ID RTC1_CLAL4 Reviewed; 1158 AA.
AC C4Y5P7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=Restriction of telomere capping protein 1;
GN Name=RTC1; ORFNames=CLUG_03481;
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; CH408079; EEQ39353.1; -; Genomic_DNA.
DR RefSeq; XP_002616240.1; XM_002616194.1.
DR AlphaFoldDB; C4Y5P7; -.
DR STRING; 306902.C4Y5P7; -.
DR GeneID; 8496811; -.
DR KEGG; clu:CLUG_03481; -.
DR VEuPathDB; FungiDB:CLUG_03481; -.
DR HOGENOM; CLU_008512_0_0_1; -.
DR InParanoid; C4Y5P7; -.
DR OMA; GRDGKCC; -.
DR OrthoDB; 119005at2759; -.
DR Proteomes; UP000007703; 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 CDD; cd16488; mRING-H2-C3H3C2_Mio-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR InterPro; IPR037590; WDR24.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR46200; GATOR COMPLEX PROTEIN WDR24; 1.
DR PANTHER; PTHR46200:SF1; GATOR COMPLEX PROTEIN WDR24; 1.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
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..1158
FT /note="Restriction of telomere capping protein 1"
FT /id="PRO_0000408782"
FT REPEAT 80..119
FT /note="WD 1"
FT REPEAT 125..163
FT /note="WD 2"
FT REPEAT 170..214
FT /note="WD 3"
FT REPEAT 233..272
FT /note="WD 4"
FT REPEAT 293..342
FT /note="WD 5"
FT ZN_FING 1110..1153
FT /note="RING-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 421..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..526
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..768
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..801
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..909
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1158 AA; 127059 MW; F66167EB28E9EBC2 CRC64;
MVSSLARYAF NIYGDTRPRE RPRRLEYPCE RELTCLSQLQ RPGQPPVVIL GGKNCLRMLA
LNADNTAVVA DSSIVDSART PQKLFSVNTL KCTSDLVACG LANGTVQVYQ VTSGGKNRLA
YKLQDHKRVV NSLDFVDDSV LVSGSQDGTV KVWDLRTFSP RPVMQLAASH HSDPVRSCQA
SAHCRVRGKT TVLSVHDSGA LCKFDLRATA GVGAGVGAGA GAGALLPERK WTFHSGPALS
LHIHPDAEYV LTGGRDRKIC VWHYGEAGSH SVAPLSIVNT YGPVMKVRWC TVAAQDPVEP
TLDLPDAPDP SCLYNYDFAC SYLNDDATIS VYNLRRRYIP KAVVASPMRK PVQNFVWVAS
RTDRRLFSIS KANVLVAHDL DVNDVDITRP LDNMPAVATA WRPGYANVSI VSQHKNDFEL
GDPVADSRDT SFDDTRDDLS HSRSTPPKER PPIVRQSTQF TVASLKSQSP VLHQRGMDSS
VRDSSARAMD LSGRGLDLPP PVRPSLPRNP SQSTQGSQSS GAAHSKSLPH APSPYVAALS
VPIPLADDTV FDILAAEYHI SVPDGFSLLD VCQMNARVAA SVSRYRDCEI WRMLGVSLEQ
EFEEHQFDDP RFDGQFEDQH TDPQNASGSQ HSEKDIDTKS VSSYLGNFVG SFNSNSTSTT
NYGGPHRSDS ATSMNKALFG SKEREGKEGK DIKHGKREKE IEQGLESPKE LNPLSTRRKD
SDSKANNADS SALDKPGDKS LDRSALDRSA PTSFRNKSLL QTSDGETPKD NNLSDEIHAY
EPRNNLSTKV SLSTMSSQKS KAIDIKAPRR YSNNAMSASM SPEIFASSES PLKHIAKLSP
SRSQTGHSWS IPSSSHDLDD ENMPASVSGS LASSGYMGGP DSRSGITGTS FHSNPRSHPS
FSSHRSSLTS GRSSFVTNRS GFYSSQVQPA PQLLEKVEEF SISSAEPKTS ELTKAMRKKK
FSYEELESSE ANEKPWSLIN LLEKAVIYAR DQGDLVMCCT LILLFHDLFK KIFSNRILSD
NACLECLALY VDTLRGKCLF TTAVNVVKEA PSSLNYKLAV YASKDVDMRY YCCWCEKLLV
NETSKAKFGP NSENFGYWYC DSCSRRQSNC IYCGEPCRGL TVVVSLNCGH RGHFGCLQEW
FLDEQSTGCP GGCEYVMD
//
