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Database: UniProt
Entry: M3ZYU7_XIPMA
LinkDB: M3ZYU7_XIPMA
Original site: M3ZYU7_XIPMA 
ID   M3ZYU7_XIPMA            Unreviewed;      1803 AA.
AC   M3ZYU7;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 51.
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   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000007391.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000007391.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000007391.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   STRING; 8083.ENSXMAP00000007391; -.
DR   Ensembl; ENSXMAT00000007399.2; ENSXMAP00000007391.2; ENSXMAG00000007367.2.
DR   eggNOG; KOG2633; Eukaryota.
DR   GeneTree; ENSGT00940000154311; -.
DR   HOGENOM; CLU_012160_2_0_1; -.
DR   InParanoid; M3ZYU7; -.
DR   OMA; QQFNCLI; -.
DR   OrthoDB; 5471082at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02907; Macro_Af1521_BAL-like; 1.
DR   CDD; cd02903; Macro_BAL-like; 1.
DR   CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   Gene3D; 3.30.720.50; -; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 3.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR037197; WWE_dom_sf.
DR   PANTHER; PTHR14453; PARP/ZINC FINGER CCCH TYPE DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR14453:SF88; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR   Pfam; PF01661; Macro; 3.
DR   Pfam; PF00644; PARP; 1.
DR   SMART; SM00506; A1pp; 3.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 3.
DR   SUPFAM; SSF117839; WWE domain; 1.
DR   PROSITE; PS51154; MACRO; 3.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50918; WWE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW   NAD {ECO:0000256|RuleBase:RU362114};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW   Transferase {ECO:0000256|RuleBase:RU362114}.
FT   DOMAIN          779..966
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          996..1181
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          1209..1383
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   DOMAIN          1527..1605
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          1612..1803
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          83..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1183..1203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1501..1535
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        85..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1803 AA;  199187 MW;  D9C1E9FACFD07106 CRC64;
     MAEEYAFHVL VELEESNTPR LKNKLVKYFQ SKKSNGGDCE VDYESGSSTA LLRFRREEDQ
     KNVLGKESHQ ISLDKGVLKM AVRLPSDGKQ KRGDSTDKGS KKSDHEGTNK QSKVQEPKPV
     DEGQTGAKGK DGDSDDEEQC SKSAVLGNIP DSLTSEFLEM IVENILRDIS SPTASQDYNL
     ELIPDISSAV VTFQSGKDAT DFIERCPQNR MFTKKELSVR PLETTKKVMV EGVSDCSEDM
     LCLYFESKGG DVEDVQLNEA EQSAVIIFKN HQDVKKVLGK KHEIKKEEIK VYPFYKSLGV
     ALYGKDKPSP KLPAAISEPI DNAVLRYLAN HKAALETVGC DLERHFCNIT LEQSAVRLSA
     SPSLLKQKDA KVIIKEWANT VKAAFSQAVS KFKTLKFSLE SDVWEESEQK IKEKLRKEDV
     VVVSDKTSGV LSVAGLENDV NTLKKPISDV LDRIEKRVRR EKLSKTQEIN VSPSMFHILS
     QDGLQDKLLQ VYPELKMSYD QNKQALKVTG FVDEIINATQ VISNATLGLK RQNLEVDEFL
     LDMLKDEQQE EATDILLTAY GIKAALEISP QRVQLVAVSD KDLMNAQDHL SQILKSEYVE
     VEDFEVLKKP EWQQLVHQQE KANSGSGMRV QIITHQQQVV VSGHKDSVDK VSSELEDFIT
     ENAHVEEFVA VKANVIIEYL KGQTTLLKQL EGVEVSFGNQ EIILSGCRSA VKDCKTIVKA
     LLASVCFDSF KVTKPGVKKC FQEKELFFAS SIKSDTDCLV QLADKSNEED DLALVQVQQP
     IYKVQTSDGV EIVVSKADMC SYSVDAVVNP STEDLKHTSG LALALSKAAG PQLQTECDQI
     IFVKGKLRPG DCVVTDAGGM LRCKKVIHAV GPYFDQAKPK KAEAQLKRTV KESLELAEKC
     GCVSVALPAI SRNLGFPLNL CLATIARAVK EYCDEKYDDN TLKKIHLVDN EDSVALGMES
     AVKQEFGNHG VSVSSQNAIP KVSQKSSLLK LVPPDPSLCR GQTKEGLNIV LKKGNIEAAK
     TEVIVNTVTE DLVLDRGAIS KAIFSAAGPK LQQLVHSQKT KGSPGEIVVT DNCKLKSKQV
     FHAIAPHWNN GQGAAEKTLA GIFKDCLDLA EKTRLSSITF PAVGTGNLGF PKNLVATLML
     DKFLEFSSQR QSNNLKKIAV VLYPGDAQTI KVFTDEFQKK FPSATGSSAA AGPASADSSK
     GKFSKVVSSS GTHETKLGNV TIQVVTGDIT KETTDVIVNS SNDNFTLKSG VSKAILDAAG
     VVVFEECQHL GSQPNPGIIM TVPGNLKCKK ILHLVGQTDP VKIHSTVKEA LQMCVKNSYT
     SVSFPAIGTG QGNVQAKQVA DSMLDAVIDV FSQNTSSSLT LIRIVIFQQP MLKDFHSSMQ
     EREATDPKEK GGFWSNVGHR LKSLFGSESF DYKQEDEVFD IETKEVEPAV FHICGASQAK
     VDAAKKKIND LMSNEQCQEE IIDNDILNLS SADCQRIVDI QMKMSVSIKK QSTNGQTSFI
     IEGLSKDVLR ASREIDNMLK KVRQEQELKK KLELAATVAD WQYQQHGLSY QSFDQMTNYE
     LEHALERATP TLKVTIHGSD YTVQMPKGPA TDGKGTKLQI RRIDKLKDED VPEFWDAMPA
     GKTCHSVILQ TASSEYAEVL NLFKATCNRA VIKIERIQNP TLWKSLQIKK HEMEVRNNHQ
     NNEKRLFHGT SENTVPIINE RGFNRSYAGK NAACYGNGSY FAVNSNYSAQ DTYSRPNAKG
     EKFMYLCKVL TGDYTLGQQT MIAPPTKGTL GIYDSVVDNT TTPSMFVVFH DTQAYPEYLI
     TFK
//
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