ID A0A183WZC1_TRIRE Unreviewed; 129 AA.
AC A0A183WZC1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 20.
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=TRE_LOCUS17474 {ECO:0000313|EMBL:VDQ13354.1};
OS Trichobilharzia regenti (Nasal bird schistosome).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Trichobilharzia.
OX NCBI_TaxID=157069 {ECO:0000313|Proteomes:UP000050795, ECO:0000313|WBParaSite:TRE_0001809101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TRE_0001809101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDQ13354.1, ECO:0000313|Proteomes:UP000280995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; UZAO01095225; VDQ13354.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A183WZC1; -.
DR STRING; 157069.A0A183WZC1; -.
DR WBParaSite; TRE_0001809101-mRNA-1; TRE_0001809101-mRNA-1; TRE_0001809101.
DR Proteomes; UP000050795; Unplaced.
DR Proteomes; UP000280995; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF112; POLY [ADP-RIBOSE] POLYMERASE 1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 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:UP000280995};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 1..34
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 43..129
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 129 AA; 15285 MW; C24E3D1CA63C1B74 CRC64;
MKAPPLLDNK KLIRTKIHML EDLLEIELAY KILSSSKSNS EKNPLDEHYE QLHTKLEPLD
NNCEDYKRII DYVRETHGST HTHYKLEVLD IFEVQRDGEE DRYAKSKSAQ HNKQLLWHGS
RQTNWMGIL
//