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Database: UniProt
Entry: A0A0G0RC00_9BACT
LinkDB: A0A0G0RC00_9BACT
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ID   A0A0G0RC00_9BACT        Unreviewed;       578 AA.
AC   A0A0G0RC00;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-MAR-2018, entry version 13.
DE   RecName: Full=Probable 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=UT38_C0002G0021 {ECO:0000313|EMBL:KKR11207.1};
OS   Microgenomates group bacterium GW2011_GWA2_39_19.
OC   Bacteria.
OX   NCBI_TaxID=1618498 {ECO:0000313|EMBL:KKR11207.1, ECO:0000313|Proteomes:UP000034208};
RN   [1] {ECO:0000313|EMBL:KKR11207.1, ECO:0000313|Proteomes:UP000034208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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       ECO:0000256|RuleBase:RU000617}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKR11207.1}.
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DR   EMBL; LBWO01000002; KKR11207.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKR11207; KKR11207; UT38_C0002G0021.
DR   Proteomes; UP000034208; 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   ECO:0000256|RuleBase:RU000617};
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00407};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034208};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00407,
KW   ECO:0000256|RuleBase:RU000617, ECO:0000313|EMBL:KKR11207.1};
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   ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034208}.
FT   DOMAIN      329    451       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    248    248       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     246    246       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     253    253       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     272    272       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     301    301       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     341    341       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     417    417       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     423    423       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   578 AA;  65037 MW;  3362CA70A125E3C0 CRC64;
     MTFSKLSEYL QKLEKTASRN EITQILAGLF KDASSGEIDK ICYLVLGRVA PQYTGIEFNF
     AEKMMIRAIG YAYKKEIETV TEKFKNIGDL GDVAEKFAEQ SKFKSKTSVS EVYDLLRKVA
     AEGGEKSQER KLTLIAELLS EVDPLSARYI ARIPVGKLRL GFSDVSMMDA LSVMEVGDKS
     ARKKIEAAYN VFVDIGKIAQ RIKKEGLTGV EKVDAEPGVP IRPSLAERLP SAEKIVEKMD
     GRFAVEPKLD GFRVQLHVWG SSDKREVKIF SRNLENVTHM YPDLVDAASK LHVKSGIFDG
     EAIGYNSKTG KFVPFQETVQ RKRKYGIEEM AKSIPLKVFV FDSLFLNGKT LLTVPFRERR
     ELMEKELGGE KGDIVLAQHH IVTEADKLRE LFNNCIKDGL EGIVAKKLDA PYRAGGRGYH
     WVKFKKTTEG KITDTIDCVL MGAYRGRGKR AQFGLGAFLI GVPGKGEKYY SISRLGTGLS
     DEQFRQMYKE VEKLKVEDKP NTYEVDKEAE PDVWVRPQLV LEILADEISL SPRHTAGRDK
     SRGYSLRFPR LIRVRDDKNP DQATSVGEIA KLYKIQKG
//
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