UniProt: A0A0B8T8W0

Database: UniProt
Entry: A0A0B8T8W0_9SPHI

LinkDB:  A0A0B8T8W0_9SPHI 
Original site:  A0A0B8T8W0_9SPHI

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (7)   
   Pfam (4)   
   PROSITE (1)   
Literature (1)   
   PubMed (1)   
All databases (24)   

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ID   A0A0B8T8W0_9SPHI        Unreviewed;       837 AA.
AC   A0A0B8T8W0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943};
GN   ORFNames=DI53_1112 {ECO:0000313|EMBL:KGE15114.1};
OS   Sphingobacterium deserti.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1229276 {ECO:0000313|EMBL:KGE15114.1, ECO:0000313|Proteomes:UP000031802};
RN   [1] {ECO:0000313|Proteomes:UP000031802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RA   Teng C., Zhou Z., Li X., Chen M., Lin M., Wang L., Su S., Zhang C.,
RA   Zhang W.;
RT   "Whole-Genome optical mapping and complete genome sequence of
RT   Sphingobacterium deserti sp. nov., a new spaces isolated from desert in the
RT   west of China.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KGE15114.1, ECO:0000313|Proteomes:UP000031802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACCC05744 {ECO:0000313|Proteomes:UP000031802};
RX   PubMed=25830331;
RA   Teng C., Zhou Z., Molnar I., Li X., Tang R., Chen M., Wang L., Su S.,
RA   Zhang W., Lin M.;
RT   "Whole-Genome Optical Mapping and Finished Genome Sequence of
RT   Sphingobacterium deserti sp. nov., a New Species Isolated from the Western
RT   Desert of China.";
RL   PLoS ONE 10:E0122254-E0122254(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGE15114.1}.
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DR   EMBL; JJMU01000019; KGE15114.1; -; Genomic_DNA.
DR   RefSeq; WP_037496400.1; NZ_JJMU01000019.1.
DR   AlphaFoldDB; A0A0B8T8W0; -.
DR   STRING; 1229276.DI53_1112; -.
DR   PATRIC; fig|1229276.3.peg.1150; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000031802; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd04865; LigD_Pol_like_2; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014143; NHEJ_ligase_prk.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; TIGR02776; NHEJ_ligase_prk; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF13298; LigD_N; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KGE15114.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031802};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          326..410
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..24
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   837 AA;  94746 MW;  E1A8248E549D34F8 CRC64;
     MAALEKYNQK RNFEKTKEPK GTLSGKGKKL RFVVQRHHAS RLHYDFRLEM AGVLKSWAVP
     KGPSLDPKDK RLAVMVEDHP LSYRTFEGEI PKGNYGFGTV SIFDEGFYTP LENTDGEREL
     LDALEKGSVK IVLQGKKLKG EFALVRIKNP QDDNAWLLIK HKDKYAVDDG YDAEDEIPKA
     IKEKGESFRK SQSGRSTPKA DRPANKPSAK QKNAASTKDE EASGTILEPM LAVLSENVNE
     DADWIFEQKL DGFRTIAQIT EKNVQLTSRN GINFNSKFPS VVKAFQNFGK SVVLDGEVVA
     EDTKGKSNFQ LLQHGEPLPA KFKLRYHVFD IMMLDGNDLR EFPLLDRKDL LERLFSKILS
     ADVLIVPKLK EDLEQALQQA RKKKWEGVIA KQTDSRYLSG KRSTLWRKLK VQQSQEAIIV
     GFTKPSGSRV GFGALVLAVQ GDQGLVYIGN VGTGFPDDVL REMKKELDKA VVEKKPFPKG
     VVVANEKSVS WVKPQLIAEI EYSEWTTDGH LRHPVFKALR EDKALADIKR VFPIRDVQNE
     RELTFGRKKL KLSNQKKIYW PADQITKGEM LDYYEQLGDF ILPYLKDKPI SMNRFPNGIE
     ASSFFQKDVD KGTGPDWLKT VELESESTGN IVNYLLCNDL PTLLWMANMG SIEINPWLAS
     YRKKNNPTFA VLDLDPNGVD FKEVVAVANT AHDILDEAGI NSFVKTSGST GIHIYIHVAG
     QYDFDVARDF IQMVAELVHE QHPQTTSLER SPSKRKNKIY LDYMQNKRAQ TVVAPYSVRP
     KPGATVSTPL DWAEVNEDLT IQQFTMQTVL ERISTKPDPW KNIFEEKANL KKAIASF
//

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