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Database: UniProt
Entry: A0A142X1Z6_9PLAN
LinkDB: A0A142X1Z6_9PLAN
Original site: A0A142X1Z6_9PLAN 
ID   A0A142X1Z6_9PLAN        Unreviewed;       593 AA.
AC   A0A142X1Z6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   Name=rpsA_1 {ECO:0000313|EMBL:AMV21103.1};
GN   ORFNames=VT03_24585 {ECO:0000313|EMBL:AMV21103.1};
OS   Planctomyces sp. SH-PL14.
OC   Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC   Planctomycetaceae; Planctomyces.
OX   NCBI_TaxID=1632864 {ECO:0000313|EMBL:AMV21103.1, ECO:0000313|Proteomes:UP000076318};
RN   [1] {ECO:0000313|EMBL:AMV21103.1, ECO:0000313|Proteomes:UP000076318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH-PL14 {ECO:0000313|EMBL:AMV21103.1,
RC   ECO:0000313|Proteomes:UP000076318};
RA   van der Voort M., Raaijmakers J.M.;
RT   "Genome minning of novel planctomycete species.";
RL   Submitted (APR-2015) 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; CP011270; AMV21103.1; -; Genomic_DNA.
DR   RefSeq; WP_075095395.1; NZ_CP011270.1.
DR   AlphaFoldDB; A0A142X1Z6; -.
DR   STRING; 1632864.VT03_24585; -.
DR   KEGG; pls:VT03_24585; -.
DR   PATRIC; fig|1632864.3.peg.5642; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000076318; 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; 2.
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: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:UP000076318};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:AMV21103.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          49..113
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          131..207
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          228..296
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          313..383
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          400..470
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          488..553
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          552..593
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  66258 MW;  0D6A8794AABEE80E CRC64;
     MVDRNLIREF QVSDEDLEAE LGDVLRQLDD GEGYADQIYD ETAQSFDVNQ LVKGVVLSID
     GDDVLVDIGY KSEGTVHLSE WGDDEEKPKT GDTIEVLLEE VEDNYGLVLL SKRKADRARE
     WIWFTTNFKE GDKVSGTVTR QIKGGLLVNI SQGASTAPPG QGINLFLPAS QVDIRRPQRI
     EAYIGQHIDC VVLKIDETRR NVVVSRRKLI EDMRAEMKRN LLAEISEGQI RKGVVKNIAD
     FGAFVDLGGI DGLLHITDMS WKRIHHPTEM VKIDDEIEVK ILHIDREKEK IALGLKQKLP
     SPWENVSQKY PVGSRVEGEV VNVMNYGAFV KLEDGIEGLV HISEMSWTKR VSHPDELVKK
     GDKVEVVVLN INTDKQEISL GMKQTQPNPW DNVTAKYPIG TTVTGTVRNL TNYGAFIELE
     EGVDGLLHVS DMSWTRKISN PSEMLKKGDV LTCQVISVDE VRKRIALGMK QLENDPWENR
     IPQQYKPGSI VEGKVTKITN FGVFVELEEQ LEGLLHVSEL GEAGEDQLKV GDSVQVKILR
     IDTDDRKIGL SRKLDAPVEQ PEVTQSDRPA APKELKGGMG DTGGPLFQMP GKN
//
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