ID A0A2K6JPC3_RHIBE Unreviewed; 993 AA.
AC A0A2K6JPC3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-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};
GN Name=TNKS2 {ECO:0000313|Ensembl:ENSRBIP00000000874.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000000874.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000000874.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000000874.1}
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; A0A2K6JPC3; -.
DR Ensembl; ENSRBIT00000004950.1; ENSRBIP00000000874.1; ENSRBIG00000003573.1.
DR GeneTree; ENSGT00940000159911; -.
DR Proteomes; UP000233180; 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; 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; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 12.
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; 11.
DR PROSITE; PS50088; ANK_REPEAT; 12.
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:UP000233180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 18..50
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 51..83
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 84..116
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 171..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 240..272
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 333..365
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 366..398
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 399..431
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 486..518
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 519..551
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 552..584
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 685..744
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 767..972
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 627..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 993 AA; 108674 MW; 890411C978F72C35 CRC64;
MMALLTPLNV NCHASDGRKS TPLHLAAGYN RVKIVQLLLQ HGADVHAKDK GDLVPLHNAC
SYGHYEVTEL LVKHGACVNA MDLWQFTPLH EAASKNRVEV CSLLLSYGAD PTLLNCHNKS
AIDLAPTPQL KERLAYEFKG HLLLQAAREA DVTRIKKHLS LEMVNFKHPQ THETALHCAA
ASPYPKRKQI CELLLRKGAN INEKTKEFLT PLHVASEKAH NDVVEVVVKH EAKVNALDNL
GQTSLHRAAY CGHLQTCRLL LSYGCDPNII SLQGFTALQM GNENVQQLLQ EGISLGNSEA
DRQLLEAAKA GDVETVKKLC TVQSVNCRDI EGRQSTPLHF AAGYNRVSVV EYLLQHGADV
HAKDKGGLVP LHNACSYGHY EVAELLVKHG AVVNVADLWK FTPLHEAAAK GKYEICKLLL
QHGADPTKKN RDGNTPLDLV KDGDTDIQDL LRGDAALLDA AKKGCLARVK KLSSPDNVNC
RDTQGRHSTP LHLAAGYNNL EVAEYLLQHG ADVNAQDKGG LIPLHNAASY GHVDVAALLI
KYNACVNATD KWAFTPLHEA AQKGRTQLCA LLLAHGADPT LKNQEGQTPL DLVSADDVSA
LLTAAMPPSA LPSCYKPQVL NGVRSPGATA DALSSGPSSP SSLSAASSLD NLSGSFSELS
SVVSSSGTEG ASGLEKKEVP GVDFSITQFV RNLGLEHLMD IFEREQITLD VLVEMGHKEL
KEIGINAYGH RHKLIKGVER LISGQQGLNP YLTLNTSGSG TILIDLSPDD KEFQSVEEEM
QSTVREHRDG GHAGGIFNRY NILKIQKVCN KKLWERYTHR RKEVSEENHN HANERMLFHG
SPFVNAIIHK GFDERHAYIG GMFGAGIYFA ENSSKSNQYV YGIGGGTGCP VHKDRSCYIC
HRQLLFCRVT LGKSFLQFSA MKMAHSPPGH HSVTGRPSVN GLALAEYVIY RGEQAYPEYL
ITYQIMRPEG NLPEFSFPRI HTPVTPNPWR IAP
//
