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Database: UniProt
Entry: A0A3S0ZXG6_ELYCH
LinkDB: A0A3S0ZXG6_ELYCH
Original site: A0A3S0ZXG6_ELYCH 
ID   A0A3S0ZXG6_ELYCH        Unreviewed;      2476 AA.
AC   A0A3S0ZXG6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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};
DE   Flags: Fragment;
GN   ORFNames=EGW08_014622 {ECO:0000313|EMBL:RUS77622.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS77622.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS77622.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS77622.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS77622.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUS77622.1}.
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DR   EMBL; RQTK01000566; RUS77622.1; -; Genomic_DNA.
DR   STRING; 188477.A0A3S0ZXG6; -.
DR   Proteomes; UP000271974; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR   CDD; cd17726; BRCT_PARP4_like; 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; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR031273; PARP4.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR   InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   InterPro; IPR013694; VIT.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR46530; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP4; 1.
DR   PANTHER; PTHR46530:SF1; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP4; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF08487; VIT; 1.
DR   Pfam; PF13768; VWA_3; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SMART; SM00609; VIT; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS51468; VIT; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|RuleBase:RU362114};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transferase {ECO:0000256|RuleBase:RU362114};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          2..97
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          395..598
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   DOMAIN          635..765
FT                   /note="VIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51468"
FT   DOMAIN          1377..1450
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50053"
FT   REGION          1548..1567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1576..1665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1715..1819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1902..1982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2051..2098
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2111..2163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1589..1665
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1715..1799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1906..1981
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2118..2163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RUS77622.1"
SQ   SEQUENCE   2476 AA;  268082 MW;  AACD5117B2C6D67E CRC64;
