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Database: UniProt
Entry: G3N798_GASAC
LinkDB: G3N798_GASAC
Original site: G3N798_GASAC 
ID   G3N798_GASAC            Unreviewed;       535 AA.
AC   G3N798;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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};
OS   Gasterosteus aculeatus (Three-spined stickleback).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC   Gasterosteus.
OX   NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000001175.1, ECO:0000313|Proteomes:UP000007635};
RN   [1] {ECO:0000313|Ensembl:ENSGACP00000001175.1, ECO:0000313|Proteomes:UP000007635}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGACP00000001175.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   AlphaFoldDB; G3N798; -.
DR   STRING; 69293.ENSGACP00000001175; -.
DR   Ensembl; ENSGACT00000001175.1; ENSGACP00000001175.1; ENSGACG00000000906.1.
DR   eggNOG; KOG1037; Eukaryota.
DR   GeneTree; ENSGT00940000158855; -.
DR   InParanoid; G3N798; -.
DR   OMA; HHITTDN; -.
DR   TreeFam; TF315407; -.
DR   Proteomes; UP000007635; Unassembled WGS sequence.
DR   Bgee; ENSGACG00000000906; Expressed in liver and 12 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
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:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd01437; parp_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; IPR036930; WGR_dom_sf.
DR   InterPro; IPR008893; WGR_domain.
DR   PANTHER; PTHR10459; DNA LIGASE; 1.
DR   PANTHER; PTHR10459:SF66; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP3; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 1.
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; PS51977; WGR; 1.
PE   3: Inferred from homology;
KW   ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU362114};
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:UP000007635};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          60..150
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          181..300
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          315..535
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   535 AA;  60350 MW;  AC86DA76CD093021 CRC64;
     MAPKRRAASG GKRGGKKVKQ EPETPEPKDA FTSAKEALLA AGPQVKGKRN VDEHCSLPSS
     NEVHEDYDCM LNQTNIGNNN NKFYVIQVIK DKSSYYTWTR WGRVGEVGQS KLNTFNESEK
     AVKDFEKKFK DKTKNNWSDR SNFVSHPGKY TLIEVDGEQD AEVKVDTVDG KNVQVAKNVQ
     DCTLDGATKS LIKLIFSNDM FKEAMECMNL DIKKMPLGKL SKIQIAKGFD VLEEIEAAMN
     KKGGNKKKNL EELSSKFFTT IPHNFGRSRP PTIDDKEIVE KKKEMLMVLA DIELAQTLKS
     ETEKSQEEMT EKVPHPLDQD YRSLNCSLTL MDKDSDRFKK IIEKYMKETS DNYRKPKIVN
     VWEVDRETEG ERFSENDGLE NRRLLWHGTN IAVVAAILKS GLRIMPHSGG RVGSGIYFAS
     ENRKSACYVR PSKNTGVMFL SEVALGKEFT ITNDDGALKE APAGYDSVVA RGSVEPDPSK
     DTIITLEGKQ VAVPQGKPVK QPQFSNSRFS NSEYLIYKES QCRLRYLLEL NINAY
//
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