ID A0A814FUH4_9BILA Unreviewed; 465 AA.
AC A0A814FUH4;
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=BJG266_LOCUS15262 {ECO:0000313|EMBL:CAF0988525.1},
GN QVE165_LOCUS14512 {ECO:0000313|EMBL:CAF0993206.1};
OS Adineta steineri.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Adinetida; Adinetidae; Adineta.
OX NCBI_TaxID=433720 {ECO:0000313|EMBL:CAF0988525.1, ECO:0000313|Proteomes:UP000663877};
RN [1] {ECO:0000313|EMBL:CAF0988525.1}
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:CAF0988525.1}.
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DR EMBL; CAJNOI010000067; CAF0988525.1; -; Genomic_DNA.
DR EMBL; CAJNOM010000077; CAF0993206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A814FUH4; -.
DR OrthoDB; 423533at2759; -.
DR Proteomes; UP000663832; Unassembled WGS sequence.
DR Proteomes; UP000663877; 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 GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.720.50; -; 1.
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 InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR004170; WWE_dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR10339; ADP-RIBOSYLTRANSFERASE; 1.
DR PANTHER; PTHR10339:SF25; SECRETED EXOENZYME S; 1.
DR Pfam; PF01129; ART; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51996; TR_MART; 1.
DR PROSITE; PS50918; WWE; 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:UP000663832};
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}.
FT DOMAIN 122..207
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
SQ SEQUENCE 465 AA; 54378 MW; BD8BAA474BC4BE05 CRC64;
MNNNHNNNKK KSNICSFTFI SQAQIPVYVT GVEQSWNFLK LEFDRQSDGL PSPNARYYQT
LYTGPKLFAV DDNDVVYYHD AEQWTPYSSA SIITYSYDSD FVEDEDESND VCVLSPDFHY
EEILNKRHMS DAIVLWYFKD KMNVSLDNDE NDHWLPYSDI ENEIIEEAYQ RKSNTESFIE
LDDYLIDFNQ LVQVSKLDNT KHQTIKRVIA SNNERKYILQ ERFSEPLSQV SPTSYTFGHE
YEWSPLIMQW IQSKVGKHCL FNAKKCVRKA IEGIMTEGRL IGKEIEASYL VRKLEPCKRL
LIKDISKICV HLFTRASFLY RVVNTALRNS DLSKIDTLGP YCYLLRAYIR SAGTEYNGYL
YRGCNLSEEQ VSQYRNAVSM KEWKTWRSFT STSKNQQVVE IFGENTLFII NVKEIGISSN
RAFNIQHISQ FPDEEEVLLP AGVLFQIVDV QKDEKTKKWI IHLQL
//
