ID A0A0M8M834_9FLAO Unreviewed; 892 AA.
AC A0A0M8M834;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=AM493_04865 {ECO:0000313|EMBL:KOS05433.1};
OS Flavobacterium akiainvivens.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1202724 {ECO:0000313|EMBL:KOS05433.1, ECO:0000313|Proteomes:UP000037755};
RN [1] {ECO:0000313|EMBL:KOS05433.1, ECO:0000313|Proteomes:UP000037755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IK-1 {ECO:0000313|EMBL:KOS05433.1,
RC ECO:0000313|Proteomes:UP000037755};
RA Wan X., Hou S., Saito J., Donachie S.;
RT "Whole genome sequence of Flavobacterium akiainvivens IK-1T, from decaying
RT Wikstroemia oahuensis, an endemic Hawaiian shrub.";
RL Submitted (AUG-2015) 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:KOS05433.1}.
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DR EMBL; LIYD01000005; KOS05433.1; -; Genomic_DNA.
DR RefSeq; WP_054406627.1; NZ_LIYD01000005.1.
DR AlphaFoldDB; A0A0M8M834; -.
DR STRING; 1202724.AM493_04865; -.
DR PATRIC; fig|1202724.3.peg.1007; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000037755; 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; 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; 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:KOS05433.1};
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:UP000037755};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 329..463
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 101225 MW; 84FF8A27577D5BB3 CRC64;
MALDKYKQKR DASKTPEPFG GKGNENKLRF VVQKHAASHL HYDFRLEMEG VLKSWAVPKG
PSVDPDVKRL AMMVEDHPYD YRNFEGIIPQ GQYGGGTVIV WDEGFYEPFE SEAATKKEQD
KELRAGLHSG KIKFVLHGEK LKGAFALVKA HGRGENGWLL MKLDDKYASE KDITLKDKSV
ISKKTLEQLA KTSKNIYGQK PAESQQEKLE KKVDTSEKPQ ELQANDLLKK GKKSKMLTEV
KPMLATLVNE PFDSPGWSYE VKWDGYRALA YVNKGKTELL SRNIKSFTEK YYPIAAVMDS
WSINAVFDGE ILVIGKDGKA NFSALQNWRS EADGDLVYYA FDILWYDGKD ITGLPLSERQ
AILREILPAN DDHVRLSRVF DINGIDFFEA AQKMGLEGIM AKKTDSTYAI DSRSKDWLKI
KVNQRQEVVI GGFTKNEGTS KQFSSLLLGV YEKGKLEYVG KVGTGFSDKK QKEMMELFKP
LIIDTMPFDT EPDVNKPSRF RPNPPKAKAT WLKPELVCEV SFIEVTADGV FRHPSFEGMR
SDKKAKDVVR ETATATATIT TNEGRKEKLV APPKRSSATT LLNPKEETQV KKVNGHNLKF
TNLSKVYWPE EGYTKRDMFN YYHQVAEYIL PHLKDRPLSL NRFPSGIHGK SFYQKDVKGK
APDWAKTYPY HTSDGEDKEF LVGNDEATLL WMASLGCIEM NPWFSKTTHP DNPDYCVIDL
DPSDKTTFEQ VIQAAREVKD VLDAINVPSY VKTSGSTGIH IYIPLGARYS YDQSQMFARL
LVSIVHDRLP DFTSLERKIK DRNGKMYLDF LQNRPGATIA CAYSLRPKPG ATVSMPLHWD
EVKKGLKMKD FTIRNALERI KSEGDLFKGT LEEGIDMEKA LEQAQDAFYK KN
//
