ID A0A3B4F0W9_9CICH Unreviewed; 1256 AA.
AC A0A3B4F0W9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=LOC102215744 {ECO:0000313|RefSeq:XP_005733623.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000004135.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000004135.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_005733623.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_005733623.1; XM_005733566.2.
DR AlphaFoldDB; A0A3B4F0W9; -.
DR Ensembl; ENSPNYT00000004240.1; ENSPNYP00000004135.1; ENSPNYG00000003131.1.
DR GeneID; 102215744; -.
DR GeneTree; ENSGT00940000156161; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000261460; Unplaced.
DR Proteomes; UP000695023; Unplaced.
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:UP000695023};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
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..326
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 327..359
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 360..392
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 447..482
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 483..515
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 516..548
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 REPEAT 642..674
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 675..707
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 762..794
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 795..827
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 828..860
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 959..1018
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1041..1246
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..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1256 AA; 135192 MW; E57365062FFA1151 CRC64;
MAVSRRSSQQ QQQQNTLQSP PRNGSLSGAP PGSPPMALLT SAVGPSENER ECSGGIEMAL
ASPDLPAPAL ASSASSTTTT SGGGSSSVSS PGSGAASPTD GSSGIGGAFR ELFEACRNGD
VSRVKRLVDS VNVNAKDMAG RKSTPLHFAA GFGRKDVVEH LLQTGANVHA RDDGGLIPLH
NACSFGHAEV VSLLLCQGAD PNARDNWNYT PLHEAAIKGK IDVCIVLLQH GADPNIRNTD
GKSALDLADP SAKAVLTGEY KKDELLEAAR SGNEEKLMAL LTPLNVNCHA SDGRKSTPLH
LAAGYNRVRI VQLLLQHGAD VHAKDKGGLV PLHNACSYGH YEVTELLLKH GACVNAMDLW
QFTPLHEAAS KNRVEVCSLL LSHGADPTLL NCHSKSAVDM APTPELKERL TYEFKGHSLL
QAAREADVAK VKKTLALEII SFKHPQTNET ALHCAVASPH PKRKQVTELL LRKGANINEK
NKDFMTPLHV AAERAHNDIL EVLQKHGAKV NAVDTLGQTA LHRAALAGHI QTCKLLLSYG
ADPSIVSLQG FTAAQMGNEA VQQILNENVP TRNSDVDYRF LEAAKAGDLD TVQQLCTPQN
VNCRDLEGRH STPLHFAAGY NRVAVVEYLL HHGADVHAKD KGGLVPLHNA CSYGHYEVAE
LLVRHGASVN VADLWKFTPL HEAAAKGKYE ICKLLLKHGA DPSKKNRDGN MPLDMVKDGD
TDIQDLLRGD AALLDAAKKG CLARVQKLCS PENINCRDTQ GRNSTPLHLA AGYNNLEVAE
YLLEHGADVN AQDKGGLIPL HNAASYGHVD IAALLIKYNT CVNATDKWAF TPLHEAAQKG
RTQLCALLLA HGADPTMKNQ EGQTALDLAT ADDIRALLMD AMPPDALPSC FKPQATVVSA
SVISPASTPS CLSAASSIDN LAGPLTELAA AAATGSSGVA DGATGTDRKE GEMAMLDMNI
SQFLKSLGLE HLRDIFEREQ ITLDVLADMG HEELKEIGIN AYGHRHKLIK GVERLLGGQQ
GGNPYLTFHC ASQGTILIDL APEDKEYQSV EEEMQSTIRE HRDGGNAGGV FSRYNIIKIQ
KVVNKKLRER YTHRQKEIAD ENHNHHNERM LFHGSPFINA IIHKGFDERH AYIGGMFGAG
IYFAENSSKS NQYVYGIGGG TGCPTHKDRS CYLCHRQMLF CRVTLGKSFL QFSAMKMAHA
PPGHHSVIGR PSVNGLAYAE YVIYRGEQAY PEYLITYQIL KPESAAQSAA GAEQKS
//
