TMA64_YEAST
ID TMA64_YEAST Reviewed; 565 AA.
AC Q04600; D6VSA2;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Translation machinery-associated protein 64;
GN Name=TMA64; OrderedLocusNames=YDR117C;
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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 DOMAINS.
RX PubMed=10093218; DOI=10.1007/pl00006472;
RA Aravind L., Koonin E.V.;
RT "Novel predicted RNA-binding domains associated with the translation
RT machinery.";
RL J. Mol. Evol. 48:291-302(1999).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
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).
CC -!- SUBUNIT: Interacts with the 40S ribosomal subunit.
CC {ECO:0000269|PubMed:16702403}.
CC -!- DOMAIN: The PUA and the SUI1 domains may be involved in RNA binding.
CC {ECO:0000269|PubMed:10093218}.
CC -!- MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the eIF2D family. {ECO:0000305}.
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DR EMBL; Z48758; CAA88670.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11962.1; -; Genomic_DNA.
DR PIR; S52682; S52682.
DR RefSeq; NP_010402.3; NM_001180425.3.
DR AlphaFoldDB; Q04600; -.
DR SMR; Q04600; -.
DR BioGRID; 32173; 263.
DR IntAct; Q04600; 6.
DR MINT; Q04600; -.
DR STRING; 4932.YDR117C; -.
DR iPTMnet; Q04600; -.
DR MaxQB; Q04600; -.
DR PaxDb; Q04600; -.
DR PRIDE; Q04600; -.
DR EnsemblFungi; YDR117C_mRNA; YDR117C; YDR117C.
DR GeneID; 851695; -.
DR KEGG; sce:YDR117C; -.
DR SGD; S000002524; TMA64.
DR VEuPathDB; FungiDB:YDR117C; -.
DR eggNOG; KOG2522; Eukaryota.
DR GeneTree; ENSGT00550000074865; -.
DR HOGENOM; CLU_012487_1_0_1; -.
DR InParanoid; Q04600; -.
DR OMA; MFLKPYR; -.
DR BioCyc; YEAST:G3O-29717-MON; -.
DR PRO; PR:Q04600; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04600; protein.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IPI:SGD.
DR CDD; cd11608; eIF2D_C; 1.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR039757; EIF2D.
DR InterPro; IPR039759; eIF2D_SUI1.
DR InterPro; IPR041366; Pre-PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR12217; PTHR12217; 1.
DR Pfam; PF17832; Pre-PUA; 1.
DR Pfam; PF01253; SUI1; 1.
DR Pfam; PF02201; SWIB; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR PROSITE; PS50890; PUA; 1.
DR PROSITE; PS50296; SUI1; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..565
FT /note="Translation machinery-associated protein 64"
FT /id="PRO_0000244640"
FT DOMAIN 89..170
FT /note="PUA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00161"
FT DOMAIN 362..447
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT DOMAIN 475..547
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
SQ SEQUENCE 565 AA; 63992 MW; 2ED921EFABEF3739 CRC64;
MFKKEPHIKA LSNLKNSERK KLLQTFQKQT NNEEYSFRTS TIKQTNFNGQ KSVGTVYTDE
NNTPILFKEK HKEQLFPTVY SCWEYPALLP IVLTHGFVIE EHLFNGANLM ISGSIPPFDP
RCKIGTLCGI ASKQAPETVL AIGIVELDLP SFDKVIGETG VAVKIIHHFN DGLSKVFKMK
LEPPFVLSTQ SKDNNISSKQ IESSEQIKAV EKEQEDVKEA SVDVEEIAEV LDHFTVSDVD
YFITRALYYT LTQDKGLELP ISASNFISNH IMRNLPPIDH NEVNVKKTSW KKSAKFLKHF
EKEGFLKLKG KGDDLTIVGK NTDKDELKNF VPYKLGCSKS ATESRESTTS KEKTSGMMYS
LTLYKPFNLA KDLLKEVNLA SHTYYTSQDI RSAVSQYISV KNLADTKDKG KVIMDDLLFD
MVNKKKKVLN ASRIIARGEI LHPLLTNNFT EFYQIFKSDD TLLFKAPMKG SLPHIKIITE
MKIGRKVITR VSNFEVFQVD PESLAADLRK ICSGSTTISE SQTFKCAEVQ VQGPHGQSII
DHLNKLGIPS KWIDFENKLK KKKRK