ID A0A085NUF0_9BILA Unreviewed; 892 AA.
AC A0A085NUF0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=M513_00218 {ECO:0000313|EMBL:KFD59055.1}, M514_00218
GN {ECO:0000313|EMBL:KFD73096.1};
OS Trichuris suis (pig whipworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=68888 {ECO:0000313|EMBL:KFD73096.1};
RN [1] {ECO:0000313|EMBL:KFD73096.1, ECO:0000313|Proteomes:UP000030764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCEP-RM93F {ECO:0000313|EMBL:KFD73096.1}, and DCEP-RM93M
RC {ECO:0000313|EMBL:KFD59055.1};
RX PubMed=24929829; DOI=10.1038/ng.3012;
RA Jex A.R., Nejsum P., Schwarz E.M., Hu L., Young N.D., Hall R.S.,
RA Korhonen P.K., Liao S., Thamsborg S., Xia J., Xu P., Wang S.,
RA Scheerlinck J.P., Hofmann A., Sternberg P.W., Wang J., Gasser R.B.;
RT "Genome and transcriptome of the porcine whipworm Trichuris suis.";
RL Nat. Genet. 46:701-706(2014).
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; KL363182; KFD59055.1; -; Genomic_DNA.
DR EMBL; KL367475; KFD73096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085NUF0; -.
DR Proteomes; UP000030758; Unassembled WGS sequence.
DR Proteomes; UP000030764; 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; 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; 1.
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; 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; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
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; 1.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 6..88
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 278..348
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 421..519
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 541..662
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 669..892
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 118..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 892 AA; 101490 MW; 9FF60DE701918752 CRC64;
MEDLPFVAEY AKSSRASCKS CQGVIEKDTL RMGIMIQSSR FDGRFPLWHH FSCFWSRAKV
KSESDVKGFD NLRWNDQEKV RQAIAVYPAI SLLFSISGFE SLSEEEKDDI KRCFTTKKRK
GSPDAEDCAQ EVKKTKQSSS RDEERKLLKI QSDEMWKVRD MIKNNLTKAD MLQLFKLNNQ
QVPSGETKIL DRLTDCVMFG ALKRCQQCNG GQLVYSSTFN AYICTGSVSG WTRCTFTTRD
PERCSLIVPE EEHFKFLSAT SSRSTSNRKR IFPTDRLPSS NTLKGVTVFV RDSDRIEAAL
EAMGAQISSV LDNSIMLAVV DKEVINADRQ LVSKLAKYRI LTVSNDFVDA LKSMHLSAAI
LAAKIGDWES DNIEAKREKL ASKPKRKRRR GDAEDNFSKP IPSSSKLLIK RGGAVEPDSD
IAHVYQDTNG TLYNAVLHAV DVQRGQNSYY KMQVLKHDSK EKYWLFRSWG RVGTTIGDSL
LEKYALVHDA LSEFKKIYAA KTANEWDNRA HFVKYPSKFV PVEIDYETEK IPQPAVKPGS
KTNLPKEVQE LIMEIFDIEK MKETMAEFSI DLTKMPLGKI SREQIERAFS VLAELQEVLK
GTDDPAVKAN KITNCTTRFY SLVPHNFGMR KPPLLDSTSI LQKKVDMLEN MREIEIAYSI
LQTDYGDEDP LDVQYEKLKA DIKPLDITSS DFEMICRYVK NTHGQTHSDY TLAVQQVYVI
DRLNEQKRYR PFKKLQNRML LWHGSRNSNY AGILCQGLRI APPEAPVTGY MFGKGIYFAD
MVTKSANYCY ATKDEPYGYL LLCEVALGNV LELKNAKYLE KLPTGKHSVK GIGETMPDPA
EQETTDDGVV IPLGKPVASN VKKTSLLYNE YIVYDISQLH IKFLVKLKFN FK
//