HBS1_YEAST
ID HBS1_YEAST Reviewed; 611 AA.
AC P32769; D6VXE4;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Elongation factor 1 alpha-like protein;
GN Name=HBS1; OrderedLocusNames=YKR084C; ORFNames=YKR404;
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].
RX PubMed=8203164; DOI=10.1002/yea.320100210;
RA Garcia-Cantalejo J.M., Baladron V., Esteban P.F., Santos M.A., Bou G.,
RA Remacha M.A., Revuelta J.L., Ballesta J.P.G., Jimenez A., del Rey F.;
RT "The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae
RT chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open
RT reading frames.";
RL Yeast 10:231-245(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 92-611.
RX PubMed=1394434; DOI=10.1016/0092-8674(92)90269-i;
RA Nelson R.J., Ziegelhoffer T., Nicolet C., Werner-Washburne M., Craig E.A.;
RT "The translation machinery and 70 kd heat shock protein cooperate in
RT protein synthesis.";
RL Cell 71:97-105(1992).
RN [5]
RP INTERACTION WITH DOM34, AND MUTAGENESIS OF VAL-176 AND HIS-255.
RX PubMed=11909951; DOI=10.1128/mcb.22.8.2564-2574.2002;
RA Carr-Schmid A., Pfund C., Craig E.A., Kinzy T.G.;
RT "Novel G-protein complex whose requirement is linked to the translational
RT status of the cell.";
RL Mol. Cell. Biol. 22:2564-2574(2002).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=16554824; DOI=10.1038/nature04530;
RA Doma M.K., Parker R.;
RT "Endonucleolytic cleavage of eukaryotic mRNAs with stalls in translation
RT elongation.";
RL Nature 440:561-564(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, 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 -!- FUNCTION: Involved in protein translation. Together with DOM34, may
CC function in recognizing stalled ribosomes and triggering
CC endonucleolytic cleavage of the mRNA, a mechanism to release non-
CC functional ribosomes and degrade damaged mRNAs.
CC {ECO:0000269|PubMed:16554824}.
CC -!- SUBUNIT: Interacts with DOM34. {ECO:0000269|PubMed:11909951}.
CC -!- INTERACTION:
CC P32769; P33309: DOM34; NbExp=8; IntAct=EBI-8194, EBI-6012;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; M98437; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z27116; CAA81635.1; -; Genomic_DNA.
DR EMBL; Z28309; CAA82163.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09234.1; -; Genomic_DNA.
DR PIR; S38162; S38162.
DR RefSeq; NP_013010.3; NM_001179874.3.
DR PDB; 3IZQ; EM; -; 1=1-611.
DR PDB; 3P26; X-ray; 2.50 A; A/B=135-611.
DR PDB; 3P27; X-ray; 2.95 A; A/B=135-611.
DR PDB; 5M1J; EM; 3.30 A; A6=1-611.
DR PDBsum; 3IZQ; -.
DR PDBsum; 3P26; -.
DR PDBsum; 3P27; -.
DR PDBsum; 5M1J; -.
DR AlphaFoldDB; P32769; -.
DR SMR; P32769; -.
DR BioGRID; 34215; 154.
DR ComplexPortal; CPX-465; DOM34-HBS1 ribosome dissociation complex.
DR DIP; DIP-762N; -.
DR IntAct; P32769; 1.
DR STRING; 4932.YKR084C; -.
DR iPTMnet; P32769; -.
DR MaxQB; P32769; -.
DR PaxDb; P32769; -.
DR PRIDE; P32769; -.
DR EnsemblFungi; YKR084C_mRNA; YKR084C; YKR084C.
DR GeneID; 853959; -.
DR KEGG; sce:YKR084C; -.
DR SGD; S000001792; HBS1.
DR VEuPathDB; FungiDB:YKR084C; -.
DR eggNOG; KOG0458; Eukaryota.
DR GeneTree; ENSGT00940000156274; -.
DR HOGENOM; CLU_007265_3_8_1; -.
DR InParanoid; P32769; -.
DR OMA; SVEDEHC; -.
DR BioCyc; YEAST:G3O-32047-MON; -.
DR Reactome; R-SCE-156842; Eukaryotic Translation Elongation.
DR Reactome; R-SCE-3371511; HSF1 activation.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8876725; Protein methylation.
DR PRO; PR:P32769; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32769; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:1990533; C:Dom34-Hbs1 complex; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IMP:SGD.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IDA:ComplexPortal.
DR GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:ComplexPortal.
DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:ComplexPortal.
DR GO; GO:0032790; P:ribosome disassembly; IDA:SGD.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR015033; HBS1-like_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF08938; HBS1_N; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Translation regulation.
FT CHAIN 1..611
FT /note="Elongation factor 1 alpha-like protein"
FT /id="PRO_0000091490"
FT DOMAIN 165..390
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 105..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..181
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 230..234
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 251..254
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 313..316
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 352..354
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT BINDING 174..181
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 251..255
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 313..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 176
FT /note="V->G: Loss of function."
FT /evidence="ECO:0000269|PubMed:11909951"
FT MUTAGEN 255
FT /note="H->E: Loss of function."
FT /evidence="ECO:0000269|PubMed:11909951"
FT CONFLICT 92..94
FT /note="NGS -> MGV (in Ref. 4; M98437)"
FT /evidence="ECO:0000305"
FT HELIX 157..163
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:3P27"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 259..266
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 291..302
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 308..313
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 322..339
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 377..392
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 397..399
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 402..409
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 419..430
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:3P26"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 443..452
FT /evidence="ECO:0007829|PDB:3P26"
FT TURN 453..455
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 473..480
FT /evidence="ECO:0007829|PDB:3P26"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 504..512
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 524..529
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 532..547
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 564..571
FT /evidence="ECO:0007829|PDB:3P26"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:3P26"
FT TURN 587..590
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 591..596
FT /evidence="ECO:0007829|PDB:3P26"
FT STRAND 599..609
FT /evidence="ECO:0007829|PDB:3P26"
SQ SEQUENCE 611 AA; 68730 MW; 11EC2CB6936396EE CRC64;
MAYSDYSDGA DDMPDFHDEG EFDDYLNDDE YDLMNEVFPT LKAQLQDYQG WDNLSLKLAL
FDNNFDLEST LAELKKTLKK KKTPKKPIAA ANGSANVTQK LANISISQQR PNDRLPDWLD
EEESEGERNG EEANDEKTVQ RYYKTTVPTK PKKPHDISAF VKSALPHLSF VVLGHVDAGK
STLMGRLLYD LNIVNQSQLR KLQRESETMG KSSFKFAWIM DQTNEERERG VTVSICTSHF
STHRANFTIV DAPGHRDFVP NAIMGISQAD MAILCVDCST NAFESGFDLD GQTKEHMLLA
SSLGIHNLII AMNKMDNVDW SQQRFEEIKS KLLPYLVDIG FFEDNINWVP ISGFSGEGVY
KIEYTDEVRQ WYNGPNLMST LENAAFKISK ENEGINKDDP FLFSVLEIIP SKKTSNDLAL
VSGKLESGSI QPGESLTIYP SEQSCIVDKI QVGSQQGQST NHEETDVAIK GDFVTLKLRK
AYPEDIQNGD LAASVDYSSI HSAQCFVLEL TTFDMNRPLL PGTPFILFIG VKEQPARIKR
LISFIDKGNT ASKKKIRHLG SKQRAFVEIE LIEVKRWIPL LTAHENDRLG RVVLRKDGRT
IAAGKISEIT Q
