ID RTC1_CANTT Reviewed; 1110 AA.
AC C5MIB1;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Restriction of telomere capping protein 1;
GN Name=RTC1; ORFNames=CTRG_05804;
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; GG692404; EER30405.1; -; Genomic_DNA.
DR RefSeq; XP_002546326.1; XM_002546280.1.
DR AlphaFoldDB; C5MIB1; -.
DR SMR; C5MIB1; -.
DR STRING; 294747.C5MIB1; -.
DR EnsemblFungi; CTRG_05804-t43_1; CTRG_05804-t43_1-p1; CTRG_05804.
DR GeneID; 8296728; -.
DR KEGG; ctp:CTRG_05804; -.
DR VEuPathDB; FungiDB:CTRG_05804; -.
DR eggNOG; KOG0269; Eukaryota.
DR HOGENOM; CLU_008512_0_0_1; -.
DR OrthoDB; 119005at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
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; 1.
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..1110
FT /note="Restriction of telomere capping protein 1"
FT /id="PRO_0000408781"
FT REPEAT 132..171
FT /note="WD 1"
FT REPEAT 177..216
FT /note="WD 2"
FT REPEAT 223..267
FT /note="WD 3"
FT REPEAT 277..316
FT /note="WD 4"
FT REPEAT 348..390
FT /note="WD 5"
FT REPEAT 393..426
FT /note="WD 6"
FT REPEAT 439..483
FT /note="WD 7"
FT REPEAT 637..675
FT /note="WD 8"
FT REPEAT 860..906
FT /note="WD 9"
FT ZN_FING 1062..1105
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 27..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..575
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..817
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 123250 MW; 23F7940CCC518E81 CRC64;
MSSSTNGHSQ SNFAKFAFNI YGTLSTTSSS TPQSHEISPS PSSSLSSSRS RRNKQSFRAA
TGHRLTYQCD KETISLSQLN YPLQVGGYGT ELHSIVIGGK NYLRLLCISE SQQRIIDDIN
LLESKSIYNS RVGSKLININ TIKTYESTIA TGLSNGVVSV YKISPNGQGK QTGRFSDHKR
TINSLDFIES ENQLLSGSQD GTIKLWDLRS SSSKPSITIQ ASMRSDPIRA CQYSPHSSVK
NKMCVLSVHD SGALCKFDLR STGGNGNIYS PEKKWNLHTG PALSLHIHPE KEYVITGGRD
QRISVFNYGE GQSNSSTPEN TIITYGPVLK VRWSSYSNIS QSGDEFEEAQ SSLSPSKINP
LYNYDIACSY LNDDPTVAIY NLSRKYVPKQ IIHSKKPIQN FIWARNGHRD RNIWTLTKSN
TFNSYNLDQI DEYDVSRPLD DLNNVAVAWD NNGNFSMANQ DKYDFELDDN DIYDRPEGSS
EAEVASHGMD PEESGNAIHF HNSATTSPVE KAALARSYTH NPMSAIQLPT KSPLPIGRNG
TGFLGHDMSL PNISTRPKLT RNTSQTTQDS SVSYGSAYPI PQSANSNTTL HMKRNIISNS
TKSSNTSAYV IPVVLPIVSN DEFVFKKLSS EYLVKLPDGF TMIDVCLLNA STAASVNSNR
TCQVWRLLAV SLQEHFDSQK APMTIEELEK QQMEQNENEE GVPNATVESA TDSMPAKSVS
SVLGNFVESY KTNSSFGTGS QINKPGKSVK SRTSSGVNLM DKINLASRTS SFSKTSFKFK
EKEGVDEDGV PEDKEKQERG KAEDQETEND KKSIHSNQEP IVIRTTRHSK VEDLDDENLN
IANSMAMKSS PTSVGISLPS SHTFSSSIAS SPQPIRGQIP PKQQLATTRE SPVHNWLDQK
KNELFRGRNV VPAISGLSLA LKSSNNGDEK LLTRAWKFKN LLRKSLDYAM LQGDVIFCST
AAILFYEFAE DTISEYEYLE WVSLYIDILQ KKKLFVTAIN ILNSTAGSIK SKLQKIYSVD
LDLRFYCSNC ETLLVNEKSQ MSQKGEFGYW YCDECNKLQS KCVYCNEPCK GLAVVVGLKC
GHQGHFGCLK EWFIQDENME CPGGCDYQIL
//
