ID A7TG89_VANPO Unreviewed; 217 AA.
AC A7TG89;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit {ECO:0000256|RuleBase:RU364004};
GN ORFNames=Kpol_1055p15 {ECO:0000313|EMBL:EDO18659.1};
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907 {ECO:0000313|Proteomes:UP000000267};
RN [1] {ECO:0000313|EMBL:EDO18659.1, ECO:0000313|Proteomes:UP000000267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 /
RC NRRL Y-8283 / UCD 57-17 {ECO:0000313|Proteomes:UP000000267};
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
CC -!- FUNCTION: Required for ribosome biogenesis. Part of a complex which
CC catalyzes pseudouridylation of rRNA. This involves the isomerization of
CC uridine such that the ribose is subsequently attached to C5, instead of
CC the normal N1. Pseudouridine ("psi") residues may serve to stabilize
CC the conformation of rRNAs. {ECO:0000256|RuleBase:RU364004}.
CC -!- SUBUNIT: Component of the small nucleolar ribonucleoprotein particles
CC containing H/ACA-type snoRNAs (H/ACA snoRNPs).
CC {ECO:0000256|RuleBase:RU364004}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604, ECO:0000256|RuleBase:RU364004}.
CC -!- SIMILARITY: Belongs to the GAR1 family. {ECO:0000256|ARBA:ARBA00038293,
CC ECO:0000256|RuleBase:RU364004}.
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DR EMBL; DS480386; EDO18659.1; -; Genomic_DNA.
DR RefSeq; XP_001646517.1; XM_001646467.1.
DR AlphaFoldDB; A7TG89; -.
DR STRING; 436907.A7TG89; -.
DR GeneID; 5546960; -.
DR KEGG; vpo:Kpol_1055p15; -.
DR eggNOG; KOG3262; Eukaryota.
DR HOGENOM; CLU_080002_1_0_1; -.
DR InParanoid; A7TG89; -.
DR OMA; KPQDGIV; -.
DR OrthoDB; 5488451at2759; -.
DR Proteomes; UP000000267; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
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; Probable tRNA pseudouridine synthase domain; 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 PANTHER; PTHR23237:SF6; H_ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT 1; 1.
DR PANTHER; PTHR23237; NUCLEOLAR PROTEIN FAMILY A MEMBER 1 SNORNP PROTEIN GAR1; 1.
DR Pfam; PF04410; Gar1; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU364004};
KW Reference proteome {ECO:0000313|Proteomes:UP000000267};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU364004};
KW Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517,
KW ECO:0000256|RuleBase:RU364004};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU364004};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552,
KW ECO:0000256|RuleBase:RU364004}.
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 217 AA; 22147 MW; D35C83DD275C37C3 CRC64;
MSFRGGSRGG FSRGGGRGGR GGSAGRGGRF SAPQGPPDSV LEMGAFLHPC EGDIVCRSIN
TKIPYFNAPI YLENKTQVGK IDEILGPLNE VYFTIKCSEG VQAASFKEGD KFYIAPDKLL
PIERFLPKPK VAGPPKPKKK KSGAPGGRGG FSRGGGFSRG GGSRGGFSRG GGSRGGFSRG
GGSRGGFSRG GGSRGGFSRG GGSRGGFSRG GGRGGRY
//