ID I1LKS7_SOYBN Unreviewed; 691 AA.
AC I1LKS7;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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 Name=100788978 {ECO:0000313|EnsemblPlants:KRH30444};
GN ORFNames=GLYMA_11G184100 {ECO:0000313|EMBL:KRH30444.1};
OS Glycine max (Soybean) (Glycine hispida).
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; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH30444.1};
RN [1] {ECO:0000313|EMBL:KRH30444.1, ECO:0000313|EnsemblPlants:KRH30444}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH30444};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH30444.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH30444}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH30444};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH30444.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH30444.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; CM000844; KRH30444.1; -; Genomic_DNA.
DR AlphaFoldDB; I1LKS7; -.
DR EnsemblPlants; KRH30444; KRH30444; GLYMA_11G184100.
DR Gramene; KRH30444; KRH30444; GLYMA_11G184100.
DR Proteomes; UP000008827; Chromosome 11.
DR ExpressionAtlas; I1LKS7; baseline and differential.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd17747; BRCT_PARP1; 1.
DR CDD; cd08001; WGR_PARP1_like; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.90.640.80; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
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 PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF106; PROTEIN ADP-RIBOSYLTRANSFERASE PARP3; 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 SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
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.
PE 3: Inferred from homology;
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
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:UP000008827};
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 182..274
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 322..422
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 449..568
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 577..691
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 77983 MW; F0AEA5C317A15956 CRC64;
MKVQETRSHV HAPGEEEKVM TRKQKAESKA HEVEHSPKKA KVEKEDGQIN GKSETGVAEE
YDEFCKVTNE HLPLEQMREI MEANSLDSSG SDLEIARRCQ DLLFYGALDK CSVCNGSLEF
DGRRYVCRGF YSEWASCTFS TRNPPRKQEP IKLPDSVQDS LASDLLKKYQ DPSHRPHRDL
GLAEKPFTGM MISLMGRLTR THHYWKTTIE KHGGKVANSI IGATCLVASP AERERGGTSK
LAEAMERGIP VVREAWLIDS IEKQEPQPLE SYDLVSDLSV DGKGIPWDKQ DPGEEAIESL
SAELKLYGKR GVYKDSKLQE QGGKIFERDG ILYNCAFSVC DQGLGLNDYC VMQLIVVPEN
PLHLYFKKGR VGDDPNAEEQ LEEWDNVDGA LKEFARLFDE ITGNEFEPWE REKKFQKKPL
KFYPIDMDDG VEVRHGALGL RQLGIAATHC KLEPLVANFM KVLCSQEIYK YALMEMGYDS
PDLPIGMVTN LHLKRCEDVL LEFIDKMKSL KETGPKAEAV WTDFSQRWFT LMHSTRPFNF
RDYQEIAEHA AAALEGVRDI TQASHLIGDM TGSTIDDPLS ETYKKLGCSI SALDKSSDDY
EMIVKYLEKT YEPVKVGDIE YGVSVENIFA VQTGGCPSYE DIVKLPNKVL LWCGSRSSNL
LRHLHKGFSP AICSLPVPGY MVIVIDLVIQ F
//
