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Database: UniProt
Entry: A0A0D1YFE9_9EURO
LinkDB: A0A0D1YFE9_9EURO
Original site: A0A0D1YFE9_9EURO 
ID   A0A0D1YFE9_9EURO        Unreviewed;       350 AA.
AC   A0A0D1YFE9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=40S ribosomal protein S27 {ECO:0000256|RuleBase:RU000671};
GN   ORFNames=PV11_07140 {ECO:0000313|EMBL:KIV79589.1};
OS   Exophiala sideris.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV79589.1, ECO:0000313|Proteomes:UP000053599};
RN   [1] {ECO:0000313|EMBL:KIV79589.1, ECO:0000313|Proteomes:UP000053599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV79589.1,
RC   ECO:0000313|Proteomes:UP000053599};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala sideris CBS121828.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU000671};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU000671};
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS27 family.
CC       {ECO:0000256|ARBA:ARBA00010919, ECO:0000256|RuleBase:RU000671}.
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DR   EMBL; KN846953; KIV79589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D1YFE9; -.
DR   STRING; 1016849.A0A0D1YFE9; -.
DR   HOGENOM; CLU_051938_2_0_1; -.
DR   OrthoDB; 517134at2759; -.
DR   Proteomes; UP000053599; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 2.20.25.100; Zn-binding ribosomal proteins; 1.
DR   HAMAP; MF_00371; Ribosomal_S27e; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR005645; FSH-like_dom.
DR   InterPro; IPR000592; Ribosomal_eS27.
DR   InterPro; IPR023407; Ribosomal_eS27_Zn-bd_dom_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   PANTHER; PTHR48070; ESTERASE OVCA2; 1.
DR   PANTHER; PTHR48070:SF6; ESTERASE OVCA2; 1.
DR   Pfam; PF03959; FSH1; 1.
DR   Pfam; PF01667; Ribosomal_S27e; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS01168; RIBOSOMAL_S27E; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU000671};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU000671};
KW   Ribosomal protein {ECO:0000256|RuleBase:RU000671,
KW   ECO:0000313|EMBL:KIV79589.1}; Zinc {ECO:0000256|RuleBase:RU000671};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000671}.
FT   DOMAIN          11..243
FT                   /note="Serine hydrolase"
FT                   /evidence="ECO:0000259|Pfam:PF03959"
SQ   SEQUENCE   350 AA;  38185 MW;  6113397917512B85 CRC64;
     MPSAKESNAG MKILMLHGYT QSGALFHAKT RATEKRLQKA FPGISFSYPT GPLRLRPSDV
     PGFDPASSED PDSIEAYGWW RRADTADPPE YVGLEDGLQT VAKVLETEGP FDGVIGFSQG
     AALAAMVTSL LEGESRKQAF EKAKSRSPLA ISYPASFEKL DHPPFKFCAA YCGFRAPGER
     YRGFYEDPHI QTPVCHFIGS LDSVVEESRT QALVDATGGL EKTQVVTHPG GHFVPSGKPY
     LDAIAAFIQQ KMSSQDQKKD QEERVEDMDV LAVDLLNPTP QAEARKHKLK TLVPAPRSFF
     MDVKCPGCFT ITTVFSHAQT VVVCAGCSTV LCQPTGGKAR LTEGCSFRRK
//
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