IF2P_CHATD
ID IF2P_CHATD Reviewed; 1116 AA.
AC G0S8G9;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 2.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Eukaryotic translation initiation factor 5B;
DE Short=eIF-5B;
DE EC=3.6.5.3 {ECO:0000269|PubMed:25225612};
DE AltName: Full=Translation initiation factor IF-2;
GN ORFNames=CTHT_0029840;
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=759272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 517-970 IN COMPLEX WITH GDP, AND
RP FUNCTION.
RX PubMed=24686316; DOI=10.1002/embj.201387344;
RA Kuhle B., Ficner R.;
RT "eIF5B employs a novel domain release mechanism to catalyze ribosomal
RT subunit joining.";
RL EMBO J. 33:1177-1191(2014).
RN [3] {ECO:0007744|PDB:4TMT, ECO:0007744|PDB:4TMV, ECO:0007744|PDB:4TMW, ECO:0007744|PDB:4TMX, ECO:0007744|PDB:4TMZ, ECO:0007744|PDB:4TN1}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 517-858 IN COMPLEXES WITH GTP;
RP MAGNESIUM; POTASSIUM AND SODIUM, COFACTOR, MUTAGENESIS OF ASP-533,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25225612; DOI=10.15252/embj.201488517;
RA Kuhle B., Ficner R.;
RT "A monovalent cation acts as structural and catalytic cofactor in
RT translational GTPases.";
RL EMBO J. 33:2547-2563(2014).
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:0000269|PubMed:24686316,
CC ECO:0000269|PubMed:25225612}.
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:0000269|PubMed:25225612};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:25225612};
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:25225612};
CC Note=Binds 1 monovalent cation per monomer in the active site, which
CC can be sodium or potassium. This structural cofactor stabilizes the
CC GTP-bound 'on' state, and may also act as a transition state stabilizer
CC of the hydrolysis reaction. {ECO:0000269|PubMed:25225612};
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 -!- SEQUENCE CAUTION:
CC Sequence=EGS21143.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL988041; EGS21143.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006693439.1; XM_006693376.1.
DR PDB; 4N3G; X-ray; 3.20 A; A=517-1116.
DR PDB; 4N3N; X-ray; 2.75 A; A=517-1116.
DR PDB; 4NCL; X-ray; 2.12 A; A/B=517-970.
DR PDB; 4NCN; X-ray; 1.87 A; A/B=517-970.
DR PDB; 4TMT; X-ray; 1.58 A; A/B=517-858.
DR PDB; 4TMV; X-ray; 1.53 A; A/B=517-858.
DR PDB; 4TMW; X-ray; 1.55 A; A/B=517-858.
DR PDB; 4TMX; X-ray; 1.50 A; A/B=517-858.
DR PDB; 4TMZ; X-ray; 2.28 A; A/B=517-858.
DR PDB; 4TN1; X-ray; 2.75 A; A/B=517-858.
DR PDBsum; 4N3G; -.
DR PDBsum; 4N3N; -.
DR PDBsum; 4NCL; -.
DR PDBsum; 4NCN; -.
DR PDBsum; 4TMT; -.
DR PDBsum; 4TMV; -.
DR PDBsum; 4TMW; -.
DR PDBsum; 4TMX; -.
DR PDBsum; 4TMZ; -.
DR PDBsum; 4TN1; -.
DR AlphaFoldDB; G0S8G9; -.
DR SMR; G0S8G9; -.
DR STRING; 759272.G0S8G9; -.
DR EnsemblFungi; EGS21143; EGS21143; CTHT_0029840.
DR GeneID; 18257022; -.
DR KEGG; cthr:CTHT_0029840; -.
DR eggNOG; KOG1144; Eukaryota.
DR HOGENOM; CLU_002656_1_0_1; -.
DR OrthoDB; 1124591at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 2.
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 3D-structure; Coiled coil; Cytoplasm; GTP-binding; Hydrolase;
KW Initiation factor; Magnesium; Metal-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1116
FT /note="Eukaryotic translation initiation factor 5B"
FT /id="PRO_0000435808"
FT DOMAIN 521..742
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 1..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..537
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 555..559
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 594..597
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 648..651
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 716..718
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..429
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..478
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 533..538
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24686316,
FT ECO:0000269|PubMed:25225612"
FT BINDING 533
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:25225612,
FT ECO:0007744|PDB:4TMZ"
FT BINDING 533
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:25225612,
FT ECO:0007744|PDB:4TMV, ECO:0007744|PDB:4TMW,
FT ECO:0007744|PDB:4TMX"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25225612"
FT BINDING 549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25225612"
FT BINDING 555..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:25225612"
FT BINDING 555
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000269|PubMed:25225612,
FT ECO:0007744|PDB:4TMZ"
FT BINDING 555
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:25225612,
FT ECO:0007744|PDB:4TMV, ECO:0007744|PDB:4TMW,
FT ECO:0007744|PDB:4TMX"
FT BINDING 557
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:25225612"
FT BINDING 648..651
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24686316,
FT ECO:0000269|PubMed:25225612"
FT BINDING 717..718
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:24686316,
FT ECO:0000269|PubMed:25225612"
FT MUTAGEN 533
FT /note="D->A,R: Reduces GTPase activity 13- to 15-fold."
FT /evidence="ECO:0000269|PubMed:25225612"
FT MUTAGEN 533
FT /note="D->N: No effect on GTPase activity."
