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Database: UniProt
Entry: A0A3P9NGV6_POERE
LinkDB: A0A3P9NGV6_POERE
Original site: A0A3P9NGV6_POERE 
ID   A0A3P9NGV6_POERE        Unreviewed;      1276 AA.
AC   A0A3P9NGV6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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   Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Poecilia.
OX   NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000008816.1, ECO:0000313|Proteomes:UP000242638};
RN   [1] {ECO:0000313|Proteomes:UP000242638}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA   Kuenstner A., Dreyer C.;
RT   "The genomic landscape of the Guanapo guppy.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPREP00000008816.1}
RP   IDENTIFICATION.
RC   STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000008816.1};
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC       {ECO:0000256|ARBA:ARBA00024347}.
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DR   AlphaFoldDB; A0A3P9NGV6; -.
DR   Ensembl; ENSPRET00000008922.1; ENSPREP00000008816.1; ENSPREG00000005920.1.
DR   GeneTree; ENSGT00940000156161; -.
DR   Proteomes; UP000242638; Unassembled WGS sequence.
DR   Bgee; ENSPREG00000005920; Expressed in head and 1 other cell type or tissue.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd09524; SAM_tankyrase1_2; 1.
DR   CDD; cd01438; tankyrase_like; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 6.20.320.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 5.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR24178:SF45; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 6.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 17.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 3.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 15.
DR   PROSITE; PS50088; ANK_REPEAT; 15.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW   NAD {ECO:0000256|RuleBase:RU362114};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU362114}.
FT   REPEAT          164..196
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          197..229
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          230..262
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          317..349
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          350..382
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          383..415
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          470..505
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          506..538
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          539..571
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          632..664
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          665..697
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          698..730
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          785..817
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          818..850
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          851..883
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          981..1040
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          1063..1266
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1276 AA;  137473 MW;  ED2EDF782926A54A CRC64;
     MATPRRSSQQ QQQQQQLSTL LSSPPRSTSI PVSPPESPSA PAEDASRFSR GAEMENVADG
     EVAPTSPNTT SPALALTPSS SNSNSSSSSS SSTTSSPTTT EGSETSPGST PDSGGANPRS
     SSTISGDANG AFRELFEACR NGDVSRVKKL VDVVNVNAKD MAGRKSTPLH FAAGFGRKDV
     VDHLLQTGAN VHARDDGGLI PLHNACSFGH SEVVSLLLCQ GADPNARDNW NYTPLHEAAI
     KGKIDVCIVL LQHGADPNIR NTDGKSALDL AEPSAKAVLT GEYKKDELLE AARSGNEEKL
     MALLTPLNVN CHASDGRKST PLHLAAGYNR VRIVQLLLQH GADVHAKDKG GLVPLHNACS
     YGHYEVTELL LKHGACVNAM DLWQFTPLHE AASKNRVEVC SLLLSHGADP TLLNCHSKSS
     VDMAPTPELK ERLTYEFKGH SLLQAAREAD MTKAKKTLAL EIINFKHPHT HETALHCAVA
     SPHPKRKQVT ELLLRKGANV NEKNKDFMTP LHVAAERAHN DIMEVLQKHG AKVNALDTLG
     QTALHRAALA GHLQTCRLLL GYGADATLVS LQGFTAAQMG NEAVQQILNE NVPVRNSDVD
     YRLLEAAKAG DLDTVKSLCT AQNVNCRDLE GRHSTPLHFA AGYNRVSVVE YLLHHGADVH
     AKDKGGLVPL HNACSYGHYE VAELLVRHGA SVNVADLWKF SPLHEAAAKG KYEICKLLLK
     HGADPTKKNR DGNTPLDLVK DGDTDIQDLL RGDAALLDAA KKGCLARVQK LCSPDNINCR
     DTQGRNSTPL HLAAGYNNLE VAEYLLEHGA DVNAQDKGGL IPLHNAASYG HVDIAALLIK
     YNTCVNATDK WAFTPLHEAA QKGRTQLCAL LLAHGADPTM KNQEGQTPLD LATADDIRAL
     LIDAMPPDAL PSCLKPQATV VSAAGGVVIS PSPSPSCLSA ASSIDNLTAP LGDIATAGAT
     GVADGASGSD RKEGESLLDM TINQFLKSLG LEHLRDIFQR EQISLDVLAD MGHEELKEIG
     INAYGHRHKL IKGIERLLGG QQGGNPYLTF HCSSQGTVLI DLAPDDKEFQ SVEEELQSTI
     REHRDGGNAG GVFMPSLFFF FVVNKKLRER YAHRQKEIAD ENHNHHNERM LFHGSPFINA
     IIHKGFDERH AYIGGMFGAG IYFAENSSKS NQYVYGIGGG TGCPTHKDRS CYVCHRQMLF
     CRVTLGKSFL QFSAMKMAHA PPGHHSVIGR PSVNGLAYAE YVIYRGEQAY PEYLITYQIM
     KPESLAAPAA TAEQKS
//
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