ID A0A3Q2WN56_HAPBU Unreviewed; 1033 AA.
AC A0A3Q2WN56;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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 Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000027878.1, ECO:0000313|Proteomes:UP000264840};
RN [1] {ECO:0000313|Ensembl:ENSHBUP00000027878.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR AlphaFoldDB; A0A3Q2WN56; -.
DR Ensembl; ENSHBUT00000031442.1; ENSHBUP00000027878.1; ENSHBUG00000011486.1.
DR GeneTree; ENSGT00940000156161; -.
DR OMA; TAETINC; -.
DR Proteomes; UP000264840; Unplaced.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
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; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1.
DR PANTHER; PTHR24189; MYOTROPHIN; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 5.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 14.
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; 12.
DR PROSITE; PS50088; ANK_REPEAT; 12.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114}; NAD {ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000264840};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 21..53
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 54..86
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 141..173
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 174..206
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 207..239
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 294..329
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 330..362
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 363..395
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 456..488
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 489..521
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 522..554
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 609..641
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 732..795
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 818..1023
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 1033 AA; 112354 MW; 7C4F3C26CBF60CD9 CRC64;
IKDVVEHLLQ TGANVHARDD GGLIPLHNAC SFGHAEVVSL LLCQGADPNA RDNWNYTPLH
EAAIKGKIDV CIVLLQHGAD PNIRNTDGKS ALDLADPSAK AVLTGEYKKD ELLEAARSGN
EEKLMALLTP LNVNCHASDG RKSTPLHLAA GYNRVRIVQL LLQHGADVHA KDKGGLVPLH
NACSYGHYEV TELLLKHGAC VNAMDLWQFT PLHEAASKNR VEVCSLLLSH GADPTLLNCH
SKSAVDMAPT PELKERLTYE FKGHSLLQAA READVAKVKK TLALEIISFK HPQTNETALH
CAVASPHPKR KQVTELLLRK GANINEKNKD FMTPLHVAAE RAHNDILEVL QKHGAKVNAV
DTLGQTALHR AALAGHIQTC KLLLSYGADP SIVSLQGFTA AQMGNEAVQQ ILNENVPTRN
SDVDYRFLEA AKAGDLDTVQ QLCTPQNVNC RDLEGRHSTP LHFAAGYNRV AVVEYLLHHG
ADVHAKDKGG LVPLHNACSY GHYEVAELLV RHGASVNVAD LWKFTPLHEA AAKGKYEICK
LLLKHGADPS KKNRDGNMPL DMVKDGDTDI QDLLRGDAAL LDAAKKGCLA RVQKLCSPEN
INCRDTQGRN STPLHLAAGY NNLEVAEYLL EHGADVNAQD KGGLIPLHNA ASYGADDIRA
LLMDAMPPDA LPSCFKPQAT VVSASVISPA STPSCLSAAS SIDNLAGPLT ELAAAAATGS
SGVADGATGT DRKEGESNQF LKSLGLEHLR DIFEREQITL DVLADMGHEE LKEIGINAYG
HRHKLIKGVE RLLGGQQGGN PYLTFHCASQ GTILIDLAPE DKEYQSVEEE MQSTIREHRD
GGNAGGVFSR YNIIKIQKVV NKKLRERYTH RQKEIADENH NHHNERMLFH GSPFINAIIH
KGFDERHAYI GGMFGAGIYF AENSSKSNQY VYGIGGGTGC PTHKDRSCYL CHRQMLFCRV
TLGKSFLQFS AMKMAHAPPG HHSVIGRPSV NGLAYAEYVI YRGEQAYPEY LITYQILKPE
SAAQSAAGAE QKS
//
