YSQQLKRL
//
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