RTC1_YEAS7
ID RTC1_YEAS7 Reviewed; 1335 AA.
AC A6ZN74;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Restriction of telomere capping protein 1;
GN Name=RTC1; ORFNames=SCY_4942;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(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; AAFW02000030; EDN63739.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZN74; -.
DR SMR; A6ZN74; -.
DR EnsemblFungi; EDN63739; EDN63739; SCY_4942.
DR HOGENOM; CLU_008512_0_0_1; -.
DR Proteomes; UP000007060; 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..1335
FT /note="Restriction of telomere capping protein 1"
FT /id="PRO_0000408791"
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..1335
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..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1037
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 786..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1030
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08281"
FT MOD_RES 1074
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 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08281"
FT MOD_RES 1117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08281"
FT MOD_RES 1127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08281"
SQ SEQUENCE 1335 AA; 148727 MW; 268B0AF6D5EEC490 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 NNDDDDDDDK IIESHLLKKY NFPENNTWAT
LMNEKVNNKK SKRNSSSSRE FDEKDVRSSI SSISASRQSH DRSRKIDKNV EAELQEKIQT
LVDLISIATH NASVYLSIDD LTNFKIWILI RDSLLWDLKW MTSSQISSDN ASNMDANESS
DFEAGENLKT GKEFPEEDGA GTSGAESLVE ERPQAFRANS DEPSDAEKKP VSKLKEQLKN
TEIIPYAQPN EDSDEVLTKL KELQNQRLES RTKMGETVSD DVIIEEDEHE HQEEEQPHDS
PTKSAQFHAS PIAKSIPILQ KREHRKSFID TFMLHSPNGY NGDTDIGNED DNISPRFTYN
SVSPRSKVSS LQSYATTTSQ LETFKKLSSH TAPIIGSPRH APSRPDSIGR EQLSSSLTKK
LAKCKKIIAD PPWDTKKLIK QLYNQATETG NVVLTVNILF LFQTIYQITE IDIAKDAIAH
FLLLLHRYEL FGIAADVLKY CPFEDIMGSE GDQSSIRLFC ERCGELITNE SSKEKLRAEA
QQTGNKKIMD KFGYWYCDSC KKKNTSCVLC ERPLKKLTMV ILPCGHEGHF QCIQEWFLDE
NEQECPGGCP GVAFI
