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Database: UniProt
Entry: A0A0N1LHC1_9PROT
LinkDB: A0A0N1LHC1_9PROT
Original site: A0A0N1LHC1_9PROT 
ID   A0A0N1LHC1_9PROT        Unreviewed;       574 AA.
AC   A0A0N1LHC1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=IP88_03815 {ECO:0000313|EMBL:KPF78447.1};
OS   alpha proteobacterium AAP81b.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria.
OX   NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF78447.1, ECO:0000313|Proteomes:UP000037971};
RN   [1] {ECO:0000313|EMBL:KPF78447.1, ECO:0000313|Proteomes:UP000037971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP81b {ECO:0000313|EMBL:KPF78447.1,
RC   ECO:0000313|Proteomes:UP000037971};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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|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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPF78447.1}.
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DR   EMBL; LJHX01000033; KPF78447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1LHC1; -.
DR   STRING; 1523432.IP88_03815; -.
DR   PATRIC; fig|1523432.3.peg.1933; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000037971; 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; 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; 5.
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:UP000037971};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:KPF78447.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          28..94
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          112..178
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          199..267
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          284..354
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          371..441
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          464..533
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   574 AA;  62807 MW;  1EE3FE2F46815763 CRC64;
     MASLAQPTRD DFAAMLESSL GKNQSFEGRV VRGIVTGIEN DLAVIDVGLK SEGRVPLREF
     AGLDGKHNIS VGDEVEVYVD RVENANGEAM LSRDRARREA SWDTLEAQFA AAERVEGVIF
     GRVKGGFTVD LNGAVAFLPG SQVDIRPVRD VTPLMNLPQP FQILKMDRKR GNIVVSRRAI
     LEESRAEQRT GLISSLAEGQ IVDGTVKNIT DYGAFVDLGG IDGLLHVTDM SYKRVNHPSE
     VLNIGDVLRV QIVRINRETQ RISLGMKQLE ADPWTTASQK YSVGSRHKGR VTNITEYGAF
     VELEAGIEGL VHVSEMSWVK KNVHPGKIVS TSQEVEVIVL EVDDDKRRIS LGLKQAQRNP
     WEVFAEQHPV GSDLEGEVKN ATEFGLFIGL DGEVDGMVHM SDIAWGLTGE AALSRHHKGE
     RVRARVLEID IEKERISLGI KQMEEGPARV ITTPTAGGTG LNKNEIVTAT VVTARDGGID
     VQLGDDGPVV FIKRGDLSRD RDEQRAERFQ PGQKVDAMVI GFEKGRRPML SIKAMQISEE
     KEAVAQYGTS DSGATLGNIL GAAFNKARED ADKN
//
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