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Database: UniProt
Entry: I7MGV0_TETTS
LinkDB: I7MGV0_TETTS
Original site: I7MGV0_TETTS 
ID   I7MGV0_TETTS            Unreviewed;      2623 AA.
AC   I7MGV0;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 2.
DT   27-MAR-2024, entry version 60.
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=TTHERM_00502600 {ECO:0000313|EMBL:EAS02069.2};
OS   Tetrahymena thermophila (strain SB210).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC   Tetrahymena.
OX   NCBI_TaxID=312017 {ECO:0000313|EMBL:EAS02069.2, ECO:0000313|Proteomes:UP000009168};
RN   [1] {ECO:0000313|Proteomes:UP000009168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168};
RX   PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA   Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA   Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA   Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA   Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA   Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA   Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA   Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA   Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA   Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA   Hamilton E.P., Orias E.;
RT   "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT   model eukaryote.";
RL   PLoS Biol. 4:1620-1642(2006).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; GG662548; EAS02069.2; -; Genomic_DNA.
DR   RefSeq; XP_001022314.2; XM_001022314.2.
DR   STRING; 312017.I7MGV0; -.
DR   GeneID; 7827201; -.
DR   KEGG; tet:TTHERM_00502600; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG1037; Eukaryota.
DR   InParanoid; I7MGV0; -.
DR   OrthoDB; 239153at2759; -.
DR   Proteomes; UP000009168; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd07997; WGR_PARP; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 7.
DR   Gene3D; 1.20.142.10; Poly(ADP-ribose) polymerase, regulatory domain; 1.
DR   Gene3D; 2.20.140.10; WGR domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR   InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR   InterPro; IPR036930; WGR_dom_sf.
DR   InterPro; IPR008893; WGR_domain.
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; PF02877; PARP_reg; 1.
DR   Pfam; PF05406; WGR; 1.
DR   SMART; SM00248; ANK; 24.
DR   SMART; SM00773; WGR; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 4.
DR   SUPFAM; SSF47587; Domain of poly(ADP-ribose) polymerase; 1.
DR   SUPFAM; SSF142921; WGR domain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 7.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
DR   PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS51977; WGR; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU362114};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU362114};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009168};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362114}.
FT   REPEAT          695..719
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          729..761
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          795..827
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1332..1367
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1368..1406
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1452..1484
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1485..1513
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          2012..2110
FT                   /note="WGR"
FT                   /evidence="ECO:0000259|PROSITE:PS51977"
FT   DOMAIN          2138..2273
FT                   /note="PARP alpha-helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51060"
FT   DOMAIN          2283..2501
