ID R7W1D9_AEGTA Unreviewed; 650 AA.
AC R7W1D9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:EMT00412};
OS Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=37682 {ECO:0000313|EnsemblPlants:EMT00412};
RN [1] {ECO:0000313|EnsemblPlants:EMT00412}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; R7W1D9; -.
DR EnsemblPlants; EMT00412; EMT00412; F775_03946.
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 GO; GO:0030592; P:DNA ADP-ribosylation; IEA:EnsemblPlants.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblPlants.
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; 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; 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; 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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..67
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 109..143
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT DOMAIN 199..295
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 324..442
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 429..650
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 650 AA; 73108 MW; 6D233E78BA7F393A CRC64;
MDGKAEGKSK RKRKRHGEGE NEEENDILDA AKLQSMGYRE LQALAKARGL NANGGKKDVL
QRLLSSPATS VVDRGVQDKK EVAQADDGKV EELKKKKIVT DVMLDAAQLQ GMGYRELQAL
AKARGLAANG IKKDVIERLL STPANSVAVA DGGFQDKKKL AKGGVGEVEE EVKKEKIVKA
TKKGAAVLDE HIPDDIKMTY HVLQVGDEIY DATLNQTNVG DNNNKYYIIQ ALESDAGGSF
MVFNRWGRVG ARGQQKLHPC STRDEAIDEF EGKFEDKTKN SWSDRKNFER YAKKYTWLEM
DYGEVDKETT QVQKKGSITD QIKETKLETR TAQFISLICN ISMMKQQMME IGYNADKLPL
GKLSKSTILK GYDVLKRISN VISRADRRQL EQLTGEFYTV IPHDFGFKKM REFLIDTPQK
LKAKLEMEDP LYARYKQLHC DFTPLEVHSK EYSMIKTYLT NTHGKTHSGY TIDILQMFKV
SRHGETERFQ KFASAGNRML LWHGSRLSNW AGIFSQGLRI APPEAPVTGY MFGKGVYFAD
MFSKSANYCY ASQTSRSGVL LLCEVALGDM NELLNAKYDA DNLPKGKLST KGVGQMAPAE
SKVTEDGVVV PLGKPKEEPS KRGSLLYNEY IVYNVEQIRM RGLLFVEQMF
//
