IF2B_PYRFU
ID IF2B_PYRFU Reviewed; 140 AA.
AC Q8U3I5;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor 2 subunit beta {ECO:0000255|HAMAP-Rule:MF_00232};
DE AltName: Full=aIF2-beta {ECO:0000255|HAMAP-Rule:MF_00232};
DE AltName: Full=eIF-2-beta {ECO:0000255|HAMAP-Rule:MF_00232};
GN Name=eif2b {ECO:0000255|HAMAP-Rule:MF_00232}; OrderedLocusNames=PF0481;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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_00232}.
CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma chain.
CC {ECO:0000255|HAMAP-Rule:MF_00232}.
CC -!- INTERACTION:
CC Q8U3I5; Q8U082: eif2g; NbExp=2; IntAct=EBI-2505077, EBI-2504997;
CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000255|HAMAP-
CC Rule:MF_00232}.
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DR EMBL; AE009950; AAL80605.1; -; Genomic_DNA.
DR RefSeq; WP_011011598.1; NZ_CP023154.1.
DR PDB; 2D74; X-ray; 2.80 A; B=1-140.
DR PDB; 2DCU; X-ray; 3.40 A; B=1-140.
DR PDBsum; 2D74; -.
DR PDBsum; 2DCU; -.
DR AlphaFoldDB; Q8U3I5; -.
DR SMR; Q8U3I5; -.
DR DIP; DIP-54411N; -.
DR IntAct; Q8U3I5; 2.
DR STRING; 186497.PF0481; -.
DR PRIDE; Q8U3I5; -.
DR EnsemblBacteria; AAL80605; AAL80605; PF0481.
DR GeneID; 41712282; -.
DR KEGG; pfu:PF0481; -.
DR PATRIC; fig|186497.12.peg.504; -.
DR eggNOG; arCOG01640; Archaea.
DR HOGENOM; CLU_026663_3_1_2; -.
DR OMA; NVKHHKS; -.
DR OrthoDB; 96453at2157; -.
DR PhylomeDB; Q8U3I5; -.
DR EvolutionaryTrace; Q8U3I5; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00232; eIF_2_beta; 1.
DR InterPro; IPR045196; IF2/IF5.
DR InterPro; IPR004458; TIF2_bsu_arc.
DR InterPro; IPR002735; Transl_init_fac_IF2/IF5_dom.
DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR PANTHER; PTHR23001; PTHR23001; 1.
DR Pfam; PF01873; eIF-5_eIF-2B; 1.
DR SMART; SM00653; eIF2B_5; 1.
DR SUPFAM; SSF100966; SSF100966; 1.
DR SUPFAM; SSF75689; SSF75689; 1.
DR TIGRFAMs; TIGR00311; aIF-2beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Initiation factor; Protein biosynthesis; Reference proteome.
FT CHAIN 1..140
FT /note="Translation initiation factor 2 subunit beta"
FT /id="PRO_0000137430"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:2D74"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:2D74"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2D74"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:2D74"
SQ SEQUENCE 140 AA; 16234 MW; 771153C98A871359 CRC64;
MEIDYYDYEK LLEKAYQELP ENVKHHKSRF EVPGALVTIE GNKTIIENFK DIADALNRDP
QHLLKFLLRE IATAGTLEGR RVVLQGRFTP YLIANKLKKY IKEYVICPVC GSPDTKIIKR
DRFHFLKCEA CGAETPIQHL
