SHQ1_YEAST
ID SHQ1_YEAST Reviewed; 507 AA.
AC P40486; D6VVI3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein SHQ1;
DE AltName: Full=Small nucleolar RNAs of the box H/ACA family quantitative accumulation protein 1;
GN Name=SHQ1; OrderedLocusNames=YIL104C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CBF5; NAF1 AND NHP2.
RX PubMed=12228251; DOI=10.1074/jbc.m207669200;
RA Yang P.K., Rotondo G., Porras T., Legrain P., Chanfreau G.;
RT "The Shq1p.Naf1p complex is required for box H/ACA small nucleolar
RT ribonucleoprotein particle biogenesis.";
RL J. Biol. Chem. 277:45235-45242(2002).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP INTERACTION WITH NAF1.
RX PubMed=15798213; DOI=10.1128/mcb.25.8.3295-3304.2005;
RA Yang P.K., Hoareau C., Froment C., Monsarrat B., Henry Y., Chanfreau G.;
RT "Cotranscriptional recruitment of the pseudouridylsynthetase Cbf5p and of
RT the RNA binding protein Naf1p during H/ACA snoRNP assembly.";
RL Mol. Cell. Biol. 25:3295-3304(2005).
CC -!- FUNCTION: Involved in the early biogenesis steps of box H/ACA snoRNP
CC assembly. {ECO:0000269|PubMed:12228251}.
CC -!- SUBUNIT: Interacts with CBF5, NAF1 and NHP2. The interaction with NAF1
CC and SHQ1 does not occur when NAF1 is associated with the chromatin.
CC {ECO:0000269|PubMed:12228251, ECO:0000269|PubMed:15798213}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12228251,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7060 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SHQ1 family. {ECO:0000305}.
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DR EMBL; Z38125; CAA86276.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08449.1; -; Genomic_DNA.
DR PIR; S48468; S48468.
DR RefSeq; NP_012162.3; NM_001179452.3.
DR PDB; 2K8Q; NMR; -; A=1-134.
DR PDB; 3EUD; X-ray; 2.40 A; A/B/C/D/E/F=1-98.
DR PDB; 3UAH; X-ray; 1.60 A; A=147-507.
DR PDB; 3UAI; X-ray; 3.06 A; D=147-507.
DR PDB; 3ZUZ; X-ray; 1.50 A; A=143-507.
DR PDB; 3ZV0; X-ray; 2.80 A; A/B=145-507.
DR PDBsum; 2K8Q; -.
DR PDBsum; 3EUD; -.
DR PDBsum; 3UAH; -.
DR PDBsum; 3UAI; -.
DR PDBsum; 3ZUZ; -.
DR PDBsum; 3ZV0; -.
DR AlphaFoldDB; P40486; -.
DR BMRB; P40486; -.
DR SMR; P40486; -.
DR BioGRID; 34887; 100.
DR DIP; DIP-4970N; -.
DR IntAct; P40486; 11.
DR MINT; P40486; -.
DR STRING; 4932.YIL104C; -.
DR iPTMnet; P40486; -.
DR MaxQB; P40486; -.
DR PaxDb; P40486; -.
DR PRIDE; P40486; -.
DR EnsemblFungi; YIL104C_mRNA; YIL104C; YIL104C.
DR GeneID; 854702; -.
DR KEGG; sce:YIL104C; -.
DR SGD; S000001366; SHQ1.
DR VEuPathDB; FungiDB:YIL104C; -.
DR eggNOG; KOG3247; Eukaryota.
DR GeneTree; ENSGT00390000007605; -.
DR HOGENOM; CLU_030217_1_0_1; -.
DR InParanoid; P40486; -.
DR OMA; NDWQLPQ; -.
DR BioCyc; YEAST:G3O-31360-MON; -.
DR Reactome; R-SCE-171319; Telomere Extension By Telomerase.
DR EvolutionaryTrace; P40486; -.
DR PRO; PR:P40486; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40486; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0000493; P:box H/ACA snoRNP assembly; IMP:SGD.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR039742; Shq1.
DR InterPro; IPR007009; Shq1_dom.
DR PANTHER; PTHR12967; PTHR12967; 1.
DR Pfam; PF04925; SHQ1; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome.
FT CHAIN 1..507
FT /note="Protein SHQ1"
FT /id="PRO_0000202966"
FT DOMAIN 1..91
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:3EUD"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:3EUD"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3EUD"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3EUD"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3EUD"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:3EUD"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3EUD"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:3EUD"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:3EUD"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3EUD"
FT HELIX 172..174
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 201..215
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 233..239
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 241..245
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 250..259
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 296..315
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 324..331
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 364..376
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 385..401
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 403..418
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 425..429
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 431..441
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT STRAND 467..471
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT TURN 476..478
FT /evidence="ECO:0007829|PDB:3ZV0"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:3ZUZ"
FT HELIX 488..504
FT /evidence="ECO:0007829|PDB:3ZUZ"
SQ SEQUENCE 507 AA; 59151 MW; 15A6A66C66E70C39 CRC64;
MITPRFSITQ DEEFIFLKIF ISNIRFSAVG LEIIIQENMI IFHLSPYYLR LRFPHELIDD
ERSTAQYDSK DECINVKVAK LNKNEYFEDL DLPTKLLARQ GDLAGADALT ENTDAKKTQK
PLIQEVETDG VSNNIKDDVK TIGQMGEGFN WEIEQKMDSS TNNGILKTKY GFDNLYDTVI
SVSTSNGNDI NELDDPEHTD ANDRVIERLR KENLKFDPEY YVSEYMTHKY GNEEDLEING
IKELLKFTPS IVKQYLQWYK DSTNPNLVMP IEFTDEEQKQ MQDNLPKKSY LVEDIKPLYV
TILSVLFSYV FEQIENEGTH TTESAWTMGK LCPQISFLDQ QLKQVNELQD GMKEISKVNK
DSSLIKIAII TGIRRALSYP LHRNYDLAMK AWTFVYYILR GGKRLVIRAL LDIHETFRFH
DVYYVYDKVL LDDLTAWFIS QGSENVIRSL ALEMRKEQES LSKQDIEFEC IASFNEQTGE
PEWETLNIRE MEILAESEYR EQQQNPQ
