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 27-MAR-2024, entry version 79.
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 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; 119005at2759; -.
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 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; IPR049566; WDR59_RTC1-like_RING_Znf.
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 Pfam; PF17120; zf-RING_16; 1.
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; 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
//
