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Database: UniProt
Entry: M5VIF4_PRUPE
LinkDB: M5VIF4_PRUPE
Original site: M5VIF4_PRUPE 
ID   M5VIF4_PRUPE            Unreviewed;       631 AA.
AC   M5VIF4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ONH93952.1};
GN   ORFNames=PRUPE_8G262600 {ECO:0000313|EMBL:ONH93952.1};
OS   Prunus persica (Peach) (Amygdalus persica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=3760 {ECO:0000313|EMBL:ONH93952.1, ECO:0000313|Proteomes:UP000006882};
RN   [1] {ECO:0000313|EMBL:ONH93952.1, ECO:0000313|Proteomes:UP000006882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nemared {ECO:0000313|Proteomes:UP000006882};
RX   PubMed=23525075; DOI=10.1038/ng.2586;
RA   Verde I., Abbott A.G., Scalabrin S., Jung S., Shu S., Marroni F.,
RA   Zhebentyayeva T., Dettori M.T., Grimwood J., Cattonaro F., Zuccolo A.,
RA   Rossini L., Jenkins J., Vendramin E., Meisel L.A., Decroocq V.,
RA   Sosinski B., Prochnik S., Mitros T., Policriti A., Cipriani G., Dondini L.,
RA   Ficklin S., Goodstein D.M., Xuan P., Del Fabbro C., Aramini V., Copetti D.,
RA   Gonzalez S., Horner D.S., Falchi R., Lucas S., Mica E., Maldonado J.,
RA   Lazzari B., Bielenberg D., Pirona R., Miculan M., Barakat A., Testolin R.,
RA   Stella A., Tartarini S., Tonutti P., Arus P., Orellana A., Wells C.,
RA   Main D., Vizzotto G., Silva H., Salamini F., Schmutz J., Morgante M.,
RA   Rokhsar D.S.;
RT   "The high-quality draft genome of peach (Prunus persica) identifies unique
RT   patterns of genetic diversity, domestication and genome evolution.";
RL   Nat. Genet. 45:487-494(2013).
CC   -!- FUNCTION: Involved in the base excision repair (BER) pathway, by
CC       catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor
CC       proteins involved in chromatin architecture and in DNA metabolism. This
CC       modification follows DNA damages and appears as an obligatory step in a
CC       detection/signaling pathway leading to the reparation of DNA strand
CC       breaks. {ECO:0000256|ARBA:ARBA00024945}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC         aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC         COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC         ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC         Evidence={ECO:0000256|ARBA:ARBA00000438};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC         glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC         COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC         ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC         Evidence={ECO:0000256|ARBA:ARBA00000459};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CM007658; ONH93952.1; -; Genomic_DNA.
DR   RefSeq; XP_007199613.1; XM_007199551.1.
DR   AlphaFoldDB; M5VIF4; -.
DR   EnsemblPlants; ONH93952; ONH93952; PRUPE_8G262600.
DR   GeneID; 18768712; -.
DR   Gramene; ONH93952; ONH93952; PRUPE_8G262600.
DR   KEGG; pper:18768712; -.
DR   eggNOG; KOG1037; Eukaryota.
DR   HOGENOM; CLU_004841_2_1_1; -.
DR   OMA; QGENDRF; -.
DR   OrthoDB; 5481368at2759; -.
DR   Proteomes; UP000006882; Chromosome g8.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd01437; parp_like; 1.
DR   CDD; cd08002; WGR_PARP3_like; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 2.
DR   Gene3D; 2.20.140.10; WGR domain; 1.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
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; PTHR10459; DNA LIGASE; 1.
DR   PANTHER; PTHR10459:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF02037; SAP; 2.
DR   Pfam; PF05406; WGR; 1.
DR   SMART; SM00513; SAP; 2.
DR   SMART; SM00773; WGR; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF68906; SAP domain; 2.
DR   SUPFAM; SSF142921; WGR domain-like; 1.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50800; SAP; 2.
DR   PROSITE; PS51977; WGR; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006882};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..36
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          80..114
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          155..252
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          282..400
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          408..631
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
SQ   SEQUENCE   631 AA;  71220 MW;  C8BBF419E1351266 CRC64;
     MASKLKVEEL RNQLAQRGLT TTGNKPTLLQ RLEVALRQEN KQPPDASDVS ASIVSRKRGR
     QSNEDGESTG SEKIKATDEF QDMSVKQLRE QATLRGISAT GSKKELLERL SEDSDDIPLG
     GANEEGNGSK EKIVTATKKG AAVLDQWLPE HIKAHYHVLQ LGDDVYDAML NQTNVGYNNN
     KFYVIQVLES DAGGTFMVYY RWGRVGVKGQ NKIQGPYTSR DSAINEFKQK FYDKTKNDWS
     NRKMFESFPH HYMWIEMDYN EEEKQLSVQE KNDSALRGQP LETQLEPRIA KFISLICNIS
     MMKQHMMEIG YNADKLPLGK LSKSTISKGY NILKRIADVI GGSNRRTIEQ LSGEFYTVIP
     HDFGFKKMSN FVIDTPQKLK QKLEMVEALD EIVVATKLLK DDTGMQEDPL YSSYQRLRCE
     LTPLGADSDE FNMIAKYLHN THAKTHSNYA VDIIQIFRAS KEGEVERFRK FSSMKNRMLL
     WHGSRLTNWA GILSQGLRIA PPEAPVTGYM FGKGIYFADM FSKSANYCYA TDGCTAGVLL
     LCEVALGDMA ELLTAKYDAD KLPEGKLSTK GVGGTEPDLS QARLLDDGVV VPLGKPKENS
     EPKGALLYNE YIVYNVEQIR MRYVVQVNFH F
//
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