ID T0Q1P2_SAPDV Unreviewed; 635 AA.
AC T0Q1P2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=SDRG_05006 {ECO:0000313|EMBL:EQC37402.1}, SDRG_14931
GN {ECO:0000313|EMBL:EQC27310.1};
OS Saprolegnia diclina (strain VS20).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=1156394 {ECO:0000313|EMBL:EQC27310.1, ECO:0000313|Proteomes:UP000030762};
RN [1] {ECO:0000313|EMBL:EQC27310.1, ECO:0000313|Proteomes:UP000030762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VS20 {ECO:0000313|EMBL:EQC27310.1,
RC ECO:0000313|Proteomes:UP000030762};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Nusbaum C., Tyler B., van West P., Dieguez-Uribeondo J.,
RA de Bruijn I., Tripathy S., Jiang R., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Saprolegnia declina VS20.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000858,
CC ECO:0000256|RuleBase:RU361228};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000256|ARBA:ARBA00033987};
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
CC -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009558, ECO:0000256|RuleBase:RU361228}.
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DR EMBL; JH767211; EQC27310.1; -; Genomic_DNA.
DR EMBL; JH767144; EQC37402.1; -; Genomic_DNA.
DR RefSeq; XP_008608922.1; XM_008610700.1.
DR RefSeq; XP_008619313.1; XM_008621091.1.
DR AlphaFoldDB; T0Q1P2; -.
DR STRING; 1156394.T0Q1P2; -.
DR EnsemblProtists; EQC27310; EQC27310; SDRG_14931.
DR EnsemblProtists; EQC37402; EQC37402; SDRG_05006.
DR GeneID; 19945733; -.
DR GeneID; 19955658; -.
DR VEuPathDB; FungiDB:SDRG_05006; -.
DR VEuPathDB; FungiDB:SDRG_14931; -.
DR eggNOG; KOG1037; Eukaryota.
DR InParanoid; T0Q1P2; -.
DR OMA; KYTIVET; -.
DR OrthoDB; 55777at2759; -.
DR Proteomes; UP000030762; Unassembled WGS sequence.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
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 CDD; cd17748; BRCT_DNA_ligase_like; 2.
DR CDD; cd08002; WGR_PARP3_like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 2.20.140.10; WGR domain; 1.
DR InterPro; IPR000768; ART.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR Pfam; PF01129; ART; 1.
DR Pfam; PF00533; BRCT; 2.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51996; TR_MART; 1.
DR PROSITE; PS51977; WGR; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU361228};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361228};
KW NADP {ECO:0000256|RuleBase:RU361228};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000030762};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361228}.
FT DOMAIN 1..88
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 84..152
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 231..324
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 307..426
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT REGION 170..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 68821 MW; 2F6570449B670735 CRC64;
MPLTGEVVAL SGKFETMTRA EATKRIQAAG GSVSSSVTKA TTLLVTTAGD ESKKYKDAVA
AGIKICMEDA LVQALDGKAA SALEGQVVAL SGKLATMTRA DATAQIVEAG GTVSSTVTKK
TSILVAADGT EGKKTQTAAA QGVVIWTEAQ LVAALSGAAP ASVVVKDEFE EKPAAKKKRA
AKDEAAPPAK KPKAEEVKPE AVKGETSDPP PALGERRGAR RPDKHLSTRE KFEIFDDYST
DLMQTNIGHN NNKFYIIQLL QATADSTFHV FTRWGRLGEA GQQNLKGFGR DVDKAIALFE
KKFRDKTKND WHQRHAFVKY DLQYQLVELD ASETGDGGGD SDAAMGKLSA AQIEKGQAVL
AQLKTSLTGK PSSALITQLS GQYYSLVPTL SGRQRPPPLN TLALVEEKEA LLDFWLRMGF
DDMEEQTHLA PIEGLMDLPK PENLGIAAAG ICHASAVKQC QSRGQQLVVS NAGAPVKPMD
KDLYGSIVLY TGNWIYAELN NALRSENRAA VKRYFKYLRL FMEAMNYMPK KSQVLWRGIS
VDLFDQYEEG KVITWWGVSS TTSDENVARG FMNSCGGSCT LLSVRCTTAM DISVLSMYPN
EKECLLAPGT QFKVLKRARK GRIAEIEIEE VGRCI
//
