ID A0A2K6QAW8_RHIRO Unreviewed; 1047 AA.
AC A0A2K6QAW8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:ENSRROP00000025911.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000025911.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000025911.1}
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; A0A2K6QAW8; -.
DR Ensembl; ENSRROT00000050134.1; ENSRROP00000025911.1; ENSRROG00000036681.1.
DR GeneTree; ENSGT00940000159911; -.
DR Proteomes; UP000233200; 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; 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; PTHR24178:SF9; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 1.
DR Pfam; PF00023; Ank; 1.
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; 14.
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; 12.
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:UP000233200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 34..66
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 67..99
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 154..186
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 187..219
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 220..252
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 307..342
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 343..375
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 376..408
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 469..501
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 502..534
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 535..567
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 622..654
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 758..817
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 840..1045
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 700..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1047 AA; 114560 MW; 02726E33E73689D1 CRC64;
TYVWTICFHL GFGRKDVVEY LLQNGANVQA RDDGGLIPLH NACSFGHAEV VNLLLRHGAD
PNARDNWNYT PLHEAAIKGK IDVCIVLLQH GAEPTIRNTD GRTALDLADP SAKAVLTGEY
KKDELLESAR SGNEEKMMAL LTPLNVNCHA SDGRKSTPLH LAAGYNRVKI VQLLLQHGAD
VHAKDKGDLV PLHNACSYGH YEVTELLVKH GACVNAMDLW QFTPLHEAAS KNRVEVCSLL
LSYGADPTLL NCHNKSAIDL APTPQLKERL AYEFKGHLLL QAAREADVTR IKKHLSLEMV
NFKHPQTHET ALHCAAASPY PKRKQICELL LRKGANINEK TKEFLTPLHV ASEKAHNDVV
EVVVKHEAKV NALDNLGQTS LHRAAYCGHL QTCRLLLSYG CDPNIISLQG FTALQMGNEN
VQQLLQEGIS LGNSEADRQL LEAAKAGDVE TVKKLCTVQS VNCRDIEGRQ STPLHFAAGY
NRVSVVEYLL QHGADVHAKD KGGLVPLHNA CSYGHYEVAE LLVKHGAVVN VADLWKFTPL
HEAAAKGKYE ICKLLLQHGA DPTKKNRDGN TPLDLVKDGD TDIQDLLRGD AALLDAAKKG
CLARVKKLSS PDNVNCRDTQ GRHSTPLHLA AGYNNLEVAE YLLQHGADVN AQDKGGLIPL
HNAASYGADD VSALLTAAMP PSALPSCYKP QVLNGVRSPG ATADALSSGP SSPSSLSAAS
SLDNLSGSFS ELSSVVSSSG TEGASGLEKK EVPGVDFSIT QFVRNLGLEH LMDIFEREQI
TLDVLVEMGH KELKEIGINA YGHRHKLIKG VERLISGQQG LNPYLTLNTS GSGTILIDLS
PDDKEFQSVE EEMQSTVREH RDGGHAGGIF NRYNILKIQK VCNKKLWERY THRRKEVSEE
NHNHANERML FHGSPFVNAI IHKGFDERHA YIGGMFGAGI YFAENSSKSN QYVYGIGGGT
GCPVHKDRSC YICHRQLLFC RVTLGKSFLQ FSAMKMAHSP PGHHSVTGRP SVNGLALAEY
VIYRGEQAYP EYLITYQIMR PEGMVDG
//
