ID A0A0S4JRK6_BODSA Unreviewed; 375 AA.
AC A0A0S4JRK6;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 05-FEB-2025, entry version 26.
DE RecName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase {ECO:0000256|RuleBase:RU361228};
DE EC=2.4.2.31 {ECO:0000256|RuleBase:RU361228};
DE AltName: Full=Mono(ADP-ribosyl)transferase {ECO:0000256|RuleBase:RU361228};
GN ORFNames=BSAL_41375 {ECO:0000313|EMBL:CUG93208.1};
OS Bodo saltans (Flagellated protozoan).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Eubodonida; Bodonidae; Bodo.
OX NCBI_TaxID=75058 {ECO:0000313|EMBL:CUG93208.1, ECO:0000313|Proteomes:UP000051952};
RN [1] {ECO:0000313|Proteomes:UP000051952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Konstanz {ECO:0000313|Proteomes:UP000051952};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = N(omega)-(ADP-D-ribosyl)-L-
CC arginyl-[protein] + nicotinamide + H(+); Xref=Rhea:RHEA:19149,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142554; EC=2.4.2.31;
CC Evidence={ECO:0000256|ARBA:ARBA00047597,
CC ECO:0000256|RuleBase:RU361228};
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009558, ECO:0000256|RuleBase:RU361228}.
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DR EMBL; CYKH01002128; CUG93208.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4JRK6; -.
DR VEuPathDB; TriTrypDB:BSAL_41375; -.
DR Proteomes; UP000051952; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 3.90.176.10; Toxin ADP-ribosyltransferase, Chain A, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000768; ART.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR Pfam; PF01129; ART; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361228}; Kinase {ECO:0000313|EMBL:CUG93208.1};
KW NAD {ECO:0000256|RuleBase:RU361228}; NADP {ECO:0000256|RuleBase:RU361228};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000051952};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361228}.
FT DOMAIN 1..103
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
SQ SEQUENCE 375 AA; 41407 MW; D156D92EA0486DA4 CRC64;
MDYTARYVPP ESATGNDVSR ESDLYSFGCV MLELITSLPP SHHLPPTSAL TALCQGIMHN
IDDYVWPLPF SKEVRALVGR FLMYNPDNRA SIAEAIGVLE NAIGAVSLQQ PEPVSSQPLD
FNWLDGVAEC SSFEVAVALL VGYRAPSDRP DTNFCSECIR SVVPQLASTL LLASPDERAL
QVYTAESPVF KIINAALSEN NKHSVNLPHV SPMCKRLFRA IQTLGTAYTG PAHRVLFAFE
SFKVAYAEGT PIEFTQFSSF TKDLSRIESF TTVAVGDESV PLIVFHCDNL TAFDISIFST
YSESEVIALP PSHFTVSSAP YKVQQAVHVH LTFQADRSHA ATYLRCQREF EVPQYANIVL
ENSQSTAGKY KKNMF
//
