ID A0A3P8SA80_AMPPE Unreviewed; 1255 AA.
AC A0A3P8SA80;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-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 Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000008985.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000008985.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000008985.1}
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; A0A3P8SA80; -.
DR Ensembl; ENSAPET00000009234.1; ENSAPEP00000008985.1; ENSAPEG00000006372.1.
DR GeneTree; ENSGT00940000156161; -.
DR Proteomes; UP000265080; Chromosome 5.
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; 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; PF13637; Ank_4; 2.
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|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:UP000265080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 140..172
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 173..205
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 206..238
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 293..325
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 326..358
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 359..391
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 446..481
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 482..514
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 515..547
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 608..640
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 641..673
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 674..706
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 761..793
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 794..826
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 827..859
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 958..1017
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1040..1245
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1255 AA; 135176 MW; 2A40B4421DDEBED8 CRC64;
MAVSRRSSQQ QQQQSTLQSP PRNSSLSGAP PASPPMSLLT SAVGPPETER ECSGGIEMAV
ASPDLPAPVL ASSASSTTTT SGGGSSVSSP GSGATSPTDG SSGIGGAFRE LFEACRNGDV
SRVKRLVDSV NVNAKDMAGR KSTPLHFAAG FGRKDVVEHL LQTGANVHAR DDGGLIPLHN
ACSFGHAEVV SLLLCQGADP NARDNWNYTP LHEAAIKGKI DVCIVLLQHG ADPNIRNTDG
KSALDLADPS AKAVLTGEYK KDELLEAARS GNEEKLMALL TPLNVNCHAS DGRKSTPLHL
AAGYNRVRIV QLLLQHGADV HAKDKGGLVP LHNACSYGHF EVTELLLKHG ACVNAMDLWQ
FTPLHEAASK NRVEVCSLLL SHGADPTLLN CHSKSAVDMA PTPELKERLT YEFKGHSLLQ
AAREADMAKV KKTLALEIIS FKHPQTNETA LHCAVASPHP KRKQVTELLL RKGANINEKN
KDFMTPLHVA AERAHNDILE VLQKHGAKVN AVDTLGQTAL HRAALAGHIQ TCKLLLSYGA
DPSIVSLQGF TAAQMGNEAV QQILNENVPT RNSDVDYRFL EAAKAGDLDT VQQLCTPQNV
NCRDLEGRHS TPLHFAAGYN RVAVVEYLLH HGADVHAKDK GGLVPLHNAC SYGHYEVAEL
LVRHGASVNV ADLWKFTPLH EAAAKGKYEI CKLLLKHGAD PSKKNRDGNM PLDMVKDGDT
DIQDLLRGDA ALLDAAKKGC LARVQKLCSP ENINCRDTQG RNSTPLHLAA GYNNLEVAEY
LLEHGADVNA QDKGGLIPLH NAASYGHVDI AALLIKYNTC VNATDKWAFT PLHEAAQKGR
TQLCALLLAH GADPTMKNQE GQTALDLATA DDIRALLMDA MPPDALPSCF KPQATVVSAS
VISPASTPSC LSAASSIDNL AGPLTELAAA AGAGTSGVAD GATGTDRKEG EMAMLDMNIS
QFLKSLGLEH LRDIFEREQI TLDVLADMGH EELKEIGINA YGHRHKLIKG VERLLGGQQG
ANPYLTFHCA NQGTILIDLA PDDKEYQSVE EEMQSTIREH RDGGNAGGVF SRYNIIKIQK
VVNKKLRERY THRQKEIADE NHNHHNERML FHGSPFINAI IHKGFDERHA YIGGMFGAGI
YFAENSSKSN QYVYGIGGGT GCPTHKDRSC YLCHRQMLFC RVTLGKSFLQ FSAMKMAHAP
PGHHSVIGRP SVNGLAYAEY VIYRGEQAFP EYLITYQILK PESAAQSAAG AEQKS
//
