IF1A1_METAC
ID IF1A1_METAC Reviewed; 111 AA.
AC Q8TSA3;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor 1A 1;
DE Short=aIF-1A 1;
GN Name=eIF1A1; OrderedLocusNames=MA_0895;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM04334.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TSA3; -.
DR SMR; Q8TSA3; -.
DR STRING; 188937.MA_0895; -.
DR EnsemblBacteria; AAM04334; AAM04334; MA_0895.
DR KEGG; mac:MA_0895; -.
DR HOGENOM; CLU_109098_1_2_2; -.
DR InParanoid; Q8TSA3; -.
DR OMA; ADITWRY; -.
DR PhylomeDB; Q8TSA3; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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 TIGRFAMs; TIGR00523; eIF-1A; 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 1"
FT /id="PRO_0000145118"
FT DOMAIN 22..96
FT /note="S1-like"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 111 AA; 12918 MW; B0CAEECEDAA8D5BF CRC64;
MTLADLKKPT SRATPSTEET FTRVRTPRRE NNEILATVES LLGANRLRLR CMDGVVRMGR
IPGSMKKKTW IREGDVVIVV PWEFQNEKAD VIWKYTRPQV DWLERKGYLK G