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51059"
FT   REGION          105..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1075..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1174..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2491..2570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..149
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        239..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1180..1197
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2530..2570
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2623 AA;  299110 MW;  5E749AEE50DCF703 CRC64;
     MADKGIFIYA VRDEDSMQGF ILVASEVDID VENSKAEKVG VYHIHSVKNK PYNYTVNKKL
     TNVRLDEFMS VVDEDLYEFN EKNRTLVFDK KGYDNLIGQL MDDLEEENDD DSSEEEEKKK
     KKPAPKAASA RKTRSSKGSD KVKGSDSESY EAADEEDEEE KKRSRGRPKK NKSTEEITED
     KDENSQEDQP KPKGKRGRPP SKDKAASVAV PKKQDKQDDK DGEENGEDQN GHEENGDEDK
     EEGEQKRVPG KRGRKPGKKT AETPAKKEAQ QNIIHNRKPQ VFLIQRPGKR GRKPAKKGSE
     SEDNEDADDE QEEVSKKGAK KKVEKYKKGS HNPNIPDVVK TDETFEGDSQ DINDVCCSFC
     TNRELLRAVY TGNSNLLKKL VQSKAKVSTL FAKRGPDADE TTLEIILKNK DKKCLDVLIN
     ALNKKSEISL ASNPECSLEE VYTGFNDRFA YGVPTRKVQM ARGGKEGNNA FVADINSFVD
     TQSWNENERL IFSLLENETE VQFLEFLRGL KDENLTTSLL EKTYVAVRAG NRKTASYLMK
     QANKFGGYGF NNLHEQVLSL DDVSKLDEFK KVSITKKSTG VYSKNSYGFG GAQGIITPIH
     CAAINPNPEF IKKLLEISPE FTIPDDLMRK PVHYAATCEG PGPLSYLLKQ GVDAREGDKK
     KITPLMLACQ FGRAKNVEIL LDANGKSNPD TRTREGYRAI HYAAHYGHLD CIKLMIEKGG
     VEVDSPGPKR MTPLHIATSR GHFEIVEYLL SKGAKVIVKD KFKRSAVIHA TANGYLKILS
     LILKNGGPFN DPDSSGNYPV HYAAAYGFQA CLDLLKQAGA DFNPQNSWNL TPLSIAMAKG
     HFGMVKKLLN YPECDVNCTD VKGRTIISRA TEKLNLNNLS QFEFILKEKK ANPNMADLQG
     QSPLHYLCNL SKDDYVSKRQ NEENAHHVTK KYEEEYEKIV QKATQILLDC GADINKLNTM
     EESPLTIAIK QQNFFILNIL LKKGGLDFSH VNQIDQNILH TLNTLILEGP SGIDQFYNIF
     EEIKKDKNVN LKEYLNKVDY HGFSPLLMYV KIFSENASHY REQRVEELSQ EIYSKKGGSA
     PNKKNPIKKQ APTRGPRVAK KAIRSAPAKS LIGFSNDGAL VQLTEKELEK VQKQADEDLL
     QFEQKFQKLI TFLVEKGSDV EAKVQKIKKY RSNMDVEDKS DNEEQQEQDE DDDENEGNKT
     LKDEMGNPIQ NKKVKYIPEY NSCGEMNIFG LALSHLSLPY LKFIHEQYPQ LVNNVDYLKR
     NHLHKFILKN DDEPATNVSH KVLEWLTTLK IDINQKDIIE STPLISAISQ KKYKFAKTLI
     NHKAQVDVKD IFGKTPLIMA INNIQSNNLE FVEYLLSNGA SANFADNYGR TPLHHAINKA
     DKGANASFDL ENLLIKNKAD INAADSLGRT PLHYCFVSLQ DQQYSTLQYD PFETVSSLCN
     QSNIKIDVKD NLGKTPLHYA AQKNSTISVI YMIEKKANID IEDANGNTPL AVAFRFKRSE
     ITTTLIQNGA NTSKFITINK NLKPNGEEEE EYKEPAKDHW GNPIKTRRRQ NYSSYGSRYL
     FQYQNQYDGF GGDQNSNNSI IKKLLSEYHI EEDSYIELVK RSITKEQFKE KGLDNLVFQE
     FRVRGDLPLG KHSFFKASIT FQWQGIAYLL LIKGNYNLFN ALEDAIKIDL YQLSITLLFK
     YPEDETITQC NSEGQNLIHI LCQRSPRDVN LQVKLFETLL NRGVDAKKLD NKKNLCLHFA
     FLHHQLTPKL LELGLDCNAY NDDQQTPFAL AIQEDAKQAL KIYTANYKPD YSKKFKAKLE
     GHQDYLQFTP LLIQFANKNK DLVLLNHLLA NGSNINEVDN LGRNALYYAI YHNSHKLVKF
     VLQTKKFDVK HVDNQGKNAV HYVVNPVEFG SYENTEILEL LHNAKIDFNV KDKDGNTAMF
     YALQQDSKKM AESLKKYGVE ALKEKKLPQR AATSIVTDAL FPDEEIDYEE DSKKFSEETT
     YDQYKEFFEQ KNAGDKVYLD KYVAGNYKKK DNYVVLDDNN EPYNLLMTKV DLGGGFAKYV
     FYIMQVIHDK NSDVYILYTR WGHMGGMGQM QHTPFATKEA AVKEFSKIFY QKSGNDWTNR
     HNFKKQDKKY QLVIFEKGND KKSFSLKPYD FERLNCSASQ LEKPIQEFIK NISNAEIFKQ
     AYRQFALSDQ YLPITKLSKA ALIEAQGILA DIREEVIEIQ KLRSKLTQGN NMQLLLEREE
     SVLRYSNRYY ELVPRAVSKW EPAQPLNHEH NISQEQRLVE NLLDFEAAIK IIMGSYTKLQ
     VMHPLDYCFN SLSIRMKQIQ NEHPEYKMIQ QYVSRTNHKA TDPNSQFIRN VFAVERRGEA
     ERIKQFSDHT KKLLWHGSGV QNLLSILNFG LRINGIHAQK SGSSLGDGIY FADLFSKASA
     YANNADVGVE SRFLLLCEVA VGKEQQIKTN ENFTKFANSN YQLMKGFNSV KLVGKSCPDE
     KKNLVLPNGT IVPIGPIIDF NENLKQKLQI EKSTKKSAKK STKKPAQKIP ARPIKKVVKA
     TKYSSDEENS QDEESQIQVE EDELDIPEDE IQSDGDEEIE EEEDNFDEEQ DEQNLLQNNF
     LYDVQHQGAK TPFNQLFTQY QNSEYVVYNS AQVRIRYLIE IRD
//
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