RTC1_ZYGRC
ID RTC1_ZYGRC Reviewed; 1273 AA.
AC C5DSV0;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
DE RecName: Full=Restriction of telomere capping protein 1;
GN Name=RTC1; OrderedLocusNames=ZYRO0C03190g;
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(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; CU928175; CAR26861.1; -; Genomic_DNA.
DR RefSeq; XP_002495794.1; XM_002495749.1.
DR AlphaFoldDB; C5DSV0; -.
DR STRING; 559307.C5DSV0; -.
DR EnsemblFungi; CAR26861; CAR26861; ZYRO0C03190g.
DR GeneID; 8202989; -.
DR KEGG; zro:ZYRO0C03190g; -.
DR HOGENOM; CLU_008512_0_0_1; -.
DR InParanoid; C5DSV0; -.
DR Proteomes; UP000008536; Chromosome C.
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; -; 2.
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; 2.
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..1273
FT /note="Restriction of telomere capping protein 1"
FT /id="PRO_0000408793"
FT REPEAT 119..164
FT /note="WD 1"
FT REPEAT 166..207
FT /note="WD 2"
FT REPEAT 215..255
FT /note="WD 3"
FT REPEAT 327..366
FT /note="WD 4"
FT REPEAT 448..486
FT /note="WD 5"
FT REPEAT 639..679
FT /note="WD 6"
FT REPEAT 784..824
FT /note="WD 7"
FT REPEAT 1058..1101
FT /note="WD 8"
FT ZN_FING 1225..1267
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 69..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..861
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 899..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1273 AA; 140762 MW; E36A7D1C24EB7EF6 CRC64;
MNNRPIPRNQ ASSSLGRNDL KPGLFGRSSF RVQHYSGTNG ISPIGSSPRT KISPRYSFAS
SFATSESSLR ESSYFDERPP VQDTGVPKSS GLYYSRASPK ELSSIDRIND SSFNGIVCAG
KTHLGLYKFS PQDKSIDCMH DFVSAGNDGN RGSNVQMGLG KRSKRTKLST IADVKAGFHN
HKNYVAICSN STVLSIYDIN KTGSIDNPLV TNCSQHVRSV NSFDFNMVQT NLIISGGQDS
CIKIWDLRSS RSRTLSRADV NINTASDSIR DVKWMPHPTA CRSASQNDLR SGVGGAAGYK
FASIHDSGLL LKFDLRQPNQ VEKRINAHSG PGLCLNWHPY QDYISTGGRD GKCCLWYVGD
GKPGTDFLQA GNTSVNTPHS MTSNLPTNLS VVPDMTINCG FPVTKLKVRP CYEKNVLNSL
VSMSSMAEDF GVSIYSLARK YIPKYNLSTS SASLGFVWWD DNLIFNIDKD NRINGWYLDR
EPTVLDNMPK IVTRWRDIEG NGLLFIDQDR GGYQVNDEVP ANIEESKKPP NQRVSINSLS
GTAGGGNSGG GSNSGMIGSI KKGISQTGLT SFAGERPALS KTGLNFSNKS LATQSMNNSH
SNSFSSYAGA GPGPLNEVAD YSGIESPFLM TIDLPYILNN MRVSQLPPER KSLYSPEVQA
IRESPVKVFK FLAKELEFSY MQEGRSGEMK NATQLSNVNE DTTKKDLMVK FGISEKSTWT
ALVNKKNEAV EAISKKSVST KEGSESLIES DGESSAKSHE SDDNSSDADK KENAKDGTMH
VQEKIDILLE LIPICGHNAS VYSYIDDLPN FKIWILIRDS LLWDLERLSV EYPDEKLPET
QSTDQIGQPI TMGNDDSLAS DTRSYMTSDL NYFVEEHPRA LRSDSDEPKD HKKPLSGLKS
QLTKIQETEA SIDDSLNPPK MLKKPDNPIK QEQIGSRLND DSDSAVLEDD DNEEKSDFDT
QIKGIPITNK RQPRQSFIDT YMGGLKSPIG SSNANNEFFM GRVGHSLGHS SPGSKGSPMA
SLNNGEFTYP GFKRMSSRND RRSSGSLFLS PLKRRESSTA EFFNKSPMRP LSPVAPVSSF
KSNPTEFLPP WNTRRLLKQI FKQAVEMGNI LLVVNILFLF QNLYQLTSTE VLKNTLAQFI
KILHKHELFE LSAAILKCSP WEVVINADGG QSLVPIFCDK CGKLITNEPS KEKFTLEAQE
KGNSMPLQRF GYWYCDSCKK PNTLCVFCER PIKTLAIGLL ECGHEGHFQC LQSWFLDEGM
AECPGGCMNQ IRL