     KMQVHVFKGL QIAVDLGTSL SFKNKSELRK AITDNGGTIS YIVTRKCHFV VTSDPEKCDI
     SSKCRMAVKY GLPVLKLDYI WDCLAACKLQ PYDVYVVGGK ASSLDFKSGK ISAGKMGNQT
     KEKRRGFGAH FNPSSVKVWI GNDPAQPEYD EKLHEVVKYS VWTCFNSAAD CEFSYVVELH
     ASSHVRPLGA DPNKCEGAQR SECFPYRVFF QCGRTISIKT GAENQCESRY TSSAEQALDV
     YAMLVNRVMG KPGAQVCRSP VRGLGSSLLR KKLAESVQVQ DGCSGQVQDL VEHVWREAMT
     EVTSLLGNLS SIKLDQVEKA EAILSKISSA LETSQSDEDI QNTIREFYNT LNHKNESLES
     VKIQWKKWLT KKRDLCQLVK DMVSVGEMTN YESQAVVEAK YAALRCRITA LSGTQREEVQ
     NLVLSSICDG SKLSVLNVFE VWRQVEDVDF RHDLKPTKLL FHSSRVENFV GILSRGLLLP
     KVIVDDYGGT RSDAGMLGSG IYFASASSTS VKYSAPSNTK GTRLLLISEV ALGATKDYTE
     HDTSLISAPD GYDSTHGVGR RQDNESLFEF DEYVVYKTNQ QRMRYLVEFA TDDDMPQSLD
     IATQDDTYIS SDTVHNDTKN DCSLHDVLDV ANPMDKVKAG LLGSGDQEVE LKGVHIRAKL
     LDLAAEVVVL QEYYNNSSHA IEAKYVFPLT EAAAVCGFEA FINGKHVVGQ VKEKEMAHKE
     YKKAISEGHG AYLMDQDEET PDVFTVSVGN LPAGACVLIK ITYITELRVE DEKVSFRLPG
     TVAPWKEKSA LLQTTQTELK SHATKAMRTS VQVAVEMPFD IRTLHCPTHK VKVKQTASKA
     FVELAGRQKF GSGFLLLIGL AEIHVPRMWV EQHPTKAHHR ACMLTFYPEF ELEALLGGEI
     TLMLDMSNSM KETQILKLAS LVLQSIPEGF KFNIVRFGSE FEELFPAPKL RSDETMEAAQ
     LFVESSRMMM GNTNMYSALR PFHLLPPGDA GSPPMMRNVF LLSDGHLLEE RLVLEEAAKF
     SWHTRIFTFG ISPTCNIHTL RALARVSAGA FEYFDLKTKS KWQAKVESQV VKARQPGLTS
     VSVEWRQYED PLMPPVQAPR QITALFSGSQ QIVYGYVPDC TMANLRAVVG GQEVSTVVST
     SELSITQGLL VHRLTARAII QDWEAGVLAR DRTDHELTKM KLKDYVIELS KEYSIVTQLT
     SFVAVEKREE NEKENLPTGP SMKELLGRET VENLPYMGWT SVPEPSVESL IEELSFEDGE
     EELETLNAWR AEKTGELEKL YQAQSARGGP CSLLTLQALE VIVNSYKSLG DVDKAQRMTV
     QALKDASSEI DEMVATANYP TIATILTNLR GQLSENIHVS EVAGVAIPWP KEGNGIIKVK
     TLTGKTCEFS CTPNMSIKQL KDLIFGHEGY PQDTQRLIYK GKQLEDGSTL GECDADFGAL
     FHLVQRLRGG GGAEDLQSFR SELSDDDSYS SSMEVALADL EEDEDFGYGL FDSSEDDTYD
     EVTTEISVTE KAETKGCDES FALEEDFVTL NEEGNEVYEG LQVLPKRPVK SAAPSRPDPV
     PLESVTIITD NEKKKKKKKK ALDSGTAFGS AGSGESTSQP TFASAGFGDS ANQPTFGSTG
     FGGSANQPTF ASAGFGDSAN QPTFGSTGFG GSANQPTFGS AGFGGSANQP TFGSTVFGGS
     ANQPTFGSTV FGGSANQQTF GSTVFGGSAN QQTFGSPGFG GSANQQTFGS AVFGGSANQP
     TFGSPGFGGS ANQPTFGSAG FGGSANQQTF GSPGFGGSAN QPTFGRAGFG GSANQQTFGR
     AGFGAPAAQS APASSLFGTS SPQSALGPYL FGTSENMSAP TSSLFGAPDS LSAPGPALFG
     APALASSFCL TPANQPLIES AIGVELYEQS KQEPMEMIMH KKSSRLQTPP PPPPPPPAAA
     FAPPQSPQSP PPPPPTAFAT PQSPQSPPPP PPTAFATSQS PQPPPPPPAA AFAPPLPPPR
     LATAAAVKAP PLPPPRLATA AAALAPPLPP PRLATAAAAF TPPPLPPKRL ATAAAAFTPP
     LPPPRLATAA AVKAPPLPPP PQKKSLAQAS IKKTRSLDPS IFELGMTRGK GKGPGFAQGL
     RASLNKEITE HQKFGSHKSS NKFPSPPKYS SESPDLSPTS PSYSPTSPSY SPTSPAYSPT
     THALSLPAPS KKCHVEVSWR SEGVGDISIA RSELWAPYQA RKSIGGLVEM SSEEFMYEGS
     GATLQSQQKN LLQEMQHKLV ERRWERHSKC LYIDQDKVSL ERQEIETERA TLASSDLKRP
     GDVFAPGIES SPPYKKLSQE VSLFSFGIGT DLSPARVSHG VRLSVGNVAN LFKLQMENGS
     WQFTEELDDL IGVKSIQCIQ VLRTSGLSSL GLTAWDEITR MLATILALFV ILRELLPQFA
     DKTNPCFADI LDHLNSVPIS DCPAVLTEGL PAIVKAVKFL IVLDKKYPAL YSRLELGSSW
     FNVAVNLMHP AVVAAA
//
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