PARP1_MAIZE
ID PARP1_MAIZE Reviewed; 980 AA.
AC Q9ZSV1; O24570;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Poly [ADP-ribose] polymerase 1;
DE Short=PARP-1;
DE EC=2.4.2.30;
DE AltName: Full=NAD(+) ADP-ribosyltransferase 1;
DE Short=ADPRT-1;
DE AltName: Full=Poly[ADP-ribose] synthase 1;
DE AltName: Full=Protein ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=PARP1;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9778846; DOI=10.1046/j.1365-313x.1998.00240.x;
RA Babiychuk E., Cottrill P.B., Storozhenko S., Fuangthong M., Chen Y.,
RA O'Farrell M.K., Van Montagu M., Inze D., Kushnir S.;
RT "Higher plants possess two structurally different poly(ADP-ribose)
RT polymerases.";
RL Plant J. 15:635-645(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9808734; DOI=10.1104/pp.118.3.895;
RA Mahajan P.B., Zuo Z.;
RT "Purification and cDNA cloning of maize poly(ADP)-ribose polymerase.";
RL Plant Physiol. 118:895-905(1998).
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}.
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:0000250|UniProtKB:P09874};
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:P09874};
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:P09874};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00264}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR EMBL; AJ222589; CAA10889.1; -; mRNA.
DR EMBL; AF093627; AAC79704.1; -; mRNA.
DR PIR; T03657; T03657.
DR RefSeq; NP_001288538.1; NM_001301609.1.
DR AlphaFoldDB; Q9ZSV1; -.
DR SMR; Q9ZSV1; -.
DR STRING; 4577.GRMZM5G831712_P02; -.
DR PaxDb; Q9ZSV1; -.
DR EnsemblPlants; Zm00001eb094840_T001; Zm00001eb094840_P001; Zm00001eb094840.
DR GeneID; 103647201; -.
DR Gramene; Zm00001eb094840_T001; Zm00001eb094840_P001; Zm00001eb094840.
DR KEGG; zma:103647201; -.
DR MaizeGDB; 403204; -.
DR eggNOG; KOG1037; Eukaryota.
DR OrthoDB; 909382at2759; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; Q9ZSV1; baseline and differential.
DR Genevisible; Q9ZSV1; ZM.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030592; P:DNA ADP-ribosylation; IEA:EnsemblPlants.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEA:EnsemblPlants.
DR GO; GO:0006979; P:response to oxidative stress; IEA:EnsemblPlants.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
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; IPR008288; PARP.
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; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF08063; PADR1; 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; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
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; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS50800; SAP; 1.
DR PROSITE; PS51977; WGR; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; DNA-binding; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..980
FT /note="Poly [ADP-ribose] polymerase 1"
FT /id="PRO_0000260500"
FT DOMAIN 257..291
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT DOMAIN 385..476
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 507..607
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 629..748
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 755..980
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 8..91
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 104..184
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 180..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 54..64
FT /note="Missing (in Ref. 1; CAA10889)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="L -> I (in Ref. 1; CAA10889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 980 AA; 110475 MW; 9D8AED26BC37E5C1 CRC64;
MAAPPKAWKA EYAKSGRASC KSCRSPIAKD QLRLGKMVQA SQFDGFMPMW NHARCIFSKK
NQIKSVDDVE GIDALRWDDQ EKIRNYVGSA SAGTSSTAAP PEKCTIEIAP SARTSCRRCS
EKITKGSVRL SAKLESEGPK GIPWYHANCF FEVSPSATVE KFSGWDTLSD EDKRTMLDLV
KKDVGNNEQN KGSKRKKSEN DIDSYKSARL DESTSEGTVR NKGQLVDPRG SNTSSADIQL
KLKEQSDTLW KLKDGLKTHV SAAELRDMLE ANGQDTSGPE RHLLDRCADG MLFGALGPCP
VCANGMYYYN GQYQCSGNVS EWSKCTYSAT EPVRVKKKWQ IPHGTKNDYL MKWFKSQKVK
KPERVLPPMS PEKSGSKATQ RTSLLSSKGL DKLRFSVVGQ SKEAANEWIE KLKLAGANFY
ARVVKDIDCL IACGELDNEN AEVRKARRLK IPIVREGYIG ECVKKNKMLP FDLYKLENAL
ESSKGSTVTV KVKGRSAVHE SSGLQDTAHI LEDGKSIYNA TLNMSDLALG VNSYYVLQII
EQDDGSECYV FRKWGRVGSE KIGGQKLEEM SKTEAIKEFK RLFLEKTGNS WEAWECKTNF
RKQPGRFYPL DVDYGVKKAP KRKDISEMKS SLAPQLLELM KMLFNVETYR AAMMEFEINM
SEMPLGKLSK ENIEKGFEAL TEIQNLLKDT ADQALAVRES LIVAASNRFF TLIPSIHPHI
IRDEDDLMIK AKMLEALQDI EIASKIVGFD SDSDESLDDK YMKLHCDITP LAHDSEDYKL
IEQYLLNTHA PTHKDWSLEL EEVFSLDRDG ELNKYSRYKN NLHNKMLLWH GSRLTNFVGI
LSQGLRIAPP EAPVTGYMFG KGLYFADLVS KSAQYCYVDR NNPVGLMLLS EVALGDMYEL
KKATSMDKPP RGKHSTKGLG KTVPLESEFV KWRDDVVVPC GKPVPSSIRS SELMYNEYIV
YNTSQVKMQF LLKVRFHHKR
