ID A0A239PYZ1_9PROT Unreviewed; 569 AA.
AC A0A239PYZ1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN ORFNames=SAMN06297382_2709 {ECO:0000313|EMBL:SNT75380.1};
OS Amphiplicatus metriothermophilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Parvularculales;
OC Parvularculaceae; Amphiplicatus.
OX NCBI_TaxID=1519374 {ECO:0000313|EMBL:SNT75380.1, ECO:0000313|Proteomes:UP000198346};
RN [1] {ECO:0000313|EMBL:SNT75380.1, ECO:0000313|Proteomes:UP000198346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12710 {ECO:0000313|EMBL:SNT75380.1,
RC ECO:0000313|Proteomes:UP000198346};
RA Sun Z.S., Albrecht U., Echele G., Lee C.C.;
RL Submitted (JUL-2017) 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|ARBA:ARBA00025604,
CC 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; FZQA01000008; SNT75380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239PYZ1; -.
DR OrthoDB; 9804077at2; -.
DR Proteomes; UP000198346; Unassembled WGS sequence.
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; 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 NCBIfam; TIGR00717; rpsA; 1.
DR PANTHER; PTHR10724; 30S RIBOSOMAL PROTEIN S1; 1.
DR PANTHER; PTHR10724:SF7; 30S RIBOSOMAL PROTEIN S1, CHLOROPLASTIC; 1.
DR Pfam; PF00575; S1; 6.
DR PIRSF; PIRSF002111; RpsA; 1.
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:UP000198346};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:SNT75380.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 30..96
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 114..180
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 201..270
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 287..357
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 374..444
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 455..531
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 569 AA; 62916 MW; F7F273D1DD726F9D CRC64;
MSATETLNPS RDAFAEMLEA SLVDRKEFEE TVVKGVVTAI EKDAAVVDIG LKTEGRVPLK
EFAQAGKPAD LKVGDEVEVY VERVENANGE AVLSREKARR EEAWERLEKM FDKGERVEGV
IFNRVKGGFT VDLGGAVAFL PGSQVDIRPV RDAGPLMNIP QPFRILKMDK RRGNIVVSRR
AVLEEDRAEH RQEVVREMNE GDVREGVVKN ITDYGAFVEL APGVDGLLHV TDMSWSRVNH
PSEVLGVNDT VKVKIIKINP ETHRISLGIK QLQPDPWEGV AAKYPVGAKF RGRVTNITDY
GAFVELEEGI EGLVHVSEMS WVKKNVHPGK VVSTSQEVEV MVLEVDENKR RISLGLKQCL
DNPWERFAED HPIGSIIEGE IKNITEFGLF VGLTEEMDGM VHLSDLDWNR PGEEAIKDYR
KGQVVKAKVL DVDPEKERIS LGIKQVGSDP LDSVGEIRKG DDVTCTVTAI ETGGIEVQVG
GEGGPKAFIR KSDLSKDRAE QRPDRFAVGD KVDARVISFD RVTRRIGLSI KAREVAEEKE
AVEQYGSADA GASLGDILGA ALKEREKKE
//