ID A6DPT5_9BACT Unreviewed; 647 AA.
AC A6DPT5;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=DNA ligase (NAD(+)) {ECO:0000256|ARBA:ARBA00012722};
DE EC=6.5.1.2 {ECO:0000256|ARBA:ARBA00012722};
GN ORFNames=LNTAR_19952 {ECO:0000313|EMBL:EDM26380.1};
OS Lentisphaera araneosa HTCC2155.
OC Bacteria; Lentisphaerota; Lentisphaeria; Lentisphaerales; Lentisphaeraceae;
OC Lentisphaera.
OX NCBI_TaxID=313628 {ECO:0000313|EMBL:EDM26380.1, ECO:0000313|Proteomes:UP000004947};
RN [1] {ECO:0000313|EMBL:EDM26380.1, ECO:0000313|Proteomes:UP000004947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC2155 {ECO:0000313|EMBL:EDM26380.1,
RC ECO:0000313|Proteomes:UP000004947};
RX PubMed=20363947; DOI=10.1128/JB.00208-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Morris R.M., Giovannoni S.J.;
RT "Genome sequence of Lentisphaera araneosa HTCC2155T, the type species of
RT the order Lentisphaerales in the phylum Lentisphaerae.";
RL J. Bacteriol. 192:2938-2939(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC nicotinamide D-nucleotide.; EC=6.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00034005};
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:EDM26380.1}.
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DR EMBL; ABCK01000017; EDM26380.1; -; Genomic_DNA.
DR RefSeq; WP_007279866.1; NZ_ABCK01000017.1.
DR AlphaFoldDB; A6DPT5; -.
DR STRING; 313628.LNTAR_19952; -.
DR eggNOG; COG0272; Bacteria.
DR OrthoDB; 9759736at2; -.
DR Proteomes; UP000004947; Unassembled WGS sequence.
DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR001679; DNA_ligase.
DR InterPro; IPR013839; DNAligase_adenylation.
DR InterPro; IPR013840; DNAligase_N.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004150; NAD_DNA_ligase_OB.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR004149; Znf_DNAligase_C4.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF01653; DNA_ligase_aden; 1.
DR Pfam; PF03120; DNA_ligase_OB; 1.
DR Pfam; PF03119; DNA_ligase_ZBD; 1.
DR PIRSF; PIRSF001604; LigA; 1.
DR SMART; SM00532; LIGANc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EDM26380.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000004947};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 542..606
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 614..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 71981 MW; 0FBA5B6D3295E914 CRC64;
MDIDALKAKL DQANQLYRTG GESPLSDAEY DYLLEQVNDQ KFRDKVGYEI EKNKVELAVP
MGSLNKIKTQ AEVFDWSKSK SIPLDTEICV TPKYDGLSLL VYFVDGIYKG AYTRGDGMFG
QDVGEHFTVN PLCDLRLPQD FTGYLIGECI MDEAKFQTKY SEKFKNPRNM VAGLLSRKTL
SRELADVCYV AYGVRSAQMA HKQDQVEFCN RYINAQWKYK VLCPLYKLED LKDAELQKVY
DSETRFQCDG LVLEINDSDL FHQIGKETNS LNPGAARAWK PESDDSLPSI VKEVVWQISK
NGAAKPVIRI EPIDLAGVTI SNVTGINARF IEDSGIAKGA TVTIIRSGDV IPKVIGVPNA
IENVDLPKQC PSCESELVWN ENRVDIVCEN KLCPATNKAA LIDFFSTLKA DEVGEGIITS
LWDAGYQSVK NLLNLTMEDL LKLEGFKQRK AKKVLDSIKI SVVDVPLPRL QHASNLFKGL
GEKKLELLQK YDQAGIKPSF EELLEVDGYS EISAKSYLDS IDAYWEFAAE LPGLKYKKVL
VNEGGMFAGQ TLVFTGFRSP ELEEQVKTEG GKIGSSVSKK TSVLVVKAKG SGSSKEKKAI
DLGVEVWGRD DLENKLNSAE DEPEEMIGIE APSDPEEQGE LIQPDLF
//
