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Database: UniProt
Entry: S7Q5Y6_MYOBR
LinkDB: S7Q5Y6_MYOBR
Original site: S7Q5Y6_MYOBR 
ID   S7Q5Y6_MYOBR            Unreviewed;      1175 AA.
AC   S7Q5Y6;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=D623_10017996 {ECO:0000313|EMBL:EPQ18803.1};
OS   Myotis brandtii (Brandt's bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC   Myotis.
OX   NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ18803.1, ECO:0000313|Proteomes:UP000052978};
RN   [1] {ECO:0000313|Proteomes:UP000052978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23962925; DOI=10.1038/ncomms3212;
RA   Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA   Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA   Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA   Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA   Krogh A., Wang J., Gladyshev V.N.;
RT   "Genome analysis reveals insights into physiology and longevity of the
RT   Brandt's bat Myotis brandtii.";
RL   Nat. Commun. 4:2212-2212(2013).
CC   -!- FUNCTION: Plays a central role during spermatogenesis by repressing
CC       transposable elements and preventing their mobilization, which is
CC       essential for the germline integrity. Acts via the piRNA metabolic
CC       process, which mediates the repression of transposable elements during
CC       meiosis by forming complexes composed of piRNAs and Piwi proteins and
CC       governs the methylation and subsequent repression of transposons. Its
CC       association with pi-bodies suggests a participation in the primary
CC       piRNAs metabolic process. Required prior to the pachytene stage to
CC       facilitate the production of multiple types of piRNAs, including those
CC       associated with repeats involved in the regulation of retrotransposons.
CC       May act by mediating protein-protein interactions during germ cell
CC       maturation. {ECO:0000256|ARBA:ARBA00025297}.
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   EMBL; KE164566; EPQ18803.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7Q5Y6; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   Proteomes; UP000052978; Unassembled WGS sequence.
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; PTHR24189; MYOTROPHIN; 1.
DR   PANTHER; PTHR24189:SF50; MYOTROPHIN; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 5.
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; 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; 13.
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, 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:UP000052978};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU362114}.
FT   REPEAT          71..97
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          98..130
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          131..163
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          218..250
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          251..283
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          284..316
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          371..406
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          407..439
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          440..472
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          533..565
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          567..599
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          600..632
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          687..719
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          720..752
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          753..785
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          886..945
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          968..1173
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1175 AA;  128541 MW;  F57A92A6B2B39C01 CRC64;
     MIIKKIKGRN VSEEKDVAPA PEKQVPALEE PTTILEGVNT VVITTAAWSL CRPPGPELQT
     EPGRSEQWNR HQRLRFGRKD VVEYLLQNGA NVQARDDGGL IPLHNACSFG HAEVVTLLLR
     HGADPNARDN WNYTPLHEAA IKGKIDVCIV LLQHGAEPTI QNTDGRTALD LADPSAKAVL
     TGEYKKDELL ESARSGNEEK MMALLTPLNV NCHASDGRKS TPLHLAAGYN RVKIVQLLLQ
     HGADVHAKDK GDLVPLHNAC SYGHYEVTEL LVKHGACVNA MDLWQFTPLH EAASKNRIEV
     CSLLLSYGAD PTLLNCHNKS AIDLAPTPQL KERLAYEFKG HSLLQAAREA DVTRIKKHLS
     LEMVNFKHPQ THETALHCAA ASPYPKRKQI CELLLRKGAN INEKTKEFLT PLHVASEKAH
     NDVVEVVVKH EAKVNALDNL GQTSLHRAAH CGHLQTCRLL LSYGCDPNII SLQGFTALQM
     GNENVQQLLQ EGIPLGNSEA DRQLLEAAKA GDVETVKKLC TVQSVNCRDI EGRQSTPLHF
     AAGYNRVSVV EYLLQHGADV HAKDKGQGLV PLHNACSYGH YEVAELLVKH GAVVNVADLW
     KFTPLHEAAA KGKYEICKLL LQHGADPTKK NRDGNTPLDL VKDGDTDIQD LLRGDSALLD
     AAKKGCLARV KKLSSPDNVN CRDIQGRHST PLHLAAGYNN LEVAEYLLQH GADVNAQDKG
     GLIPLHNAAS YGHVDVAALL IKYNACVNAT DKWAFTPLHE AAQKGRTQLC ALLLAHGADP
     TLKNQEGQTP LDLVSADDVS ALLTAAMPPS ALPSCYKPQV LNGMRSPGVS ADALSSGPSS
     PSSLSAASSL DNLSGSFSEL SSVVSSSGTE GASSLEKKEV PGVDFSITQF VRILGLEHLM
     DIFEREQITL DVLVEMGHKE LKEIGINAYG HRHKLIKGVE RLISGQQGLN PYLTLNTSGS
     GTILIDLSPD DKEFQSVEEE MQSTVREHRD GGHAGGIFNR YNILKIQKVC NKKLWERYTH
     RRKEVSEENH NHANERMLFH GSPFVNAIIH KGFDERHAYI GGMFGAGIYF AENSSKSNQY
     VYGIGGGTGC PVHKDRSCYI CHRQLLFCRV TLGKSFLQFS AMKMAHSPPG HHSVTGRPSV
     NGLALAEYVI YRGEQAYPEY LITYQIVRPE GMVDG
//
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