IF2A_METST
ID IF2A_METST Reviewed; 260 AA.
AC Q2NE59;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor 2 subunit alpha {ECO:0000255|HAMAP-Rule:MF_00231};
DE AltName: Full=aIF2-alpha {ECO:0000255|HAMAP-Rule:MF_00231};
DE AltName: Full=eIF-2-alpha {ECO:0000255|HAMAP-Rule:MF_00231};
GN Name=eif2a {ECO:0000255|HAMAP-Rule:MF_00231}; OrderedLocusNames=Msp_1527;
OS Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS MCB-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX NCBI_TaxID=339860;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA Gottschalk G., Thauer R.K.;
RT "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT intestinal archaeon is restricted to methanol and H2 for methane formation
RT and ATP synthesis.";
RL J. Bacteriol. 188:642-658(2006).
CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis by
CC forming a ternary complex with GTP and initiator tRNA.
CC {ECO:0000255|HAMAP-Rule:MF_00231}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000255|HAMAP-Rule:MF_00231}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_00231}.
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; CP000102; ABC57894.1; -; Genomic_DNA.
DR RefSeq; WP_011407093.1; NC_007681.1.
DR AlphaFoldDB; Q2NE59; -.
DR SMR; Q2NE59; -.
DR STRING; 339860.Msp_1527; -.
DR EnsemblBacteria; ABC57894; ABC57894; Msp_1527.
DR GeneID; 41326103; -.
DR KEGG; mst:Msp_1527; -.
DR eggNOG; arCOG04107; Archaea.
DR HOGENOM; CLU_033458_0_2_2; -.
DR OMA; DVNEHQR; -.
DR OrthoDB; 84684at2157; -.
DR Proteomes; UP000001931; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd04452; S1_IF2_alpha; 1.
DR Gene3D; 1.10.150.190; -; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.70.1130; -; 1.
DR HAMAP; MF_00231; eIF_2_alpha; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR044126; S1_IF2_alpha.
DR InterPro; IPR022964; TIF2_asu_arc.
DR InterPro; IPR024055; TIF2_asu_C.
DR InterPro; IPR024054; TIF2_asu_middle_sf.
DR InterPro; IPR011488; TIF_2_asu.
DR PANTHER; PTHR10602; PTHR10602; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; SSF110993; 1.
DR SUPFAM; SSF116742; SSF116742; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Initiation factor; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..260
FT /note="Translation initiation factor 2 subunit alpha"
FT /id="PRO_1000021646"
FT DOMAIN 12..83
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00231"
SQ SEQUENCE 260 AA; 29509 MW; BA04BD94A999AAA3 CRC64;
MVRMSKEWPE EGDLIVGTVH KVLGYGAFAK LEEYEGKEAF IHISEVSSGW VKNIRDYVRE
NQKIVARVLR VNPKKGHVDA SLKRIREDQR TRRMQQWKIE QKAEKLLEIS AKSINKTLDE
AYDEVGYLIM EEFGDLYEGF ELASDDGENV LLDVDVSPEW AKIITEVAKK NISTPEVQIT
GYVDLTSYKS NGVEIIIEAL QSIESDNVEV QCVGSPTYRI MVTTEDYPTA EKILSEAANK
CIGIVEENDG EGSFHRELED