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YTM1_VANPO
ID   YTM1_VANPO              Reviewed;         453 AA.
AC   A7TMF9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Ribosome biogenesis protein YTM1 {ECO:0000255|HAMAP-Rule:MF_03029};
GN   Name=YTM1 {ECO:0000255|HAMAP-Rule:MF_03029}; ORFNames=Kpol_1064p35;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC   -!- FUNCTION: Component of the NOP7 complex, which is required for
CC       maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S
CC       ribosome. {ECO:0000255|HAMAP-Rule:MF_03029}.
CC   -!- SUBUNIT: Component of the NOP7 complex, composed of ERB1, NOP7 and
CC       YTM1. The complex is held together by ERB1, which interacts with NOP7
CC       via its N-terminal domain and with YTM1 via a high-affinity interaction
CC       between the seven-bladed beta-propeller domains of the 2 proteins. The
CC       NOP7 complex associates with the 66S pre-ribosome. Interacts (via UBL
CC       domain) with MDN1 (via VWFA/MIDAS domain). {ECO:0000255|HAMAP-
CC       Rule:MF_03029}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000255|HAMAP-
CC       Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
CC   -!- SIMILARITY: Belongs to the WD repeat WDR12/YTM1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_03029}.
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DR   EMBL; DS480422; EDO16553.1; -; Genomic_DNA.
DR   RefSeq; XP_001644411.1; XM_001644361.1.
DR   AlphaFoldDB; A7TMF9; -.
DR   SMR; A7TMF9; -.
DR   STRING; 436907.A7TMF9; -.
DR   EnsemblFungi; EDO16553; EDO16553; Kpol_1064p35.
DR   GeneID; 5544684; -.
DR   KEGG; vpo:Kpol_1064p35; -.
DR   eggNOG; KOG0313; Eukaryota.
DR   HOGENOM; CLU_000288_57_0_1; -.
DR   InParanoid; A7TMF9; -.
DR   OMA; VDCTRTK; -.
DR   OrthoDB; 1540178at2759; -.
DR   PhylomeDB; A7TMF9; -.
DR   Proteomes; UP000000267; Unassembled WGS sequence.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030687; C:preribosome, large subunit precursor; IEA:UniProtKB-UniRule.
DR   GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000466; P:maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:UniProtKB-UniRule.
DR   Gene3D; 2.130.10.10; -; 1.
DR   HAMAP; MF_03029; WDR12; 1.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR012972; NLE.
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; IPR028599; WDR12/Ytm1.
DR   Pfam; PF08154; NLE; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Repeat; Ribosome biogenesis; rRNA processing;
KW   WD repeat.
FT   CHAIN           1..453
FT                   /note="Ribosome biogenesis protein YTM1"
FT                   /id="PRO_0000369602"
FT   REPEAT          101..139
FT                   /note="WD 1"
FT   REPEAT          141..179
FT                   /note="WD 2"
FT   REPEAT          199..237
FT                   /note="WD 3"
FT   REPEAT          278..318
FT                   /note="WD 4"
FT   REPEAT          320..359
FT                   /note="WD 5"
FT   REPEAT          366..406
FT                   /note="WD 6"
FT   REPEAT          417..453
FT                   /note="WD 7"
FT   REGION          8..89
FT                   /note="Ubiquitin-like (UBL) domain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03029"
FT   REGION          99..453
FT                   /note="Sufficient for interaction with ERB1 and association
FT                   with 66S pre-ribosomes"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   453 AA;  50713 MW;  E639AF5972D36A48 CRC64;
     MSSDSSQVKL RFFTREQDES LHVQDAPMYA PISLKRYGLS EVVNHLLGFE KPVPFDFLID
     GELLRISLQE YLTKHGLSSE TFLNVEYTRA VLPPSFLSSF SNEDWVSSLD VGDNNKIISG
     SYDGVVRTWN LSGKIEKQYS GHSAPIRAVK YISNTRMVSG GNDRTLRLWK TKNEDLKQPV
     VDEDDEDIED GKTLAILEGH KAPVVSIDVS DNSRILSGSY DNTIGFWSTI YKEMTVVDPM
     EELKNNDSKM STAAKKRRKL TLKDGTIRRR APLALLESHT GPVEQVSFDF KDNTVGYSIS
     QDHTIKTWDL VTSRCIDTKT TSYSLLSLAQ LPTLNLLACG SSARHITLHD PRIGSTSKIT
     QQQLVGHKNF VVSLDTCPEN EYMLCSGSHD GTVKVWDVRA NSPMYTITRE EQSVEKGVND
     KVFAVNWSKN VGIISAGQDK KIQINKGDNI FKS
 
 
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