ID A0A0M0K4X1_9EUKA Unreviewed; 1020 AA.
AC A0A0M0K4X1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=Ctob_009915 {ECO:0000313|EMBL:KOO33423.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO33423.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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 -!- 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:KOO33423.1}.
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DR EMBL; JWZX01001523; KOO33423.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0K4X1; -.
DR OrthoDB; 47012at2759; -.
DR Proteomes; UP000037460; 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; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000768; ART.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR24193:SF121; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24193; ANKYRIN REPEAT PROTEIN; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01129; ART; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51996; TR_MART; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
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:UP000037460};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361228}.
FT REPEAT 962..994
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 125..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1020 AA; 111611 MW; 6D317F0054474FD4 CRC64;
MLQSLEYATD TLAGCIGEGA GWTLVTLIEA WKCACRYRLL QLTAPGELLR SFVSEGKERK
TLASAVQRLR ASMAPFEHVC AADPLAVAAA ERDAYLVRIG EVLHVAQPLA YILLLVAQQR
GASSLSDEKK TVGAPTDRSS LPNERVAKAP PKAPLIAKAL SKLGALNEAD EGLTKEAALL
LKEAVDGAGG SENVPDDGGG GGDSRPPLKG IATVGNLLTK INKLKGLPTK KKKEVEAAEA
KRAEWMAEWK KWVVNINVPE LVTEALQMPT ESEADAFEYM RQLTREAVQE LLEKAGLVGL
LDHVMAGLGK VMGQIAPSGP ALAEQYKTSA KFTMGFGDLS DFFNGLEALL GPPQMAKDPA
TGEATIFRAM EVEHCFECDS EKEFTSSNGV TTTSMLEWEF VVKPDLNRAE RHVLDAETGE
PTGEKLGPYP ERLHLAEQHP EWCRKPRSRE ELDELLEKKA NSKLREQFGE DAVLITEEFL
AAVLYTGPMF QKYNAVLRSK TKDEFLVSLW KKQCGKNTYT TTIHAISSAV IKLSKLSKAG
KVYRGVCYGR FPDKFWVADE MGVRGGVEFG FSSTTRERQQ AVHYADGGGN AKSGEAKTIL
EMQMGMIDRG ADIYWLSQYP HERECLLPPL TGIEVIGSEV QEDKLVIHSR LSLNLAADTL
DQVLSRRRKM LMDMARGIEL EIKEALKTQE RLIEPATRIL RKAIAYGALN QEPEWYNNDD
NFAKVMQETL YLQRTLISEV KTLWAAIELP DLNLKGWKAT GPARVMLLAG WLLCRSSPVD
VCIDLQQCRL TSDDGIKLAK LMKDMPKLAS IDVRGNESLG EEGARALIDW LQWDKNEKTV
GRKLRSLCGV GMGGSSRIDV PRSGLASLDA GGAKINYIKP VELSILCAEL ETNIFAEGVS
AGMGGKGGGQ CTSLNRRGHA GVGEWQPLVW AAKDNNLAVA CKLLDTGTDV NLQEPLEDKG
SSGYAALHWA AMRGFKEMIS MLLKRGANLE LVDKHGNTAL MLAQKKGNKE VMALLTKGRG
//
