ID V4BHH9_LOTGI Unreviewed; 987 AA.
AC V4BHH9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|PIRNR:PIRNR000489, ECO:0000256|RuleBase:RU362114};
DE EC=2.4.2.30 {ECO:0000256|PIRNR:PIRNR000489};
GN ORFNames=LOTGIDRAFT_206927 {ECO:0000313|EMBL:ESO88129.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESO88129.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESO88129.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000256|PIRNR:PIRNR000489};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000256|PIRNR:PIRNR000489};
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 ECO:0000256|PIRNR:PIRNR000489};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR000489}.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; KB202752; ESO88129.1; -; Genomic_DNA.
DR RefSeq; XP_009061157.1; XM_009062909.1.
DR AlphaFoldDB; V4BHH9; -.
DR STRING; 225164.V4BHH9; -.
DR EnsemblMetazoa; LotgiT206927; LotgiP206927; LotgiG206927.
DR GeneID; 20245944; -.
DR KEGG; lgi:LOTGIDRAFT_206927; -.
DR CTD; 20245944; -.
DR HOGENOM; CLU_004841_0_0_1; -.
DR OMA; MNFKYKY; -.
DR OrthoDB; 5481368at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd17747; BRCT_PARP1; 1.
DR CDD; cd01437; parp_like; 1.
DR CDD; cd08001; WGR_PARP1_like; 1.
DR Gene3D; 1.10.20.130; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR Gene3D; 3.30.1740.10; Zinc finger, PARP-type; 2.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR038650; PADR1_C_dom_sf.
DR InterPro; IPR008288; PARP.
DR InterPro; IPR049296; PARP1-like_PADR1_N.
DR InterPro; IPR012982; PARP1-like_PADR1_Zn_ribbon.
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 InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR PANTHER; PTHR10459; DNA LIGASE; 1.
DR PANTHER; PTHR10459:SF112; POLY [ADP-RIBOSE] POLYMERASE 1; 1.
DR Pfam; PF21728; PADR1_N; 1.
DR Pfam; PF08063; PADR1_Zn_ribbon; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR SUPFAM; SSF142921; WGR domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS52007; PADR1; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS51977; WGR; 1.
DR PROSITE; PS00347; ZF_PARP_1; 1.
DR PROSITE; PS50064; ZF_PARP_2; 2.
PE 3: Inferred from homology;
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR000489};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|PIRNR:PIRNR000489};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000489};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRNR:PIRNR000489};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000489};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR000489};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 9..88
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 110..196
FT /note="PARP-type"
FT /evidence="ECO:0000259|PROSITE:PS50064"
FT DOMAIN 363..438
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 518..616
FT /note="WGR"
FT /evidence="ECO:0000259|PROSITE:PS51977"
FT DOMAIN 639..756
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000259|PROSITE:PS51060"
FT DOMAIN 763..987
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 184..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 112028 MW; 2B7BE74E01B16DE4 CRC64;
MSDSSTCPFK AEYAKSDRSS CKACKTKIGK DSLRLAVMVQ SPHFDGKVPN WFHYSCFWRR
AGDVEQVDDI HGYHTLRWED QQKLKSRISG ETTATDDVDG KIEEHDLLSF RTEYAKSNRS
QCQSCRTKID QGEVRISCKE VDDPKYGAVD KWYHVDCFVQ NRDELNFNFD VKLLPGLRRL
KKPDQEELHK KLAPKSGKKR KADGAAGSSK KVKVEETDEE KLLRTQSAEV WKYRDLLQKN
VNNQAMKLLL ELNKQHVPVG ESKLLDAMSD ALVFGALEPC SECKDGAFFY TPEGYKCAGN
MTGWTKCMNI VRNPKRRAFK IPPEFHDVEF LKKYKYKANI RVFPTIHVSS LETAMDSVDG
AVSNDKPLDQ MKFAIIGKTK KSKAVLTKEI ANLGGTVVSK IDNTIAACIS TKTDVAKKSK
NVKEAEKADV HVVDEEFLDN LKSDTVVANI LKHALSSWGS DPQTRIGDIK PKVVKRKMYK
SGMSEMEEMR YKKDVPTKKK MTVKGGAAVD PDSELEDVAH VIQDDKKGIL SVVLGLVDIV
KGTNSFYKLQ ALEKDNNKQW YLFRSWGRVG TNIGGNKIEK MSKKENAIIA FRDLYLEKTG
NSWEDRDSFV KHPNKFYPLE IDYGQEDEKI QSLDSSREGS KLPKPVQDVV CAIFDIDQMK
KAMIEYEIDM KKMPLGKLSK RQIEQAYSVL TELNGLIEKK GSQSLFLDAS NRFYTLIPHD
FGMKKPPLLD DPEIIKTKTE MLDSLLEIEV AYNLLKSGDT GANPIDVHYK QLKCKMEPME
KKSEMYKRLS KYVKNTHATT HNQYGLEVLD IFEIDREGEE EKYQPFQDLH NRQLLWHGSR
TTNYAGILSQ GLRIAPPEAP VTGYMFGKGV YFADMVSKSA NYCRTTQVDN VAYMLLCEVA
LGNTYDLLGS KFIHSLPKGK HSTKGCGMTA PDEAGAFVTD DGCKIPMGQG KDASIGRSSL
LYNEYIVYDT SQIRMKYMLK MKFNYKW
//
