ID M0CI03_9EURY Unreviewed; 44 AA.
AC M0CI03;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Small ribosomal subunit protein eS31 {ECO:0000256|HAMAP-Rule:MF_00777};
GN Name=rps27ae {ECO:0000256|HAMAP-Rule:MF_00777};
GN ORFNames=C476_06132 {ECO:0000313|EMBL:ELZ21987.1};
OS Natrinema limicola JCM 13563.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrinema.
OX NCBI_TaxID=1230457 {ECO:0000313|EMBL:ELZ21987.1, ECO:0000313|Proteomes:UP000011615};
RN [1] {ECO:0000313|EMBL:ELZ21987.1, ECO:0000313|Proteomes:UP000011615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13563 {ECO:0000313|EMBL:ELZ21987.1,
RC ECO:0000313|Proteomes:UP000011615};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00777};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00777};
CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00777}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS31 family.
CC {ECO:0000256|HAMAP-Rule:MF_00777}.
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:ELZ21987.1}.
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DR EMBL; AOIT01000029; ELZ21987.1; -; Genomic_DNA.
DR RefSeq; WP_008010935.1; NZ_AOIT01000029.1.
DR AlphaFoldDB; M0CI03; -.
DR STRING; 1230457.C476_06132; -.
DR PATRIC; fig|1230457.4.peg.1226; -.
DR eggNOG; arCOG04183; Archaea.
DR OrthoDB; 25142at2157; -.
DR Proteomes; UP000011615; 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:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR Gene3D; 6.20.50.180; -; 1.
DR HAMAP; MF_00777; Ribosomal_S27ae; 1.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR022845; Ribosomal_eS31_arc.
DR InterPro; IPR011332; Ribosomal_zn-bd.
DR Pfam; PF01599; Ribosomal_S27; 1.
DR SMART; SM01402; Ribosomal_S27; 1.
DR SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00777};
KW Reference proteome {ECO:0000313|Proteomes:UP000011615};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_00777};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_00777};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00777};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00777}.
FT DOMAIN 3..41
FT /note="Small ribosomal subunit protein eS31"
FT /evidence="ECO:0000259|SMART:SM01402"
FT ZN_FING 18..38
FT /note="C4-type"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
FT BINDING 35
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
SQ SEQUENCE 44 AA; 4986 MW; D6B7AE33AE9B02FE CRC64;
MARYDLYNDD GTTSGELCPR CGDVFLADHG DRKHCGKCGY TEWE
//
