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RTC1_ASHGO
ID   RTC1_ASHGO              Reviewed;        1361 AA.
AC   Q75AV6;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Restriction of telomere capping protein 1;
GN   Name=RTC1; OrderedLocusNames=ADL186C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016817; AAS51734.2; -; Genomic_DNA.
DR   RefSeq; NP_983910.2; NM_209263.2.
DR   AlphaFoldDB; Q75AV6; -.
DR   STRING; 33169.AAS51734; -.
DR   EnsemblFungi; AAS51734; AAS51734; AGOS_ADL186C.
DR   GeneID; 4620052; -.
DR   KEGG; ago:AGOS_ADL186C; -.
DR   eggNOG; KOG0269; Eukaryota.
DR   HOGENOM; CLU_008512_0_0_1; -.
DR   InParanoid; Q75AV6; -.
DR   OMA; GGRDGKC; -.
DR   Proteomes; UP000000591; Chromosome IV.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0061700; C:GATOR2 complex; IBA:GO_Central.
DR   GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034198; P:cellular response to amino acid starvation; IBA:GO_Central.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IBA:GO_Central.
DR   GO; GO:1904263; P:positive regulation of TORC1 signaling; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 2.
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; 2.
DR   SMART; SM00320; WD40; 4.
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; 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..1361
FT                   /note="Restriction of telomere capping protein 1"
FT                   /id="PRO_0000408776"
FT   REPEAT          180..221
FT                   /note="WD 1"
FT   REPEAT          229..269
FT                   /note="WD 2"
FT   REPEAT          277..315
FT                   /note="WD 3"
FT   REPEAT          337..376
FT                   /note="WD 4"
FT   REPEAT          405..452
FT                   /note="WD 5"
FT   REPEAT          455..493
FT                   /note="WD 6"
FT   REPEAT          849..890
FT                   /note="WD 7"
FT   REPEAT          1146..1192
FT                   /note="WD 8"
FT   REPEAT          1240..1278
FT                   /note="WD 9"
FT   ZN_FING         1314..1356
FT                   /note="RING-type; degenerate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          896..916
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..982
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1091..1113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..593
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..982
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1361 AA;  150385 MW;  D6248E4EEEFBB62E CRC64;
     MGARRESGLH SFLNRKTPPT ADMQQGSGGT RPQPFSRFTY GSKSAQSSGG MGGQVACSPK
     GRGSQRSLLS SNFPFMESVF EDRTAAPQRT PTPRDERSEY FGEAEGSSGL RSSLQCNREL
     ASLDKINDAQ ARMVVVAGKS HLGLYKFDEA YRMQQVHDYM TPGSLGGGTK FSSSMRRNMR
     KISTISDVKA GFHHHKNYIA ICGTSTSVSI YDINRASAKD SPLITTLSEH SRSINSVDFN
     MGQTHLLISG GQDGCIKVWD LRSHSYKVNR SDLNFNSGSD SVRDVKWMPT YDFASLGADT
     SLCSSGRSNK FASVHDSGLL LTFDMRQPNQ VERKINAHSG PGLCMHWHPH MDYIISGGRD
     GKCALWYVGD KVNSMVSVPQ GHNSATSYSI NTAPITTGYL ETVINTSHPV SKLKFRPKYV
     HNMLNSLIAT SSMGEDSDVT IYSLARKHIP QNILTTAAPS LGFVWWNEDI VFNIDKQSVI
     SAWDIRYEPT LLDNLPKGIV KWRDMDGSGL VFVAQEKGTY SMDNGGVTDS VGKGAANRMS
     NTTLNSTNNM GRDQEVFTYS FQQQYKHQDQ EAADRESDHD KELEKERETE VDQHYHYLRE
     QEREHHQEYQ EWEHEPFGRH DDHQGNPQTD FYSHAYSDRP MLSKALSTYS SKIASPILSY
     YGAQTLSHHT SIVSNSPSIS GAALEYPGGI ESPIMITLDL PQVFGSVRAS RLADRKTSKN
     KGNAPAVRES AVDIFKYLVR ELELCHVQER NDPKSISVDD RSKSLDDTEL KIQLMENIGL
     SEHNTWATLI RSTTSMDTND PAGSHTQGHS KLVDMVKLQG SNILSPDNSD MEDDLGDKLD
     EMGTARLQEN VNHLVGLIFL STHNAETYAS VNDLQNFKIW MLIRDSLLND LKEAADGSTG
     RRDASGGAAN SDKNGIYTTT STVNHARQDS ITSNFSSFEP SDISRSDGEE KLNLGRLSEQ
     NLKATNQNTT AKLDDTRKLA SSSSLNSSEP LLLLEGGNQA KEQSIGLSDL KTCLKERYTA
     SNESVLDIEE ESSATVAYSS KQANTECSSS IPIRKTEART SFIDTIMTNL RSPGLSHLDV
     DNDAIFGKGK TSTSLGSGAS KRSSMHSTDS YHKRPYSSPI TYSKITTAAQ KAKLGLADHD
     GLPNRGSISF LANIDAAHAD KLLLGKLGLA SSPDDGKLLP PWDTGRLIQQ LYRYSVETGN
     IILTVCIILL FQTMYKVTST RIVKSTLAEF ITILHRYEMF EISAHLLKNC PWDDILGAGS
     GQSTVRLFCE NCGKLIVNEH SKTILSKRHQ AGESNMTNFG YWYCDSCRKP NSLCVYCEQP
     MKKLALSFLN CGHGGHFECL QQWFLDEGMS ECPSGCSGVL L
 
 
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