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Database: UniProt
Entry: F6EHZ0_HOYSD
LinkDB: F6EHZ0_HOYSD
Original site: F6EHZ0_HOYSD 
ID   F6EHZ0_HOYSD            Unreviewed;       489 AA.
AC   F6EHZ0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=RNA binding S1 domain protein {ECO:0000313|EMBL:AEF39939.1};
GN   OrderedLocusNames=AS9A_1487 {ECO:0000313|EMBL:AEF39939.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 / DQS3-9A1)
OS   (Amycolicicoccus subflavus).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Hoyosellaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF39939.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF39939.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bS1 family.
CC       {ECO:0000256|ARBA:ARBA00006767}.
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DR   EMBL; CP002786; AEF39939.1; -; Genomic_DNA.
DR   RefSeq; WP_013806288.1; NC_015564.1.
DR   AlphaFoldDB; F6EHZ0; -.
DR   STRING; 443218.AS9A_1487; -.
DR   KEGG; asd:AS9A_1487; -.
DR   eggNOG; COG0539; Bacteria.
DR   HOGENOM; CLU_015805_4_1_11; -.
DR   OrthoDB; 9804077at2; -.
DR   Proteomes; UP000009235; Chromosome.
DR   GO; GO:0003676; F:nucleic acid binding; 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; 4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; 4.
DR   PRINTS; PR00681; RIBOSOMALS1.
DR   SMART; SM00316; S1; 4.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 4.
DR   PROSITE; PS50126; S1; 4.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009235}.
FT   DOMAIN          36..105
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          123..188
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          209..277
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          294..363
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          440..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          404..431
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   489 AA;  54220 MW;  CA635D00D5483F51 CRC64;
     MPTTTTTSPQ VAINDIGSAE EFLAAVDATI KYFNDGDIVE GTIVKVDRDE VLLDIGYKTE
     GVIPSRELSI KHDVDPSEVV NVGDEVEALV LTKEDKDGRL ILSKKRAQYE RAWGTIEELK
     EKDEAVKGTV IEVVKGGLIL DIGLRGFLPA SLVEMRRVRD LQPYVGKEIE AKIIELDKNR
     NNVVLSRRAW LEQTQSEVRS EFLHQLQKSQ VRKGVVSSIV NFGAFVDLGG VDGLVHVSEL
     SWKHIDHPSE VVQVGDEVTV EVLDVDMDRE RVSLSLKATQ EDPWRQFART HAIGQIVPGK
     VTKLVPFGAF VRVEEGIEGL VHISELAERH VEVPDQVVAV NDDAMVKVID IDLERRRISL
     SLKQANEEYT EEFDPAKYGM ADSYDEAGNY IFPEGFDPET NEWLEGFEKQ REEWEARYAE
     AERRHKMHTT QMEKFAKVEA EAAEAAPSNY SSDGAAQAPA ASAAPAQSGG TLASDEQLAA
     LREKLSGGA
//
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