ID M7BVP7_CHEMY Unreviewed; 1132 AA.
AC M7BVP7;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=UY3_06685 {ECO:0000313|EMBL:EMP36163.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP36163.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR EMBL; KB526247; EMP36163.1; -; Genomic_DNA.
DR AlphaFoldDB; M7BVP7; -.
DR STRING; 8469.M7BVP7; -.
DR eggNOG; KOG4177; Eukaryota.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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; PTHR24123; ANKYRIN REPEAT-CONTAINING; 1.
DR Pfam; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 5.
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; 2.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 13.
DR PROSITE; PS50088; ANK_REPEAT; 14.
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}; Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 38..70
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 71..103
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 158..190
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 191..223
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 224..256
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 311..346
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 347..379
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 380..412
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 473..505
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 506..538
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 539..571
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 626..658
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 659..691
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 692..724
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 825..884
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 932..1130
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 1132 AA; 123621 MW; 558F74191A54A373 CRC64;
MAPRADCLVL SHDTGFGRKD VVEYLLQSGA NVHARDDGGL IPLHNACSFG HAEVVNLLLR
HGADPNARDN WNYTPLHEAA IKGKIDVCIV LLQHGAEPAI RNTDGRTALD LADPSAKAVL
TGEYKKDELL ESARGGNEEK MMALLTPLNV NCHASDGRKS TPLHLAAGYN RVKIVQLLLQ
HGADVHAKDK GDLVPLHNAC SYGHYEVTEL LVKHGACVNA MDLWQFTPLH EAASKNRVEV
CSLLLSYGAD PTLLNCHNKS TIDLAPTPQL KERLAYEFKG HSLLQAARES DVARIKKYLS
LETVNFKHPQ THETALHCAA ASLYPKRKQV CELLLRKGAN INEKTKDFLT PLHVASEKAH
NDVVEVVVKH EAKVNALDNL GQTSLHRAAH CGHLQTCRLL LSSGCDPSIV SLQGFTALQM
GNESVQQLLQ EGIPLSNSDA DRQLLEAAKA GDVDTVKKLC TIQSVNCRDI EGRQSTPLHF
AAGYNRVSVV EYLLQHGADV HAKDKGGLVP LHNACSYGHY EVAELLVKHG AVVNVADLWK
FTPLHEAAAK GKYEICKLLL QHGADSTKKN RDGNTALDLV KDGDTDIQDL LRGDAALLDA
AKKGCLARVK KLCSPDNVNC RDTQGRHSTP LHLAAGYNNL EVAEYLLQHG ADVNAQDKGG
LIPLHNAASY GHVDVAALLI KYNACVNATD KWAFTPLHEA AQKGRTQLCA LLLAHGADPT
LKNQEGQTPL DLVTADDVNT LLTAAMPPSA LPSCYKPQVI NVSQTTGSTA DCLSSVPSSP
SSLSAASSLD NLSGSFSELP SVVGTNSAEG ATVLEKKEVP GVDFSINQFV RNLGLEHLID
VFEREQITLD VLVEMGHKEL KEIGINAYGH RHKIIKGVER LISGQQGSDD RGSQWLWFAA
PGQWELLEAA WAEERIGHHF QQLPLAWTAG LNPYLTLNTS GSGTILIDLS PDDKEFQSVE
EEIQKVCNKK LWERYTHRRK EVSEENHNHA NERMLFHGSP FVNAIIHKGF DERHAYIGGM
FGAGIYFAEN SSKSNQYVYG IGGGTGCPVH KDRSCYACHR QLLFCRVTLG KSFLQFSAMK
MAHSPPGHHS VTGRPSVNGL ALAEYVIYRG EQAYPEYLIT YQIMKPEATM EA
//
