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Database: UniProt/TrEMBL
Entry: A0A0E3SB80_9EURY
LinkDB: A0A0E3SB80_9EURY
Original site: A0A0E3SB80_9EURY 
ID   A0A0E3SB80_9EURY        Unreviewed;       568 AA.
AC   A0A0E3SB80;
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=MSHOH_2566 {ECO:0000313|EMBL:AKB79049.1};
OS   Methanosarcina horonobensis HB-1 = JCM 15518.
OC   Archaea; Euryarchaeota; Methanomicrobia; Methanosarcinales;
OC   Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434110 {ECO:0000313|EMBL:AKB79049.1, ECO:0000313|Proteomes:UP000033101};
RN   [1] {ECO:0000313|EMBL:AKB79049.1, ECO:0000313|Proteomes:UP000033101}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HB-1 {ECO:0000313|EMBL:AKB79049.1,
RC   ECO:0000313|Proteomes:UP000033101};
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; CP009516; AKB79049.1; -; Genomic_DNA.
DR   RefSeq; WP_048140426.1; NZ_CP009516.1.
DR   EnsemblBacteria; AKB79049; AKB79049; MSHOH_2566.
DR   GeneID; 24831857; -.
DR   KEGG; mhor:MSHOH_2566; -.
DR   PATRIC; fig|1434110.4.peg.3298; -.
DR   KO; K10747; -.
DR   OrthoDB; POG093Z03L0; -.
DR   Proteomes; UP000033101; 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:UP000033101};
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:AKB79049.1};
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;  63230 MW;  421099C05540758A CRC64;
     MTSFREFAET CQAIEKTSST IETTNKVADL LKKVDVEELP LATHFIMSEV FPAWSGQQLG
     IGTSLLYVSL SKASGMSIHS IESLIRTTGD IGDTALLILK EKRKNQVTFS SFLEEQSELS
     ITEVYRRFKT ASEASGKGSQ DVKVKNLQFL FTSSTPREAK YISRLALEEL RIGVGEGVVR
     DAIAKAFLVP AEIVEHSFMV TNDLGIVAAA AKKGGIEALE SLGIEINRPI KMMLSQISPD
     IDADIRDMKE AAIEWKFDGA RVQIHKNGDS VSLFSRKLEN VTNSLPDIVE IVRKHIKAES
     AILDGEAVAV DEDGKPRAFQ EILKRFRRKY DVKEKVLGIP IQLNLFDIMY LNGKTLIDLP
     LLERRKALES CVESSVEDSK SICVDKQVIT GDLELVEKIY REALKAGHEG VMVKNPTSVY
     SPGKRGKNWL KKKPLMDTLD LVIVGAEWGF GRRANLIGSY TVACYDPETS RFLQVGKVGT
     GLTDEQLKEL TEILSGLMEG GEAGGVFAIR PKVVLEIAFE EIQKSPNYDS GFSLRFPRFI
     RIRDDKDPEE ADTIQRIGRV YSQQLKRL
//
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