ID A0A1I3DSV7_9FLAO Unreviewed; 838 AA.
AC A0A1I3DSV7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=SAMN05443292_0688 {ECO:0000313|EMBL:SFH89830.1};
OS Halpernia frigidisoli.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Halpernia.
OX NCBI_TaxID=1125876 {ECO:0000313|EMBL:SFH89830.1, ECO:0000313|Proteomes:UP000198931};
RN [1] {ECO:0000313|EMBL:SFH89830.1, ECO:0000313|Proteomes:UP000198931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26000 {ECO:0000313|EMBL:SFH89830.1,
RC ECO:0000313|Proteomes:UP000198931};
RA de Groot N.N.;
RL Submitted (OCT-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; FOQT01000001; SFH89830.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3DSV7; -.
DR STRING; 1125876.SAMN05443292_0688; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000198931; Unassembled WGS sequence.
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; 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:SF3; -; 1.
DR PANTHER; PTHR42705; 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 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:SFH89830.1};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000198931};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 308..443
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 838 AA; 95794 MW; 5FFAF880ACAA5CD3 CRC64;
MSLEDYQKKR DFKETSEPKG KIESSENKLI FVIQRHAASR LHYDFRLEMD GVLKSWAIPK
GPSLNPADKR LAMKVEDHPY SYKDFEGSIP KGNYGAGEVE IWDSGTYEAL QKKEGKTDDL
ILRNELHKGS LKFILHGEKL KGEFALVKIK NPKDDNAWLL IKHKDEFAET DYDAENHISE
NSKVSEVLEK KSDNKPGVKS SFKNYTPALS NEKKLTDFIK PMLAKTAEAA FDKKDWVFEI
KWDGYRAIAD LRESASLLYS RNGLSFKEKF HKVSDALETQ NHKMILDGEI VAFNSEGKPD
FQKLQQIGEN PNMALTYQVF DLLWLNGHST ESLTLLERKE LLKDALVENE VVKYCDHVPE
KGKDFFEQIK SMELEGMIAK KADSKYVEGS RSDDWLKIKF QQTEDVIICG FTEGKGSRKS
FGALILGKYE NEKLVYCGHT GTGFSDETLE SLANVFEPLI SKKCPFEQVP KTNAPATWLK
PELICEIKFT EITKDGVFRH PVFIGLREDK AVEDLRDDEK LEYQKSEPKK GIKKSISKKS
KIEIVNLKLT NQEKIYFPES SFTKGDVVEY YQSVSEYILP HLKDRPQSLN RFPNGIKGLS
FYQKDAGNDA PNWIEKVAIH SDSNDKDINY LICNSKESLA YLNNLGCIDL NPWNSTTKNL
ENPTWMAIDL DPSDKNTFDE VIETALAVKE VLDLAKIKGF PKTSGSSGIH IFVPMENQYF
FDQVKNFAHI LMQKVEKKLP KLTTLERALK TRSDKKIYLD YLQNRSGQTL ASVYSIRPKE
FAPVSMPLKW EELKVGLKPT DFNIENSLER INKNGDLFKP VLRKGIDMLK ALENLSDS
//
