ID A0A815D0M1_9BILA Unreviewed; 332 AA.
AC A0A815D0M1;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
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=JXQ802_LOCUS44848 {ECO:0000313|EMBL:CAF1567056.1},
GN PYM288_LOCUS29375 {ECO:0000313|EMBL:CAF1290686.1};
OS Rotaria sordida.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Philodinida; Philodinidae; Rotaria.
OX NCBI_TaxID=392033 {ECO:0000313|EMBL:CAF1290686.1, ECO:0000313|Proteomes:UP000663854};
RN [1] {ECO:0000313|EMBL:CAF1290686.1}
RP NUCLEOTIDE SEQUENCE.
RA Nowell W R.;
RL Submitted (FEB-2021) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009558, ECO:0000256|RuleBase:RU361228}.
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:CAF1290686.1}.
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DR EMBL; CAJNOH010002391; CAF1290686.1; -; Genomic_DNA.
DR EMBL; CAJNOL010003561; CAF1567056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A815D0M1; -.
DR Proteomes; UP000663854; Unassembled WGS sequence.
DR Proteomes; UP000663870; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ poly-ADP-ribosyltransferase activity; IEA:TreeGrafter.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.176.10; Toxin ADP-ribosyltransferase, Chain A, domain 1; 1.
DR InterPro; IPR050999; ADP-ribosyltransferase_ARG.
DR InterPro; IPR000768; ART.
DR PANTHER; PTHR10339; ADP-RIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10339:SF25; SECRETED EXOENZYME S; 1.
DR Pfam; PF01129; ART; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361228}; NAD {ECO:0000256|RuleBase:RU361228};
KW NADP {ECO:0000256|RuleBase:RU361228};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000663870};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361228};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
SQ SEQUENCE 332 AA; 36871 MW; 32ECEFA018DDE5D7 CRC64;
MATSGGEEAI AQRILRLTDI VQEPLRFIAP IGGYEEMPIV TLEKAVEPLV PILPAVQSHA
YVAKQICENP ADGLTQDESA SIMLYTMGWE PLDKCLYVVL NDTLRSSERQ QKLKPWYLFM
RLFLSALFRL PPLPKVAYRG VKLDLSERYV EGKTIVWWGF SSCTTAVGVL KSEQFLGTAG
DRTMFTLQCQ SARDIRKHSY YTAEDEVLLM AGTQFKVMGC LDQGNLHIVQ LEETRPPFPL
LQPVLIVIPK PISSTPSKAS ITTAVVTTEA KKQTQSSKSQ KDTTAVAATA SAINVGTNSI
MKQISTMEIK ASPNKVYKIL WHFVLISSVR LT
//
