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Database: UniProt
Entry: I3TCD9_THEC1
LinkDB: I3TCD9_THEC1
Original site: I3TCD9_THEC1 
ID   I3TCD9_THEC1            Unreviewed;       600 AA.
AC   I3TCD9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   28-MAR-2018, entry version 34.
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=TCELL_0002 {ECO:0000313|EMBL:AFK50427.1};
OS   Thermogladius calderae (strain DSM 22663 / VKM B-2946 / 1633).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Thermogladius.
OX   NCBI_TaxID=1184251 {ECO:0000313|EMBL:AFK50427.1, ECO:0000313|Proteomes:UP000005270};
RN   [1] {ECO:0000313|EMBL:AFK50427.1, ECO:0000313|Proteomes:UP000005270}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22663 / VKM B-2946 / 1633
RC   {ECO:0000313|Proteomes:UP000005270};
RX   PubMed=22843584; DOI=10.1128/JB.00894-12;
RA   Mardanov A.V., Kochetkova T.V., Beletsky A.V.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of the hyperthermophilic cellulolytic
RT   Crenarchaeon 'Thermogladius cellulolyticus' 1633.";
RL   J. Bacteriol. 194:4446-4447(2012).
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; CP003531; AFK50427.1; -; Genomic_DNA.
DR   RefSeq; WP_014736678.1; NC_017954.1.
DR   EnsemblBacteria; AFK50427; AFK50427; TCELL_0002.
DR   GeneID; 13012922; -.
DR   KEGG; thg:TCELL_0002; -.
DR   KO; K10747; -.
DR   OMA; WIKYKRD; -.
DR   OrthoDB; POG093Z03L0; -.
DR   BioCyc; TCEL1184251:G1H5J-2-MONOMER; -.
DR   Proteomes; UP000005270; 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; PS00333; DNA_LIGASE_A2; 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:UP000005270};
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:AFK50427.1};
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:UP000005270}.
FT   DOMAIN      337    472       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   ACT_SITE    259    259       N6-AMP-lysine intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     257    257       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     264    264       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     279    279       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     309    309       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     349    349       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     426    426       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
FT   BINDING     432    432       ATP. {ECO:0000256|HAMAP-Rule:MF_00407}.
SQ   SEQUENCE   600 AA;  67052 MW;  AE608C6118CADAF6 CRC64;
     MLADTFESLE SITARTQMVN ILVALLKKTP AEIIDRVVYI IEERLWPDWK GLPELGVAEK
     SIIRAIAVAT GQSDDVVERT AKTLGDLGKA AESLISTVRE KQKRTTSLLS FVTSRRELTV
     SRVYDTFVRI AMAQGEGSKD IKIRLLSGLL AEASPKEARY IVRFAEGKLR LGVGEATLMD
     ALAVAFGGGS FARPIIERAY NLRADLGEVA RVVATKGIEE LKALKPVVGI PIRPMLAERH
     NNPKEILEKV GGVGFVEYKY DGERAQIHKK GDEVVIFSRR LENITHQYPD VVDYVKRGVK
     AEEAIVEGEI VAIDPDTGEF KPFQELMHRK RKHDVMSVVK EIPVRVYLFD LLYLNGVDYT
     VKPLPERRKA LEEVIEKNEG LDIAEYITAK NPVELEKFFM GAISDGAEGV MVKAIHKDSI
     YQAGTRGWLW IKFKRDYRSE MIDTVDLVVV GAFYGRGRRG GKFGALLMAA YNEEKDVFET
     VCKVGSGFTD EDLNQLPDLL KPYIVDKKPA RVVSNIQPDV WVVPKLVAEI IGAELTLSPL
     HTCAVGKVRG DAGISIRFPR FIRWRDDKSP EDATTSNELF EMYKNQLKKI AEKPGEGEAT
//
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