KRR1_YEASV
ID KRR1_YEASV Reviewed; 316 AA.
AC E7LRT8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 41.
DE RecName: Full=KRR1 small subunit processome component {ECO:0000250|UniProtKB:P25586};
DE AltName: Full=KRR-R motif-containing protein 1 {ECO:0000250|UniProtKB:P25586};
DE AltName: Full=Ribosomal RNA assembly protein KRR1 {ECO:0000250|UniProtKB:P25586};
GN Name=KRR1 {ECO:0000250|UniProtKB:P25586}; ORFNames=VIN13_0432;
OS Saccharomyces cerevisiae (strain VIN 13) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=764099;
RN [1] {ECO:0000312|EMBL:EGA79798.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN 13 {ECO:0000312|EMBL:EGA79798.1};
RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "Whole-genome comparison reveals novel genetic elements that characterize
RT the genome of industrial strains of Saccharomyces cerevisiae.";
RL PLoS Genet. 7:E1001287-E1001287(2011).
CC -!- FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar
CC processing of pre-18S ribosomal RNA and ribosome assembly. Essential
CC for vegetative growth (By similarity). {ECO:0000250|UniProtKB:P25586}.
CC -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome
CC composed of at least 40 protein subunits and snoRNA U3. Interacts with
CC snoRNA U3. Interacts with MPP10, KRI1 and with ribosomal proteins
CC RPS1A, RPS4A, RPS4B, RPS8A, RPS8B, RPS11A, RPS11B, RPS13, RPS24, RPS25,
CC RPL4A, RPL7B, RPL8, RPL23, RPL25 and RPL28 (By similarity).
CC {ECO:0000250|UniProtKB:P25586}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P25586}.
CC -!- SIMILARITY: Belongs to the KRR1 family. {ECO:0000255}.
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DR EMBL; ADXC01000007; EGA79798.1; -; Genomic_DNA.
DR AlphaFoldDB; E7LRT8; -.
DR SMR; E7LRT8; -.
DR EnsemblFungi; EGA79798; EGA79798; VIN13_0432.
DR HOGENOM; CLU_040185_0_2_1; -.
DR OMA; HKKEKFV; -.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1370.10; -; 2.
DR InterPro; IPR041174; KH_8.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR024166; rRNA_assembly_KRR1.
DR PANTHER; PTHR12581; PTHR12581; 1.
DR Pfam; PF17903; KH_8; 1.
DR PIRSF; PIRSF006515; KRR1; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 3: Inferred from homology;
KW Nucleus; Ribonucleoprotein; Ribosome biogenesis; RNA-binding;
KW rRNA processing.
FT CHAIN 1..316
FT /note="KRR1 small subunit processome component"
FT /id="PRO_0000415659"
FT DOMAIN 122..192
FT /note="KH"
FT /evidence="ECO:0000255"
FT REGION 279..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 37159 MW; 7A7F964E2C7FD056 CRC64;
MVSTHNRDKP WDTDDIDKWK IEEFKEEDNA SGQPFAEESS FMTLFPKYRE SYLKTIWNDV
TRALDKHNIA CVLDLVEGSM TVKTTRKTYD PAIILKARDL IKLLARSVPF PQAVKILQDD
MACDVIKIGN FVTNKERFVK RRQRLVGPNG NTLKALELLT KCYILVQGNT VSAMGPFKGL
KEVRRVVEDC MKNIHPIYHI KELMIKRELA KRPELANEDW SRFLPMFKKR NVARKKPKKI
RNVEKKVYTP FPPAQLPRKV DLEIESGEYF LSKREKQMKK LNEQKEKQME REIERQEERA
KDFIAPEEEA YKPNQN
