ID L0G0E4_ECHVK Unreviewed; 592 AA.
AC L0G0E4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN OrderedLocusNames=Echvi_2093 {ECO:0000313|EMBL:AGA78345.1};
OS Echinicola vietnamensis (strain DSM 17526 / LMG 23754 / KMM 6221).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Echinicola.
OX NCBI_TaxID=926556 {ECO:0000313|EMBL:AGA78345.1, ECO:0000313|Proteomes:UP000010796};
RN [1] {ECO:0000313|Proteomes:UP000010796}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17526 / LMG 23754 / KMM 6221
RC {ECO:0000313|Proteomes:UP000010796};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Echinicola vietnamensis DSM 17526.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds mRNA; thus facilitating recognition of the initiation
CC point. It is needed to translate mRNA with a short Shine-Dalgarno (SD)
CC purine-rich sequence. {ECO:0000256|PIRNR:PIRNR002111}.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC {ECO:0000256|ARBA:ARBA00006767, ECO:0000256|PIRNR:PIRNR002111}.
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DR EMBL; CP003346; AGA78345.1; -; Genomic_DNA.
DR RefSeq; WP_015265905.1; NC_019904.1.
DR AlphaFoldDB; L0G0E4; -.
DR STRING; 926556.Echvi_2093; -.
DR KEGG; evi:Echvi_2093; -.
DR PATRIC; fig|926556.3.peg.2215; -.
DR eggNOG; COG0539; Bacteria.
DR HOGENOM; CLU_015805_2_0_10; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000010796; Chromosome.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd05687; S1_RPS1_repeat_ec1_hs1; 1.
DR CDD; cd04465; S1_RPS1_repeat_ec2_hs2; 1.
DR CDD; cd05688; S1_RPS1_repeat_ec3; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 6.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000110; Ribosomal_bS1.
DR InterPro; IPR035104; Ribosomal_protein_S1-like.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF13; 30S RIBOSOMAL PROTEIN S1; 1.
DR Pfam; PF00575; S1; 6.
DR PIRSF; PIRSF002111; RpsA; 3.
DR PRINTS; PR00681; RIBOSOMALS1.
DR SMART; SM00316; S1; 6.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 6.
DR PROSITE; PS50126; S1; 6.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000010796};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:AGA78345.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 43..106
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 124..190
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 211..279
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 296..366
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 385..455
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 472..537
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 541..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 66034 MW; B85B2AB1CEAFCE71 CRC64;
MSNNEDFNWD KFETKGFGEG YTSAERAEME KLYDETLTEI SEKEVIKGTV VGINDKDVII
NIGFKSDGLV PRTEFRDLPD LKIGDEVELF IEEQENALGQ LVLSRKKAKM VRAWQDIEDA
LEYDNVIEGL VKRRTKGGLI VDIYGVEAFL PGSQIDVKPI RDFDVYVGKK MEVKVVKINH
ANDNVVVSHK VLIEKDLEKQ KAEILNNLEK GQVLEGVIKN MTNFGVFIDL GGVDGLLHIT
DISWGRINHP EEVLNLDDKV QVVVLDFDDD KKRISLGMKQ LTAHPWDSLS AELEVGSKVK
GKIVNVADYG AFLELAPGVE GLIHVSEMSW SQHLRNPADF VKVGDEIEAV VLTLDKEERK
MSLGIKQLTE DPWTKQDMVT KYAVGTKHQG VVRNLTNFGL FLELEEGIDG LVHVSDLSWT
KKIKHPSEYV KVNDELEVVV LELDVDNRRL ALGHKQLEEN PWDTFEGVFP VGSSHKCTVV
SKNDKGAVLE LPYGLEGFAT IKNLEKEDGS QVEVGDAVDF VVTEFSKDDK RIVLSHTATF
REDAMPSKQP AKKAPSTAKK KPAGGDPQEK STLGDLDALS ALKEKMEGGD KK
//
