ID K6TXV8_9EURY Unreviewed; 259 AA.
AC K6TXV8;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Translation initiation factor 2 subunit alpha {ECO:0000256|ARBA:ARBA00013678, ECO:0000256|HAMAP-Rule:MF_00231};
DE AltName: Full=aIF2-alpha {ECO:0000256|ARBA:ARBA00030860, ECO:0000256|HAMAP-Rule:MF_00231};
DE AltName: Full=eIF-2-alpha {ECO:0000256|ARBA:ARBA00033333, ECO:0000256|HAMAP-Rule:MF_00231};
GN Name=eif2a {ECO:0000256|HAMAP-Rule:MF_00231};
GN ORFNames=B655_2070 {ECO:0000313|EMBL:EKQ51957.1};
OS Methanobacterium sp. Maddingley MBC34.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1220534 {ECO:0000313|EMBL:EKQ51957.1, ECO:0000313|Proteomes:UP000001147};
RN [1] {ECO:0000313|EMBL:EKQ51957.1, ECO:0000313|Proteomes:UP000001147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Maddingley MBC34 {ECO:0000313|Proteomes:UP000001147};
RX PubMed=23405289;
RA Rosewarne C.P., Greenfield P., Li D., Tran-Dinh N., Midgley D.J.,
RA Hendry P.;
RT "Draft Genome Sequence of Methanobacterium sp. Maddingley, Reconstructed
RT from Metagenomic Sequencing of a Methanogenic Microbial Consortium Enriched
RT from Coal-Seam Gas Formation Water.";
RL Genome Announc. 1:E00082-12(2013).
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:0000256|ARBA:ARBA00003323, ECO:0000256|HAMAP-Rule:MF_00231}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000256|ARBA:ARBA00011243, ECO:0000256|HAMAP-Rule:MF_00231}.
CC -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC {ECO:0000256|ARBA:ARBA00007223, ECO:0000256|HAMAP-Rule:MF_00231}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ51957.1}.
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DR EMBL; AMGN01000054; EKQ51957.1; -; Genomic_DNA.
DR AlphaFoldDB; K6TXV8; -.
DR STRING; 1220534.B655_2070; -.
DR PATRIC; fig|1220534.3.peg.2051; -.
DR eggNOG; arCOG04107; Archaea.
DR Proteomes; UP000001147; Unassembled WGS sequence.
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; 3.30.70.1130; EIF_2_alpha; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00231; eIF_2_alpha; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR PANTHER; PTHR10602:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 2 SUBUNIT 1; 1.
DR Pfam; PF07541; EIF_2_alpha; 1.
DR Pfam; PF00575; S1; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF110993; eIF-2-alpha, C-terminal domain; 1.
DR SUPFAM; SSF116742; eIF2alpha middle domain-like; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00231};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00231};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00231}.
FT DOMAIN 12..83
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 259 AA; 29222 MW; 24D8455C0FEA80D4 CRC64;
MVRMKHKWPQ EGDLIVATVH KVLNYGAFAK LEEYPGEEAF IHISEVSAGW VKNIRDHVRE
NQKIVARVLR VNPKKGHVDV SMKRIREDQR TRKIQQWKIE QKAEKLLEFA AKSIDKNLDM
AYDEVGYAMM DEFGDLYGAF EISAEEGADS LIERGMDEIW ANAITEVAQK NISPPEVQIT
GYVDLTSYAP DGVDIIRNAL TSINKDNIVV QCVGAPRYRL LVKSSDYITA ETILKDAADE
AIATVLEAGG EGEFHRELE
//
