ID A0A1E5V675_9POAL Unreviewed; 1039 AA.
AC A0A1E5V675;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
DE Short=PARP {ECO:0000256|RuleBase:RU362114};
DE EC=2.4.2.- {ECO:0000256|RuleBase:RU362114};
GN ORFNames=BAE44_0018405 {ECO:0000313|EMBL:OEL20577.1};
OS Dichanthelium oligosanthes.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Dichantheliinae; Dichanthelium.
OX NCBI_TaxID=888268 {ECO:0000313|EMBL:OEL20577.1, ECO:0000313|Proteomes:UP000095767};
RN [1] {ECO:0000313|EMBL:OEL20577.1, ECO:0000313|Proteomes:UP000095767}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Kellogg 1175 {ECO:0000313|Proteomes:UP000095767};
RC TISSUE=Leaf {ECO:0000313|EMBL:OEL20577.1};
RA Studer A.J., Schnable J.C., Brutnell T.P.;
RT "The draft genome of Dichanthelium oligosanthes: A C3 panicoid grass
RT species.";
RL Submitted (SEP-2016) 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. {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}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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:OEL20577.1}.
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DR EMBL; LWDX02050258; OEL20577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E5V675; -.
DR STRING; 888268.A0A1E5V675; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000095767; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01437; parp_like; 1.
DR CDD; cd08001; WGR_PARP1_like; 1.
DR Gene3D; 1.10.20.130; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR038650; PADR1_C_dom_sf.
DR InterPro; IPR008288; PARP.
DR InterPro; IPR049296; PARP1-like_PADR1_N.
DR InterPro; IPR012982; PARP1-like_PADR1_Zn_ribbon.
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 InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF80; POLY [ADP-RIBOSE] POLYMERASE 1; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF21728; PADR1_N; 1.
DR Pfam; PF08063; PADR1_Zn_ribbon; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 2.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS52007; PADR1; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
DR PROSITE; PS50064; ZF_PARP_2; 2.
PE 3: Inferred from homology;
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000095767};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 8..91
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 104..176
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 459..523
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 554..666
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 688..807
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 814..1039
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 184..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1039 AA; 117107 MW; 071E20E7943AB66F CRC64;
MAAPPKAWKA EYAKSGRASC KSCRSPIAKD QLRLGKMVQA TQFDGFMPMW NHASCIFGKK
NQIKSADDVE GIDALRWDDQ EKIRNYVGSA SAATSSTAAV PDKCTIEVAP SARTSCRRCS
EKITKGTVRV SAKLEGQASK GIPWYHVNCF FEVSPSATVE KFSGWDTLSD EDKRTVLDLV
KKYVGHNEPP KGSKRKKGEN DMQSCKAAKL DGNTSEGIVQ HKGKLVDTCD SNASSADIQQ
KLKEQSDTLW KLKDELKKHV SAAELRDMLE ANEQDTSGPE RHLLDCCADG MLFGALGPCP
VCTNSLYYYN GQYQCGGNVS EWSKCTYSTT EPVRIKKKWQ IPVGIKNDYL TKWFKSQKVK
KPERVLPPMS PEKSGSKATQ RAWLLSSEGL DKLRFCIVGQ SKEVVVLCNC VDLTQNKAFV
SFPKESMPTN CLSMSCISGS STHISMILLQ VLDEWIQKLK HAGANFHARV AKDIDCLISC
GELDNENAEV RKARRLKIPV VREDYIGECI SKNRVLPFDL YKVEDALESS KGGTVTVKVK
GQSAVHESSG LQDTAHILED GKSIYNTTLN MSDLARGVNR QGPSQYFLLG FRTHFCWVIE
EDDGSECYVF RKWGRVGNEQ IGGKKVEEMS KTDAIHEFKR LFLEKTGNPW EAWEQKTNFK
KQPGRFYPLD IDYGVKQAPK RKDISEMKSS LAPRLLELMK MLFNVETYRA AMMEFEINMS
EMPLGKLSKE NIQKGFEALT EIQNLLRNTA DQALAVRESL IVAASNRFFT LIPSIHPHII
RDEDDLMIKA KMLEALQDIE IASKLVGFDS DNDESLDDKY MKLHCNITPL PHDSEDYKLV
ERYLLNTHAP THKDWSLELE EVFSLDRDGE LNKYSRYKNN LHNKMLLWHG SRLTNFVGIL
SQGLRIAPPE APVTGYMFGK GLYFADLVSK SAQYCYVDRD NPVGLMLLSE VALGDMYELK
KATSMDKPPR GKHSTKGLGK TVPLESEFVN WRDDVVVPCG KPVPSSVRSS ELLYNEYIVY
NTSQVKMQFL LKVRFHHKR
//
