GAR1_PICST
ID GAR1_PICST Reviewed; 202 AA.
AC A3GHP2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit GAR1;
DE AltName: Full=snoRNP protein GAR1;
GN Name=GAR1; ORFNames=PICST_75322;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- FUNCTION: Non-catalytic component of the H/ACA small nucleolar
CC ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of
CC rRNA and is required for ribosome biogenesis. This involves the
CC isomerization of uridine such that the ribose is subsequently attached
CC to C5, instead of the normal N1. Pseudouridine ('psi') residues may
CC serve to stabilize the conformation of rRNAs. The H/ACA snoRNP complex
CC also mediates pseudouridylation of other types of RNAs. The H/ACA
CC snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA.
CC {ECO:0000250|UniProtKB:P28007}.
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs).
CC {ECO:0000250|UniProtKB:P28007}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P28007}.
CC -!- SIMILARITY: Belongs to the GAR1 family. {ECO:0000305}.
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DR EMBL; AAVQ01000002; EAZ63083.1; -; Genomic_DNA.
DR RefSeq; XP_001387106.1; XM_001387069.1.
DR AlphaFoldDB; A3GHP2; -.
DR SMR; A3GHP2; -.
DR STRING; 4924.XP_001387106.1; -.
DR EnsemblFungi; EAZ63083; EAZ63083; PICST_75322.
DR GeneID; 4851791; -.
DR KEGG; pic:PICST_75322; -.
DR eggNOG; KOG3262; Eukaryota.
DR HOGENOM; CLU_080002_1_0_1; -.
DR InParanoid; A3GHP2; -.
DR OMA; HSCEGEM; -.
DR OrthoDB; 1530008at2759; -.
DR Proteomes; UP000002258; Chromosome 1.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.10.230; -; 1.
DR InterPro; IPR038664; Gar1/Naf1_Cbf5-bd_sf.
DR InterPro; IPR007504; H/ACA_rnp_Gar1/Naf1.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR Pfam; PF04410; Gar1; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
PE 3: Inferred from homology;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..202
FT /note="H/ACA ribonucleoprotein complex subunit GAR1"
FT /id="PRO_0000327531"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5..17
FT /note="RGG-box 1"
FT REGION 113..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..200
FT /note="RGG-box 2"
SQ SEQUENCE 202 AA; 20676 MW; CCA2064E6F695B8B CRC64;
MNRGRGGFRG GRGGRTGPSQ FQQGPPDTVL EMGAFMQACE GDIVCRSINV KIPYFNAPIY
LENKTQIGKV DEILGPLNEV FFTIKPSEGV KADSFKEGDK FFIGPDKLLP LERFLPKPKE
VGPKPKRKSG GAGGASRGGF GGRGGARGGF GGRGGARGGF GGRGGSRGGF SGGRGGSRGG
FGGRGGSRGG FGGSRGGRGG RF