ID A0A3B3RTT5_9TELE Unreviewed; 1027 AA.
AC A0A3B3RTT5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:ENSPKIP00000021952.1};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000021952.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000021952.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A3B3RTT5; -.
DR Ensembl; ENSPKIT00000002604.1; ENSPKIP00000021952.1; ENSPKIG00000006010.1.
DR GeneTree; ENSGT00940000159911; -.
DR Proteomes; UP000261540; 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; PTHR24178:SF9; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24178; MOLTING PROTEIN MLT-4; 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; 16.
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; 13.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT REPEAT 5..37
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
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 DOMAIN 755..814
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 820..1025
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 708..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1027 AA; 112188 MW; D21EA861A338655D CRC64;
MTGTKTVSPL PWPSGFGRRD VVEYLLQNGA NVHARDDGGL ISLHNACSFG HAEVVSLLLH
HGADANSKDN WNYTPLHEAA IKGKIDVCIV LLQHGADPTI RNTDGRTPLD LAEPSTKAVL
NGEYRKDDLL ESARSGNEEK LMSLLTPLNV NCHASDGRKS TPLHLAAGYN RVKTVQLLLQ
HGADVHAKDK GDLVPLHNAC SYGHYEVTDL LVKHGACVNA MDLWQFTPLH EAASKNRVEV
CSLLLCHGAD PTFLNCHNKS AIDLAPTAQL RERLAYEFKG HALLQASRDA DVARVKKHLT
AESINFRHPQ TYETALHYAA ASPYPKRKQV CELLLRKGGN INEKCRDFLT PLHLASEKSH
NDVIEVLVKH EAKVNALDSM GQTALHRAAR CGHLQTCRLL LSSGCDPLIM SLQGFSPSQM
GNQSVQEVLQ EGVFIGNSDV DRQLLEASKS GDVEIVKKLC TLQNVNCRDV EGRQSTPLHF
AAGYNRVAVV DYLLQHGADV HAKDKGGLVP LHNACSYGHY EVAELLVMHG AVVNVADLWK
FTPLHEAAAK GKYEICKLLL QHGADPTKKN RDGNTPLDLV RDSDTDIQDL LRGDAALLDA
AKKGCLARVK KLCRPDNVNC RDTLGRHSTP LHLAAGYNNL EVAEYLLQHD AEVNSQDKGG
LIPLHNAASY GADDVRALLT AAMPPSALPS CYKPQVISIT GASAPSALPA GPPAGPPGGA
LDPQGGFPEL PALMGTAGAE GATEVDKKEP GLDLSIDQFL NNLGLEQLLE IFEREQITLD
VLVEMGHKEL KEIGINAYGH RHKIIKGAER LITGPQSLNP YLSLNTANSG TILIDLGVDD
KEFQSVEEEV LLGTSLLRFQ MCNKKLWERY THRRKEVSEE NHNHSNERML FHGSPFVNAI
IHKGFDERHA YIGGMFGAGI YFAENSSKSN QYVYGIGGGT GCPLHKDRSC YVCQRHLLFC
RVTLGKSFLQ FSAMKMAHSP PGHHSVTGRP SVNGLALAEY VIYRGEQAYP EYLITYQIIK
PEGNADG
//
