FCF2_YEAST
ID FCF2_YEAST Reviewed; 217 AA.
AC Q12035; D6VY53;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=rRNA-processing protein FCF2;
DE AltName: Full=FAF1 copurifying factor 2;
GN Name=FCF2; OrderedLocusNames=YLR051C; ORFNames=L2128;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 [4]
RP FUNCTION, AND INTERACTION WITH FAF1.
RX PubMed=16762320; DOI=10.1016/j.bbrc.2006.05.140;
RA Rempola B., Karkusiewicz I., Piekarska I., Rytka J.;
RT "Fcf1p and Fcf2p are novel nucleolar Saccharomyces cerevisiae proteins
RT involved in pre-rRNA processing.";
RL Biochem. Biophys. Res. Commun. 346:546-554(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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: Essential protein involved in pre-rRNA processing and 40S
CC ribosomal subunit assembly. Required for the early cleavage steps of
CC 35S rRNA at the A(0), A(1), and A(2) sites.
CC {ECO:0000269|PubMed:16762320}.
CC -!- SUBUNIT: Interacts with FAF1. {ECO:0000269|PubMed:16762320}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
CC -!- SIMILARITY: Belongs to the FCF2 family. {ECO:0000305}.
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DR EMBL; X94607; CAA64298.1; -; Genomic_DNA.
DR EMBL; Z73223; CAA97581.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09369.1; -; Genomic_DNA.
DR PIR; S61625; S61625.
DR RefSeq; NP_013152.1; NM_001181938.1.
DR PDB; 5WLC; EM; 3.80 A; SQ=1-217.
DR PDB; 6KE6; EM; 3.40 A; 5J=1-217.
DR PDB; 6LQP; EM; 3.20 A; 5J=1-217.
DR PDB; 6LQQ; EM; 4.10 A; 5J=1-217.
DR PDB; 6LQR; EM; 8.60 A; 5J=1-217.
DR PDB; 6LQS; EM; 3.80 A; 5J=1-217.
DR PDB; 6LQT; EM; 4.90 A; 5J=1-217.
DR PDB; 6LQU; EM; 3.70 A; 5J=1-217.
DR PDB; 6LQV; EM; 4.80 A; 5J=1-217.
DR PDB; 6ZQA; EM; 4.40 A; JM=1-217.
DR PDB; 6ZQB; EM; 3.90 A; JM=1-217.
DR PDB; 6ZQC; EM; 3.80 A; JM=1-217.
DR PDB; 6ZQD; EM; 3.80 A; JM=1-217.
DR PDB; 6ZQE; EM; 7.10 A; JM=1-217.
DR PDB; 7AJT; EM; 4.60 A; JM=1-217.
DR PDB; 7AJU; EM; 3.80 A; JM=1-217.
DR PDB; 7D4I; EM; 4.00 A; 5J=1-217.
DR PDB; 7D5S; EM; 4.60 A; 5J=1-217.
DR PDB; 7D5T; EM; 6.00 A; 5J=1-217.
DR PDB; 7D63; EM; 12.30 A; 5J=1-217.
DR PDBsum; 5WLC; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6LQV; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5S; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR AlphaFoldDB; Q12035; -.
DR SMR; Q12035; -.
DR BioGRID; 31326; 167.
DR DIP; DIP-2131N; -.
DR IntAct; Q12035; 6.
DR MINT; Q12035; -.
DR STRING; 4932.YLR051C; -.
DR iPTMnet; Q12035; -.
DR MaxQB; Q12035; -.
DR PaxDb; Q12035; -.
DR PRIDE; Q12035; -.
DR EnsemblFungi; YLR051C_mRNA; YLR051C; YLR051C.
DR GeneID; 850740; -.
DR KEGG; sce:YLR051C; -.
DR SGD; S000004041; FCF2.
DR VEuPathDB; FungiDB:YLR051C; -.
DR eggNOG; KOG3100; Eukaryota.
DR GeneTree; ENSGT00510000048142; -.
DR HOGENOM; CLU_075129_2_0_1; -.
DR InParanoid; Q12035; -.
DR OMA; RHYKKDR; -.
DR BioCyc; YEAST:G3O-32207-MON; -.
DR PRO; PR:Q12035; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12035; protein.
DR GO; GO:0005730; C:nucleolus; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR InterPro; IPR039883; Fcf2/DNTTIP2.
DR InterPro; IPR014810; Fcf2_C.
DR PANTHER; PTHR21686; PTHR21686; 1.
DR Pfam; PF08698; Fcf2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Reference proteome;
KW Ribosome biogenesis; rRNA processing.
FT CHAIN 1..217
FT /note="rRNA-processing protein FCF2"
FT /id="PRO_0000253819"
FT REGION 76..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..217
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 217 AA; 25636 MW; 0F79F36CBBA3B12C CRC64;
MDQSVEDLFG ALRDASASLE VKNSAKEQVS LQQEDVLQIG NNDDEVEIES KFQEIETNLK
KLPKLETGFD ALANKKKKKN VLPSVETEDK RKPNKSDKND NDWFTLPKPD DNMRREVQRD
LLLIKHRAAL DPKRHYKKQR WEVPERFAIG TIIEDKSEFY SSRMNRKERK STILETLMGD
EASNKYFKRK YNEIQEKSTS GRKAHYKKMK EMRKKRR
