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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//