GAR1_SCHPO
ID GAR1_SCHPO Reviewed; 194 AA.
AC Q06975;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit gar1;
DE AltName: Full=snoRNP protein GAR1;
GN Name=gar1; ORFNames=SPBC20F10.01, SPBC25H2.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=8502556; DOI=10.1093/nar/21.9.2149;
RA Girard J.-P., Caizergues-Ferrer M., Lapeyre B.;
RT "The SpGAR1 gene of Schizosaccharomyces pombe encodes the functional
RT homologue of the snoRNP protein GAR1 of Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 21:2149-2155(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; Z19576; CAA79628.1; -; Genomic_DNA.
DR EMBL; AB000537; BAA19143.1; -; mRNA.
DR EMBL; CU329671; CAB08787.1; -; Genomic_DNA.
DR PIR; S33691; S33691.
DR RefSeq; NP_596365.1; NM_001022286.2.
DR AlphaFoldDB; Q06975; -.
DR SMR; Q06975; -.
DR BioGRID; 277228; 19.
DR STRING; 4896.SPBC20F10.01.1; -.
DR MaxQB; Q06975; -.
DR PaxDb; Q06975; -.
DR EnsemblFungi; SPBC20F10.01.1; SPBC20F10.01.1:pep; SPBC20F10.01.
DR GeneID; 2540705; -.
DR KEGG; spo:SPBC20F10.01; -.
DR PomBase; SPBC20F10.01; gar1.
DR VEuPathDB; FungiDB:SPBC20F10.01; -.
DR eggNOG; KOG3262; Eukaryota.
DR HOGENOM; CLU_080002_1_0_1; -.
DR InParanoid; Q06975; -.
DR OMA; HSCEGEM; -.
DR PRO; PR:Q06975; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0031429; C:box H/ACA snoRNP complex; ISO:PomBase.
DR GO; GO:0005730; C:nucleolus; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0034513; F:box H/ACA snoRNA binding; ISO:PomBase.
DR GO; GO:0000454; P:snoRNA guided rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031120; P:snRNA pseudouridine synthesis; ISO:PomBase.
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 2: Evidence at transcript level;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosome biogenesis; RNA-binding; rRNA processing.
FT CHAIN 1..194
FT /note="H/ACA ribonucleoprotein complex subunit gar1"
FT /id="PRO_0000208565"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4..17
FT /note="RGG-box 1"
FT REGION 115..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..194
FT /note="RGG-box 2"
SQ SEQUENCE 194 AA; 20131 MW; 5C2BC416535D38D8 CRC64;
MSFRGGRGGG FRGGRGGSRP FTPSGPPDQV IELGLFMHDC EGEMVCQSTN VKIPYFNAPI
YLENKSQIGK IDEVFGPMNQ VYFTVKPSEG IVSSSFKVGD KVYLSGDKLI PLDRFLPKPK
TVGPKKPKGA RNGPAGRGGR GGFRGGRGGS RGGFGGNSRG GFGGGSRGGF GGGSRGGSRG
GFRGGSRGGF RGRF