NAF1_YEAS7
ID NAF1_YEAS7 Reviewed; 492 AA.
AC A6ZRW0; B0KZS1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=H/ACA ribonucleoprotein complex non-core subunit NAF1;
DE AltName: Full=Nuclear assembly factor 1;
GN Name=NAF1; ORFNames=SCY_4671;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 371-492.
RX PubMed=18780730; DOI=10.1534/genetics.108.092932;
RA Sinha H., David L., Pascon R.C., Clauder-Muenster S., Krishnakumar S.,
RA Nguyen M., Shi G., Dean J., Davis R.W., Oefner P.J., McCusker J.H.,
RA Steinmetz L.M.;
RT "Sequential elimination of major-effect contributors identifies additional
RT quantitative trait loci conditioning high-temperature growth in yeast.";
RL Genetics 180:1661-1670(2008).
CC -!- FUNCTION: RNA-binding protein required for the maturation of box H/ACA
CC snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA
CC snoRNPs complex, it associates with the complex and disappears during
CC maturation of the complex and is replaced by GAR1 to yield mature H/ACA
CC snoRNPs complex. Acts as a competitive binder for CBF5 probably
CC required to prevent non-cognate RNAs from being loaded during transport
CC of the particle by inducing a non-productive conformation of CBF5 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: During assembly of the complex, component of the small
CC nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs
CC (H/ACA snoRNPs) which contains CBF5, NAF1, NHP2 and NOP10 proteins (By
CC similarity). Interacts with SHQ1. Interacts directly with CBF5.
CC Interacts with hyperphosphorylated C-terminal domain (CTD) of RNA
CC polymerase II large subunit (RPB1) (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Mostly present in the
CC nucleoplasm. Absent from the nucleolus (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The central region (136-221) reveals a striking structural
CC homology with the core domain of GAR1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAF1 family. {ECO:0000305}.
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DR EMBL; EF125227; ABN58633.1; -; Genomic_DNA.
DR EMBL; AAFW02000067; EDN62692.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZRW0; -.
DR SMR; A6ZRW0; -.
DR PRIDE; A6ZRW0; -.
DR EnsemblFungi; EDN62692; EDN62692; SCY_4671.
DR HOGENOM; CLU_025072_1_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000493; P:box H/ACA snoRNP assembly; IEA:InterPro.
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; IPR040309; Naf1.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR31633; PTHR31633; 1.
DR Pfam; PF04410; Gar1; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
PE 3: Inferred from homology;
KW Nucleus; Phosphoprotein; Ribonucleoprotein; Ribosome biogenesis;
KW RNA-binding; rRNA processing.
FT CHAIN 1..492
FT /note="H/ACA ribonucleoprotein complex non-core subunit
FT NAF1"
FT /id="PRO_0000373820"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..230
FT /note="RNA-binding"
FT /evidence="ECO:0000250"
FT REGION 237..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..457
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..485
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P53919"
SQ SEQUENCE 492 AA; 54839 MW; 681C5A654795715B CRC64;
MSDDLFSKAL ENPDQDLNVE LPKDDVDLGL LGDGGNERKT DEPAADAERS TGLGSGSSES
ESDSGSDSDS DSGSSGSEDD SADQDVEGED EGGDAIENED EDEDPSPSGP ILSKNEILEE
TVPELPEDYE ISEKTIITPI GVLKSAFENN IIIHATMSGE KRVLKEGSIF CLEDRTLIGM
LTEVFGPLQN PFYRIKLPDS KKNLFDELKV RLGEKAFIVT PDAHWIDTFE LKRNKGTDAS
NGYDEELPEE EQEFSDDEKE ALFKKMKKQQ QQRKKRDNRK LANDSDNVKV KRARQPKANS
LPKLVPPLGM SSNAPMQHGY KSRNARENIK RESSATSNRN GSSPVPITQL HQQQFSANNY
PFPQQPNGMP YPPYSPFPQP TNFQYPPPPF GQATPAQFSN TVPYGSLPPA YNNMSPPTQQ
SFMPMAQSQP PLPYGVPPMN QMQNPMYIQP PPQAPPQGNG NFQQVMELHQ ILLQQQQQQH
QYQHQHQQDP RT
