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IF5A_CALMQ
ID   IF5A_CALMQ              Reviewed;         132 AA.
AC   A8MD73;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Translation initiation factor 5A {ECO:0000255|HAMAP-Rule:MF_00085};
DE   AltName: Full=Hypusine-containing protein {ECO:0000255|HAMAP-Rule:MF_00085};
DE   AltName: Full=eIF-5A {ECO:0000255|HAMAP-Rule:MF_00085};
GN   Name=eIF5A; OrderedLocusNames=Cmaq_0895;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions by promoting the formation of the first peptide
CC       bond. {ECO:0000255|HAMAP-Rule:MF_00085}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00085}.
CC   -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000255|HAMAP-
CC       Rule:MF_00085}.
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DR   EMBL; CP000852; ABW01729.1; -; Genomic_DNA.
DR   RefSeq; WP_012185948.1; NC_009954.1.
DR   AlphaFoldDB; A8MD73; -.
DR   SMR; A8MD73; -.
DR   STRING; 397948.Cmaq_0895; -.
DR   EnsemblBacteria; ABW01729; ABW01729; Cmaq_0895.
DR   GeneID; 5709626; -.
DR   KEGG; cma:Cmaq_0895; -.
DR   eggNOG; arCOG04277; Archaea.
DR   HOGENOM; CLU_102600_3_0_2; -.
DR   OMA; QIMDMET; -.
DR   OrthoDB; 98221at2157; -.
DR   Proteomes; UP000001137; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045901; P:positive regulation of translational elongation; IEA:InterPro.
DR   GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR   Gene3D; 2.30.30.30; -; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00085; eIF_5A; 1.
DR   InterPro; IPR001884; IF5A-like.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014722; Rib_L2_dom2.
DR   InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR   InterPro; IPR022847; Transl_elong_IF5A_arc.
DR   InterPro; IPR020189; Transl_elong_IF5A_C.
DR   InterPro; IPR013185; Transl_elong_KOW-like.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11673; PTHR11673; 1.
DR   Pfam; PF08207; EFP_N; 1.
DR   Pfam; PF01287; eIF-5a; 1.
DR   PIRSF; PIRSF003025; eIF5A; 1.
DR   SMART; SM01376; eIF-5a; 1.
DR   SUPFAM; SSF50104; SSF50104; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00037; eIF_5A; 1.
DR   PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hypusine; Initiation factor; Protein biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..132
FT                   /note="Translation initiation factor 5A"
FT                   /id="PRO_1000093006"
FT   MOD_RES         36
FT                   /note="Hypusine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00085"
SQ   SEQUENCE   132 AA;  14432 MW;  C7CEA3D5DA27296A CRC64;
     MSTRTASAGD IKEGSYIMID NMPCRVVEVE KSKTGKHGSA KARIVGIGVI DGVKRTIVVP
     TDAAVEVPVI EKFTAQVISI SGDSVQLMDL RNYQTFEIPS SYIEDEAKGK LEPGVQVEVW
     DVAGYKKIMR TR
 
 
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