ID A0A1G0NAL7_9PROT Unreviewed; 573 AA.
AC A0A1G0NAL7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=30S ribosomal protein S1 {ECO:0000256|PIRNR:PIRNR002111};
GN ORFNames=A2580_15465 {ECO:0000313|EMBL:OGU20481.1};
OS Hydrogenophilales bacterium RIFOXYD1_FULL_62_11.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1798415 {ECO:0000313|EMBL:OGU20481.1, ECO:0000313|Proteomes:UP000179278};
RN [1] {ECO:0000313|EMBL:OGU20481.1, ECO:0000313|Proteomes:UP000179278}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGU20481.1}.
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DR EMBL; MGZO01000115; OGU20481.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0NAL7; -.
DR Proteomes; UP000179278; 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 CDD; cd05689; S1_RPS1_repeat_ec4; 1.
DR CDD; cd05691; S1_RPS1_repeat_ec6; 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 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; 5.
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 Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ribonucleoprotein {ECO:0000256|PIRNR:PIRNR002111};
KW Ribosomal protein {ECO:0000256|PIRNR:PIRNR002111,
KW ECO:0000313|EMBL:OGU20481.1}; RNA-binding {ECO:0000256|PIRNR:PIRNR002111}.
FT DOMAIN 32..98
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 116..182
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 203..271
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 288..358
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 375..445
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT DOMAIN 462..531
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 573 AA; 62880 MW; E2960B4ED6DA3DA5 CRC64;
MSTATASTNL DSMDDFAAMF EESLEHQEMR QGEVITAEIV GIDGNFVTVN AGLKSESLIP
IEEFKNDLGE IEAKIGDFVA VAIESIEDGF GATKLSRERA KKLAAWLDLE VAMNEGRIVT
GMVQGKVKGG LTVLVGGLRA FLPGSLVDTR PVKDTTPFEY KEMEFKVIKL DRKRNNVVVS
RRAVLEETMG ADREAMMENL KEGSIVKGVV KNITDYGAFV DLGGIDGLLH ITDMAWRRVK
HPSEVVTVGM ELEAKILRYD TEKNRVSLGI KQLGDDPWVG IARRYPQGTR MFGKVANLTD
YGAFVEIEAG IEGLVHVSEM DWTNKNVSPN KIVQLGDEVE VMVLDIDEDK RRISLGMKQC
KSNPWEDFSM NFKKGDKVSG AIKSITDFGV FIGLAGGIDG LVHLSDLSWN VPGEEAVQNF
RKGQDVEAVV LGIDLERERI SLGIKQIEGD PLTSYATGNE KGSIVKGTIK TVEAKGATVQ
LDSDMEGYLR ASEVSRDRVE DMRTHYKEGD EIEAMIINVD RKNRVINLSI KAKDMTEQDS
AMKKMAADTS AAATGSTNLG ALLKAKLENK NAE
//
