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Database: UniProt
Entry: A0A1I7U269_9PELO
LinkDB: A0A1I7U269_9PELO
Original site: A0A1I7U269_9PELO 
ID   A0A1I7U269_9PELO        Unreviewed;       590 AA.
AC   A0A1I7U269;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=NAD(+) ADP-ribosyltransferase {ECO:0000256|ARBA:ARBA00012020};
DE            EC=2.4.2.30 {ECO:0000256|ARBA:ARBA00012020};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g14099.t2};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g14099.t2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC         ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC         Evidence={ECO:0000256|ARBA:ARBA00033987};
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   AlphaFoldDB; A0A1I7U269; -.
DR   STRING; 1561998.A0A1I7U269; -.
DR   WBParaSite; Csp11.Scaffold629.g14099.t2; Csp11.Scaffold629.g14099.t2; Csp11.Scaffold629.g14099.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd08001; WGR_PARP1_like; 1.
DR   Gene3D; 3.90.640.80; -; 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; IPR049296; PARP1-like_PADR1_N.
DR   InterPro; IPR012982; PARP1-like_PADR1_Zn_ribbon.
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:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR   Pfam; PF21728; PADR1_N; 1.
DR   Pfam; PF08063; PADR1_Zn_ribbon; 1.
DR   Pfam; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 1.
DR   SMART; SM01335; PADR1; 1.
DR   SMART; SM00773; WGR; 1.
DR   SMART; SM01336; zf-PARP; 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; PS52007; PADR1; 1.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51977; WGR; 1.
DR   PROSITE; PS50064; ZF_PARP_2; 1.
PE   3: Inferred from homology;
KW   ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          17..84
FT                   /note="PARP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50064"
FT   DOMAIN          417..516
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          539..590
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   REGION          184..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   590 AA;  68539 MW;  74194A273490D78A CRC64;
     MRIYLIQSST QSTPTVKDAG SLRCSINRPA YHSEGYIDSW YHYDCFWKKL VRGKGQINIS
     SIRGVDLIRW EDQEELRERI RKFKESRGCS YLSEEIYLHD VFIEPSFSNR GKCTKCSIYF
     QKGEIKVTHS VHFKCFIASF DKIHGKLEDM PRWKMISNKW RTAAAADFDE IMMAKQTQVK
     NEVVENTEKS TVDDMTSSSV TGKRRSSSDK PIENDSEEIM EQESEFARKR RLGKSARLAL
     IQERKLEKQT DELRKNLQIF NSMSVPDRII VLKENGQEVP EGGYDRNKQI VERLSDYALF
     GCPIHCVKCF NGIIVYNSSR RLYTCSGYVS EYTKCTYETK TPTQTPFILP RHFYEKYKLH
     DAVFNLMSER LYHKEEDSEE VLVRVSTPIK LSEEKNNSTQ IIKNGTLVDA KFLYAGHCHV
     LKNEDDGTIY QATLSLADLT TNKNSFYKMQ LLQDDITKHC YLFKSWGRVG TDVGSSNYDC
     ECNKEYAIAK FEQLFHEKTG NEWKYRKYFR KMPGRYNQVE TDDSEIIEIG EQYVAPGSKT
     CLPQSVKEVV MTIFNIGNME TALKFFKMDT NKMPLGCLSR NQINSSFQCS
//
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