KRR1_BOVIN
ID KRR1_BOVIN Reviewed; 382 AA.
AC Q3B7L9; F1N7H6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=KRR1 small subunit processome component homolog;
DE AltName: Full=KRR-R motif-containing protein 1;
GN Name=KRR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for 40S ribosome biogenesis. Involved in nucleolar
CC processing of pre-18S ribosomal RNA and ribosome assembly (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the ribosomal small subunit (SSU) processome.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13601}. Nucleus
CC {ECO:0000250|UniProtKB:Q13601}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q13601}.
CC -!- SIMILARITY: Belongs to the KRR1 family. {ECO:0000305}.
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DR EMBL; DAAA02012357; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC107550; AAI07551.1; -; mRNA.
DR RefSeq; NP_001032908.1; NM_001037819.1.
DR AlphaFoldDB; Q3B7L9; -.
DR SMR; Q3B7L9; -.
DR STRING; 9913.ENSBTAP00000015401; -.
DR PaxDb; Q3B7L9; -.
DR PRIDE; Q3B7L9; -.
DR Ensembl; ENSBTAT00000015401; ENSBTAP00000015401; ENSBTAG00000011591.
DR GeneID; 513714; -.
DR KEGG; bta:513714; -.
DR CTD; 11103; -.
DR VEuPathDB; HostDB:ENSBTAG00000011591; -.
DR VGNC; VGNC:30715; KRR1.
DR eggNOG; KOG2874; Eukaryota.
DR GeneTree; ENSGT00390000018775; -.
DR HOGENOM; CLU_040185_0_0_1; -.
DR InParanoid; Q3B7L9; -.
DR OMA; HKKEKFV; -.
DR OrthoDB; 944899at2759; -.
DR TreeFam; TF105745; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011591; Expressed in neutrophil and 106 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosome biogenesis; RNA-binding;
KW rRNA processing; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CHAIN 2..382
FT /note="KRR1 small subunit processome component homolog"
FT /id="PRO_0000342400"
FT DOMAIN 154..206
FT /note="KH"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CROSSLNK 342
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13601"
FT CONFLICT 198
FT /note="G -> V (in Ref. 2; AAI07551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 43650 MW; C233C99FD81EA056 CRC64;
MASSKQNGPT TASGKSELRS PKPTSENRDE SELLTVPDGW KEPAFSKEDN PRGLLEESSF
ATLFPKYREA YLKECWPLVQ KALNEHHINA TLDLIEGSMT VCTTKKTFDP YIIIRARDLI
KLLARSVSFE QAIRILQDDV ACDIIKIGSL VRNKERFVKR RQRLIGPKGS TLKALELLTN
CYIMVQGNTV SAIGPFSGLK EVRKVVLDTM KNIHPIYNIK TLMIKRELAK DSELRSQSWE
RFLPQFKHKN VNKRKEPKKK TVKKEYTPFP PPQPESQIDK ELASGEYFLK ASQKKRQKME
AIKAKQAEAL SKRQEERNKA FIPPKEKPVH LKKPKEASTE TKIDVAALKE KVKKAKNKKL
GALTAEEVKL KMEADEKKKK KK
