ID   G8T6U3_NIAKG            Unreviewed;       934 AA.
AC   G8T6U3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, 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=Niako_1577 {ECO:0000313|EMBL:AEV97946.1};
OS   Niastella koreensis (strain DSM 17620 / KACC 11465 / NBRC 106392 /
OS   GR20-10).
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niastella.
OX   NCBI_TaxID=700598 {ECO:0000313|EMBL:AEV97946.1, ECO:0000313|Proteomes:UP000005438};
RN   [1] {ECO:0000313|EMBL:AEV97946.1, ECO:0000313|Proteomes:UP000005438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17620 / KACC 11465 / NBRC 106392 / GR20-10
RC   {ECO:0000313|Proteomes:UP000005438};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Davenport K.,
RA   Saunders E., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Niastella koreensis GR20-10.";
RL   Submitted (DEC-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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP003178; AEV97946.1; -; Genomic_DNA.
DR   RefSeq; WP_014217860.1; NC_016609.1.
DR   AlphaFoldDB; G8T6U3; -.
DR   STRING; 700598.Niako_1577; -.
DR   KEGG; nko:Niako_1577; -.
DR   PATRIC; fig|700598.3.peg.1608; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_0_2_10; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000005438; Chromosome.
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:AEV97946.1};
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          346..481
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..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..208
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..576
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   934 AA;  105997 MW;  3D02F5F475119273 CRC64;
     MSLATYKKKR SFNQTPEPEG KKPAGKKTAV SSQLHFVVQK HDATRLHYDF RLEMEGVLKS
     WAVPKGPSMN PADKRLAMMV EDHPYDYKDF EGIIPEGNYG AGTVIVWDEG TYEPIEPFDD
     PKKAEKHLLE QLRKGSLKIV LHGQKLKGEF ALVQIKSSED NAWLLIKHND KYATQTDVTK
     KAKSVQSGMK LEQVAKESTH EWVSNKKSTT KKKSSAAKKS PAQSAVASKK QPAKKKVPQA
     IDGLLRKGKK QAMPSGIIPM LATLTDNSFD DKNWIFEIKY DGYRALSYIN DSEVTIMSRK
     DLSFNKKFPP VAEALKQLEL EAILDGEIVA LNEEGRSDFQ LLQQWQKNGE GELVYYVFDL
     LWLNGYNLMH LPLVERKEIL QQILPEHPMI RYSDHIEQKG RQFFEVANKQ GLEGIMAKER
     DSAYTPKIRT RQWLKIKTVQ RQEVVIAGFT ETRGSRSHFG ALVLGVYEKD KLIYVGHTGS
     GFTEKSLAAV YKKLQPLIID KSPFATKPKT NMPCTWIKPV LVGEVKFSEW TKDNILRQPI
     FVGLREDKNA KDVHKENAVH NSTAVEEGEA ETRSTKKQSS QKMPTKKAAK SSKPKAKSKI
     QNRKMEANDK RVARSVNITS EKTLLNDSDK EQVVTIDKKE LTFTNLDKIY WPADKYTKRD
     LINYYDQMAA FILPYLKDRP QSMNRHPNGI DKPGFYQKDV SGGKVADWLE KHDYLSESDG
     ETKQYLVCTD EASLLYMANL GCIEMNPWHS TTKKPENPSW CVIDLDPGNI SFDKVIEAAQ
     VIKQLTDELG IDTYCKTSGS TGLHIYIPLA AAYDYDQSRQ LAELIVTMAY NEMPSFTSLE
     RSPAKRKNKI YLDYLQNRTI QTIAAPYSLR PKPGATASAP LHWEEVKKGL AIQDFTIENM
     YSRAKEVGDI FKPVLGKGIN LKKVLTKINS MQSK
//