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Database: UniProt/TrEMBL
Entry: E6THW1_MYCSR
LinkDB: E6THW1_MYCSR
Original site: E6THW1_MYCSR 
ID   E6THW1_MYCSR            Unreviewed;       766 AA.
AC   E6THW1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=Mspyr1_12280 {ECO:0000313|EMBL:ADT97908.1};
OS   Mycolicibacterium gilvum (strain DSM 45189 / LMG 24558 / Spyr1)
OS   (Mycobacterium gilvum).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=278137 {ECO:0000313|EMBL:ADT97908.1, ECO:0000313|Proteomes:UP000008916};
RN   [1] {ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., LaButti K., Ivanova N.M., Mikhailova N.M., Land M., Hauser L.,
RA   Koukkou A.I., Drainas C., Kyrpides N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium sp. Spyr1.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADT97908.1, ECO:0000313|Proteomes:UP000008916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45189 / LMG 24558 / Spyr1
RC   {ECO:0000313|Proteomes:UP000008916};
RX   PubMed=22180818;
RA   Kallimanis A., Karabika E., Mavromatis K., Lapidus A., Labutti K.M.,
RA   Liolios K., Ivanova N., Goodwin L., Woyke T., Velentzas A.D.,
RA   Perisynakis A., Ouzounis C.C., Kyrpides N.C., Koukkou A.I., Drainas C.;
RT   "Complete genome sequence of Mycobacterium sp. strain (Spyr1) and
RT   reclassification to Mycobacterium gilvum Spyr1.";
RL   Stand. Genomic Sci. 5:144-153(2011).
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; CP002385; ADT97908.1; -; Genomic_DNA.
DR   RefSeq; WP_013470919.1; NC_014814.1.
DR   AlphaFoldDB; E6THW1; -.
DR   KEGG; msp:Mspyr1_12280; -.
DR   HOGENOM; CLU_008325_2_1_11; -.
DR   OMA; QWLAHRM; -.
DR   Proteomes; UP000008916; 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; 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; 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   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 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:ADT97908.1};
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          553..675
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          306..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   766 AA;  85303 MW;  CF2191657045E8FE CRC64;
     MVDRYDRVKL TNPDKVLYPA SGTTKAQVFE YYVNVAEGML PHIAGRAVTR KRWPNGVEES
     SFFEKQLASS APDWLDRGTI AHKSGTTTYP VIDTVEGLAW IAQQAALEVH VPQWRFTRGG
     QSGAADGGDG KPGPATRIVF DLDPGEGVTF RQLCEVAHEV RELITDIGLT TFPLTSGSKG
     LHLYVPLEDP ISSRGASVLA KRVAQQLEQS MPKRVTATMT KSLRDGKVFL DWSQNNGNKT
     TIAPYSLRGR ERPTVAAPRT WDEIEDPDLR HLTFDEVLDR LERDGDLLAD LDPPLPATDK
     LTRYRSMRDR TKTPEPVPAE PPETGANDKF VIQEHHARRL HYDFRLERDG VLVSWAVPKN
     LPDTPSVNHL AVHTEDHPMD YIDFAGEIPK GEYGGGEVHI WDTGTYETEK FRDNPPDGPA
     KGGEVIVTLH GQKIEGRYAL IQTDGKNWLA HRMKDQQKPT AADLAPMLTT EGSVERLTRG
     QWAFEGKWDG YRLLVDADHG KLTLRSRRGR DVTAEYPQLK ALAADLADHH VILDGEAVAL
     DEDGVPSFGE MQNRARSTRV EFWAFDILFL DGRLLTKATY TDRRKLLEAL AEGGGLIVPP
     ALEGDGPEAL EYARSQRWEG VIAKKRDSTY QPGRRSSAWI KDKIWNTQEV VIGGWRQGEG
     GRTSGIGALV LGVPDDDGLH FVGRVGTGFT DKQLASLKKS LEPLRTDESP FAAELPKQDA
     KGVTFVRPEL VGEVRYSERT SDGRLRQASW RGLRDDKVPE DVRWEG
//
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