NARE_CHICK
ID NARE_CHICK Reviewed; 300 AA.
AC Q92080; Q91050;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Erythroblast NAD(P)(+)--arginine ADP-ribosyltransferase;
DE EC=2.4.2.31;
DE AltName: Full=Mono(ADP-ribosyl)transferase;
DE Flags: Precursor;
GN Name=MADPRT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Blood;
RX PubMed=7590361; DOI=10.1016/0378-1119(95)00504-y;
RA Davis T., Shall S.;
RT "Sequence of a chicken erythroblast mono(ADP-ribosyl)transferase-encoding
RT gene and its upstream region.";
RL Gene 164:371-372(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC ribosyl)-L-arginyl-[protein] + nicotinamide; 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 -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000305}.
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DR EMBL; X83676; CAA58649.1; -; Genomic_DNA.
DR EMBL; X82397; CAA57793.1; -; mRNA.
DR PIR; JC4367; JC4367.
DR AlphaFoldDB; Q92080; -.
DR SMR; Q92080; -.
DR STRING; 9031.ENSGALP00000035605; -.
DR VEuPathDB; HostDB:LOC121109081; -.
DR eggNOG; ENOG502QUE9; Eukaryota.
DR InParanoid; Q92080; -.
DR PhylomeDB; Q92080; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR InterPro; IPR000768; ART.
DR Pfam; PF01129; ART; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
DR PROSITE; PS01291; ART; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycosyltransferase; NAD; NADP; Nucleotidyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..300
FT /note="Erythroblast NAD(P)(+)--arginine ADP-
FT ribosyltransferase"
FT /id="PRO_0000019341"
FT DOMAIN 70..256
FT /note="TR mART core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT REGION 276..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT ACT_SITE 224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT BINDING 107
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT DISULFID 51..260
FT /evidence="ECO:0000250"
FT DISULFID 159..208
FT /evidence="ECO:0000250"
FT CONFLICT 60
FT /note="Q -> E (in Ref. 1; CAA58649)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="E -> K (in Ref. 1; CAA58649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 34008 MW; 1D33BE2850D18158 CRC64;
MEEPLLHAIL GLVLLLSTRT DASAARSKKG PIKEVVMDMA PHSFDDQYQG CIDLMEAELQ
ELNRTEFANE TFAEGWRSAT EEWQRRWGRV SSPMVLRQDQ AIAVLAYTME GELYRVFNNA
TLTAGRSRQH YLSSYPFKTL HFLLSRALHT LQESQTQPCH NVFRGVRGTR FTAQQGTVVR
FGQFTSSSLQ KKVAEFFGLD TFFSVETCYG VPIKDLSTFP GEDEVLIPPF EQFRVTNSTY
TAGRSFIQLR SQGKSSTYNC EFVKEKRCKE RPCAFSADKS SPLPRSPWPG WAPLAAPHSH