ID A0A183BM04_GLOPA Unreviewed; 869 AA.
AC A0A183BM04;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000163900};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_000163900}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR AlphaFoldDB; A0A183BM04; -.
DR WBParaSite; GPLIN_000163900; GPLIN_000163900; GPLIN_000163900.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP 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 CDD; cd01437; parp_like; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR InterPro; IPR013641; KTI12/PSTK.
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 PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF60; POLY [ADP-RIBOSE] POLYMERASE 2; 1.
DR Pfam; PF08433; KTI12; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR SMART; SM00773; WGR; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 379..479
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 511..628
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 630..869
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT COILED 283..366
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 869 AA; 99901 MW; A1AC565B6E86C5C4 CRC64;
MCETELPRNV NLPLEQVYAT LVKGKELSAN KCMKLQIPVV SSTFITELDQ QTQQILDRLL
ALQRRATVGD TLTVLDGERG HANGVAFSRI RPLPQLSRLR HHFLGGSGGS DFEFEGRKVI
FDLRLMRQCD SEGRVTRNIR CAVRSTGGGA QVKFVWSHQY GPRKQWISFP ADLSLRLEAK
FGGVSPTQIV RDQKMEFTLN GEKVQIDWGT KKMTILNTKK QCLFRRIESN AQPSNPSVSP
FPNRMRRGKN FLINEEGTAK TKNGRSLYLE KDKEKMGGSE GKVEREVKRK KKVEEVEEEV
KRKKKVEEVE EEVKRKKKAE DMVEVEVKRK KKAEDMVEVE VKRKKKAEEM QQLDKNESKL
NDVQSEVEVD AECRELRATV RVYVDEKGRC YDVMLNQTDI YQNNNKFYLM QLLCDLTAKN
KIWLWRRWGR VGFRGQSNLI PFGSEFDGAL AMFLNKFSDK TRNDFLKGTE NFQKVAGKYD
LIKIDHDRRK ATEKKIDVKL RQNVSPTEAK ALVMDERVRA LLTTICDLKA MECDARRLEY
DFKRIPLGKI TKEQLNFGYE ALSRIERQIQ KADFGREFVK AMNDYYTRIP HSFGMRTPPP
IRSPEELKRE TELLELLTGI EITVANIGGD PLECHYARLR WNLMPLERED ENYKIVEEYL
RETHGPTHDR YQLKLRNVFE FKPKGTSDGK NAEGVGGTRK EIGVGNRKLL WHGSHLANWY
SILAQGLRIA PPEAPSTGFM FGKGVYFADI SSKSANYSLC DPDKPGFLLL SEVALGEVLD
LKESDSKMHQ KLPKGKDSVK GVGRYVPLPN GGRKIDGNVE VPCGKPTRNA ELDAEDETSL
IYNEFVVYNL DQIRERFLVE VEYMFDFKL
//
