ID   C8XIX5_NAKMY            Unreviewed;       831 AA.
AC   C8XIX5;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   02-SEP-2026, entry version 76.
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=Namu_0128 {ECO:0000313|EMBL:ACV76562.1};
OS   Nakamurella multipartita (strain ATCC 700099 / DSM 44233 / CIP 104796 / JCM
OS   9543 / NBRC 105858 / Y-104) (Microsphaera multipartita).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Nakamurellales;
OC   Nakamurellaceae; Nakamurella.
OX   NCBI_TaxID=479431 {ECO:0000313|EMBL:ACV76562.1, ECO:0000313|Proteomes:UP000002218};
RN   [1] {ECO:0000313|Proteomes:UP000002218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC   Y-104 {ECO:0000313|Proteomes:UP000002218};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Ovchinnikova G., Sims D., Meincke L., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Nakamurella multipartita DSM 44233.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ACV76562.1, ECO:0000313|Proteomes:UP000002218}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700099 / DSM 44233 / CIP 104796 / JCM 9543 / NBRC 105858 /
RC   Y-104 {ECO:0000313|Proteomes:UP000002218};
RX   PubMed=21304699;
RA   Tice H., Mayilraj S., Sims D., Lapidus A., Nolan M., Lucas S.,
RA   Glavina Del Rio T., Copeland A., Cheng J.F., Meincke L., Bruce D.,
RA   Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA   Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Chen F.;
RT   "Complete genome sequence of Nakamurella multipartita type strain (Y-
RT   104).";
RL   Stand. Genomic Sci. 2:168-175(2010).
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   -!- SIMILARITY: In the C-terminal section; belongs to the ATP-dependent DNA
CC       ligase family. {ECO:0000256|ARBA:ARBA00049981}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the LigD polymerase
CC       family. {ECO:0000256|ARBA:ARBA00049990}.
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DR   EMBL; CP001737; ACV76562.1; -; Genomic_DNA.
DR   RefSeq; WP_012814037.1; NC_013235.1.
DR   AlphaFoldDB; C8XIX5; -.
DR   FunCoup; C8XIX5; 1.
DR   STRING; 479431.Namu_0128; -.
DR   KEGG; nml:Namu_0128; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   HOGENOM; CLU_008325_2_1_11; -.
DR   InParanoid; C8XIX5; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000002218; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
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; cd04863; MtLigD_Pol_like; 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; IPR033649; MtLigD_Pol-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR052171; NHEJ_LigD.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; NF007210; PRK09632.1; 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; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   3: Inferred from homology;
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};
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:UP000002218};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          611..734
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          296..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..339
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..501
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   831 AA;  91090 MW;  1D4EC185FB362C25 CRC64;
     MAADSATVEV DGHRIALTHL RKVLYPASGT TKSEVIAYFA EVAHAMIPHL ADRPVTRKRW
     PDGVTTAPFF HKDLPKGTPS WVPRRTIRHS DGPKDYPLVD SPATLAWLGQ IAALELHVPQ
     WTFGSAAASV AGGDGEITEA VFDAVHPNRL VFDLDPGPGV ELVDCAHVAR AVRERMGGAA
     LVPVTSGSKG IHLYAWLDGS LTSDDASAYA REIAEAIEQD MPDLVVSRMA KSLRRGKVFI
     DWSQNNGSKT TIAPYSLRGR EHPTVAAPRT WEELADPELR HLEYTEVLEL LAAAPDPMQG
     LEDGDNDGAE TRGGSRRRGR GPDTKLDTYR SMRSADKTPE PVPEPGLLPQ GDDDTFVIQE
     HHARRLHYDF RLERDGVLVS WAVPKGVPES TGRNHLAVHT EDHPMDYADF AGEIPHGEYG
     GGTVSIWDRG TYATEKWRED EVIIVLHGGK ARGRYALIRT GGKNWLMHRM KDQSPQPKQY
     DDHRPATPTA PVTARPAPAR STRPEPPKDL RPMLATAGSV EDVADERRWR FEGKWDGIRA
     IATVGPSGLT LRSRLGNDVT PTYPELAVLA ELLDGHSAVL DGEIVALQDG RTSFHEMQKR
     MNVQRARDVA RVMRDVPVQF WIFDVLNLDG ISLLDKRYDD RRRILEALPL TGGVCLVPPQ
     LAGPARDALR GSADRQWEGI VAKLGDSTYQ PGRRSHSWLK IKNFLDLEVV VVGWSPGTGR
     REGTVGALLL AVPDGAGGLR YAGKVGTGFT DAILDQLMQA LAPLRADRSA VADTIPRADA
     AGAIWVRPEL VGEVKYGQWT PERRLRATSW RGLRPDKTVA DLIAGSAPPP S
//