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Database: UniProt
Entry: A0A1F0FW19_9PORP
LinkDB: A0A1F0FW19_9PORP
Original site: A0A1F0FW19_9PORP 
ID   A0A1F0FW19_9PORP        Unreviewed;       596 AA.
AC   A0A1F0FW19;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN   ORFNames=HMPREF3027_06340 {ECO:0000313|EMBL:OFO52542.1};
OS   Porphyromonas sp. HMSC077F02.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC   Porphyromonas.
OX   NCBI_TaxID=1739529 {ECO:0000313|EMBL:OFO52542.1, ECO:0000313|Proteomes:UP000178655};
RN   [1] {ECO:0000313|Proteomes:UP000178655}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMSC077F02 {ECO:0000313|Proteomes:UP000178655};
RA   Mitreva M., Pepin K.H., Mihindukulasuriya K.A., Fulton R., Fronick C.,
RA   O'Laughlin M., Miner T., Herter B., Rosa B.A., Cordes M., Tomlinson C.,
RA   Wollam A., Palsikar V.B., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2016) 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:OFO52542.1}.
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DR   EMBL; LTSX01000146; OFO52542.1; -; Genomic_DNA.
DR   RefSeq; WP_018029043.1; NZ_KV820675.1.
DR   AlphaFoldDB; A0A1F0FW19; -.
DR   STRING; 1739529.HMPREF3027_06340; -.
DR   Proteomes; UP000178655; 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; 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:SF7; 30S RIBOSOMAL PROTEIN S1, CHLOROPLASTIC; 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:UP000178655};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW   Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW   ECO:0000313|EMBL:OFO52542.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT   DOMAIN          47..110
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          128..194
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          215..283
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          300..370
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          387..457
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   DOMAIN          474..539
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          542..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  67258 MW;  4ADF41F0536AB321 CRC64;
     MKNYYEEVKP LEGFDWDSFE RATEESPESI KKMEEQYAAT MGEVSEGEIV TGTVESISKR
     EVIVDVGFKS FGVVSSAEFR YNPDLAVGDK VEVYVEVQEN KEGQLILSHR KAMQARAWER
     INEAMEKQEV VKGFIKNRTR GGMIVEIFGI EAFLPGSQID VKPIRDFDEF VGKTMEFRII
     KVNEEYKNVV VSHKALIEEE LEAQRSEIIS KLEKGQVLEG TVKNIVPYGA FIDLGGVDGL
     IHITDLSWGR IRTPEEVVSL DEKINVVILD FDEERNRIAL GLKQLTPHPW DSLDENLKVG
     DKVEGTVVVI TEYGAFVEVL PGVEGLIHVS EMSWTQHVRS PHDLLKVGEK VEAQILTLDR
     EDRKMSLGIK QLTPDPWADI ESKYPVGSRH TAKVRNFTNF GIFVEFEDGI DGLIHISDLS
     WTKRIKHPSE FTKIGDDIDV VVLEIDKENR RLSLGHKQTT TDPWENLGTV FSVGTIHQGK
     IVELLDRGAV IELPHGIEGF ATPKHLVKED GKQAELGETL DFKVIEFNSD SKRIILSHSR
     IREDQEKGAR QEERAAAQAT REMIRQESAQ AEKSTLGDID ALAALRDKIE KANSEE
//
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