ID A0A137P582_CONC2 Unreviewed; 160 AA.
AC A0A137P582;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Nucleic acid-binding protein {ECO:0000313|EMBL:KXN70081.1};
DE Flags: Fragment;
GN ORFNames=CONCODRAFT_39798 {ECO:0000313|EMBL:KXN70081.1};
OS Conidiobolus coronatus (strain ATCC 28846 / CBS 209.66 / NRRL 28638)
OS (Delacroixia coronata).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC Entomophthoromycotina; Entomophthoromycetes; Entomophthorales;
OC Ancylistaceae; Conidiobolus.
OX NCBI_TaxID=796925 {ECO:0000313|EMBL:KXN70081.1, ECO:0000313|Proteomes:UP000070444};
RN [1] {ECO:0000313|EMBL:KXN70081.1, ECO:0000313|Proteomes:UP000070444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 28638 {ECO:0000313|EMBL:KXN70081.1,
RC ECO:0000313|Proteomes:UP000070444};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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. {ECO:0000256|ARBA:ARBA00025502}.
CC -!- SIMILARITY: Belongs to the eIF-1A family.
CC {ECO:0000256|RuleBase:RU004364}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KQ964513; KXN70081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A137P582; -.
DR STRING; 796925.A0A137P582; -.
DR EnsemblFungi; KXN70081; KXN70081; CONCODRAFT_39798.
DR OMA; RKKVWMS; -.
DR OrthoDB; 2919581at2759; -.
DR Proteomes; UP000070444; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00523; eIF-1A; 1.
DR PANTHER; PTHR21668; EIF-1A; 1.
DR PANTHER; PTHR21668:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 4C; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00652; eIF1a; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|PROSITE-ProRule:PRU00181};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protein biosynthesis {ECO:0000256|PROSITE-ProRule:PRU00181};
KW Reference proteome {ECO:0000313|Proteomes:UP000070444};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..89
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXN70081.1"
SQ SEQUENCE 160 AA; 18763 MW; 0D04D1E945F54730 CRC64;
GGKNRRRGKN DTEGDKRELV FKEEGQEYAQ VLKLLGNGRI DAQCFDGVKR LALIRGKMRK
KVWINAGDIV LLSLRDFQDD KADVILKYNP DEARMLKSYG ELPDNAQINE TTMFGEEDDD
DVEFDDVEID DVILFLFFYF IKLLTYKFFR FNQFLSWNLL
//
