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Database: UniProt
Entry: RTC1_DEBHA
LinkDB: RTC1_DEBHA
Original site: RTC1_DEBHA 
ID   RTC1_DEBHA              Reviewed;        1386 AA.
AC   Q6BXX5;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Restriction of telomere capping protein 1;
GN   Name=RTC1; OrderedLocusNames=DEHA2A14124g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: May be involved in a process influencing telomere capping.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat RTC1 family. {ECO:0000305}.
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DR   EMBL; CR382133; CAG84922.2; -; Genomic_DNA.
DR   RefSeq; XP_456944.2; XM_456944.1.
DR   AlphaFoldDB; Q6BXX5; -.
DR   SMR; Q6BXX5; -.
DR   STRING; 284592.Q6BXX5; -.
DR   GeneID; 2899395; -.
DR   KEGG; dha:DEHA2A14124g; -.
DR   VEuPathDB; FungiDB:DEHA2A14124g; -.
DR   eggNOG; KOG0269; Eukaryota.
DR   HOGENOM; CLU_008512_0_0_1; -.
DR   InParanoid; Q6BXX5; -.
DR   OMA; GRDGKCC; -.
DR   OrthoDB; 119005at2759; -.
DR   Proteomes; UP000000599; Chromosome A.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032008; P:positive regulation of TOR signaling; IEA:InterPro.
DR   CDD; cd16488; mRING-H2-C3H3C2_Mio-like; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR001680; WD40_rpt.
DR   InterPro; IPR037590; WDR24.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR46200; GATOR COMPLEX PROTEIN WDR24; 1.
DR   PANTHER; PTHR46200:SF1; GATOR COMPLEX PROTEIN WDR24; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; WD40 repeat-like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Metal-binding; Reference proteome; Repeat; Vacuole; WD repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1386
FT                   /note="Restriction of telomere capping protein 1"
FT                   /id="PRO_0000408783"
FT   REPEAT          180..227
FT                   /note="WD 1"
FT   REPEAT          234..278
FT                   /note="WD 2"
FT   REPEAT          290..329
FT                   /note="WD 3"
FT   REPEAT          382..428
FT                   /note="WD 4"
FT   REPEAT          1171..1212
FT                   /note="WD 5"
FT   ZN_FING         1338..1381
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          31..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          595..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          647..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1090..1157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..945
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1021
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1090..1149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1386 AA;  154884 MW;  E71A249386484993 CRC64;
     MPDPNELNAN QSSLSRFAFN IYGALNQAQS LEGNSSASPT PSMNPKQHNK SGTSSSNKEK
     LVYNCEREVS CISQFNHSLN GLVKNYEEDP LHHLIIGGKN YLKLLAMNND QTKIVHEVDI
     LESSKSIYSS SRTLSSNKLT SVNTIESQHD TIACELATGL ISVYKVQNNG KCKLVRKYSD
     HIRCVNSLDF INQSNVANSS SPYQLISGSQ DGTIKLWDLR SASNKPTLTI SSNSHSDPVR
     SCQYSPHSTV RNKLTILSVH DSGALCKYDL RSPNGGYQHN INVPERKWNF HTGPALSLNI
     HPEKEYVITG GRDQKVCIWN YGDSPTHQNK ISPDYMINTY GPVMKIRWSV YPDNIPSKTD
     TSSSQYQQIL ESKRYDDKTS SNERETISTM SSVGKNDPLF NYDFACSFLN EDPTISIYNL
     KRKYIPKEVI SSNSNKPFQN FMWAQNISHS RRVWTISKSN QFMSYDLDTA QSDPNIIKPL
     DNLTSVSMAW NSGLGDFCFV NQEKDEFESI SQLENDSFRS ESEEYDPEFA LASDGSGLAS
     NSGMEDHPTD ERSLKYRISS NSLDNSSIYN NHSKITVASI PIASNASNTP LSYQNPSFSN
     SVSPPFEQTT KPSLHRSATH NPMIQPPKPL SSILQNRSSV GIEALMEHGN NNSGSNSASV
     SGNHLRPTLN RNHSQSTQGS NVSLSSSIQG YQAPPPVSKR VISVNHPSPY IVPLSLPLPQ
     NDEHAFEILS NNYLITVNDG LSLIDVCLYN ANIAAGVNKF RDCQTWRVLA VSLEEDKFSL
     INYEENIRSQ FEKAETAITY GSLDTYENNS NTSNSKTQLN QTNDNRSILS ELDNFVGSFN
     SNSTSTSNYG GVHSEKDTSN NIELSNANNN GSRKASFSEI KPLSNLNSPS HLKDVLNQSR
     SNSNSPVISR SNSMLLKNRK TINTGSTRAE NHESAIDDDD GMGNAKTCEL NENDSQFGMK
     NSELKKHSSM SAIDSEAIDN DFPYNIESAK ASPIKIGSQH KHEKNTTSGS MSPQNKDSNH
     RGNIINYQRR LSLDPENSRK NSRNAFNYRH TNTWDLDDEN SNIIGNRAQW ATNSSLSSCG
     VSSYQPRIGS PNYSDQLHHS YSSTHSSPRP YYNSTTPGSS RRNSHISPVH GFHNKTSYAK
     QSPVSQKLMR DEQSRTELKD VQEQIEDLES IEETKVTSVN FGKSELTRAI TGNNTGSPNT
     LYKPWKTEYL LKEALEFASL QGDILLCSIL TILFYDYLKV GKDSHVFSKE QSLDWLSLYV
     EILHRKQLFS NAMYVVNMAP KELLPDLANL ASTEVNLRFF CCWCQKLLVN EKSKRKALNE
     DSFGYWYCDE CSTKQSNCIY CDEPCKGLNI VTSLSCGHRG HFGCLREWFI DQENIVCPGG
     CDEQVI
//
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