ID A0A3B3XMC7_9TELE Unreviewed; 1257 AA.
AC A0A3B3XMC7;
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};
OS Poecilia mexicana.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48701 {ECO:0000313|Ensembl:ENSPMEP00000016181.1, ECO:0000313|Proteomes:UP000261480};
RN [1] {ECO:0000313|Ensembl:ENSPMEP00000016181.1}
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; A0A3B3XMC7; -.
DR STRING; 48701.ENSPMEP00000016181; -.
DR Ensembl; ENSPMET00000024686.1; ENSPMEP00000016181.1; ENSPMEG00000018884.1.
DR Proteomes; UP000261480; 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; 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 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..1247
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1257 AA; 135311 MW; 9166EFB61233EEE6 CRC64;
MAVSRRSSQQ QQQQTTLQSP PRNGSLSGAS PASPPMALLS PAVGSSESER ECSGGVDMAL
ASPDLPVQVL ASSASSTSTT SGGGSSSVSS PGSGATSPID GSSGVVGAFR 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
QAAREADMAK VKKTLALEII GFKHPQSNET ALHCAVASPH PKRKQVTELL LRKGANINEK
NKDFMTPLHV AAERAHNDIL EVLQKHGAKV NAADTLGQTA LHRAALAGHI QTCKLLLSYG
ADPSIVSLQG FTAAQMGNEA VQQILNENVP TRNSDVDYRF LEAAKAGDLD TVQQLCSPQN
VNCRDLEGRH STPLHFAAGY NRVAVVEYLL HHGADVHAKD KGGLVPLHNA CSYGHYEVAE
LLVRHGASVN VADLWKFTPL HEAAAKGKYE ICKLLLKHGA DPTKKNRDGN IPLDMVKDGD
TDIQDLLRGD AALLDAAKKG CLARVQKLCS PENINCRDAQ GRNSTPLHLA AGYNNLEVAE
YLLEHGADVN AQDKGGLIPL HNAASYGHVD IAALLIKYNT CVNATDKWAF TPLHEAAQKG
RTQLCALLLA HGADPTMKNQ EGQTALDLAT ADDIRALLMD AMPPDALPSC FKPQATVVSA
SVISPASTPS CLSAASSIDN LAGPLTELAA SAAAGASGVA DGASGTDRKE GEMTMLDMNI
SQFLKSLGLE HLRDIFEREQ ITLDVLADMG HEELKEIGIN AYGHRHKLIK GVERLLGGQQ
GGNPYLTFHC ANQGTILIDL SPDDKEYQSV EEEMQSTIRE HRDGGNAGGV FSRYNIIKIQ
KVVNKKLRER YTHRQKEIAD ENHNHHNERM LFHGSPFINA IIHKGFDERH AYIGGMFGAG
IYFAENSSKS NQYVYGIGGG TGCPTHKDRS CYLCHRLQML FCRVTLGKSF LQFSAMKMAH
APPGHHSVIG RPSVNGLAYA EYVIYRGEQA YPEYLITYQI LKPESAAQSA AAAEQKS
//
