GenomeNet

Database: UniProt
Entry: A0A183WZC1_TRIRE
LinkDB: A0A183WZC1_TRIRE
Original site: A0A183WZC1_TRIRE 
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
//
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