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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//