IF2P_SCHPO
ID IF2P_SCHPO Reviewed; 1079 AA.
AC Q10251;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Eukaryotic translation initiation factor 5B;
DE Short=eIF-5B;
DE EC=3.6.5.3;
DE AltName: Full=Translation initiation factor IF-2;
GN ORFNames=SPAC56F8.03;
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]
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-77; SER-82; SER-127
RP AND THR-364, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Plays a role in translation initiation. Translational GTPase
CC that catalyzes the joining of the 40S and 60S subunits to form the 80S
CC initiation complex with the initiator methionine-tRNA in the P-site
CC base paired to the start codon. GTP binding and hydrolysis induces
CC conformational changes in the enzyme that renders it active for
CC productive interactions with the ribosome. The release of the enzyme
CC after formation of the initiation complex is a prerequisite to form
CC elongation-competent ribosomes. {ECO:0000250|UniProtKB:P39730}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3;
CC Evidence={ECO:0000250|UniProtKB:P39730};
CC -!- COFACTOR:
CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242;
CC Evidence={ECO:0000250|UniProtKB:G0S8G9};
CC Note=Binds 1 monovalent cation per monomer in the active site.
CC Structural cofactor that stabilizes the GTP-bound 'on' state. May also
CC act as a transition state stabilizer of the hydrolysis reaction.
CC {ECO:0000250|UniProtKB:G0S8G9};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39730}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAA93574.1; -; Genomic_DNA.
DR PIR; T38913; T38913.
DR RefSeq; NP_593218.1; NM_001018614.2.
DR AlphaFoldDB; Q10251; -.
DR SMR; Q10251; -.
DR BioGRID; 279669; 2.
DR STRING; 4896.SPAC56F8.03.1; -.
DR iPTMnet; Q10251; -.
DR MaxQB; Q10251; -.
DR PaxDb; Q10251; -.
DR PRIDE; Q10251; -.
DR EnsemblFungi; SPAC56F8.03.1; SPAC56F8.03.1:pep; SPAC56F8.03.
DR GeneID; 2543241; -.
DR KEGG; spo:SPAC56F8.03; -.
DR PomBase; SPAC56F8.03; -.
DR VEuPathDB; FungiDB:SPAC56F8.03; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_1_0_1; -.
DR InParanoid; Q10251; -.
DR OMA; RDVMMAG; -.
DR PhylomeDB; Q10251; -.
DR Reactome; R-SPO-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR PRO; PR:Q10251; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0033290; C:eukaryotic 48S preinitiation complex; ISO:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IC:PomBase.
DR GO; GO:0003924; F:GTPase activity; ISO:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; ISO:PomBase.
DR GO; GO:0002183; P:cytoplasmic translational initiation; ISO:PomBase.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR015760; TIF_IF2.
DR InterPro; IPR023115; TIF_IF2_dom3.
DR InterPro; IPR036925; TIF_IF2_dom3_sf.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Hydrolase; Initiation factor; Metal-binding;
KW Nucleotide-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..1079
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000137295"
FT DOMAIN 482..700
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..498
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 516..520
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 555..558
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 609..612
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 677..679
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 24..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..412
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 491..498
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1079 AA; 119931 MW; 73A01CE933C1F6AA CRC64;
MGKKGKKSGY ADWEDDLGED ISGQNEYLDN TSQDSPQNDE LAEKSENLAV SSEKTTSKKK
KGKKNKGNKN QVSDDESQEL ESPQGPKELT AVTELDDDEF DYKPKKGKKG KKSKKVEEDD
EPQEIESPQG PKELTAVTEL DDDEFDYKPK KGKKGKKAQN NNESEAAAPP EIPEVRVKTK
KEKEREKKER EKLRKKQQQA KKKGSTGEDT LASSEVSSEV DISTPAENDS SAKGKQAAGS
KRKGPNVTAL QKMLEEKRAR EEEEQRIREE EARIAEEEKR LAEVEEARKE EARLKKKEKE
RKKKEEMKAQ GKYLSKKQKE QQALAQRRLQ QMLESGVRVA GLSNGEKKQK PVYTNKKKSN
RSGTSSISSS GILESSPATS ISVDEPQKDS KDDSEKVEKE TEVERKEENE AEAEAVFDDW
EAALEEPEVA ENNEVVTEKK ETDIKSDAVE HSIKDKEDSK TDKVDDIPQA APAESNVSES
DLRSPICCIL GHVDTGKTKL LDNLRRSNVQ EGEAGGITQQ IGATYFPIES IKQKTKVVNK
KGKLQYNIPG LLIIDTPGHE SFTNLRSRGT SLCNIAILVI DIMHGLEPQT IESIRLLRDQ
KTPFVVALNK VDRLYGWHSI KDNAIQDSLS KQKKAIQREF RDRVESIILQ LNEQGLNAAL
YFENKNLGRY VSLVPTSAQS GEGVPDLVAL LISLTQTRMS DRIKYITTLE CTVLEVKVIE
GLGATIDVIL SNGVLHEGDR IVLCGMGGPI ITTVRALLTP QPLKEMRVKS AYVHHKEIKA
AMGVKICAND LEKAVAGSRL LVVGPDDDEE DLAEEIMEDL ENLLGRIDTS GIGVSVQAST
LGSLEALLEF LKQMKIPVAS VNIGPVYKKD VMRCATMLEK AKEYALMLCF DVKVDRDAED
LAEQLGVKIF SANVIYHLFD AFTAHQKKIL EQKREESSDV AVFPCVLKTV AAFNKRDPII
LGVDVVEGVL RINTPIVAVK QLPNGEPQII ELGRVASLEM NHKPVDKVKK GQAGAGVAMK
LESSGSQILF GRQVTESDAL YSHITRQSID SLKDPAFRDE VSRDEWQLII QLKKLFGII
