HBS1_SCHPO
ID HBS1_SCHPO Reviewed; 592 AA.
AC O74774;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 4.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Elongation factor 1 alpha-like protein;
GN Name=hbs1 {ECO:0000250|UniProtKB:P32769}; ORFNames=SPBC25B2.01, SPBC2G5.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAA21259.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P32769}.
CC -!- INTERACTION:
CC O74774; Q9USL5: dom34; NbExp=5; IntAct=EBI-15882111, EBI-15882140;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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; CU329671; CAA21259.2; -; Genomic_DNA.
DR RefSeq; XP_001713137.1; XM_001713085.2.
DR PDB; 3MCA; X-ray; 2.74 A; A=1-592.
DR PDBsum; 3MCA; -.
DR AlphaFoldDB; O74774; -.
DR SMR; O74774; -.
DR BioGRID; 276958; 22.
DR DIP; DIP-59037N; -.
DR IntAct; O74774; 1.
DR STRING; 4896.SPBC25B2.01.1; -.
DR iPTMnet; O74774; -.
DR MaxQB; O74774; -.
DR PaxDb; O74774; -.
DR PRIDE; O74774; -.
DR EnsemblFungi; SPBC25B2.01.1; SPBC25B2.01.1:pep; SPBC25B2.01.
DR PomBase; SPBC25B2.01; hbs1.
DR VEuPathDB; FungiDB:SPBC25B2.01; -.
DR eggNOG; KOG0458; Eukaryota.
DR HOGENOM; CLU_007265_3_2_1; -.
DR InParanoid; O74774; -.
DR OMA; ELASWYT; -.
DR PhylomeDB; O74774; -.
DR Reactome; R-SPO-429958; mRNA decay by 3' to 5' exoribonuclease.
DR EvolutionaryTrace; O74774; -.
DR PRO; PR:O74774; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990533; C:Dom34-Hbs1 complex; IDA:PomBase.
DR GO; GO:0005525; F:GTP binding; IDA:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0003747; F:translation release factor activity; IC:PomBase.
DR GO; GO:0002184; P:cytoplasmic translational termination; IC:PomBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:PomBase.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; ISO:PomBase.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR DisProt; DP02049; -.
DR Gene3D; 3.40.50.300; -; 1.
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; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Elongation factor; GTP-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Translation regulation.
FT CHAIN 1..592
FT /note="Elongation factor 1 alpha-like protein"
FT /id="PRO_0000326088"
FT DOMAIN 175..401
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..191
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 240..244
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 261..264
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 323..326
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 363..365
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 13..31
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 184..191
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32769"
FT BINDING 261..265
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32769"
FT BINDING 323..326
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P32769"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 318..323
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 332..346
FT /evidence="ECO:0007829|PDB:3MCA"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 377..380
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 387..392
FT /evidence="ECO:0007829|PDB:3MCA"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 406..415
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 418..431
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 435..438
FT /evidence="ECO:0007829|PDB:3MCA"
FT TURN 439..442
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 443..451
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 453..455
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 466..474
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 493..504
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 515..520
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 525..538
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 548..558
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:3MCA"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 569..572
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 573..592
FT /evidence="ECO:0007829|PDB:3MCA"
SQ SEQUENCE 592 AA; 66016 MW; 44BE2B324C97B455 CRC64;
MSRHRDVKNL DLDDYELDEE PGEEELTEEQ EEEFRSAVAT VRETLLGVPI SEKEIADTVW
YYYFDVEKSV NYLLQKASSK AGAKEKQNTD SQKEKKQNKS KEALADAKDP LDESSNGIKN
LSLNKNDEPA FQTNGEVKMK NSSESDNQPE KKKIKKQNPT DLVSVPEIFE QSNPKPVVHL
VVTGHVDSGK STMLGRIMFE LGEINSRSMQ KLHNEAANSG KGSFSYAWLL DTTEEERARG
VTMDVASTTF ESDKKIYEIG DAPGHRDFIS GMIAGASSAD FAVLVVDSSQ NNFERGFLEN
GQTREHAYLL RALGISEIVV SVNKLDLMSW SEDRFQEIKN IVSDFLIKMV GFKTSNVHFV
PISAISGTNL IQKDSSDLYK WYKGPTLLSA LDQLVPPEKP YRKPLRLSID DVYRSPRSVT
VTGRVEAGNV QVNQVLYDVS SQEDAYVKNV IRNSDPSSTW AVAGDTVTLQ LADIEVNQLR
PGDILSNYEN PVRRVRSFVA EIQTFDIHGP ILSGSTLVLH LGRTVTSVSL KIVTVNNKRS
RHIASRKRAL VRISFLDGLF PLCLAEECPA LGRFILRRSG DTVAAGIVKE LC
