ID A0A3B4DVX9_PYGNA Unreviewed; 1040 AA.
AC A0A3B4DVX9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, 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};
GN Name=TNKS2 {ECO:0000313|Ensembl:ENSPNAP00000027221.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000027221.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000027221.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B4DVX9; -.
DR Ensembl; ENSPNAT00000003148.1; ENSPNAP00000027221.1; ENSPNAG00000002397.1.
DR GeneTree; ENSGT00940000159911; -.
DR Proteomes; UP000261440; 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; PF13637; Ank_4; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 16.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 11.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1040
FT /note="Poly [ADP-ribose] polymerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017287381"
FT REPEAT 36..68
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 69..101
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 156..188
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 189..221
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 222..254
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 309..344
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 345..377
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 378..410
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 471..503
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 504..536
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 537..569
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 624..656
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 755..814
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 837..1039
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 1040 AA; 113836 MW; C3C2EC7A3C6581AA CRC64;
LYFVFSVFIF LISFGRRDVV DYLLEHGADV YARDDGGLIS LHNACSFGHA EVVSLLLHHG
ADANSRDNWN YTPLHEAAIK GKIDVCIVLL QHGAKPTVRN TDGRTALDLA EPSTKAVLTG
KCPTPLLLKN TRFTAAKKLM SLLTPLNVNC HASDGRKSTP LHLAAGYNRV KTVQLLLEHG
ADVHAKDKGD LVPLHNACSY GHYEVTELLV KHGACVNAMD LWQFTPLHEA ASKNRVEVCS
LLLSHGADPT FLNCHNKSAI DLAPTMLLKE RLAYEFKGHA LLQAARQADL IRIKKHLSLE
TINFRHPHTH ETALHCASAS SYPKRRQVCE MLLRKGANVN EKTKDLLTPL HLASEKSHND
VIEVLLKHEA KVNAVDSQGQ TPLHRAARCG QLQTCRLLIS AGCDPLITSL QGFAPAQLAN
ESIQQVLQEG ALVGNSDTDR QLLEASKSGD LETVKKLCTL QNVNCRDVEG RQSTPLHFAA
GYNRVSVVEY LLQHGADVHA KDKGGLVPLH NACSYGHYEV AELLVIHGAV INVADLWKFT
PLHEAAAKGK YEICKLLLQH GADPTKKNRD GNTPLDLVKE GDMDIQDLLR GDAALLDAAK
KGCLARVKKL CRPNNVNCRD SQGRHSTPLH LAAGYNNLEV AEYLLQHGAE VNSQDKGGLI
PLHNAASYGA DDVRALLTAA MPPSALPACY KPQVISVSAS SGMVSSTLSS SSIPHPSGSS
LDPQAGAFPE VLGPSGAEGA IGVEKTEEGG PVELSISQFL HKLGLEHLLE IFDREQISLD
VLVEMGHKEL KEIGINAYGH RHKIIKGVER LVSGPQSLNP YLTLNTANSG TILIDLASDD
KEFQSVEEEM QSTIREHRDG GHAGGVFSRY NILKIQKVCN KKLWERYTHR RKEVSEENHN
HSNERMLFHG SPFVNAIIHK GFDERHAYIG GMFGAGIYFA ENSSKSNQYV YGIGGGTGCP
LHKDRSCYIH LLFCRVTLGK SFLQFSAMKM AHSPPGHHSV SGRPSVNGLA LAEYVIYRGE
QAYPEYLITY QIIRPDGTTE
//
