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IF1A_AERPE
ID   IF1A_AERPE              Reviewed;         111 AA.
AC   P57676; Q05E50;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Translation initiation factor 1A;
DE            Short=aIF-1A;
GN   Name=eIF1A; OrderedLocusNames=APE_0749.1;
OS   Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS   K1).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Aeropyrum.
OX   NCBI_TaxID=272557;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX   PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA   Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA   Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA   Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA   Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA   Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT   "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT   Aeropyrum pernix K1.";
RL   DNA Res. 6:83-101(1999).
CC   -!- FUNCTION: Seems to be required for maximal rate of protein
CC       biosynthesis. Enhances ribosome dissociation into subunits and
CC       stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal
CC       subunits (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}.
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DR   EMBL; BA000002; BAF34751.1; -; Genomic_DNA.
DR   AlphaFoldDB; P57676; -.
DR   SMR; P57676; -.
DR   STRING; 272557.APE_0748a; -.
DR   PRIDE; P57676; -.
DR   EnsemblBacteria; BAF34751; BAF34751; APE_0748a.
DR   KEGG; ape:APE_0748a; -.
DR   eggNOG; arCOG01179; Archaea.
DR   OMA; ADITWRY; -.
DR   Proteomes; UP000002518; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd05793; S1_IF1A; 1.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00216; aIF_1A; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR   InterPro; IPR001253; TIF_eIF-1A.
DR   InterPro; IPR018104; TIF_eIF-1A_CS.
DR   PANTHER; PTHR21668; PTHR21668; 1.
DR   Pfam; PF01176; eIF-1a; 1.
DR   SMART; SM00652; eIF1a; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   PROSITE; PS01262; IF1A; 1.
DR   PROSITE; PS50832; S1_IF1_TYPE; 1.
PE   3: Inferred from homology;
KW   Initiation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..111
FT                   /note="Translation initiation factor 1A"
FT                   /id="PRO_0000145114"
FT   DOMAIN          12..86
FT                   /note="S1-like"
SQ   SEQUENCE   111 AA;  12736 MW;  4BFCF934E7F663E3 CRC64;
     MARGRGRHER RGEMPLPSED EGTMLCIVQR VVGAGFLEVL CTDGEVYMAR IPGKMRRRVW
     MREGDVVLFL PWGTADKKGE VVYRYLRDEV RKLIDMNLLP EELVEEVAGA E
 
 
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