ID CBF5_EMENI STANDARD; PRT; 481 AA. AC O43100; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 25-JAN-2005 (Rel. 46, Last annotation update) DE Centromere/microtubule binding protein CBF5 (Centromere-binding factor DE 5) (Small nucleolar RNP protein CBF5) (H/ACA snoRNP protein CBF5). GN Name=cbf5; OS Emericella nidulans (Aspergillus nidulans). OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiales; Trichocomaceae; Emericella. OX NCBI_TaxID=162425; RN [1] RP NUCLEOTIDE SEQUENCE. RA Jiang W., Clifford J., Koltin Y.; RT "A highly conserved nucleolar protein Cbf5p may be involved in the RT centromere DNA-binding activity of protein complex CBF3."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds in vitro to centromeres and microtubules. It is a CC centromere DNA-CBF3-binding factor and is involved in mitotic CC chromosome segregation. Essential for cell growth (By similarity). CC -!- FUNCTION: Involved in ribosome biogenesis; more specifically in CC 18S rRNA pseudouridylation and in cleavage of pre-rRNA. May CC function as a pseudouridine synthase (By similarity). CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein CC particles containing H/ACA-type snoRNAs (H/ACA snoRNPs) (By CC similarity). CC -!- SUBCELLULAR LOCATION: Nuclear; nucleolar (By similarity). CC -!- SIMILARITY: Belongs to the pseudouridine synthase truB family. CC -!- SIMILARITY: Contains 1 PUA domain. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U59148; AAB94296.1; -. DR HSSP; P09171; 1K8W. DR InterPro; IPR004802; Cbf5_synth. DR InterPro; IPR002478; PUA. DR InterPro; IPR002501; TruB__synth_N. DR InterPro; IPR004521; Unchar_dom_2. DR Pfam; PF01472; PUA; 1. DR Pfam; PF01509; TruB_N; 1. DR SMART; SM00359; PUA; 1. DR TIGRFAMs; TIGR00425; CBF5; 1. DR TIGRFAMs; TIGR00451; unchar_dom_2; 1. DR PROSITE; PS50890; PUA; 1. KW Centromere; DNA-binding; Microtubule; Nuclear protein; Repeat; KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing. FT DOMAIN 268 343 PUA. SQ SEQUENCE 481 AA; 54204 MW; A671BB6C57CE9590 CRC64; MAKEVDYTIK PEATASNINT EDWPLLLKNY DKLMVRTGHF TPIPAGSSPL KRDLKSYINS GVINLDKPSN PSSHEVVAWM KRILRAEKTG HSGTLDPKVT GCLIVCIDRA TRLVKSQQGA GKEYVCVIRL HDKIPGGEAQ FKRALETLTG ALFQRPPLIS AVKRQLRIRT IHESKLYEFD NERHLGVFWV SCEAGTYIRT LCVHLGLLLG VGAHMQELRR VRSGAMSENE GMVTLHDVLD AQWLYDNQRD ESYLRKVIKP LESLLTTYKR IVVKDSAVNA VCYGAKLMIP GLLRFEAGIE LGEEVVLMTT KGEAIAIGIA QMSTVELSTC DHGVVAKVKR CIMERDLYPR RWGLGPVALE KKKLKSSGKL DKYGRANEAT PAKWKSEYKD YSAPDGDSSQ QAVDVVAKEE ASPKEEPSLE ANESKMDIDD AQDDEDKKKR KRHEGETPEE RAERKRKKKE KKEKKERRKS KQEKDDSDDS D //