EF1B_PYRHO
ID EF1B_PYRHO Reviewed; 91 AA.
AC P58748;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
DE AltName: Full=aEF-1beta;
GN Name=ef1b; OrderedLocusNames=PH0026.1;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP IDENTIFICATION.
RA Michoud K.;
RL Unpublished observations (AUG-2001).
CC -!- FUNCTION: Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus
CC allowing the regeneration of EF-1-alpha/GTP that could then be used to
CC form the ternary complex EF-1-alpha/GTP/AAtRNA. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; BA000001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_010884146.1; NC_000961.1.
DR PDB; 2YY3; X-ray; 2.50 A; A/B/C=1-91.
DR PDB; 7CSL; X-ray; 2.00 A; C/D=1-91.
DR PDBsum; 2YY3; -.
DR PDBsum; 7CSL; -.
DR AlphaFoldDB; P58748; -.
DR SMR; P58748; -.
DR GeneID; 1443928; -.
DR OMA; VMPNSPE; -.
DR OrthoDB; 124073at2157; -.
DR EvolutionaryTrace; P58748; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR HAMAP; MF_00043; EF1_beta; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR004542; Transl_elong_EF1B_B_arc.
DR PANTHER; PTHR39647; PTHR39647; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR PIRSF; PIRSF006521; Transl_elong_EF1B_B_arc; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR TIGRFAMs; TIGR00489; aEF-1_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Elongation factor; Protein biosynthesis.
FT CHAIN 1..91
FT /note="Elongation factor 1-beta"
FT /id="PRO_0000155065"
FT STRAND 6..16
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 37..47
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 50..59
FT /evidence="ECO:0007829|PDB:7CSL"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:7CSL"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:7CSL"
SQ SEQUENCE 91 AA; 10353 MW; C48B142ABF8625F2 CRC64;
MSDFNLVGVI RVMPTDPDVN LDELEEKLKK VIPEKYGLAK VEREPIAFGL VALKFYVLGR
DEEGYSFDEV AEKFEEVENV ESAEVETVSR I