ID A0A3Q3G4H4_KRYMA Unreviewed; 1170 AA.
AC A0A3Q3G4H4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000019152.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000019152.1}
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; A0A3Q3G4H4; -.
DR Ensembl; ENSKMAT00000019415.1; ENSKMAP00000019152.1; ENSKMAG00000014133.1.
DR GeneTree; ENSGT00940000156161; -.
DR OMA; VFSQYNI; -.
DR Proteomes; UP000264800; Unplaced.
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; 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; MYOTROPHIN; 1.
DR PANTHER; PTHR24189:SF50; MYOTROPHIN; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 6.
DR Pfam; PF13637; Ank_4; 1.
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:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 54..86
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 87..119
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 120..152
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 240..272
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 273..305
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 360..395
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 396..428
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 429..461
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 522..554
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 555..587
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 588..620
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 708..740
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 741..773
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 873..932
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 955..1160
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 1170 AA; 126631 MW; 6D0B99D52607701E CRC64;
NGDASSLLSA AAAAELPAVL PTPELFEACR NGDVSRVKKL VDAVNVNAKD MAGRKSTPLH
FAAGFGRKDV VDHLLQTGAN VHARDDGGLI PLHNACSFGH SEVVSSLLCQ GADPNARDNW
NYTPLHEAAI KGKIDVCIVL LQHGADPNIR NTDGKSALDL AEPSAKAVLT GEYKKDELLE
AARSGNEEKL MALLTPLNVN CHASDGRKST PLHLAAGYNR VRIVQLLLQH GADVHAKDKG
GLVPLHNACS YGHYEVTELL LKHGACVNAM DLWQFTPLHE AASKNRVEVC SLLLSHGADP
TLLNCHSKSS VDMAPTPELK ERLTYEFKGH SLLQAAREAD MAKAKKTLAL EIINFKHPHT
HETALHCAVA SPHPKRKQVT ELLLRKGANV NEKNKDFMTP LHVAAERAHN DIMEVLQKHG
AKVNALDTLG QTALHRAALA GHLQTCRLLL GYGADASLVS LQGFTAAQMG NEAVQQILNE
NVPVRNSDVD YRLLEAAKAG DLDTVKSLCT AQNVNCRDLE GRHSTPLHFA AGYNRVSVVE
YLLHHGADVH AKDKGGLVPL HNACSYGHYE VAELLVRHGA SVNVADLWKF TPLHEAAAKG
KYEICKLLLK HGADPTKKNR DGNTPLDLVK DGDTDIQDLL RGDAALLDAA KKGCLARVQK
LCSPDNINCR DTQGRNSTPL HLAAGYNNLE VAEYLLEHGA DVNAQDKGGL IPLHNAASYG
HVDIAALLIK YNTCVNATDK WAFTPLHEAA QKGRTQLCAL LLAHGADPTM KNQEGQTPLD
LATADDIRAL LIDAMPPDAL PSCLKPQVSA NVVSTGAAGG VVISPSPSPS CLSAASSIDN
LNTPLGDITV GGASGIADGA SGSDRKEALL DMTINQFLKS LGLEHLRDIF QREQISLDVL
ADMGHEELKE IGINAYGHRH KLIKGIERLL GGQQGGNPYL TFHCSSQGTV LIDLAPDDKE
FQSVEQELQS TIREHRDGGN AGGVFSRYNI IKIQKVVNKK LRERYSHRQK EIADENHNHH
NERMLFHGSP FINAIIHKGF DERHAYIGGM FGAGIYFAEN SSKSNQYVYG IGGGTGCPPH
KDRSCYVCHR QMLFCRVTLG KSFLQFSAMK MAHAPPGHHS VIGRPSVNGL AYAEYVIYRG
EQAYPEYLIT YQIMKPESQA APAASAEQKS
//