ID A0A0M0JW67_9EUKA Unreviewed; 1178 AA.
AC A0A0M0JW67;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
DE Flags: Fragment;
GN ORFNames=Ctob_008953 {ECO:0000313|EMBL:KOO30795.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO30795.1, 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:KOO30795.1}.
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DR EMBL; JWZX01002160; KOO30795.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0JW67; -.
DR OrthoDB; 4079569at2759; -.
DR Proteomes; UP000037460; 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 Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000768; ART.
DR InterPro; IPR004155; PBS_lyase_HEAT.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR PANTHER; PTHR12697:SF5; DEOXYHYPUSINE HYDROXYLASE; 1.
DR PANTHER; PTHR12697; PBS LYASE HEAT-LIKE PROTEIN; 1.
DR Pfam; PF01129; ART; 1.
DR Pfam; PF13646; HEAT_2; 3.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00567; EZ_HEAT; 8.
DR SMART; SM00513; SAP; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF68906; SAP domain; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS50800; SAP; 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}; 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 DOMAIN 11..129
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 387..421
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 440..546
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1178
FT /evidence="ECO:0000313|EMBL:KOO30795.1"
SQ SEQUENCE 1178 AA; 128301 MW; 0DECBF76BEDF40C2 CRC64;
MPPRVPKGKQ KAEPDADVED EAPAAKKPKG KQKAEPDADV EDDAPSGAAL GKLTREQIEK
GQAVLATIRT HLESEGSAPS SLTNDFYSLI PTVVGRAKPP TINSFGILGE KEALLEFWLR
MGFEDCTITM TNPLEQLAST PRPPNLTKAA TGIADLGSIG QALSRGKTLA DAAAGGPKKP
MDDQMYGAIV LYTGNAIYRA LNEALRVKHA NVPRYLPYVK LFFAAAECLP KKAEQLWRGI
AADLYAEYEE GKEIVWWTVS STTASEMVAR GFMSQLGGKA TLLKLDTVNA INIEPLSIYP
HEQERLLVPG TRLKVLSRKQ MGNLAEIHVK EVGNALEDKF SMSSRVPKGK QKAEPDADVE
DEAPAAKKPK GKQKAEPVRP TIAPEAVAKM SMGELKEELS ARGLDTSGKK AELVSEMRRG
LRHKLSCALR VDRAVPGGAQ YAVYEDYDVK LSQHPLVDGA NVNKYYFLQV LQKQGGTFAT
YFKFGLIGEK DYGDKLDGPF ESAAEAIQSF EAKFHEKTRG KKDKSPKEAA WAAYKAGQFE
KREGYYGVVE TKVGVNVGVN ETLGQLKPAT LAQHGAALVA RLEDEDAGVR RAVVQTLGQL
ELATLAQYGA ALVARLEDED AFVRRAVVQT LGQLEPATLA QYGAALVARL EDSDAFVRRA
HGDALVAMLE DSDADVRRAV VQTLGQLELA TLAQHGKALV ARLEDSHDFV RRAVVEMLGK
LELATLAQHG AALVAMLEDQ EWEVRQAVVE TLGQLELATL AQHGAALVAG LEDEDEGVRR
AVVETLGKLE PGTLAQHGVA LVARLEDYDY FVRCAVVETL GKLEPGTLAQ YGAALVAMLK
DSDEFVRHAV VETLGKLEPG TLAQYGAALV AMLKDSDEGV RCAVVETLEK DEGVRCAVVE
TLEKLEPGTL APHTPHTRPA HAKFLHYYPQ SDGRDAERLE GNTSELKLID GVELRSSSRS
QGGPLRADMF SVELIQSDHP RYDPLATGAL SKVVDIKVVS GDVTYPLLLR MRHHASAEQF
GQLAFYRAET PDSEMQLVEG GCFWSDGYAE VEVTSFSVWK IALEAAKFAF AVWNTYIDHP
VGVTAFAPED LDLPLILKFV LHPQNDIPPN NNFEGFCKVG EDKDVPICRG KEVTIALKDF
PELSVTFQPW KNKRQSEEMN GVVELRPSSS HKAVIKGI
//
