ID PARP1_CHICK Reviewed; 1011 AA. AC P26446; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 24-JAN-2024, entry version 170. DE RecName: Full=Poly [ADP-ribose] polymerase 1; DE Short=PARP-1; DE EC=2.4.2.30 {ECO:0000250|UniProtKB:P09874}; DE AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 1; DE Short=ARTD1; DE AltName: Full=DNA ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874}; DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874}; DE AltName: Full=NAD(+) ADP-ribosyltransferase 1; DE Short=ADPRT 1; DE AltName: Full=Poly[ADP-ribose] synthase 1; DE AltName: Full=Protein poly-ADP-ribosyltransferase PARP1 {ECO:0000250|UniProtKB:P09874}; DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874}; GN Name=PARP1; Synonyms=ADPRT; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; OC Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Oviduct; RX PubMed=1840535; DOI=10.1016/0378-1119(91)90073-k; RA Ittel M.-E., Garnier J.-M., Jeltsch J.-M., Niedergang C.; RT "Chicken poly(ADP-ribose) synthetase: complete deduced amino acid sequence RT and comparison with mammalian enzyme sequences."; RL Gene 102:157-164(1991). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 659-1011. RX PubMed=8755499; DOI=10.1073/pnas.93.15.7481; RA Ruf A., Mennissier-de Murcia J., de Murcia G.M., Schulz G.E.; RT "Structure of the catalytic fragment of poly(AD-ribose) polymerase from RT chicken."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7481-7485(1996). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 659-1011, AND SEQUENCE REVISION TO RP 895. RX PubMed=9521710; DOI=10.1021/bi972383s; RA Ruf A., de Murcia G.M., Schulz G.E.; RT "Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from RT crystal structures and homology modeling."; RL Biochemistry 37:3893-3900(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 659-1011. RX PubMed=9571033; DOI=10.1006/jmbi.1998.1673; RA Ruf A., Rolli V., de Murcia G.M., Schulz G.E.; RT "The mechanism of the elongation and branching reaction of poly(ADP-ribose) RT polymerase as derived from crystal structures and mutagenesis."; RL J. Mol. Biol. 278:57-65(1998). CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP- CC ribosylation of proteins and plays a key role in DNA repair (By CC similarity). Mediates glutamate, aspartate, serine, histidine or CC tyrosine ADP-ribosylation of proteins: the ADP-D-ribosyl group of CC NAD(+) is transferred to the acceptor carboxyl group of target residues CC and further ADP-ribosyl groups are transferred to the 2'-position of CC the terminal adenosine moiety, building up a polymer with an average CC chain length of 20-30 units. Serine ADP-ribosylation of proteins CC constitutes the primary form of ADP-ribosylation of proteins in CC response to DNA damage (By similarity). Specificity for the different CC amino acids is conferred by interacting factors, such as hpf1 and CC nmnat1 (By similarity). Following interaction with hpf1, catalyzes CC serine ADP-ribosylation of target proteins; hpf1 confers serine CC specificity by completing the parp1 active site. Also catalyzes CC tyrosine ADP-ribosylation of target proteins following interaction with CC hpf1 (By similarity). Following interaction with nmnat1, catalyzes CC glutamate and aspartate ADP-ribosylation of target proteins; nmnat1 CC confers glutamate and aspartate specificity (By similarity). Parp1 CC initiates the repair of DNA breaks: recognizes and binds DNA breaks CC within chromatin and recruits hpf1, licensing serine ADP-ribosylation CC of target proteins, such as histones (H2BS6ADPr and H3S10ADPr), thereby CC promoting decompaction of chromatin and the recruitment of repair CC factors leading to the reparation of DNA strand breaks. In addition to CC base excision repair (BER) pathway, also involved in double-strand CC breaks (DSBs) repair. Mediates the poly-ADP-ribosylation of a number of CC proteins. In addition to proteins, also able to ADP-ribosylate DNA: CC catalyzes ADP-ribosylation of DNA strand break termini containing CC terminal phosphates and a 2'-OH group in single- and double-stranded CC DNA, respectively (By similarity). Parp1-mediated DNA repair in neurons CC plays a role in sleep: senses DNA damage in neurons and promotes sleep, CC facilitating efficient DNA repair (By similarity). In addition to DNA CC repair, also involved in other processes, such as transcription CC regulation, programmed cell death, membrane repair, adipogenesis and CC innate immunity (By similarity). Acts as a repressor of transcription: CC binds to nucleosomes and modulates chromatin structure in a manner CC similar to histone H1, thereby altering RNA polymerase II. Acts both as CC a positive and negative regulator of transcription elongation, CC depending on the context (By similarity). Poly-ADP-ribose chains CC generated by parp1 also play a role in poly-ADP-ribose-dependent cell CC death, a process named parthanatos. Also acts as a negative regulator CC of the cGAS-STING pathway by mediating poly-ADP-ribosylation and CC inactivation of cgas. Acts as a negative regulator of adipogenesis by CC catalyzing poly ADP-ribosylation of histone H2B on 'Glu-35' CC (H2BE35ADPr) (By similarity). {ECO:0000250|UniProtKB:P09874, CC ECO:0000250|UniProtKB:P11103, ECO:0000250|UniProtKB:Q5RHR0}. 