ID A0A6F8USN9_9HYPH Unreviewed; 191 AA. AC A0A6F8USN9; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 24-JUL-2024, entry version 12. DE RecName: Full=DarT domain-containing protein {ECO:0000259|PROSITE:PS52018}; GN ORFNames=OCUBac02_09740 {ECO:0000313|EMBL:BCB18080.1}; OS Bosea sp. ANAM02. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; Boseaceae; OC Bosea. OX NCBI_TaxID=2020412 {ECO:0000313|EMBL:BCB18080.1, ECO:0000313|Proteomes:UP000502683}; RN [1] {ECO:0000313|EMBL:BCB18080.1, ECO:0000313|Proteomes:UP000502683} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ANAM02 {ECO:0000313|EMBL:BCB18080.1, RC ECO:0000313|Proteomes:UP000502683}; RA Tsubouchi T., Okabe Y., Son C., Kaneko Y.; RT "Complete genome sequence of Bosea sp. ANAM02."; RL Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=a thymidine in DNA + NAD(+) = an N-(ADP-alpha-D-ribosyl)- CC thymidine in DNA + H(+) + nicotinamide; Xref=Rhea:RHEA:71651, CC Rhea:RHEA-COMP:13556, Rhea:RHEA-COMP:18051, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:137386, CC ChEBI:CHEBI:191199; Evidence={ECO:0000256|PROSITE-ProRule:PRU01362}; CC -!- SIMILARITY: Belongs to the DarT ADP-ribosyltransferase family. CC {ECO:0000256|PROSITE-ProRule:PRU01362}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01362}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP022848; BCB18080.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6F8USN9; -. DR Proteomes; UP000502683; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-UniRule. DR InterPro; IPR029494; DarT. DR Pfam; PF14487; DarT; 1. DR PROSITE; PS52018; DART; 1. PE 3: Inferred from homology; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE- KW ProRule:PRU01362}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|PROSITE- KW ProRule:PRU01362}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|PROSITE- KW ProRule:PRU01362}; KW Toxin-antitoxin system {ECO:0000256|ARBA:ARBA00022649, ECO:0000256|PROSITE- KW ProRule:PRU01362}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE- KW ProRule:PRU01362}. FT DOMAIN 1..191 FT /note="DarT" FT /evidence="ECO:0000259|PROSITE:PS52018" FT ACT_SITE 37 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01362" FT ACT_SITE 139 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01362" FT BINDING 2..4 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01362" FT BINDING 37 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01362" SQ SEQUENCE 191 AA; 21114 MW; 7F46702AB1BDD716 CRC64; MHFTRTANLA SIIRNGIYPV SRVGEIGVKP VINDEWRLDG HLGGISVSIG HPNYRMFFKL RKDNPDIDWV VLCIKPSVLW TKDCAFCRHN AADARISSQP LCDLKTPAAF AGIYDEVEGL ETRADQRLKS HDPTDAQAEI LVFDAIEPNL IVGAAFETAA VLEPFKGILG DRQVIVPGTG RGPFSSRKFV R //