ID A0A8T2NE50_9TELE Unreviewed; 520 AA.
AC A0A8T2NE50;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 15.
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=JZ751_003371 {ECO:0000313|EMBL:KAG9335972.1};
OS Albula glossodonta (roundjaw bonefish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Albuliformes; Albulidae; Albula.
OX NCBI_TaxID=121402 {ECO:0000313|EMBL:KAG9335972.1, ECO:0000313|Proteomes:UP000824540};
RN [1] {ECO:0000313|EMBL:KAG9335972.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HI-2016 {ECO:0000313|EMBL:KAG9335972.1};
RA Pickett B.D.;
RT "Applications of and Algorithms for Genome Assembly and Genomic Analyses
RT with an Emphasis on Marine Teleosts.";
RL Thesis (2021), BYU ScholarsArchive, Provo, UT, USA.
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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:KAG9335972.1}.
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DR EMBL; JAFBMS010000104; KAG9335972.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8T2NE50; -.
DR OrthoDB; 8300214at2759; -.
DR Proteomes; UP000824540; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0004046; F:aminoacylase activity; IEA:TreeGrafter.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.20.25.160; -; 1.
DR Gene3D; 3.90.176.10; Toxin ADP-ribosyltransferase, Chain A, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000768; ART.
DR InterPro; IPR050178; AspA/AstE_fam.
DR InterPro; IPR055438; AstE_AspA_cat.
DR InterPro; IPR007036; Aste_AspA_hybrid_dom.
DR NCBIfam; NF002601; PRK02259.1; 1.
DR PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR PANTHER; PTHR15162:SF5; N-ACYL-AROMATIC-L-AMINO ACID AMIDOHYDROLASE (CARBOXYLATE-FORMING); 1.
DR Pfam; PF01129; ART; 1.
DR Pfam; PF24827; AstE_AspA_cat; 2.
DR Pfam; PF04952; AstE_AspA_hybrid; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS01291; ART; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361228}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|RuleBase:RU361228}; NADP {ECO:0000256|RuleBase:RU361228};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000824540};
KW Signal {ECO:0000256|RuleBase:RU361228};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361228};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU361228"
FT CHAIN 24..520
FT /note="NAD(P)(+)--arginine ADP-ribosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361228"
FT /id="PRO_5035967981"
FT DOMAIN 227..276
FT /note="Succinylglutamate desuccinylase/Aspartoacylase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF24827"
FT DOMAIN 284..407
FT /note="Succinylglutamate desuccinylase/Aspartoacylase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF24827"
FT DOMAIN 426..506
FT /note="AstE/AspA barrel-sandwich hybrid"
FT /evidence="ECO:0000259|Pfam:PF04952"
SQ SEQUENCE 520 AA; 57517 MW; F36F38AA1CE20D02 CRC64;
MGSLTAGGIT LLLITAIIHI VDSAVKMDMS PSAVDDQFLK CRERMLQKVL GGLLQQELRA
NIKFQQAWGN TVCEHPIPKG TVQHTKALAM YTHETKGFST EFDTAVQSQG GNARSYEGFP
FKALHFLLTD ALRLLGGKGC GTVCHHSDDL YEVSEGAEVR FGTFMAAIHS CDDSDTPDKG
TLFEITSCTA VQVDNHACDP EEVEMLIQPF EVFKVLEMEP ASLPAVSRMA LCGGTHGNEL
SGVYLVREWQ KKKRELEGEA EPITVMTLIS NPRAVQHTLV SDGVPYEIAR AQELNALLGP
RGSDGAVDLI CDLHNTTANM GLCLITNSDC DWICLHIYKY IQARISDPRT TKLSSMPVRL
LNLNAPPDQN YFLASVGKHA LSIEIGPQPH GLVRADILST MKEGVHLMIE WLRLFNSGTE
FEGGIVEVYS FLKNIDFPRD PETHDITAII HPQLQDQDFC LLKPGDPIFL SFSGESVVYE
GGEPLYPVFV NESSYYEKGT AFTLTRMKKV EIPPLRLKRD
//
