ID A0A493SZ34_ANAPP Unreviewed; 1116 AA.
AC A0A493SZ34;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=TNKS {ECO:0000313|Ensembl:ENSAPLP00000018735.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000018735.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000018735.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000018735.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR AlphaFoldDB; A0A493SZ34; -.
DR Ensembl; ENSAPLT00000028559.1; ENSAPLP00000018735.1; ENSAPLG00000002335.2.
DR GeneTree; ENSGT00940000156161; -.
DR Proteomes; UP000016666; Chromosome 4.
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; PTHR24118:SF99; CHARON; 1.
DR PANTHER; PTHR24118; POTE ANKYRIN DOMAIN; 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; 18.
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|PROSITE-ProRule:PRU00023};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 4..36
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 37..69
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 70..102
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 157..189
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 190..222
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 223..255
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 310..345
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 346..378
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 379..411
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 472..504
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 505..537
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 538..570
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 625..657
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 658..690
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 691..723
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 819..878
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 901..1106
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 1116 AA; 121589 MW; A9F1558203FAB9ED CRC64;
MAGRKSTPLH FAAGFGRKDV VEHLLQTGAS VHARDDGGLI PLHNACSFGH AEVVSLLLCQ
GADPNARDNW NYTPLHEAAI KGKIDVCIVL LQHGADPNIR NTDGKSALDL ADPSAKAVLT
GEYKKDELLE AARSGNEEKL MALLTPLNVN CHASDGRKST PLHLAAGYNR VRIVQLLLQH
GADVHAKDKG GLVPLHNACS YGHYEVTELL LKHGACVNAM DLWQFTPLHE AASKNRVEVC
SLLLSHGADP TLVNCHGKSA VDMAPTPELR ERLTYEFKGH SLLQAAREAD LAKVKKTLAL
EIINFKQPQS HETALHCAVA AVHPKRKQVT ELLLRKGANV NEKNKDFMTP LHVAAEKAHN
DVMEVLHKHG AKMNALDTLG QTALHRAALA GHLQTCRLLL NYGSDPSIIS LQGFTAAQMG
NEAVQQILSE STPVRTSDVD YRLLEASKAG DLETVKQLCS PQNVNCRDLE GRHSTPLHFA
AGYNRVSVVE YLLHHGADVH AKDKGGLVPL HNACSYGHYE VAELLVRHGA SVNVADLWKF
TPLHEAAAKG KYEICKLLLK HGADPTKKNR DGNTPLDLVK EGDTDIQDLL RGDAALLDAA
KKGCLARVQK LCTQENINCR DTQGRNSTPL HLAAGYNNLE VAEYLLEHGA DVNAQDKGGL
IPLHNAASYG HVDIAALLIK YNTCVNATDK WAFTPLHEAA QKGRTQLCAL LLAHGADPTM
KNQEGQTPLD LATADDIRAL LIDAMPPEAL PTCFKPQATV VSASLISPAS TPSCLSAASS
IDNLTGPLAE LAVGGPSNAG DGAAGTERKE GEVSGLDMNI TQFLKSLGLE HLRDIFETEQ
ITLDVLADMG HEELKEIGIN AYGHRHKLIK GVERLLGGQQ GTNPYLTFHC VSQGTILLDL
APDDKEYQSV EEEMQSTIRE HRDGGNAGGI FNRYNVIRIQ KVVNKKLRER FCHRQKEVSE
ENHNHHNERM LFHGSPFINA IIHKGFDERH AYIGGMFGAG IYFAENSSKS NQYVYGIGGG
TGCPTHKDRS CYICHRQMLF CRVTLGKSFL QFSTMKMAHA PPGHHSVIGR PSVNGLAYAE
YVIYRGEQAY PEYLITYQIV KPEAPSQTAT AAEQKT
//
