TMA46_YEAST
ID TMA46_YEAST Reviewed; 345 AA.
AC Q12000; D6W2F2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Translation machinery-associated protein 46;
DE AltName: Full=DRG family-regulatory protein 1;
GN Name=TMA46; Synonyms=DFRP1; OrderedLocusNames=YOR091W; ORFNames=YOR3160w;
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 [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [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 IDENTIFICATION.
RX PubMed=15676025; DOI=10.1111/j.1365-2443.2005.00825.x;
RA Ishikawa K., Azuma S., Ikawa S., Semba K., Inoue J.;
RT "Identification of DRG family regulatory proteins (DFRPs): specific
RT regulation of DRG1 and DRG2.";
RL Genes Cells 10:139-150(2005).
RN [7]
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=15905473; DOI=10.1093/nar/gki583;
RA Zhang Z., Dietrich F.S.;
RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT SAGE.";
RL Nucleic Acids Res. 33:2838-2851(2005).
RN [8]
RP INTERACTION WITH RIBOSOMES AND RBG1.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [9]
RP INTERACTION WITH RBG1.
RX PubMed=19448108; DOI=10.1128/ec.00356-08;
RA Wout P.K., Sattlegger E., Sullivan S.M., Maddock J.R.;
RT "Saccharomyces cerevisiae Rbg1 protein and its binding partner Gir2
RT interact on polyribosomes with Gcn1.";
RL Eukaryot. Cell 8:1061-1071(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, AND IDENTIFICATION BY
RP 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).
CC -!- SUBUNIT: Interacts with RBG1 and with translating ribosomes.
CC {ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:19448108}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 4220 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ZC3H15/TMA46 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64012.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA99288.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X94335; CAA64012.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74999; CAA99288.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006948; DAA10868.1; -; Genomic_DNA.
DR PIR; S61651; S61651.
DR RefSeq; NP_014734.2; NM_001183510.1.
DR PDB; 4A9A; X-ray; 2.67 A; C/D=205-345.
DR PDBsum; 4A9A; -.
DR AlphaFoldDB; Q12000; -.
DR SMR; Q12000; -.
DR BioGRID; 34489; 306.
DR IntAct; Q12000; 5.
DR MINT; Q12000; -.
DR STRING; 4932.YOR091W; -.
DR iPTMnet; Q12000; -.
DR MaxQB; Q12000; -.
DR PaxDb; Q12000; -.
DR PRIDE; Q12000; -.
DR EnsemblFungi; YOR091W_mRNA; YOR091W; YOR091W.
DR GeneID; 854258; -.
DR KEGG; sce:YOR091W; -.
DR SGD; S000005617; TMA46.
DR VEuPathDB; FungiDB:YOR091W; -.
DR eggNOG; KOG1763; Eukaryota.
DR GeneTree; ENSGT00390000015818; -.
DR HOGENOM; CLU_042870_1_0_1; -.
DR InParanoid; Q12000; -.
DR OMA; DGPMEEG; -.
DR BioCyc; YEAST:G3O-33625-MON; -.
DR PRO; PR:Q12000; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12000; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IGI:SGD.
DR DisProt; DP02474; -.
DR InterPro; IPR032378; ZC3H15/TMA46_C.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF16543; DFRP_C; 1.
DR SMART; SM00356; ZnF_C3H1; 2.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Zinc; Zinc-finger.
FT CHAIN 1..345
FT /note="Translation machinery-associated protein 46"
FT /id="PRO_0000237638"
FT ZN_FING 87..114
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 158..196
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 243..265
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 306..317
FT /evidence="ECO:0007829|PDB:4A9A"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:4A9A"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:4A9A"
SQ SEQUENCE 345 AA; 39514 MW; F1D2C384881C4DAA CRC64;
MPPKKGKQAQ AAGKKKDNVD KTFGMKNKNR STKVQKYIKQ VQSQSDPKKE EMRLKKLEEK
KRREAEEAER RALFNPVADQ RVRAGVDPKS MVCALFKLGN CNKGAKCKFS HDLNVGRRME
KKDLYQDTRS EKENDTMDNW DEEKLRKVIL SKHGNPKTTT DKVCKYFIEA VENGKYGWFW
ICPNGGDKCM YRHSLPEGFV LKTNEQKRLE RESLEKQPKI TLEEFIETER GKLDKSKLTP
ITIANFAQWK KDHVIAKINA EKKLSSKRKP TGREIILKMS AENKSFETDN ADMPDDVTQG
SAWDLTEFTD ALKKADHQDD GGIKDYGDGS NPTFDIKKAN SATLA