FT HELIX 518..520
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 525..531
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 536..544
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 548..551
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 553..555
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:4NCL"
FT STRAND 561..566
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 567..573
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 588..594
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 602..611
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 613..620
FT /evidence="ECO:0007829|PDB:4TMX"
FT TURN 621..623
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 627..639
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 643..648
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 650..652
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 664..669
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 673..692
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:4TMX"
FT TURN 706..708
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 709..714
FT /evidence="ECO:0007829|PDB:4TMX"
FT TURN 717..719
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 723..736
FT /evidence="ECO:0007829|PDB:4TMX"
FT HELIX 740..743
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 749..758
FT /evidence="ECO:0007829|PDB:4TMX"
FT TURN 759..761
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 762..775
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 779..784
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 787..792
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 794..798
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 803..807
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 811..813
FT /evidence="ECO:0007829|PDB:4TMV"
FT STRAND 815..826
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 838..841
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:4NCL"
FT HELIX 848..855
FT /evidence="ECO:0007829|PDB:4TMX"
FT STRAND 872..879
FT /evidence="ECO:0007829|PDB:4NCL"
FT HELIX 880..892
FT /evidence="ECO:0007829|PDB:4NCL"
FT STRAND 897..905
FT /evidence="ECO:0007829|PDB:4NCL"
FT HELIX 907..919
FT /evidence="ECO:0007829|PDB:4NCL"
FT HELIX 921..923
FT /evidence="ECO:0007829|PDB:4NCL"
FT STRAND 925..930
FT /evidence="ECO:0007829|PDB:4NCL"
FT HELIX 935..943
FT /evidence="ECO:0007829|PDB:4NCL"
FT STRAND 947..953
FT /evidence="ECO:0007829|PDB:4NCL"
FT HELIX 954..969
FT /evidence="ECO:0007829|PDB:4NCL"
FT TURN 976..979
FT /evidence="ECO:0007829|PDB:4N3G"
FT STRAND 984..1010
FT /evidence="ECO:0007829|PDB:4N3N"
FT STRAND 1014..1020
FT /evidence="ECO:0007829|PDB:4N3N"
FT TURN 1022..1024
FT /evidence="ECO:0007829|PDB:4N3N"
FT STRAND 1027..1040
FT /evidence="ECO:0007829|PDB:4N3N"
FT STRAND 1043..1049
FT /evidence="ECO:0007829|PDB:4N3N"
FT STRAND 1055..1060
FT /evidence="ECO:0007829|PDB:4N3N"
FT HELIX 1068..1071
FT /evidence="ECO:0007829|PDB:4N3N"
FT STRAND 1078..1080
FT /evidence="ECO:0007829|PDB:4N3N"
FT HELIX 1084..1093
FT /evidence="ECO:0007829|PDB:4N3N"
FT TURN 1095..1097
FT /evidence="ECO:0007829|PDB:4N3N"
FT HELIX 1100..1112
FT /evidence="ECO:0007829|PDB:4N3N"
SQ SEQUENCE 1116 AA; 125348 MW; CBB82903DFC341BD CRC64;
MPPKGKKNRK NDDWDADLGE SIAPVNPAAA APAAAEAPAA AEKEEEAPVG GLMALMRKNK
EKRKKKGLSE DWLDGETPEG QAPAAAPEPD LSAKQAEEAN LEDEWALPDK KGKKGGKQQQ
NKKQQQEEKK KDDEEVPEIR VLTKAEKERL KKEREKQRKK EQAAKKKAAG PAQPQKAEPA
KPAEEEKKPE EPAPAPAPAP EPAAGGSKKK IPAHLRLIQK QQEELRRRQE EEQRRLEEER
RRIEEEERRA EEERKRKEEE KARKKQKEKE KIEQLKREGK YLTKAQREEK ARNQRMLEQM
RAAGIKIAAL EEKNKEEGAA EGEKEKKEKK KPEKKRRPNK VDEQKALEEA AERARQQAEA
AAREAEEKAR LEREKAEAEE KAKQAAAEES VDEDWEAAAE SDKEDVPDSW DAAASDEEKE
EEEEEEEEEE KPAPKKTEKK PEPKTEEKKK AEPKKPEAKK EEVKKPEPKK EEPKKAEANG
KPATTTLPTR SKEEEKPKAA EAEKKEVAAR PKKPVVNKDN LRSPICCILG HVDTGKTKLL
DKIRQTNVQE GEAGGITQQI GATYFPVEAI KQKTAVVNKD GKFEFKVPGL LIIDTPGHES
FSNLRSRGSS LCNIAILVVD IMHGLEPQTI ESLRLLRERK TPFVVALNKI DRLYGWKKIE
NNGFRESFAL QNKAVQNEFR NRLDQVKLQF AEQGFNSELF YENKNFARYV SLVPTSAHTG
EGIPDMLKLI VQLCQERMAS SLMYLSELQA TVLEVKAIEG FGVTIDVILS NGILREGDRI
VLCGLEGPIK TNIRALLTPA PMRELRIKGQ YIHHKEVKAA QGVKISAPGL EGAIAGSRLL
VVGPDDDEEE LEEEVESDLQ SLFSRVEKTG KGVSVQASTL GSLEALLDFL KDCKIPVANV
GIGPVYKRDV MQCGIMLEKA PDYAVMLCFD VKVDKEAQQY ADENGIKIFT ADIIYHLFDQ
FTKHMQEQLE KKKEESKMLA VFPCVLNPVA VFNKTNPIVV GVDVVDGQLK LNTPIAAVKM
NPTTGQKEII SLGRVTGIER DHKPLQVCKK GQPAVAIKIE MGGHQPAYGR HLDEKDVLYS
HISRASIDVL KQFYRDVVTT DEWQLIIKLK SVFDVQ
