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Database: UniProt
Entry: A0A126YZR1_9MICO
LinkDB: A0A126YZR1_9MICO
Original site: A0A126YZR1_9MICO 
ID   A0A126YZR1_9MICO        Unreviewed;       848 AA.
AC   A0A126YZR1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=AX769_10440 {ECO:0000313|EMBL:AMM20489.1};
OS   Frondihabitans sp. PAMC 28766.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Frondihabitans.
OX   NCBI_TaxID=1795630 {ECO:0000313|EMBL:AMM20489.1, ECO:0000313|Proteomes:UP000070552};
RN   [1] {ECO:0000313|EMBL:AMM20489.1, ECO:0000313|Proteomes:UP000070552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC28744 {ECO:0000313|Proteomes:UP000070552};
RA   Park H.;
RT   "Complete genome of Frondihabitans sp.";
RL   Submitted (FEB-2016) 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; CP014513; AMM20489.1; -; Genomic_DNA.
DR   RefSeq; WP_066278940.1; NZ_CP014513.1.
DR   AlphaFoldDB; A0A126YZR1; -.
DR   STRING; 1795630.AX769_10440; -.
DR   KEGG; frp:AX769_10440; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000070552; 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; 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   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; 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; PS00697; DNA_LIGASE_A1; 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:AMM20489.1};
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:UP000070552};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          625..751
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          284..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          825..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..840
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   848 AA;  93486 MW;  C7DFD9EFA8DAF73C CRC64;
     MATKGRGERV SVGGHTLQLT NLDKVLYQAT GTTKGDVIAY YAAVAEWMLP HTEDRPATRK
     RWVNGVDGEV FFEKNLPDSA PDWVASHTIE HSDHSNVYPL VNDLATLTWL GQVAALEIHV
     PQWRFGPRGA QRNPDRLVLD LDPGEGVGLP ECVAVAQELK KIVDGMGLGL MPVTSGSKGI
     HLYAALDGKQ SPQQVSDIAH ELAKAMEADH PDLVLSTMGK QDRRGKVFLD WSQNNGNKTT
     IAPYSLRGRE HPTVAMPRTW RELASRTLRQ MEYPDVLKAL KRRGDPLADL SSGTPVPPGE
     LDRETMHNSE TPVSAREDRL AKYRSMRDPS KTREPVPAEA PEPSDNQTFV IQEHHATRLH
     WDFRLEHDGV LVSWALPKGE PQDVKQNHLA VQTEDHPLEY GTFEGTIAKG EYGAGEVTIW
     DSGTYDLEKW RDGKEVIVVL HGEQRGSRRI ALIHTGHGGG AGSSTAKQEH NWLIHRMKDD
     DADDAGSGGK ASRPSSKGGH QDPAPRPQTK RTTRKRPVGD PVQPMLASPG DAAAIGDASD
     WAYEMKWDGV RAVVTVHDGA VTLTSRNGHD MSASYPEFDG LPDRLGDVGD AVLDGEIVAV
     DRNGRPDFGL LQTRMKLTRP RDVERVRETA PVRLLLFDVM SLDGQSLEDD DYDTRRAALQ
     KAVELKPRDK TIDVPPAFEG SLAEAMSFSK RLKLEGVVAK RRDSGYSAGR RSRAWIKLKH
     HATQEVVIAG WRPGAGRRAN GVGSLLMGLP TDEGLKYVGR VGTGFSDKEL DELLPTFGRE
     ARKTSPLVDV PTADARDAHW ITASRVGEVE FAEWTSTGRL RQPSWRGWRP DKDVDQVVRE
     SGDPSRAS
//
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