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-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D- CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA- CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:P09874}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233; 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:P11103}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; CC Evidence={ECO:0000250|UniProtKB:P11103}; 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:P11103}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; CC Evidence={ECO:0000250|UniProtKB:P11103}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-tyrosyl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D- CC ribosyl)-L-tyrosyl-[protein]; Xref=Rhea:RHEA:58236, Rhea:RHEA- CC COMP:10136, Rhea:RHEA-COMP:15092, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:46858, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:142557; Evidence={ECO:0000250|UniProtKB:P09874}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58237; CC Evidence={ECO:0000250|UniProtKB:P09874}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-histidyl-[protein] + NAD(+) = H(+) + N(tele)-(ADP-D- CC ribosyl)-L-histidyl-[protein] + nicotinamide; Xref=Rhea:RHEA:72071, CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:18085, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29979, ChEBI:CHEBI:57540, CC ChEBI:CHEBI:191398; Evidence={ECO:0000250|UniProtKB:P09874}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72072; CC Evidence={ECO:0000250|UniProtKB:P09874}; CC -!- ACTIVITY REGULATION: ADP-ribosyltransferase activity is regulated via CC an allosteric activation mechanism. In absence of activation signal, CC parp1 is autoinhibited by the PARP alpha-helical domain (also named HD CC region), which prevents effective NAD(+)-binding. Activity is highly CC stimulated by signals, such as DNA strand breaks. Binding to damaged CC DNA unfolds the PARP alpha-helical domain, relieving autoinhibition. CC Poly-ADP-ribosyltransferase activity is tightly regulated and parp1 is CC removed from damaged chromatin following initial poly-ADP-ribosylation CC of chromatin to avoid prolonged residence (trapping) that has cytotoxic CC consequences. A number of factors or post-translational modifications CC (auto-poly-ADP-ribosylation) promote parp1 removal from chromatin. CC {ECO:0000250|UniProtKB:P09874}. CC -!- SUBUNIT: Homodimer; PARP-type zinc-fingers from separate parp1 CC molecules form a dimer module that specifically recognizes DNA strand CC breaks. {ECO:0000250|UniProtKB:P09874}. CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000250|UniProtKB:P09874}. CC Nucleus {ECO:0000250|UniProtKB:P09874}. Nucleus, nucleolus CC {ECO:0000250|UniProtKB:P09874}. Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P09874}. Note=Localizes to sites of DNA damage. CC Recognizes (via PARP-type zinc-fingers) and binds DNA strand breaks. CC Also binds normal/undamaged chromatin. Auto poly-ADP-ribosylation CC promotes dissociation from chromatin. {ECO:0000250|UniProtKB:P09874}. CC -!- DOMAIN: The two PARP-type zinc-fingers (also named Zn1 and Zn2) CC specifically recognize DNA strand breaks: PARP-type zinc-finger 1 binds CC PARP-type zinc-finger 2 from a separate parp1 molecule to form a CC dimeric module that specifically recognizes DNA strand breaks. CC {ECO:0000250|UniProtKB:P09874}. CC -!- DOMAIN: The PADR1-type (also named Zn3) zinc-finger mediates an CC interdomain contact and is required for the ability of parp1 to CC regulate chromatin structure. {ECO:0000250|UniProtKB:P09874}. CC -!- DOMAIN: The BRCT domain is able to bind intact DNA without activating CC the poly-ADP-ribosyltransferase activity. The BRCT domain mediates DNA CC intrastrand transfer (named 'monkey-bar mechanism') that allows rapid CC movements of parp1 through the nucleus. {ECO:0000250|UniProtKB:P09874}. CC -!- DOMAIN: The WGR domain bridges two nucleosomes, with the broken DNA CC aligned in a position suitable for ligation. The bridging induces CC structural changes in parp1 that signal the recognition of a DNA break CC to the catalytic domain of parp1. {ECO:0000250|UniProtKB:Q9UGN5}. CC -!- DOMAIN: The PARP alpha-helical domain (also named HD region) prevents CC effective NAD(+)-binding in absence of activation signal. Binding to CC damaged DNA unfolds the PARP alpha-helical domain, relieving CC autoinhibition. {ECO:0000250|UniProtKB:P09874}. CC -!- PTM: Poly-ADP-ribosylated on serine, glutamate and aspartate residues CC by autocatalysis. Auto-ADP-ribosylation on serine takes place following CC interaction with HPF1. Auto poly-ADP-ribosylation on serine residues CC promotes its dissociation from chromatin. CC {ECO:0000250|UniProtKB:P09874}. CC -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000255|PROSITE- CC ProRule:PRU01351, ECO:0000305}. 