ID A0A1G9HL62_9BACT Unreviewed; 823 AA.
AC A0A1G9HL62;
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=SAMN04488090_0107 {ECO:0000313|EMBL:SDL13721.1};
OS Siphonobacter aquaeclarae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Siphonobacter.
OX NCBI_TaxID=563176 {ECO:0000313|EMBL:SDL13721.1, ECO:0000313|Proteomes:UP000198901};
RN [1] {ECO:0000313|EMBL:SDL13721.1, ECO:0000313|Proteomes:UP000198901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21668 {ECO:0000313|EMBL:SDL13721.1,
RC ECO:0000313|Proteomes:UP000198901};
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; FNGS01000001; SDL13721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9HL62; -.
DR STRING; 563176.SAMN04488090_0107; -.
DR OrthoDB; 9802472at2; -.
DR Proteomes; UP000198901; 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; 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};
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:UP000198901};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 296..397
FT /note="ATP-dependent DNA ligase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50160"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 93128 MW; F9270D139300461A CRC64;
MGLQKYKKKR SFEKTPEPKG GKAGSGALRF VVQKHDASCL HYDFRLEMDG VLKSWAIPKG
PSTDPSVRRL AVQVEDHPYA YKDFEGTIPE GNYGAGTVII WDEGEYEPIT PAKGKKAQEK
ELLNELRDGS LKIILHGQKL KGEFALVRAG GMGDNAWLLI KHRDAEASSR DITKDNKSVR
TGEPLAPRHR GKKKPAADES GEAPPPVAPM LATLTDAPFD REGWSFEIKW DGYRALCFRD
GAKTELRSRN DQSFNERFYP IYDAVAAWDI RAVVDGEIVV ADENGVSHFN DLQHWHSKED
GPLYYYVFDL LWLNGRSLLN RPLSERQELL RGLIPPRGPI RMGIVVETSG LSFYQAAQKL
GLEGIMAKRM DSLYRPGTRS KDWLKMKIQQ RQEVVIAGYT RKRDSPRSFS SLLLALREKG
QWRYAGKVGT GFSDAFQKEL LSKLKPRDTS PLSGPLTGGA ALPPHTEIVW TEPERVAEIN
YTEITPDGVF RHPSFVALRD DKRPANVQPE TATKSMKPSF LPDENDAKVR VGKRTLSFSN
LNKKYWPDLT KRDLLNYYHE VAPFLLPYLK DRPLSLNRYP NGISGKMFLQ KDVSGQVPDW
LHTLLYHPED DPDADKHFAM ADDEASLLYL VNMGTIDPHP WSSTASRPDH PTWCIIDIDP
DKQTYDQVVE TALAVRDILS EYGIESYPKT SGATGMHVYL PLAGKYTYEQ SRTLAEYIAS
RVHERLPDFT TLERSVKARK GKLYIDYLQN RPQATVAPPY IVRPRPGAPV STPLHWDEVR
KGLDPARFHL RNTLDRLRET GDLFAPVLKK GADLRRLLET GKE
//