ID   RTC1_YEAS2              Reviewed;        1342 AA.
AC   C7GV13;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Restriction of telomere capping protein 1;
GN   Name=RTC1; ORFNames=C1Q_04279;
OS   Saccharomyces cerevisiae (strain JAY291) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=574961;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAY291;
RX   PubMed=19812109; DOI=10.1101/gr.091777.109;
RA   Argueso J.L., Carazzolle M.F., Mieczkowski P.A., Duarte F.M., Netto O.V.C.,
RA   Missawa S.K., Galzerani F., Costa G.G.L., Vidal R.O., Noronha M.F.,
RA   Dominska M., Andrietta M.G.S., Andrietta S.R., Cunha A.F., Gomes L.H.,
RA   Tavares F.C.A., Alcarde A.R., Dietrich F.S., McCusker J.H., Petes T.D.,
RA   Pereira G.A.G.;
RT   "Genome structure of a Saccharomyces cerevisiae strain widely used in
RT   bioethanol production.";
RL   Genome Res. 19:2258-2270(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACFL01000329; EEU05348.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7GV13; -.
DR   SMR; C7GV13; -.
DR   IntAct; C7GV13; 1.
DR   Proteomes; UP000008073; 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   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; 2.
DR   SMART; SM00320; WD40; 2.
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; Phosphoprotein; Repeat; Vacuole; WD repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1342
FT                   /note="Restriction of telomere capping protein 1"
FT                   /id="PRO_0000408790"
FT   REPEAT          207..248
FT                   /note="WD 1"
FT   REPEAT          256..296
FT                   /note="WD 2"
FT   REPEAT          305..342
FT                   /note="WD 3"
FT   REPEAT          367..406
FT                   /note="WD 4"
FT   REPEAT          439..486
FT                   /note="WD 5"
FT   REPEAT          489..527
FT                   /note="WD 6"
FT   REPEAT          844..884
FT                   /note="WD 7"
FT   REPEAT          1130..1170
FT                   /note="WD 8"
FT   REPEAT          1217..1256
FT                   /note="WD 9"
FT   ZN_FING         1294..1336
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          942..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1014..1047
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        559..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        630..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..766
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        793..814
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1037
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08281"
FT   MOD_RES         1081
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08281"
FT   MOD_RES         1088
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08281"
FT   MOD_RES         1090
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08281"
FT   MOD_RES         1124
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08281"
FT   MOD_RES         1134
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08281"
SQ   SEQUENCE   1342 AA;  149461 MW;  F7AF897A6B3C9CEB CRC64;
     MSLSPHVENA SIPKGSTPIP KNRNVSSIGK GEFLGSSSSN NSSFRMNHYS NSGQPSVLDS
     IRRPNLTPTF SYSNGVYMPE SHRTSSFNDS YLPYDKNPYA KTTGSMSNKS NMKIKTKKNA
     INTNTRKSSG LIYTTKVDKE LSSIDKVNDP NINGLVCAGK THLGLYKFSP SDRSIKCVHD
     FITPNSNTST RGTTSLLPKL SKRTRQNKFS TIADVKTGFN NYKNCIAVCN NSTAISIYDL
     NKSSSIDNPL ITSLCEHTRS INSFDFNMVE SNLIISGGQD SCVKIWDLRS NKSKSSNRSD
     ISINTASDSI RDVKWMPGYN FASKNDQGSS TYGNLKSGYK FASIHDSGYL LKFDLRQPAQ
     YEKKLNAHTG PGLCLNWHPN QEYIATGGRD GKCCLWFVGD NANAAENTVL NYGNSPSLHA
     PNTSLNNSGS LAFPKLTINT GYPVTKLKFK PAYSSNIYNS LLGISSMGDE AEVRIYSLAR
     KYIPKHVLLS ETPSLGLVWW DENLIFNIDK GTRINGWDIN KEPTVLENLS KNTTTWRDLD
     GNGLLSVDQE IGSYEVVEPE LQPTSSTTCK KHPGTIKNPK NGNPENQGII GGIKKGFSHT
     GLTSFTPERP PTLKAGPTFS SKSLTLASGA SSFNSSSASL TSLTPQTENR EEIAIEPPCI
     ITLDIPQIFN NIRLTKIAHS RKKNVISESS SMKNSPVEKF KYLARQLKFS YIREHNVSDS
     ADTAYKNDIE NIDVVKNATE THGDNTTTTN NNDDGDDDDD DDDDDDKIIE SHLLKKYNFP
     ENNTWATLMN EKVNNKKSKR NSSSSREFDE KDVRSSISSI SASRQSHDRS RKIDKNVEAE
     LQEKIQTLVD LISIATHNAS VYLSIDDLTN FKIWILIRDS LLWDLKWMTS SQISSDNASN
     MDANESSDFE AGENLKTGKE FPEEDGAGTS GAESLVEERP QAFRANSDEP SDAEKKPVSK
     LKEQLKNTEI IPYAQPNEDS DEVLTKLKEL QNQRLESRTK MGETVSDDVI IEEDEHEHQE
     EEQPHDSPTK SAQFHASPIA KSIPILQKRE HRKSFIDTFM LHSPNGYNGD TDIGNEDDNI
     SPRFTYNSVS PRSKVSSLQS YATTTSQLET FKKLSSHTAP IIGSPRHAPS RPDSIGREQL
     SSSLTKKLAK CKKIIADPPW DTKKLIKQLY NQATETGNVV LTVNILFLFQ TIYQITEIDI
     AKDAIAHFLL LLHRYELFGI AADVLKYCPF EDIMGSEGDQ SSIRLFCERC GELITNESSK
     EKLRAEAQQT GNKKIMDKFG YWYCDSCKKK NTSCVLCERP LKKLTMVILP CGHEGHFQCI
     QEWFLDENEQ ECPGGCPGVA FI