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 EMBL; X52690; CAA36917.1; -; mRNA. DR PIR; JH0581; JH0581. DR PDB; 1A26; X-ray; 2.25 A; A=652-1011. DR PDB; 1EFY; X-ray; 2.20 A; A=659-1008. DR PDB; 1PAX; X-ray; 2.40 A; A=652-1011. DR PDB; 2PAW; X-ray; 2.30 A; A=652-1011. DR PDB; 2PAX; X-ray; 2.40 A; A=652-1011. DR PDB; 3PAX; X-ray; 2.40 A; A=652-1011. DR PDB; 4PAX; X-ray; 2.80 A; A=652-1011. DR PDB; 6I8M; X-ray; 2.10 A; A=651-1011. DR PDB; 6I8T; X-ray; 2.10 A; A=651-1011. DR PDBsum; 1A26; -. DR PDBsum; 1EFY; -. DR PDBsum; 1PAX; -. DR PDBsum; 2PAW; -. DR PDBsum; 2PAX; -. DR PDBsum; 3PAX; -. DR PDBsum; 4PAX; -. DR PDBsum; 6I8M; -. DR PDBsum; 6I8T; -. DR AlphaFoldDB; P26446; -. DR SMR; P26446; -. DR STRING; 9031.ENSGALP00000038037; -. DR PaxDb; 9031-ENSGALP00000015000; -. DR VEuPathDB; HostDB:geneid_396199; -. DR eggNOG; KOG1037; Eukaryota. DR InParanoid; P26446; -. DR PhylomeDB; P26446; -. DR EvolutionaryTrace; P26446; -. DR Proteomes; UP000000539; Unassembled WGS sequence. DR GO; GO:0000785; C:chromatin; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0043596; C:nuclear replication fork; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; IBA:GO_Central. DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; ISS:UniProtKB. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0140806; F:NAD+- protein-aspartate ADP-ribosyltransferase activity; ISS:UniProtKB. DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0140807; F:NAD+-protein-glutamate ADP-ribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0140815; F:NAD+-protein-histidine ADP-ribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0140805; F:NAD+-protein-serine ADP-ribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0140808; F:NAD+-protein-tyrosine ADP-ribosyltransferase activity; ISS:UniProtKB. DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:1990966; P:ATP generation from poly-ADP-D-ribose; ISS:UniProtKB. DR GO; GO:0030592; P:DNA ADP-ribosylation; ISS:UniProtKB. DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045824; P:negative regulation of innate immune response; ISS:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB. DR GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB. DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IDA:UniProtKB. DR GO; GO:0071932; P:replication fork reversal; ISS:UniProtKB. DR CDD; cd17747; BRCT_PARP1; 1. 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:SF112; 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; 1. 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; PS00347; ZF_PARP_1; 2. DR PROSITE; PS50064; ZF_PARP_2; 2. PE 1: Evidence at protein level; KW 3D-structure; ADP-ribosylation; Allosteric enzyme; Chromosome; Cytoplasm; KW DNA damage; DNA repair; DNA-binding; Glycosyltransferase; Immunity; KW Innate immunity; Isopeptide bond; Metal-binding; NAD; KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transcription; KW Transcription regulation; Transferase; Zinc; Zinc-finger. FT CHAIN 1..1011 FT /note="Poly [ADP-ribose] polymerase 1" FT /id="PRO_0000211322" FT DOMAIN 224..358 FT /note="PADR1 zinc-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01351" FT DOMAIN 382..473 FT /note="BRCT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033" FT DOMAIN 539..635 FT /note="WGR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321" FT DOMAIN 659..776 FT /note="PARP alpha-helical" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398" FT DOMAIN 785..1011 FT /note="PARP catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397" FT ZN_FING 9..91 FT /note="PARP-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT ZN_FING 113..203 FT /note="PARP-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT REGION 198..235 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 289..331 FT /note="Zinc ribbon" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01351" FT REGION 359..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 371..522 FT /note="Automodification domain" FT /evidence="ECO:0000250|UniProtKB:P09874" FT REGION 496..519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 207..209 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:P09874" FT MOTIF 220..225 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:P09874" FT ACT_SITE 985 FT /note="For poly [ADP-ribose] polymerase activity" FT /evidence="ECO:0000250|UniProtKB:P09874" FT BINDING 21 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 24 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 56 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 125 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 128 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 159 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 162 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264" FT BINDING 294 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01351" FT BINDING 297 