ID A0A815JQ99_9BILA Unreviewed; 735 AA.
AC A0A815JQ99;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 28-JAN-2026, entry version 13.
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_LOCUS19395 {ECO:0000313|EMBL:CAF1065271.1},
GN QVE165_LOCUS28443 {ECO:0000313|EMBL:CAF1249826.1}, QVE165_LOCUS35717
GN {ECO:0000313|EMBL:CAF1382072.1};
OS Adineta steineri.
OC Eukaryota; Metazoa; Spiralia; Gnathifera; Rotifera; Eurotatoria;
OC Bdelloidea; Adinetida; Adinetidae; Adineta.
OX NCBI_TaxID=433720 {ECO:0000313|EMBL:CAF1382072.1, ECO:0000313|Proteomes:UP000663832};
RN [1] {ECO:0000313|EMBL:CAF1382072.1}
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 -!- 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:CAF1382072.1}.
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DR EMBL; CAJNOI010000104; CAF1065271.1; -; Genomic_DNA.
DR EMBL; CAJNOM010000222; CAF1249826.1; -; Genomic_DNA.
DR EMBL; CAJNOM010000350; CAF1382072.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A815JQ99; -.
DR OrthoDB; 9994557at2759; -.
DR Proteomes; UP000663832; Unassembled WGS sequence.
DR Proteomes; UP000663877; Unassembled WGS sequence.
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 Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR Gene3D; 3.90.176.10; Toxin ADP-ribosyltransferase, Chain A, domain 1; 1.
DR InterPro; IPR000768; ART.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_rpt.
DR Pfam; PF01129; ART; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 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:UP000663832};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361228}.
FT REPEAT 505..538
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 735 AA; 87269 MW; 6F746FF4477826A7 CRC64;
MEKYNLSFTE LNETQNHEDF NIIWLSSDAV PFSISDNYLK QFDCCEACIS YIRKFKSERK
FLLVLTMDLE YLSSFEDLSQ IQSIYILKKS NEHIQFNKQN CLKLVDRFEN IDELINRLRK
DILLLYTSDL PVNISSLNEN NIEESLISLH RNSLTILWYK SFIYHLIQSS NVNMEELKQI
MLDQCRLEYQ NSENELIKIN SFNMYCSNET ILNWYTQDSF LYRLLNKAFR TRNIHFICRF
QYFLKGVYKK FQELSEIQQE TYPLIVYRGQ ILNTNDLKRL QSNVDPLILM NTFVSTTRNE
EIARLFIRGT RLSALFKINI HSRFQSYIDI SSFSSMPYEQ EILFFPGTIF SVDSIRQEND
STWIIELTLN NEISEHIDNL ISDFQNHIPV FKNKHNVFMK TDDFRLIKQY YKMLTGEEFW
LNNESLNMIY IYVAFMFSNL GCYEKAIELY KKYLLIGNIS IDSSKSKVIH MMIGYLYYNF
SAYDSAFLHY GIVLSLLDEG NLLTLELYNH IGDVWNTIDN IDYAISCYQQ ALNVGSINNI
CRSDINQKLN DLLLKKKHSA SNYIYQRQIN DIDEHYRSII NPDNETELKD CQCQLNNEHN
LTPIQHIDVL YRFGICLMRK GDFCYALEIF LKTKQMVIDQ PPDDENNSTS IWFIDLSYQI
GLCWMKKGDF NQVLKNLLTA EQIIIKNPPL WDRFPQLLAT LYDNITILYF FLNEPFKALI
MWKKSNDIKT NFSYD
//