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Database: UniProt
Entry: A0A0A2M7D5_9FLAO
LinkDB: A0A0A2M7D5_9FLAO
Original site: A0A0A2M7D5_9FLAO 
ID   A0A0A2M7D5_9FLAO        Unreviewed;       933 AA.
AC   A0A0A2M7D5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=Q765_01300 {ECO:0000313|EMBL:KGO88572.1};
OS   Flavobacterium rivuli WB 3.3-2 = DSM 21788.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1121895 {ECO:0000313|EMBL:KGO88572.1, ECO:0000313|Proteomes:UP000030152};
RN   [1] {ECO:0000313|EMBL:KGO88572.1, ECO:0000313|Proteomes:UP000030152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WB 3.3-2 {ECO:0000313|EMBL:KGO88572.1,
RC   ECO:0000313|Proteomes:UP000030152};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO88572.1}.
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DR   EMBL; JRLX01000001; KGO88572.1; -; Genomic_DNA.
DR   RefSeq; WP_020211589.1; NZ_KB899966.1.
DR   AlphaFoldDB; A0A0A2M7D5; -.
DR   STRING; 1121895.GCA_000378485_00465; -.
DR   eggNOG; COG1793; Bacteria.
DR   eggNOG; COG3285; Bacteria.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000030152; Unassembled WGS sequence.
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   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; 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};
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:UP000030152};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          362..477
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          563..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        574..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   933 AA;  105481 MW;  41E94E0449E87E7A CRC64;
     MPKLSEYNKK RDFNKTAEPK GTVKKGGKEL RFVVQKHAAS HLHYDFRLEI DGVLVSWAVP
     KGPIADTSVK RLAMHVEDHP MDYIDFEGTI PKGEYGGGTV MVWDTGTYLA EGIDNVADSE
     KVLRKMYKEG NIKIVMNGKK LKGSYHIVQM HGREENSWLL LKGKDEYADK KDFDQTSVLT
     GRTLEEIGKD KKSDVWESNH DGKTETKNPN KIDLEEVADA VEQLKTDSES KKKTATETET
     SQTFTAEDVA DAKKLDEFPT NWLPQLATLA DEVFDNEDWI YETKYDGYRA IIEVNDGDVN
     LVSRNGISFN DRYKPLVKAF DAITNDVILD GEIVVEDTKG ISHFQWLQYY ADNPDRGTLK
     CYVFDILYFN GFDLTSLELV QRKRILEALL PQSDQIIYSG HIKGKGSKAL KEVEQKGGEG
     LIAKKASSKY YINKRSKDWL KIKISKEQEM VIGGFTDPKG SRTAFGSLLL GYYEDGKLIY
     SGKVGTGFNE ESLKDIYEKL TALEQKTSPF SIKPKEPGAH WIKPDLVAQI KYSEWTETNS
     LRHPVFMGLR TDKDPKDVIK EIAGPLTPEG GNLEAEKTTK KNAVKKADKV KPAKADSDKK
     PAKETKTKTA EKVIEEKTPA KKAAAKTKST SKTMKSKAGY DTEKVEVTHP EKIFWPKEGY
     TKGDVIAYYN EMADYILPYI KDRPESMRRT PDGIVKEGFF QKNVAGMVPD WAQTEKIHSD
     STKEDIEYLI CNDKETLIYM ANLGCIEINP WSSRVGTLDN PDYIIFDLDP NKTTIENLVT
     TAKKVKEILD SLNIKGYLKT SGGKGLHVFI PIKPKYTYEQ SRDFSHIISQ AVNAALPDIT
     SLERMPKKRE GKVYLDFLQN GKGKTMACAY SLRPREGATA SAPLEWDELD DTFDLKNYNI
     KTLPKRVKEK GDLWEGFFKD ALDLEEVLNK LSQ
//
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