PARP3_MEDTR
ID PARP3_MEDTR Reviewed; 799 AA.
AC Q1SGF1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Protein ADP-ribosyltransferase PARP3 {ECO:0000250|UniProtKB:Q9Y6F1};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q9Y6F1};
DE AltName: Full=NAD(+) ADP-ribosyltransferase 3;
DE Short=ADPRT-3;
DE AltName: Full=Poly[ADP-ribose] synthase 3;
DE AltName: Full=Putative poly [ADP-ribose] polymerase 3;
DE Short=PARP-3;
GN Name=PARP3;
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The International Medicago Genome Annotation Group;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250|UniProtKB:Q9Y6F1}.
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:0000250|UniProtKB:Q9Y6F1};
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:0000250|UniProtKB:Q9Y6F1};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AC144515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q1SGF1; -.
DR SMR; Q1SGF1; -.
DR STRING; 3880.AES88336; -.
DR eggNOG; KOG1037; Eukaryota.
DR ExpressionAtlas; Q1SGF1; differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
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; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 3: Inferred from homology;
KW ADP-ribosylation; DNA-binding; Glycosyltransferase; NAD;
KW Nucleotidyltransferase; Nucleus; Transferase.
FT CHAIN 1..799
FT /note="Protein ADP-ribosyltransferase PARP3"
FT /id="PRO_0000260501"
FT DOMAIN 71..105
FT /note="SAP"
FT DOMAIN 165..261
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 309..409
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 436..555
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 564..795
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 799 AA; 89991 MW; 0B108316557FDE8A CRC64;
MKVESRSHNV HHAHGEEEKV MTRKQKAESK AHEVEHSPKK AKVEDEKNGH TNGKSASDVV
QEYDEFCKAT NEQLSLEQMK EILEANDLDS SGSDLEITRR CQDLLFFGAL EKCMVCNGNM
EFDGRRYGCR GFYSEWSSCT FSTREPPRKD EPIKLPDSVQ NSPVSDLLKK YQDPSKRPQR
DLGLAIKPFT GMMISLMGRL NRTHLNFSGA SCLVASPAER DRGGTSKLAD AMERGIPVVR
EAWLTDSIEK QEPQPLESYD LVSDLSVDGK GIPWDKQDPG EEAIESLSAE LKLYGKRGVY
KDTKLHEQDG KIFEKDGILY NCAFSLCDQG RKLNDYCVMQ LIVVPENSLH LYFKKGRVGD
DPSAEERLEE CENVDNAIKE FVRLFEEITG NEFESWEREK KFQKKPLKFY PIDMDDGVEV
RHGALGLRQL GIAATHCKLE PMVANFMKVL CSQEIYKYAL MEMGYDSPDL PIGMVTNLHL
KRCEEILLEF IEKVKTLKET GPKADAIWSD FSQKWFTLMH STRPFIFRDY QEIADHAAAA
LEGVRDITLA SHLIGDMSGS TIDDPLSDTY KKLGCSITPL EKNSNDYEMI VKYLEKTYEP
VKVGDIEYGV SVENIFTVES SACPSYADIV KMPNKVLLWC GSRSSNLLRH LHKGFLPAIC
SLPVPGYMFG KAIVCSDAAA EAARYGFTAV DRPEGFLVLA IASLGNEITE LKSPPEDTTS
LEEKKVGVKG LGKKKTDESE HFVWKDDIKV PCGSIIASEH EDSPLEYNEY AVYDPKQVRI
SYLVGVKYEE KDAVIDTAE
