ID   A0A1L8FES1_XENLA        Unreviewed;      1165 AA.
AC   A0A1L8FES1;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Poly [ADP-ribose] polymerase tankyrase-2 {ECO:0000313|RefSeq:XP_018082988.1};
GN   Name=tnks2.S {ECO:0000313|RefSeq:XP_018082988.1,
GN   ECO:0000313|Xenbase:XB-GENE-5828061};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018082988.1};
RN   [1] {ECO:0000313|RefSeq:XP_018082988.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018082988.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018082988.1};
RG   RefSeq;
RL   Submitted (NOV-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   RefSeq; XP_018082988.1; XM_018227499.2.
DR   AlphaFoldDB; A0A1L8FES1; -.
DR   STRING; 8355.A0A1L8FES1; -.
DR   PaxDb; 8355-A0A1L8FES1; -.
DR   GeneID; 100036993; -.
DR   KEGG; xla:100036993; -.
DR   AGR; Xenbase:XB-GENE-5828061; -.
DR   CTD; 100036993; -.
DR   Xenbase; XB-GENE-5828061; tnks2.S.
DR   OMA; CKLLLQX; -.
DR   OrthoDB; 5477658at2759; -.
DR   Proteomes; UP000186698; Chromosome 7S.
DR   Bgee; 100036993; Expressed in brain and 19 other cell types or tissues.
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; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1.
DR   PANTHER; PTHR24189; MYOTROPHIN; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13637; Ank_4; 4.
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; 3.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 14.
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};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022695}.
SQ   SEQUENCE   1165 AA;  126684 MW;  FB982DBF662CE57B CRC64;
     MSGRRCAGAS GSAASHGNIG AGGEPARELF EACRNGDVER VRKLVNSDNV NSRDTAGRKS
     TPLHFAAGFG RKDVVEHLLQ SGANVHARDD GGLIPIHNAC SFGHAEVVSL LLRHGADPNA
     RDNWNYTPLH EAAIKGKIDV CIVLFQHGAD PTIRNTDSRT ALDLSDPSAK AVLTGEYKKD
     ELLESARSGN EEKMMALLTP LNVNCHASDG RKSTPLHLAA GYNRVKIVQL LLQHGADVHA
     KDKGDLVPLH NACSYGHYEV TELLVKHGAS VNAMDLWQFT SLHEAASKNR VEVCSLLLSY
     GADPTMLNCH NKSAIDLAPT PQLKERLSYE FKGHSLLQAA READLTRIKK HLSLEIVNFK
     HPQTHDTALH CAASSPYPKR KQVCELLFRK GANVNEKTKD FLTPLHIASD KAHNDIVELL
     IKHEAKVNAL DNLGQTSLHR AAHCGHLQTC RLLLNSGCDP SIVSLQGFTA LQMGNESVQQ
     LLQEGLPFSN SDADSQLLEA AKAGDLDVVK KLCTSQSVNC RDVEGRQSTP LHFAAGYNRV
     AVVEYLLQHG ADVHAKDKGG LVALHNACSY GHYEVTELLV KHGAVINVAD LWKFTPLHEA
     AAKGKYEICK LLLLHGADST KKNRDGNTPL DLVKDGDTDI QDLLRGDAAL LDAAKKGCVS
     RVKKLCTPEN VNCRDTQGRH STPLHLAAGY NNLEVAEYLL QHGADVNAAD KGGLIPLHNA
     ASYGHVDVAA LLIKYNACVN ANDKWAFTPL HEAAQKGRTQ LCALLLAHGA DPALKNQEGQ
     APLDLVTADD VRALLTAAMP PAALPTFYKP QLLNVPQPST TAIAALSSVP LSSPTLSAAS
     SLDNLASSFS ETTSVSSGGA EGASGLDKKD EGVDLNINQF LRNLGLEHLI DVFEREQITL
     DVLIEMGHKE FKEIGISAYG HRHKIIKGVE RLISGQHGLN PYLTLNTSNS GTILIDLAPD
     DKEFLSVEEE MQSTVREHRD GGHAGGVFTK YNILKIQKVC NKKLWEKYTH RQKEVTEENH
     NHSNERMLFH GSPFVNAIIH KGFDERHAYI GGMFGAGIYF AENSSKSNQY VYGIGGGTGC
     PIHKDRSCYV CHRQLLFCRV TLGKSFLQFS AMKMAHSPPG HHSVTGRPSV NGLALAEYVI
     YRGEQAYPEY IITYQIMKPE AVAEG
//