ID A0A3S2P2X3_ORYJA Unreviewed; 1015 AA. AC A0A3S2P2X3; DT 10-APR-2019, integrated into UniProtKB/TrEMBL. DT 10-APR-2019, sequence version 1. DT 07-APR-2021, entry version 11. DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|PIRNR:PIRNR000489, ECO:0000256|RuleBase:RU362114}; DE EC=2.4.2.30 {ECO:0000256|PIRNR:PIRNR000489}; GN ORFNames=OJAV_G00229600 {ECO:0000313|EMBL:RVE55796.1}; OS Oryzias javanicus (Javanese ricefish) (Aplocheilus javanicus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae; OC Oryzias. OX NCBI_TaxID=123683 {ECO:0000313|EMBL:RVE55796.1, ECO:0000313|Proteomes:UP000283210}; RN [1] {ECO:0000313|EMBL:RVE55796.1, ECO:0000313|Proteomes:UP000283210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS831 {ECO:0000313|EMBL:RVE55796.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:RVE55796.1}; RA Lopez-Roques C., Donnadieu C., Bouchez O., Klopp C., Cabau C., Zahm M.; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:RVE55796.1, ECO:0000313|Proteomes:UP000283210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RS831 {ECO:0000313|EMBL:RVE55796.1}; RC TISSUE=Whole body {ECO:0000313|EMBL:RVE55796.1}; RA Herpin A., Takehana Y., Naruse K., Ansai S., Kawaguchi M.; RT "A chromosome length genome reference of the Java medaka (oryzias RT javanicus)."; RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP- CC ribosylation of proteins and plays a key role in DNA repair. CC {ECO:0000256|PIRNR:PIRNR000489}. 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|PIRNR:PIRNR000489}; 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|PIRNR:PIRNR000489}; CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D- CC ribosyl)(n+1)-acceptor.; EC=2.4.2.30; CC Evidence={ECO:0000256|ARBA:ARBA00001645, CC ECO:0000256|PIRNR:PIRNR000489}; CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|PIRNR:PIRNR000489}. CC Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR000489}. 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; CM012460; RVE55796.1; -; Genomic_DNA. DR Ensembl; ENSOJAT00000036795; ENSOJAP00000034543; ENSOJAG00000017082. DR Proteomes; UP000283210; Chromosome 24. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule. DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro. DR Gene3D; 1.20.142.10; -; 1. DR Gene3D; 2.20.140.10; -; 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; IPR036930; WGR_dom_sf. DR InterPro; IPR008893; WGR_domain. DR InterPro; IPR001510; Znf_PARP. DR InterPro; IPR036957; Znf_PARP_sf. DR Pfam; PF00533; BRCT; 1. 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; PS00347; PARP_ZN_FINGER_1; 1. DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2. PE 4: Predicted; KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765}; KW Chromosome {ECO:0000256|PIRNR:PIRNR000489}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR000489}; KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676, KW ECO:0000256|PIRNR:PIRNR000489}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR000489}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000489}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000489}; KW Reference proteome {ECO:0000313|Proteomes:UP000283210}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000489}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000489}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}. FT DOMAIN 10..92 FT /note="PARP-type" FT /evidence="ECO:0000259|PROSITE:PS50064" FT DOMAIN 114..204 FT /note="PARP-type" FT /evidence="ECO:0000259|PROSITE:PS50064" FT DOMAIN 388..464 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT DOMAIN 663..780 FT /note="PARP alpha-helical" FT /evidence="ECO:0000259|PROSITE:PS51060" FT DOMAIN 789..1015 FT /note="PARP catalytic" FT /evidence="ECO:0000259|PROSITE:PS51059" FT REGION 199..225 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 495..527 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 401..421 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 509..523 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1015 AA; 112866 MW; 6F252885537EE33E CRC64; MADSQNDKLF RAEYAKSGQA SCKKCKEKIA KESLRMAIVV QSPMFDGKVP HWHHFSCFWQ RASVQSTADV GGFSDLRWAD QEAVKKAIES GGVAGTGKGN SGSAAKGEKT LNDFAVEYAK SNRSTCKGCQ QKIEKDQIRV SKKVVDPEKP QLGLIDRWYH TACFVSSREE LAFKPNYSAA QLKGFNALRA EDKEELKKRL PAVKTEGKRP GDELDGVSKK LKQEEEEENK KLVENLKNQS QLIWGIKDKL RKHCSTNDMK ELLIANAQDV PSGESNVVDR VADGMAFGAL EACKECQGQL VFKGDAYYCT GDISAWTKCV FKTTTPPRKD WIIPKEFHEV PFLKKFKFKR QDRVYPKEAP TQTVTTAKGE PLASGSGALK EPLPEGAPSD KPLTGMKLLA VGKLSKNKEE LKTEVEEMGG KITGTANKAS LCLSTKKEVE KMGKKMEEIR DAGVRVVSED FLRDIKSSGK ALQELVSLHA ISTWGAEVKV EPQAPAAASK SGALAAKSTG RVKEEEGGNK SKKMKLTVKG GAAVDPDSGL ENSAHVLEQS GKMYSATLGL VDIVRGTNSY YKLQLLEDDL HKRYWVFRSW GRVGTTIGGN KLDKFHDKNS ALDNFLSVYK EKTGNEWGSS NFIKYPTKFY PLEIDYGQDE EAVKRLTASA GTKSKLAKPV QELIKMIFDV ESMKKAMVEF EIDLQKMPLG KLSKRQIQSA YALLTEVQQA VSDCVPEAQI LDLSNRFYTL IPHDFGMKKP PLLNSLDYIQ AKVEMLDNLL DIEVAYSLLR GGAQDNEHDP IDINYEKLKT KIEVVDKSSQ EAEVITQYVK NTHAATHNTY TLEVQEIFKI GREGERQRFR PFEELHNRQL LWHGSRTTNY AGIMSQGLRI APPEAPVTGY MFGKGVYFAD MVSKSANYCH TSQSDPVGLL LLAEVALGNM HELKKASHIT KLPKGKHSVK GLGRTAPDPN ATVTLDGVQV PLGKGVQTNI DDTSLLYNEY IVYDVAQINL KYLLKIKFNY QTSLW //