UniProt: A7RNW1

Database: UniProt
Entry: A7RNW1_NEMVE

LinkDB:  A7RNW1_NEMVE 
Original site:  A7RNW1_NEMVE

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Ontology (8)   
   GO (8)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (29)   
   InterPro (12)   
   Pfam (7)   
   PROSITE (6)   
   SMART (4)   
Literature (1)   
   PubMed (1)   
All databases (40)   

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ID   A7RNW1_NEMVE            Unreviewed;       968 AA.
AC   A7RNW1;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
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};
DE   Flags: Fragment;
GN   ORFNames=NEMVEDRAFT_v1g88355 {ECO:0000313|EMBL:EDO46812.1};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351 {ECO:0000313|EMBL:EDO46812.1, ECO:0000313|Proteomes:UP000001593};
RN   [1] {ECO:0000313|EMBL:EDO46812.1, ECO:0000313|Proteomes:UP000001593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CH2 X CH6 {ECO:0000313|Proteomes:UP000001593};
RX   PubMed=17615350; DOI=10.1126/science.1139158;
RA   Putnam N.H., Srivastava M., Hellsten U., Dirks B., Chapman J., Salamov A.,
RA   Terry A., Shapiro H., Lindquist E., Kapitonov V.V., Jurka J.,
RA   Genikhovich G., Grigoriev I.V., Lucas S.M., Steele R.E., Finnerty J.R.,
RA   Technau U., Martindale M.Q., Rokhsar D.S.;
RT   "Sea anemone genome reveals ancestral eumetazoan gene repertoire and
RT   genomic organization.";
RL   Science 317:86-94(2007).
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   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   EMBL; DS469524; EDO46812.1; -; Genomic_DNA.
DR   RefSeq; XP_001638875.1; XM_001638825.1.
DR   AlphaFoldDB; A7RNW1; -.
DR   STRING; 45351.A7RNW1; -.
DR   eggNOG; KOG1037; Eukaryota.
DR   HOGENOM; CLU_004841_0_1_1; -.
DR   InParanoid; A7RNW1; -.
DR   OMA; MNFKYKY; -.
DR   PhylomeDB; A7RNW1; -.
DR   Proteomes; UP000001593; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   CDD; cd17747; BRCT_PARP1; 1.
DR   CDD; cd01437; parp_like; 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   Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_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; 1.
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; PS50064; ZF_PARP_2; 2.
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:UP000001593};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
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          5..50
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          69..156
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          334..409
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          494..592
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          616..733
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          742..968
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          160..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         968
FT                   /evidence="ECO:0000313|EMBL:EDO46812.1"
SQ   SEQUENCE   968 AA;  108524 MW;  E577BBA2F33BBAF2 CRC64;
     FFPLKVPNWF HFSCFFKKQF KPKSLAEIAG IDGLRWDDQE KFRAQVYGGA SDVPDTTAAA
     TVSVEQPDLL AEYAKSSRST CKHCDEQIVK GELRLAKVMD GEKYGPVPKW HHVPCFLKAM
     PDLDISGILT AQHFTGFQKL GKDDQKLLID KFGSQKQISK KKGKKKSLEA SAAMPVKSAS
     EEKEEQQLKE QSEAIWKIRD ELKTNCSLSE LREMLEDNEI NPQGGETSVF DRCSDGMLFG
     RLLPCHECHG GMLVYRSDGY HCTGNVSGWT KCAFTTQDPK RTKWVISKEL KKTNDFLKTF
     KCKEMKRLFP KLTAIQPGAS TVFFPMFLDS FLAIPGKPLS NMMVAVIGKL KRTKADVASC
     VAQLGGTTMD RVTSKVDCCI STQAEVSKSS KKMKDAEKFN IPVVSEEFLD AIKDGEFNSN
     IAKHSLVSWG KIKALDIVDG PLPLRRKASD SKYELGKTQD NTTLIHGEDS LPKKVKLSVK
     GGAAVDPASE MEDDCHVLEV KGVVYSATLG MVDISRGTNS YYKLQVLKKD KSSRCYLFRS
     WGRVGTTIGG SKLEDCGNSH NSAVQSFEEL YREKTGNEWS ERDNFVKHPN RFYPLEIDYG
     QAHEDVVKAK IEMGSKSKLP SQIQELIKMI FDVESMKKTL IEFEIDLKKM PLGKLTKRQI
     EKAYSVLGEA QQILSEAASK TAVLDVSNRF YTLIPHDFGM RKPPLLDNQE LIKTKIEMLD
     NLIDIEVAFS LLQSSDGEDA EDPIDINYKK LKTDIEVLDH KSAEFGLISE YVSNTHADTH
     RQYELELLDV FKIKREGEEA LFKPFKQLHN RQLLWHGSRT TNYAGILSQG LRIAPPEAPV
     TGYMFGKGVY FADMVSKSAN YCCTSPSNNI GLLLLCEVAL GNMHELKHAS FIKKVPKGKH
     SVKGLGKTAP DPSATHTFED GTIVPKGKGC PAPVKDSSLL YNEYIVYDTA QINMKYLLKT
     KFKYKYGW
//

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