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Database: UniProt
Entry: A0A085NUF0_9BILA
LinkDB: A0A085NUF0_9BILA
Original site: A0A085NUF0_9BILA 
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
//
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