ID   F4CFH6_SPHS2            Unreviewed;       905 AA.
AC   F4CFH6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
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   OrderedLocusNames=Sph21_2578 {ECO:0000313|EMBL:ADZ79129.1};
OS   Sphingobacterium sp. (strain 21).
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ79129.1};
RN   [1] {ECO:0000313|EMBL:ADZ79129.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=21 {ECO:0000313|EMBL:ADZ79129.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA   Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT   "Complete sequence of Sphingobacterium sp. 21.";
RL   Submitted (MAR-2011) 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; CP002584; ADZ79129.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4CFH6; -.
DR   STRING; 743722.Sph21_2578; -.
DR   KEGG; shg:Sph21_2578; -.
DR   PATRIC; fig|743722.3.peg.2763; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_2_10; -.
DR   OrthoDB; 9802472at2; -.
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; IPR016059; DNA_ligase_ATP-dep_CS.
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; PS00333; DNA_LIGASE_A2; 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:ADZ79129.1};
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   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          343..477
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          192..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  103105 MW;  0715E0840A4F9F80 CRC64;
     MPLDQYRNKR DFKKTSEPKS GKSPNRKQLT FVVQKHKASR LHYDFRLEMD GVLKSWAVPK
     GPSTDPQNKR LAMMVEDHPM DYRQFEGIIP KGQYGGGTVI VWDEGTYEPI EGLKSKKAQE
     KHLLEQLHKG SLKIRLHGHK LKGEYALVKT QGMGENGWLL IKHKDEFASK SDITKKDKSV
     LSDKALEEIE KSSNKVWQNG REKTVEKSRK TTQAKKSKNA DEHLADDVNE AGEPQKMDVP
     SLLKKAPEST IPKSIKPMKA TLIDEPFDDP DWLYEVKWDG YRAIAKVSKT DVKLISRNNI
     PFDKYYPLVD LLKGWRINAV IDGEIVVLDE KGLSDFGALQ NWRSEADGNL VYYVFDILWY
     EGKNLMGLPL VERQAILQDI LPTDDDRIRQ SKVFAARGID FFDAAEQVGL EGIIAKKADS
     KYTSDLRSKE WLKIKVQRRQ EVVIAGFTRN EGTSKAFSAL VMGVYDGKKL RYAGKVGTGF
     SDSKQKEMMK LFKPLITDRS PFDVEPDVDK PSRFRPQRLG AKPTWLKPEL VCEVNYAEVT
     SEGIFRQASF KGMREDKEAD DVVLEKAADT ESTVAEVEEE DKGTKHAIKP AKTERRTLLN
     PREETQTRKV NGKELKFTHL SKVYWPDDGI TKRDMFNYYY RIAEFILPYL KDRPMSLNRF
     PNGIKGPSFY QKDVKGKVPE WVSKTYPYTT SEGEHKEYLV GDDEATLLWM ASLGCIEMNP
     WFSRVQSPDN PDYCVIDLDP DKNTFEQVIE AAQEVRKVLD ALGVSSYPKT SGSTGIHIYI
     PLGAKYSYEQ SQLFAKVIVS LVHEQLPDFT SLKRKVSDRK GKMYLDFLQN RPGATIAGPY
     SLRPKPGATV SMPLAWDEVK RGLKMSDFTI HNAYDRLKET GDLFKGVLGK GIELNKIIKK
     AQNDL
//