ID   RTC1_CANDC              Reviewed;        1098 AA.
AC   B9WN49;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Restriction of telomere capping protein 1;
GN   Name=RTC1; ORFNames=CD36_35350;
OS   Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS   NRRL Y-17841) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=573826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX   PubMed=19745113; DOI=10.1101/gr.097501.109;
RA   Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA   Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA   de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA   Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA   Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT   "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT   Candida albicans.";
RL   Genome Res. 19:2231-2244(2009).
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; FM992695; CAX40516.1; -; Genomic_DNA.
DR   RefSeq; XP_002422508.1; XM_002422463.1.
DR   AlphaFoldDB; B9WN49; -.
DR   STRING; 42374.XP_002422508.1; -.
DR   PRIDE; B9WN49; -.
DR   EnsemblFungi; CAX40516; CAX40516; CD36_35350.
DR   GeneID; 8050233; -.
DR   KEGG; cdu:CD36_35350; -.
DR   CGD; CAL0000159868; Cd36_35350.
DR   VEuPathDB; FungiDB:CD36_35350; -.
DR   eggNOG; KOG0269; Eukaryota.
DR   HOGENOM; CLU_008512_0_0_1; -.
DR   OrthoDB; 590848at2759; -.
DR   Proteomes; UP000002605; Chromosome R.
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   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   InterPro; IPR037590; WDR24.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR46200; PTHR46200; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 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; Repeat; Vacuole; WD repeat; Zinc; Zinc-finger.
FT   CHAIN           1..1098
FT                   /note="Restriction of telomere capping protein 1"
FT                   /id="PRO_0000408779"
FT   REPEAT          131..170
FT                   /note="WD 1"
FT   REPEAT          176..215
FT                   /note="WD 2"
FT   REPEAT          222..266
FT                   /note="WD 3"
FT   REPEAT          275..314
FT                   /note="WD 4"
FT   REPEAT          367..417
FT                   /note="WD 5"
FT   REPEAT          432..473
FT                   /note="WD 6"
FT   REPEAT          635..673
FT                   /note="WD 7"
FT   REPEAT          891..934
FT                   /note="WD 8"
FT   ZN_FING         1050..1093
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          26..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..843
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        754..778
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        779..805
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1098 AA;  122339 MW;  60137416A83F61D1 CRC64;
     MSQPNSQGQS NLAKFAFNIY GTLSTNSSTP QSHEISPSSS LGSSRSNKQT NQYSSQETNN
     NRLSYYCEKE IMSLSQLNYP LSIGGYNGDL QHHVVIGGKN YLRLLCVSET QQRIISDINL
     LESKSIYNSR ATNKLINVNT IKTYADTIAA GLSNGVVLIY RVSPNGQSKV VGKYSDHSRT
     INSLDFIDSE NQLLSGSQDG TIKLWDLRSS STKPVMTIQA NLHSDPIRAC QYSRHSAVRN
     KICVLSVHDS GALCKFDLRT KNGGKVYSPE KKWNLHTGPV LSLHIHPEKE YVVTGGRDKR
     ISVFNYGDGQ SRNTPDSLIN TYGPVVKVRW STYANTKEIV EEFEENQQPN PNPLYNYDIA
     CSYLNDDPTI AIYNLGRKFI PKQIIHSKKP VQNFIWAQNN SKSRKIWTLS KPNSFNSYNL
     YGLDDSDVSR PIEDLSNVAM TWDNNNDFCA VSQARYDYDL ESFGNAINET YEDNYDTERN
     CSLDNEEFVH SQANSLTASP IEKPQLTRSM TYNPVQSFST FSPAPVARTA TGFLQNEPVT
     PSSSSSIPNM HLSSSRPKLT RNTSQTTQDS SSSQLSSVIP PPSSSQTYSS PQYKRNQSSR
     CLNTPAYVIP VSIPVPSNDE YVFQKLSSES LVNIPDGFTL VDVCLINASV AASVNNNRTS
     QVWKLLAVSI QEEFESGSKL RRILGPETET VSKIPQEVHE SLAKTNEALS SDIAKSNSVS
     SVLGNFVESF KSTSTSGSQF GKQNDKDDRK LQNKNSSGNL MDMINKASRN SSFSTTSFRL
     KEQERREHEL RNTQNFRDEN EKVSTHSKSA PISISSHPED LDDENMSATN SAGLKSSPPS
     VGVSIPSTRT FSSSLASSPK SIRIMNGVNS NVARSQPSPP VQTWLKQRNF DVSNGVTMMG
     TSGLSLALKR NKTNEEGCEF VKVWKFKSLL RKSLDYAALQ GDIIFCSTVA LLFYDIVPDV
     ISQFECLEWL SIYIEILQRK RLFVNAINVI KCATADIQEK LQKLYCSDLS LRFYCSRCQA
     LLVNDKSKFS GKGEFGYWYC DECSRLQSQC VYCNEPCKGL AVTVGLKCGH QGHFGCLKEW
     FIEDQNTECP GGCDYQVI