IF6_METJA
ID IF6_METJA Reviewed; 228 AA.
AC Q60357;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_00032};
DE Short=aIF-6 {ECO:0000255|HAMAP-Rule:MF_00032};
GN Name=eif6 {ECO:0000255|HAMAP-Rule:MF_00032}; OrderedLocusNames=MJ0048;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, MASS SPECTROMETRY, AND X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS).
RX PubMed=11101899; DOI=10.1038/82017;
RA Groft C.M., Beckmann R., Sali A., Burley S.K.;
RT "Crystal structures of ribosome anti-association factor IF6.";
RL Nat. Struct. Biol. 7:1156-1164(2000).
CC -!- FUNCTION: Binds to the 50S ribosomal subunit and prevents its
CC association with the 30S ribosomal subunit to form the 70S initiation
CC complex. {ECO:0000255|HAMAP-Rule:MF_00032,
CC ECO:0000269|PubMed:11101899}.
CC -!- MASS SPECTROMETRY: Mass=24948; Mass_error=6; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11101899};
CC -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000255|HAMAP-
CC Rule:MF_00032}.
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DR EMBL; L77117; AAB98029.1; -; Genomic_DNA.
DR PIR; H64305; H64305.
DR PDB; 1G61; X-ray; 1.30 A; A/B=1-228.
DR PDBsum; 1G61; -.
DR AlphaFoldDB; Q60357; -.
DR SMR; Q60357; -.
DR STRING; 243232.MJ_0048; -.
DR EnsemblBacteria; AAB98029; AAB98029; MJ_0048.
DR KEGG; mja:MJ_0048; -.
DR eggNOG; arCOG04176; Archaea.
DR HOGENOM; CLU_071894_1_0_2; -.
DR InParanoid; Q60357; -.
DR OMA; GEDTTGP; -.
DR PhylomeDB; Q60357; -.
DR EvolutionaryTrace; Q60357; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IBA:GO_Central.
DR GO; GO:0043023; F:ribosomal large subunit binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IBA:GO_Central.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0000470; P:maturation of LSU-rRNA; IBA:GO_Central.
DR GO; GO:0042256; P:mature ribosome assembly; IEA:InterPro.
DR CDD; cd00527; IF6; 1.
DR HAMAP; MF_00032; eIF_6; 1.
DR InterPro; IPR002769; eIF6.
DR PANTHER; PTHR10784; PTHR10784; 1.
DR Pfam; PF01912; eIF-6; 1.
DR PIRSF; PIRSF006413; IF-6; 1.
DR SMART; SM00654; eIF6; 1.
DR TIGRFAMs; TIGR00323; eIF-6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..228
FT /note="Translation initiation factor 6"
FT /id="PRO_0000153746"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 59..62
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 78..90
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 122..127
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 128..135
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1G61"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1G61"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1G61"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:1G61"
FT HELIX 215..225
FT /evidence="ECO:0007829|PDB:1G61"
SQ SEQUENCE 228 AA; 24459 MW; 94DA7E11C10FCB47 CRC64;
MTMIIRKYFS GIPTIGVLAL TTEEITLLPI FLDKDDVNEV SEVLETKCLQ TNIGGSSLVG
SLSVANKYGL LLPKIVEDEE LDRIKNFLKE NNLDLNVEII KSKNTALGNL ILTNDKGALI
SPELKDFKKD IEDSLNVEVE IGTIAELPTV GSNAVVTNKG CLTHPLVEDD ELEFLKSLFK
VEYIGKGTAN KGTTSVGACI IANSKGAVVG GDTTGPELLI IEDALGLI
