ID A1RXC8_THEPD Unreviewed; 53 AA.
AC A1RXC8;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Small ribosomal subunit protein eS31 {ECO:0000256|HAMAP-Rule:MF_00777};
GN Name=rps27ae {ECO:0000256|HAMAP-Rule:MF_00777};
GN OrderedLocusNames=Tpen_0449 {ECO:0000313|EMBL:ABL77858.1};
OS Thermofilum pendens (strain DSM 2475 / Hrk 5).
OC Archaea; Thermoproteota; Thermoprotei; Thermofilales; Thermofilaceae;
OC Thermofilum.
OX NCBI_TaxID=368408 {ECO:0000313|EMBL:ABL77858.1, ECO:0000313|Proteomes:UP000000641};
RN [1] {ECO:0000313|Proteomes:UP000000641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2475 / Hrk 5 {ECO:0000313|Proteomes:UP000000641};
RX PubMed=18263724; DOI=10.1128/JB.01949-07;
RA Anderson I., Rodriguez J., Susanti D., Porat I., Reich C., Ulrich L.E.,
RA Elkins J.G., Mavromatis K., Lykidis A., Kim E., Thompson L.S., Nolan M.,
RA Land M., Copeland A., Lapidus A., Lucas S., Detter C., Zhulin I.B.,
RA Olsen G.J., Whitman W., Mukhopadhyay B., Bristow J., Kyrpides N.;
RT "Genome sequence of Thermofilum pendens reveals an exceptional loss of
RT biosynthetic pathways without genome reduction.";
RL J. Bacteriol. 190:2957-2965(2008).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00777}.
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DR EMBL; CP000505; ABL77858.1; -; Genomic_DNA.
DR AlphaFoldDB; A1RXC8; -.
DR STRING; 368408.Tpen_0449; -.
DR EnsemblBacteria; ABL77858; ABL77858; Tpen_0449.
DR KEGG; tpe:Tpen_0449; -.
DR eggNOG; arCOG04183; Archaea.
DR HOGENOM; CLU_179743_1_0_2; -.
DR OrthoDB; 25142at2157; -.
DR Proteomes; UP000000641; Chromosome.
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:UP000000641};
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 4..49
FT /note="Small ribosomal subunit protein eS31"
FT /evidence="ECO:0000259|SMART:SM01402"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00777"
SQ SEQUENCE 53 AA; 6331 MW; B22E7BDC761259C5 CRC64;
MAKVHELYEY DYKTGTIRLK NKKCPRCGSI MAHHLKPVER WHCGKCGYTE YRT
//