ID A0A0T6B3Q7_9SCAR Unreviewed; 939 AA.
AC A0A0T6B3Q7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
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=AMK59_5757 {ECO:0000313|EMBL:KRT82026.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT82026.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT82026.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT82026.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT82026.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT82026.1}.
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DR EMBL; LJIG01015963; KRT82026.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6B3Q7; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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; 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; PF16589; BRCT_2; 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 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 DNA-binding {ECO:0000256|ARBA:ARBA00023125};
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:UP000051574};
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 1..50
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 74..163
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 328..403
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 474..571
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 594..711
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 717..939
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRT82026.1"
SQ SEQUENCE 939 AA; 107413 MW; 3C99755ED236AB66 CRC64;
YKFDGKTPNW FHFKCFFGKQ RPKSVDEIEN FESLRYNDQK EIRQKIDESG SGVIVPPKKG
AKRNAATMVG LQDYKVEYSK SGRASCRGCE QKILKDQIRI SKKDFETEVG RRYGGQDLWH
HLTCFAKLRS ELGYFAGGDA LPGFKSLKKD DQQEVKKQLP SIKQEDIPDG KKVKKEEDDP
LEKEIEKQNE IMFKYRDDLK QKKIKPTLQK LLTANDQAVP RGEEEMLDRI ADVMTFGALL
PCPQCNGQFV FNKIGYICEG NLTEWTKCGV IEKTPPRRKF VVPKEIAADY PFLKKYKYVK
RTRVIKEVSI PVPVKKEDEV DSKPKVEKEK PPLYEMQFVI VGKPPRGKEE IKKQITELGG
KVITKISNTV MAVISTPEEV EKNNARMGEV RAADVHVVSE DFVDAAKNCS GGIPELVIEK
SIADWGTDPN TRLPPETSKS QKSKSMYTKS GPSKIKMTVK GGSAVDPDSG IDHTSHVYSD
GNDKYTVVLG LTDIQRKKNS FYKLQLLESD AGNRYWLFRS WGRIGTNIGD NKLEQCSSLI
DAKSQFWSLY EEKTGNKWEY RDNFQKVPGR MFPIDIDYGD EDEDSNLEIN SELPSKLAQP
IQNLMKIIFD VKSMKQVMKE FELDTEKMPL GKLSKKQLQS AYNVLSELQS LIDKKGSQAQ
FIDATNRFYT FVPHSFGIDN PPVIDDEETI KKKVEMLENL MELEVAYSLM KTSDGDNSVD
SYYEQLKTDI DILETESEEF NIIKEYVKNT HAPTHTQYDL EVLEAFKVRR QGEEKRYKPF
RKLHNRKLLW HGSRKTNFAG ILSQGLRIAP PEAPVTGYMF GKGIYFADMV SKSANYCCTN
AMDRTGLMLL CEVALGDMYE RTQADYIEKL PKGKHSCKGI GRTHPDPSLV KKINNVEVPI
GKPTDISQYS SLLYNEYIVY DVAQVNIKYL LQMDFKYKY
//
