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Database: UniProt
Entry: F0ZDM9_DICPU
LinkDB: F0ZDM9_DICPU
Original site: F0ZDM9_DICPU 
ID   F0ZDM9_DICPU            Unreviewed;       449 AA.
AC   F0ZDM9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 53.
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   ORFNames=DICPUDRAFT_29490 {ECO:0000313|EMBL:EGC37965.1};
OS   Dictyostelium purpureum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=5786 {ECO:0000313|EMBL:EGC37965.1, ECO:0000313|Proteomes:UP000001064};
RN   [1] {ECO:0000313|Proteomes:UP000001064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QSDP1 {ECO:0000313|Proteomes:UP000001064};
RX   PubMed=21356102; DOI=10.1186/gb-2011-12-2-r20;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Sucgang R., Kuo A., Tian X., Salerno W., Parikh A., Feasley C.L., Dalin E.,
RA   Tu H., Huang E., Barry K., Lindquist E., Shapiro H., Bruce D., Schmutz J.,
RA   Salamov A., Fey P., Gaudet P., Anjard C., Babu M.M., Basu S.,
RA   Bushmanova Y., van der Wel H., Katoh-Kurasawa M., Dinh C., Coutinho P.M.,
RA   Saito T., Elias M., Schaap P., Kay R.R., Henrissat B., Eichinger L.,
RA   Rivero F., Putnam N.H., West C.M., Loomis W.F., Chisholm R.L., Shaulsky G.,
RA   Strassmann J.E., Queller D.C., Kuspa A., Grigoriev I.V.;
RT   "Comparative genomics of the social amoebae Dictyostelium discoideum and
RT   Dictyostelium purpureum.";
RL   Genome Biol. 12:R20.1-R20.23(2011).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; GL870987; EGC37965.1; -; Genomic_DNA.
DR   RefSeq; XP_003285536.1; XM_003285488.1.
DR   AlphaFoldDB; F0ZDM9; -.
DR   STRING; 5786.F0ZDM9; -.
DR   EnsemblProtists; EGC37965; EGC37965; DICPUDRAFT_29490.
DR   GeneID; 10503035; -.
DR   KEGG; dpp:DICPUDRAFT_29490; -.
DR   eggNOG; KOG1037; Eukaryota.
DR   InParanoid; F0ZDM9; -.
DR   OMA; ICDISMM; -.
DR   OrthoDB; 8343at2759; -.
DR   Proteomes; UP000001064; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IBA:GO_Central.
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:0006302; P:double-strand break repair; IBA:GO_Central.
DR   CDD; cd01437; parp_like; 1.
DR   CDD; cd07997; WGR_PARP; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory 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:SF108; POLY [ADP-RIBOSE] POLYMERASE TANKYRASE; 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   4: Predicted;
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:UP000001064};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          1..77
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          103..222
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          231..449
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
SQ   SEQUENCE   449 AA;  51811 MW;  EC309909973610E5 CRC64;
     MYGENNFYKL QIIYNPNLDR YFIFNRWGRI GDSGQYQKTP YSKEEAINEF CKLFKQKTGN
     IFSQATMTNF QRVDGKYHLL NIDRTDRSKK EVLHPFDLSK YPPSKLPKEI FDVMSQFCNV
     EAISNQLKSL KIDTDIMPLG RLSKDAINNA VAILGKNDDT LPPINEVLES QLELSNKFFE
     LIPHSDFRTE KMQVLRHQHE IATKIKLLQN LDEMETVSKI LIAAHQNSSM HPYDYCFKAV
     NVCMEKLNEN TPEFEIIKKY TLNTGCHQKI HNVYKIQRKG EPEKFQQHKS LKNHYLLWHG
     SLTTNYLSIL SQGLKIAPPE APATGYMFGK GVYFADMFQK SINYCKSWQT PNTSNRNFLL
     LSEVALGTMA EFKSAHYMES PQTGTNSTKG VGKNGPNFDN SIILNNGVCI PLSKPEQVKD
     TTGYFLEMNE YIVYNTSQIR MRYLVEVSQ
//
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