RTC1_YEAS8
ID RTC1_YEAS8 Reviewed; 1342 AA.
AC C8ZHH9;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=Restriction of telomere capping protein 1;
GN Name=RTC1; ORFNames=EC1118_1O4_0265g;
OS Saccharomyces cerevisiae (strain Lalvin EC1118 / Prise de mousse) (Baker's
OS yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=643680;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lalvin EC1118 / Prise de mousse;
RX PubMed=19805302; DOI=10.1073/pnas.0904673106;
RA Novo M., Bigey F., Beyne E., Galeote V., Gavory F., Mallet S., Cambon B.,
RA Legras J.-L., Wincker P., Casaregola S., Dequin S.;
RT "Eukaryote-to-eukaryote gene transfer events revealed by the genome
RT sequence of the wine yeast Saccharomyces cerevisiae EC1118.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:16333-16338(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; FN394216; CAY86154.1; -; Genomic_DNA.
DR AlphaFoldDB; C8ZHH9; -.
DR SMR; C8ZHH9; -.
DR EnsemblFungi; CAY86154; CAY86154; EC1118_1O4_0265g.
DR HOGENOM; CLU_008512_0_0_1; -.
DR Proteomes; UP000000286; Chromosome XV, Scaffold EC1118_1O4.
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_0000408792"
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..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1043
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; 149503 MW; B1F8FC43DC468028 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 TKSLTLASGA 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 DEVLIKLKEL QNQRLESRTK MGETVSDDVI IEEDEHEHQE
EEQPHDSPTK SAQFHASPIA KSIPILQKRE HRKSFIDTFM LHSPNGYNGD TDIGNEDDNI
SLRFTYNSVS 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