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01351" FT BINDING 310 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01351" FT BINDING 320 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01351" FT BINDING 859..861 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q9UGN5" FT BINDING 868 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q9UGN5" FT BINDING 875 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q9UGN5" FT BINDING 901 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000250|UniProtKB:Q9UGN5" FT MOD_RES 403 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 404 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 410 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 411 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 432 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 434 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 441 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 442 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 453 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 454 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 468 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 481 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 485 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 488 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 509 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 510 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT MOD_RES 517 FT /note="PolyADP-ribosyl glutamic acid" FT /evidence="ECO:0000255" FT CONFLICT 895 FT /note="A -> R (in Ref. 1; CAA36917)" FT /evidence="ECO:0000305" FT HELIX 664..673 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 676..685 FT /evidence="ECO:0007829|PDB:6I8M" FT TURN 690..692 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 695..697 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 700..719 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 723..736 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 742..744 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 752..776 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 782..784 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 786..793 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 796..800 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 806..817 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 821..823 FT /evidence="ECO:0007829|PDB:1EFY" FT STRAND 827..838 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 841..845 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 846..850 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 854..861 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 863..865 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 866..872 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 883..885 FT /evidence="ECO:0007829|PDB:1EFY" FT STRAND 890..897 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 898..902 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 903..905 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 909..911 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 913..922 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 925..931 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 944..947 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 950..953 FT /evidence="ECO:0007829|PDB:6I8M" FT TURN 955..957 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 959..961 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 964..966 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 971..973 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 978..980 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 985..990 FT /evidence="ECO:0007829|PDB:6I8M" FT HELIX 991..993 FT /evidence="ECO:0007829|PDB:6I8M" FT STRAND 994..1005 FT /evidence="ECO:0007829|PDB:6I8M" SQ SEQUENCE 1011 AA; 113520 MW; 261AED9383139144 CRC64; MAETGDKPYR AEYAKSGRAS CKKCGESIAK DSLRLALMVQ SPMFDGKVPH WHHYSCFWKR ARIVSHTDID GFPELRWEDQ EKIKKAIETG ALQEEKGGTR KEVGKAEKSL TDFAAEYAKS NRSTCKGCEQ KIEKGQIRIS KKMVHPEKPQ LGMIDNWYHP DCFVSRRAEL GFLPAYGATQ LLGFSILKAE DKETLKKQLP ATKTEGKRKG EEVDGNVVAK KKSRKEKEKE SKQEKQLKEQ TELIWGIKDE LRKVCSTNDL KELLIANKQE VPSGENAILD RVADGMAFGA LLPCEECKGQ FVFKSDAYYC SGDITAWTKC VAKTQTPNRK DWVIPKEFRE IPYLKKFKCK KQDRIFPPEA ATVNSAPPPP ASAPLTETVT APQDKPLTNM KILTLGKLSK NKEEVKNIVE ELGGKMTTTA NKATLCISTQ KEVEKMSKKM EEVKDAKVRV VSEEFLKDVK SSNKGFQELL SLHAISPWGA EVKTEHQEVA VDGKCSKPAN MKSAGKVKEE QGPSKSEKKM KLTVKGGAAV DPDSGLEDSA HVFEKGGKIF SATLGLVDIV KGTNSYYKLQ LLEDDRESRY WVFRSWGRVG TVIGSNKLEQ MPSKEDAVEH FLNLYEEKTG NSWHSKNFTK YPKKFYPLEI DYGQDEEAVR KLTVSAGTKS KLAKPIQDLI KMIFDVESMK KAMVEFEIDL QKMPLGKLSK RQIQSAYSIL NEVQQAVSDG GSESQILDLS NRFYTLIPHD FGMKKPPLLS NLEYIQAKVQ MLDNLLDIEV AYSLLRGGNE DGDKDPIDIN YEKLRTDIKV VDKDSEEAKI IKQYVKNTHA ATHNAYDLKV VEIFRIEREG ESQRYKPFKQ LHNRQLLWHG SRTTNFAGIL SQGLRIAPPE APVTGYMFGK GIYFADMVSK SANYCHTSQA DPIGLILLGE VALGNMYELK NASHITKLPK GKHSVKGLGK TAPDPTATTT LDGVEVPLGN GISTGINDTC LLYNEYIVYD VAQVNLKYLL KLKFNYKTSL W //