ID A0A0A0L4Q7_CUCSA Unreviewed; 142 AA.
AC A0A0A0L4Q7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=S1-like domain-containing protein {ECO:0000259|PROSITE:PS50832};
GN ORFNames=Csa_4G637710 {ECO:0000313|EMBL:KGN55131.1};
OS Cucumis sativus (Cucumber).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN55131.1, ECO:0000313|Proteomes:UP000029981};
RN [1] {ECO:0000313|EMBL:KGN55131.1, ECO:0000313|Proteomes:UP000029981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX PubMed=19881527; DOI=10.1038/ng.475;
RA Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT "The genome of the cucumber, Cucumis sativus L.";
RL Nat. Genet. 41:1275-1281(2009).
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit
CC to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps
CC modulate mRNA selection, yielding the 30S pre-initiation complex (PIC).
CC Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are
CC released leaving the mature 70S translation initiation complex.
CC {ECO:0000256|ARBA:ARBA00003935}.
CC -!- SUBUNIT: Component of the 30S ribosomal translation pre-initiation
CC complex which assembles on the 30S ribosome in the order IF-2 and IF-3,
CC IF-1 and N-formylmethionyl-tRNA(fMet); mRNA recruitment can occur at
CC any time during PIC assembly. {ECO:0000256|ARBA:ARBA00011599}.
CC -!- SIMILARITY: Belongs to the IF-1 family.
CC {ECO:0000256|ARBA:ARBA00010939}.
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DR EMBL; CM002925; KGN55131.1; -; Genomic_DNA.
DR RefSeq; XP_011654076.1; XM_011655774.1.
DR AlphaFoldDB; A0A0A0L4Q7; -.
DR STRING; 3659.A0A0A0L4Q7; -.
DR EnsemblPlants; KGN55131; KGN55131; Csa_4G637710.
DR GeneID; 101206284; -.
DR Gramene; KGN55131; KGN55131; Csa_4G637710.
DR KEGG; csv:101206284; -.
DR eggNOG; ENOG502S8M9; Eukaryota.
DR OrthoDB; 1054at2759; -.
DR Proteomes; UP000029981; Chromosome 4.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd04451; S1_IF1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_00075; IF_1; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR006196; RNA-binding_domain_S1_IF1.
DR InterPro; IPR003029; S1_domain.
DR InterPro; IPR004368; TIF_IF1.
DR NCBIfam; TIGR00008; infA; 1.
DR PANTHER; PTHR33370; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR33370:SF1; TRANSLATION INITIATION FACTOR IF-1, CHLOROPLASTIC; 1.
DR Pfam; PF01176; eIF-1a; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50832; S1_IF1_TYPE; 1.
PE 3: Inferred from homology;
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|PROSITE-
KW ProRule:PRU00181}; Plastid {ECO:0000256|ARBA:ARBA00022528};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|PROSITE-
KW ProRule:PRU00181}; Reference proteome {ECO:0000313|Proteomes:UP000029981}.
FT DOMAIN 61..135
FT /note="S1-like"
FT /evidence="ECO:0000259|PROSITE:PS50832"
SQ SEQUENCE 142 AA; 15917 MW; DF02EC01F8692D8A CRC64;
MSSTNLLQFP LLQSHFRPPS TLLFPAVKSH LSLASISFPT SQFLHTPSHA SPAFVLMAKS
PKNDTSEQKL SHEGSVVESL PNGMFRVRLD NQDLILGYIS GKIRKNFVRI LPGDRVRVEV
SRYDSTKGRI VYRMRSTKDS SS
//
