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RTC1_CANAW
ID   RTC1_CANAW              Reviewed;        1088 AA.
AC   C4YN69;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Restriction of telomere capping protein 1;
GN   Name=RTC1; ORFNames=CAWG_02309;
OS   Candida albicans (strain WO-1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294748;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WO-1;
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; CM000309; EEQ44050.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4YN69; -.
DR   SMR; C4YN69; -.
DR   STRING; 5476.C4YN69; -.
DR   EnsemblFungi; EEQ44050; EEQ44050; CAWG_02309.
DR   VEuPathDB; FungiDB:CAWG_02309; -.
DR   HOGENOM; CLU_008512_0_0_1; -.
DR   OMA; GGRDGKC; -.
DR   Proteomes; UP000001429; Chromosome R.
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   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   PANTHER; PTHR46200; PTHR46200; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 4.
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; Repeat; Vacuole; WD repeat; Zinc; Zinc-finger.
FT   CHAIN           1..1088
FT                   /note="Restriction of telomere capping protein 1"
FT                   /id="PRO_0000408778"
FT   REPEAT          131..170
FT                   /note="WD 1"
FT   REPEAT          176..215
FT                   /note="WD 2"
FT   REPEAT          222..266
FT                   /note="WD 3"
FT   REPEAT          275..314
FT                   /note="WD 4"
FT   REPEAT          367..417
FT                   /note="WD 5"
FT   REPEAT          432..473
FT                   /note="WD 6"
FT   REPEAT          502..546
FT                   /note="WD 7"
FT   REPEAT          631..671
FT                   /note="WD 8"
FT   ZN_FING         1040..1083
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          26..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..751
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          764..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..871
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        709..731
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..795
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        815..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  120974 MW;  13C5D1E1948A7191 CRC64;
     MSQSNSHGQS NLAKFAFNIY GTLSTNSSTP QSHEISPSSS LSSSRSKKQT SQYNTQDTNN
     NRLSYYCDKE IISLSQLNCS LSIGGYSGDL QHHVVIGGKN YLRLLCVSES QQRIISGINL
     LESKSIYNSR APNKLINVNT IKTFADTIAT GLSNGVVSIY KISPNGQSKV TGKYSDHNRT
     INSLDFIESE NQLLSGSQDG TIKLWDLRSS STKPVMTVQA NLHSDPIRAC QYSPHSAVRN
     KICVLSVHDS GALCKFDLRT KSGGKVYSPE KKWNLHTGPA LSLHIHPEKE LVVTGGRDKR
     ISIFNYGERQ SRNTPQNLIN TYGPVVKVRW STYTNTEETA EEFEENKQAK PNTLYNYDIA
     CSYLNDDPTI TIYNLGRKFI PKQIIHSKKP IQNFIWARNE TRSRKIWTIS KSSTFSSYNL
     DRLEDSDVSR PIEDLNNIAM TWNNNNDFCA VSQARYDYDL ETYENGINET TEENFDAERN
     YSLGNEELIH SQANSLTASP VDKPQLTRSL TFNPASSFST FSPVLVARAA TGFLQNDSAT
     SSSSIPNMQV SSSRPKLTRN TSQTTQDSSS SQFASVLPPP SASQTYSSPQ YKKNNPPRFM
     NNPAYVIPVS IPIPANDEYV FRKLSSESLV STPDGFTLVD VCLLNASVAA SVGNNRTSQI
     WRLLAVSIQE EFESGIEPRR IYAFQPEAIN KLPQDVQETS TNANDTLHAE TTNSNFVESF
     KSTSTSGSQF GKQSDKDERK LQSKNSSGNL MDMINKANRT NSFSATSFKF KEQERKEDES
     QKAQSIKDEN ERASIHSKSA PISISSHPED LDDENMGSNN SAALKFSPPS VGVSIPSTRI
     ISSSLASSPK SVRGPSGVKS HISRSRPSPP VQTWLKQKNL EVSNGSAMAS TSGLSLTLKR
     NKTNEEGDQL TKAWKFKSLL RKSLDYATLQ GDIIFCSTAA LLFYDIVPEI ISQFECLEWL
     GIYIEVLQRK RLFVNAINVI KCATADIQEK LQKLYCQDLS LRFYCSNCQA LLVNEKSKFS
     GKGEFGYWYC DECSKLQSQC VYCNEPCKGL AVTVGLKCGH HGHFGCLKEW FIEDQNTECP
     GGCGYQII
 
 
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