ID A0A182PE54_9DIPT Unreviewed; 1001 AA.
AC A0A182PE54;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
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};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI005209-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI005209-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI005209-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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 + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000256|ARBA:ARBA00033987,
CC ECO:0000256|PIRNR:PIRNR000489};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR000489}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR AlphaFoldDB; A0A182PE54; -.
DR STRING; 199890.A0A182PE54; -.
DR EnsemblMetazoa; AEPI005209-RA; AEPI005209-PA; AEPI005209.
DR VEuPathDB; VectorBase:AEPI005209; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; 1.
DR PROSITE; PS50064; ZF_PARP_2; 2.
PE 3: Inferred from homology;
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
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 Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000489};
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 8..90
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 116..205
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 384..461
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 529..627
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 649..766
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 777..1001
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 937..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 211..238
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1001 AA; 113426 MW; F0A725CA91D75B08 CRC64;
MDAEQLPFRA EYSKSNRASC RLCKQKIDKD VLRLAAMVQS PMYDGKVAQW YHEKCFFQKQ
RPTTEGDIDN FEALRYEDQK KIREAIALFA KGVVPAAGKG KGKKRSAAEA QSLKDYGVEY
ASSGRAMCRG CEIKILKDEM RIKKVAYDTE VGMKYGGQAL WHHAECFAKL RTDLGYYEKG
ESLPGYRTMK PEDQAILKKL LPAIKMEDVP AKKVKEEVKD EVDKAAETLE EKQIAEQQKA
FYKIRDKLKS LGVKKVELIE ILSLNNQDIP VGNDPVLDLV CDTLMFGALQ RCVKCGGQYV
FQKSAYVCQG NLTEWVKCMN AEKAPPRKEA IIPVDLQANY SFMKKYKSVV TDRVLRYVPP
SVNTMLKKGV KKEEELPSEP KIKREKPPLY NMEFVVLGKT ATPKDQLKLK IQKLGGKLVT
KIASHTAAII STPEEIERMG SRMQDAKLLQ IQVVPEDFLE DVTGGGAISF ITSRSICDWG
SDPLKRIPTE EESKSRSKKS IYEKSVPAKV KLQVKSGLVV DPDSGLADKA HVYKYHDVIY
NCVLNKVDIQ SDKNSFYKMQ VLESDTKKKY WLFRAWGRIG TTIGGNKVES YSAADDAMNS
FENLFLEKTG NDWERHNSVY HKMPGLFYPI EIDYSETKTK RLAENSGIKS KLAPAVQELV
RMLFDVDAMN RVMMEFELDM EKMPLGKLSK RQLQSAMKVL SEISDLIGSG GSNAQFIDAS
NRFYSFIPHN FGVSSVQVLD TIEQVKDKQT MLESLMEIEF AYSLLSEGGE SDQDGKNPLD
AHYEQLKTAI EPMARDSEEF ALLEQYVRNT HAETHKSYEL EIAEIFRIKR KGEDRRYQPF
KKLHNRKLLW HGSRLTNFAG ILTHGLKIAP PEAPVTGYMF GKGIYFADMV SKSANYCCTN
VTDSTGLMLL CEVALGDMQE YQQAHYVTKL QTGKHSVKGI GRTQPDPTGS HVRPDGVEIP
MGKGVTNEKL KSSLLYNEFI VYDVGQVNCQ YLFKMNFKYK Y
//
