IF6_SACS2
ID IF6_SACS2 Reviewed; 223 AA.
AC Q980G0;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 96.
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=SSO0351;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, INTERACTION WITH L14 (RPL14P), SUBUNIT, SUBCELLULAR LOCATION,
RP POSSIBLE POST-TRANSLATIONAL MODIFICATION, INDUCTION, AND RRNA-BINDING.
RX PubMed=19036786; DOI=10.1093/nar/gkn959;
RA Benelli D., Marzi S., Mancone C., Alonzi T., la Teana A., Londei P.;
RT "Function and ribosomal localization of aIF6, a translational regulator
RT shared by archaea and eukarya.";
RL Nucleic Acids Res. 37:256-267(2009).
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. Inhibits translation of both leadered and leaderless mRNAs,
CC maybe by binding to the 50S ribosome subunit, preventing it from
CC binding to the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_00032,
CC ECO:0000269|PubMed:19036786}.
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit, specifically with
CC protein L14. Binds to 23S rRNA, possibly between where the 30S and 50S
CC subunits associate to initiate translation.
CC {ECO:0000269|PubMed:19036786}.
CC -!- INDUCTION: Constitutively expressed, further induced by cold (60) or
CC heat (90 degrees Celsius) shock (at protein level).
CC {ECO:0000269|PubMed:19036786}.
CC -!- PTM: Modified in an unknown fashion (not phosphorylation) following
CC release from 50S ribosomal subunits.
CC -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000255|HAMAP-
CC Rule:MF_00032}.
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DR EMBL; AE006641; AAK40681.1; -; Genomic_DNA.
DR PIR; B90178; B90178.
DR RefSeq; WP_009990645.1; NC_002754.1.
DR AlphaFoldDB; Q980G0; -.
DR SMR; Q980G0; -.
DR STRING; 273057.SSO0351; -.
DR EnsemblBacteria; AAK40681; AAK40681; SSO0351.
DR GeneID; 44129322; -.
DR KEGG; sso:SSO0351; -.
DR PATRIC; fig|273057.12.peg.342; -.
DR eggNOG; arCOG04176; Archaea.
DR HOGENOM; CLU_071894_1_0_2; -.
DR InParanoid; Q980G0; -.
DR OMA; GEDTTGP; -.
DR PhylomeDB; Q980G0; -.
DR Proteomes; UP000001974; 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:0019843; F:rRNA binding; IEA:UniProtKB-KW.
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 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 Initiation factor; Protein biosynthesis; Reference proteome; RNA-binding;
KW rRNA-binding; Stress response.
FT CHAIN 1..223
FT /note="Translation initiation factor 6"
FT /id="PRO_0000153759"
SQ SEQUENCE 223 AA; 24373 MW; 764B8D4CDA444C68 CRC64;
MNLQRLSVFG TDNIGVYIYT NNKYTIIPRG LDSETKENIA QVLGTELLEA EISRSFLLGI
FISGNDNGIL LPKSTIDDEF RFLKENLRDC RVEILNSKVT ALGNTILANN KAALIYPEFN
DIEEKIIKET LGVEDIKRGK IAQMITVGSV GVITNKGGLV HVDTSEKELK ELEKLFGVKI
DIGTVNFGSV FIKSGLVAND KGTLVGASTT GPEILRIQKA LGE