ID   RTC1_PICST              Reviewed;        1105 AA.
AC   A3GIA4;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Restriction of telomere capping protein 1;
GN   Name=RTC1; ORFNames=PICST_53206;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
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; AAVQ01000002; EAZ63199.2; -; Genomic_DNA.
DR   RefSeq; XP_001387222.2; XM_001387185.1.
DR   AlphaFoldDB; A3GIA4; -.
DR   SMR; A3GIA4; -.
DR   STRING; 4924.XP_001387222.2; -.
DR   EnsemblFungi; EAZ63199; EAZ63199; PICST_53206.
DR   GeneID; 4852003; -.
DR   KEGG; pic:PICST_53206; -.
DR   eggNOG; KOG0269; Eukaryota.
DR   HOGENOM; CLU_008512_0_0_1; -.
DR   InParanoid; A3GIA4; -.
DR   OMA; GGRDGKC; -.
DR   OrthoDB; 590848at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
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   Gene3D; 3.30.40.10; -; 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   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46200; PTHR46200; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 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..1105
FT                   /note="Restriction of telomere capping protein 1"
FT                   /id="PRO_0000408787"
FT   REPEAT          135..172
FT                   /note="WD 1"
FT   REPEAT          178..223
FT                   /note="WD 2"
FT   REPEAT          230..274
FT                   /note="WD 3"
FT   REPEAT          280..319
FT                   /note="WD 4"
FT   REPEAT          377..420
FT                   /note="WD 5"
FT   REPEAT          560..601
FT                   /note="WD 6"
FT   REPEAT          917..959
FT                   /note="WD 7"
FT   ZN_FING         1057..1100
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          481..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          692..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..754
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1105 AA;  123028 MW;  B7F02BDB7EC41C58 CRC64;
     MSSNANSQHS TLAKFAFNIY GSLNHATPSY EGSASPSSSY SSSRSKTNEP YNYRFNKLVY
     NCEREVTTLS QLNYPLSLSN TFQSDQNLSH HVIIGGRNYL KLLALNEDQS RIVQDINVLD
     QSSIYTHNSR VPSTNKLNNI NTVKAQSDTI GCGLSNGLIT VYKVGSNGKC RLIHKFSDHK
     RCINSLDYVG IRNLYDAPTQ MISGSQDGSI KLWDMRSSSP RPMLTISSGS HSDPIRSCQY
     SPHSQGRNKL VVLSVHDSGA LCKFDLRLSN GHGPERKWNI HTGPALSLHI HPEKEYVVTG
     GRDQKICVFN YGDSQISNRI TPDEMINTYG PVMKVRWCLY PDASTSQFGE PLDTFQQSND
     FNSSSLYSYD LACSYLNDDS TVAIYNLNRK FIPKEVITTS SNKPIQNFIW ANNPGSSRKI
     WTITKSNVFS SYDLDMHDSL LESEISKPLD ELANVTVDWN NGFGDLCLAN QEKYEFEITE
     VESQASDNDM GDIDTEYSSR YERSNSNSVI DESSLIGSSS AEKPPLFRSS THYSMHMAKS
     PSPVPRRGST SFAAHSESQP NLSNMQGLSM SRPKLTRNLS QATEDSSISI GSAPQSNIHL
     KSKRSFQVSY ASPYLVPVSL PLSLNDENVF EILSNNYLIS IPDGFTLVDV CLLNASVAAS
     VQRFRECQIW RVLAVSLEED YVQIDNTTFL SDPELEHNET NQDEKIDDQK DAKSISSDLG
     NFVGSYNSNS TSTTNYGGLG SLSAKDTTKA NNSNNLMDMI NRSRVNSMNH LQSISPSGSH
     TFIRNAIHEN KSNENAIVDD DETDAAVHGT EGRIGTSHVS EDLDNENLNI LNNAVLNSSP
     NSAMTTPHPQ SNSPNYSNFF SLPKLSSTFM SPIYDEFAEK QEQPRSLKAE SLLNNDVSDR
     TTTKSELTKA IKEEVDNSSG APLKKAWKSS SLLEKALAHA SNEGDIILCS TLSLLFYDSF
     KQVIPQSSCL DWLGLYIEIL QRKRLFVNAI HVVNNAPDDV RSKLKNLTSG DVDLRFFCCW
     CQKLLVNEKS KEKLKNDVNA DFGYWYCDEC SQKQSNCIYC NEPCKGLTVV VSLKCGHRGH
     FGCLREWFIE DENNECPGGC DYSVV