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Database: UniProt/TrEMBL
Entry: A0A0S3EWK5_9SPHN
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Original site: A0A0S3EWK5_9SPHN 
ID   A0A0S3EWK5_9SPHN        Unreviewed;       834 AA.
AC   A0A0S3EWK5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=ATN00_05035 {ECO:0000313|EMBL:ALR19771.1};
OS   Sphingobium baderi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR19771.1, ECO:0000313|Proteomes:UP000056968};
RN   [1] {ECO:0000313|EMBL:ALR19771.1, ECO:0000313|Proteomes:UP000056968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DE-13 {ECO:0000313|EMBL:ALR19771.1,
RC   ECO:0000313|Proteomes:UP000056968};
RA   Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT   "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT   para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT   Sphingobium baderi DE-13.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; CP013264; ALR19771.1; -; Genomic_DNA.
DR   RefSeq; WP_062062882.1; NZ_CP013264.1.
DR   AlphaFoldDB; A0A0S3EWK5; -.
DR   STRING; 1332080.ATN00_05035; -.
DR   KEGG; sbd:ATN00_05035; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000056968; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   CDD; cd04862; PaeLigD_Pol_like; 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   InterPro; IPR033651; PaeLigD_Pol-like.
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; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING 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:ALR19771.1};
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:UP000056968};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          331..422
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          534..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   834 AA;  91973 MW;  09D65410367D0367 CRC64;
     MADRDALAPY NAKRDFARTR EPKGVLAKKG GNSFVVQKHE ATRLHWDFRL EVDGVLKSWA
     VTKGPSLDPA DRRLAVRTED HPLSYGDFEG IIPKGEYGGG TVMLWDRGTW EPVEGKSAAD
     IDKGHLHFIL HGERMKGEWL LVKMKGRSGE KRENWLLRKI DDDQADTQTV LVDRALTSVL
     TGRSMAQIAA DKKGAQSLAG AKGKAFAQKM QAARDHNAKL KPKARKGAAT LPRFVKPQLA
     TLVDSVPAGN DWLHEIKFDG YRALIAVAGE KVTVFTRSGL DWTEKFGPLV RAMAALALPP
     ALIDGEIVAF GPDGNPSFSA LQAVLKRGHG AEREDAPLSF FAFDLLSLDG ADLKPLSTIE
     RKERLEALLH QAQPPIHVAD HVIGAGETLY RSMCEAGQEG IISKRVDAPY RGERTRSWVK
     VKCTRRQEFI IIGWTKSNAK GRGFRSLLLA QQEGRKLVYK GKVGTGFDAQ GMAHLAEAME
     SLEVEEPPAD VPREDARGAR WIAPKLVAEI AFSEFTGDGR VRHGSFLGLR ADKKAKDVKP
     EKSQTAPAPR SDVKISNRDR VIFPESGQTK GELADYYSRI APLMLPFAAN RPISLVRCPQ
     GRAKKCFFQK HDSGAFGEHV RQVAIQEKDG GSEDYIYVED ADGLLACVQM GTIEFHGWES
     RADAVEKPDR MIFDLDPDEG LDFGAVKRAA RDIHDRLSDI GLVSFAMLSG GKGVHVVVPL
     TPGHDWDSHK DFASRFAQAL SVTEPERFVA TMSKAKRKGR IFIDWLRNQR GSTAILPYSA
     RARAGAPVAV PIGWDEMEEM KDAHPFGIGD AERLIDRADS LKGWGFATQR LPEI
//
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