FAF1_YEAST
ID FAF1_YEAST Reviewed; 346 AA.
AC P40546; D6VVR0; Q6Q5G5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protein FAF1;
DE AltName: Full=Forty S assembly factor;
GN Name=FAF1; OrderedLocusNames=YIL019W;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KRR1.
RX PubMed=15178413; DOI=10.1016/j.bbrc.2004.05.012;
RA Karkusiewicz I., Rempola B., Gromadka R., Grynberg M., Rytka J.;
RT "Functional and physical interactions of Faf1p, a Saccharomyces cerevisiae
RT nucleolar protein.";
RL Biochem. Biophys. Res. Commun. 319:349-357(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for pre-rRNA processing and 40S ribosomal subunit
CC assembly. Seems to act in the processing of 35S rRNA at the A(0), A(1),
CC and A(2) cleavage sites. {ECO:0000269|PubMed:15178413}.
CC -!- SUBUNIT: Interacts with KRR1. {ECO:0000269|PubMed:15178413}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15178413}.
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DR EMBL; Z46881; CAA86973.1; -; Genomic_DNA.
DR EMBL; AY558089; AAS56415.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08526.1; -; Genomic_DNA.
DR PIR; S49963; S49963.
DR RefSeq; NP_012245.1; NM_001179369.1.
DR PDB; 4QMF; X-ray; 2.80 A; A/C=145-220.
DR PDB; 5WLC; EM; 3.80 A; NE=1-346.
DR PDB; 6KE6; EM; 3.40 A; RV=1-346.
DR PDB; 6LQP; EM; 3.20 A; RV=1-346.
DR PDB; 6LQQ; EM; 4.10 A; RV=1-346.
DR PDB; 6LQU; EM; 3.70 A; RV=1-346.
DR PDB; 6ZQA; EM; 4.40 A; JN=1-346.
DR PDB; 6ZQB; EM; 3.90 A; JN=1-346.
DR PDB; 6ZQC; EM; 3.80 A; JN=1-346.
DR PDB; 7AJT; EM; 4.60 A; JN=1-346.
DR PDBsum; 4QMF; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 7AJT; -.
DR AlphaFoldDB; P40546; -.
DR SMR; P40546; -.
DR BioGRID; 34969; 99.
DR DIP; DIP-4404N; -.
DR IntAct; P40546; 45.
DR MINT; P40546; -.
DR STRING; 4932.YIL019W; -.
DR MaxQB; P40546; -.
DR PaxDb; P40546; -.
DR PRIDE; P40546; -.
DR EnsemblFungi; YIL019W_mRNA; YIL019W; YIL019W.
DR GeneID; 854793; -.
DR KEGG; sce:YIL019W; -.
DR SGD; S000001281; FAF1.
DR VEuPathDB; FungiDB:YIL019W; -.
DR eggNOG; ENOG502QVP1; Eukaryota.
DR HOGENOM; CLU_069402_0_0_1; -.
DR InParanoid; P40546; -.
DR OMA; RNFEAQF; -.
DR BioCyc; YEAST:G3O-31295-MON; -.
DR PRO; PR:P40546; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40546; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Ribosome biogenesis.
FT CHAIN 1..346
FT /note="Protein FAF1"
FT /id="PRO_0000087172"
FT REGION 22..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 146..162
FT /evidence="ECO:0007829|PDB:4QMF"
SQ SEQUENCE 346 AA; 38889 MW; 7DE47A11F3952575 CRC64;
MTLDDDDYIK QMELQRKAFE SQFGSLESMG FEDKTKNIRT EVDTRDSSGD EIDNSDHGSD
FKDGTIESSN SSDEDSGNET AEENNQDSKP KTQPKVIRFN GPSDVYVPPS KKTQKLLRSG
KTLTQINKKL ESTEAKEEKE DETLEAENLQ NDLELQQFLR ESHLLSAFNN GGSGSTNSGV
SLTLQSMGGG NDDGIVYQDD QVIGKARSRT LEMRLNRLSR VNGHQDKINK LEKVPMHIRR
GMIDKHVKRI KKYEQEAAEG GIVLSKVKKG QFRKIESTYK KDIERRIGGS IKARDKEKAT
KRERGLKISS VGRSTRNGLI VSKRDIARIS GGERSGKFNG KKKSRR
