ID A0A091KQJ1_9GRUI Unreviewed; 926 AA.
AC A0A091KQJ1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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};
DE Flags: Fragment;
GN ORFNames=N324_01659 {ECO:0000313|EMBL:KFP41565.1};
OS Chlamydotis macqueenii (Macqueen's bustard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Gruiformes; Otididae; Chlamydotis.
OX NCBI_TaxID=187382 {ECO:0000313|EMBL:KFP41565.1, ECO:0000313|Proteomes:UP000053330};
RN [1] {ECO:0000313|EMBL:KFP41565.1, ECO:0000313|Proteomes:UP000053330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N324 {ECO:0000313|EMBL:KFP41565.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK750273; KFP41565.1; -; Genomic_DNA.
DR RefSeq; XP_010117928.1; XM_010119626.1.
DR AlphaFoldDB; A0A091KQJ1; -.
DR GeneID; 104479076; -.
DR KEGG; cmac:104479076; -.
DR OrthoDB; 5477658at2759; -.
DR Proteomes; UP000053330; Unassembled WGS sequence.
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; 4.
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; PF12796; Ank_2; 4.
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; 13.
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; 11.
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:UP000053330};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 1..32
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 33..65
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 120..155
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 282..314
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 315..347
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 348..380
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 435..467
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 468..500
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 501..533
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 629..688
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 711..916
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP41565.1"
FT NON_TER 926
FT /evidence="ECO:0000313|EMBL:KFP41565.1"
SQ SEQUENCE 926 AA; 101251 MW; 6B511C844C289FEC CRC64;
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
LAVGGASNAG 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
//
