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IF2B_METB6
ID   IF2B_METB6              Reviewed;         204 AA.
AC   A7I5J0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 71.
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=Mboo_0483;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00232}.
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DR   EMBL; CP000780; ABS55001.1; -; Genomic_DNA.
DR   RefSeq; WP_012106020.1; NC_009712.1.
DR   AlphaFoldDB; A7I5J0; -.
DR   SMR; A7I5J0; -.
DR   STRING; 456442.Mboo_0483; -.
DR   EnsemblBacteria; ABS55001; ABS55001; Mboo_0483.
DR   GeneID; 5410168; -.
DR   KEGG; mbn:Mboo_0483; -.
DR   eggNOG; arCOG01640; Archaea.
DR   HOGENOM; CLU_026663_3_0_2; -.
DR   OMA; GKPDTRL; -.
DR   OrthoDB; 73843at2157; -.
DR   Proteomes; UP000002408; Chromosome.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00232; eIF_2_beta; 1.
DR   InterPro; IPR045196; IF2/IF5.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004458; TIF2_bsu_arc.
DR   InterPro; IPR002792; TRAM_dom.
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   Pfam; PF01938; TRAM; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SUPFAM; SSF100966; SSF100966; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF75689; SSF75689; 1.
DR   TIGRFAMs; TIGR00311; aIF-2beta; 1.
DR   PROSITE; PS50926; TRAM; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..204
FT                   /note="Translation initiation factor 2 subunit beta"
FT                   /id="PRO_1000021648"
FT   DOMAIN          146..204
FT                   /note="TRAM"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00232"
SQ   SEQUENCE   204 AA;  22945 MW;  FA5685B1E5009C25 CRC64;
     MTDSYENLLK KAYSHISEKS ASSERFVVPE AKAYVEGKTT ILENFAEIAD TVRRDKDHLM
     KYMLGELGTS GKIEGNRAIF NGKFEISQIR MIIKSYVDDY VICSECGKPD TRLVKDDRVL
     LLRCDACGGH RPVRKRKART EPASENLEEG QVLDVEIQSL SKRGDGVVKM GRYIMYVSNA
     KPGQSVKIKI SRISGSIVFT ERAE
 
 
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