ID   A0A0B7N9R5_9FUNG        Unreviewed;       555 AA.
AC   A0A0B7N9R5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   08-NOV-2023, entry version 31.
DE   RecName: Full=40S ribosomal protein S27 {ECO:0000256|RuleBase:RU000671};
GN   Name=PARPA_05601.1 scaffold 18730 {ECO:0000313|EMBL:CEP11719.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11719.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP11719.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11719.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) 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; LN726786; CEP11719.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7N9R5; -.
DR   STRING; 35722.A0A0B7N9R5; -.
DR   OrthoDB; 2728187at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
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   CDD; cd07992; LPLAT_AAK14816-like; 1.
DR   Gene3D; 2.20.25.100; Zn-binding ribosomal proteins; 1.
DR   HAMAP; MF_00371; Ribosomal_S27e; 1.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   InterPro; IPR000592; Ribosomal_eS27.
DR   InterPro; IPR023407; Ribosomal_eS27_Zn-bd_dom_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   PANTHER; PTHR31605; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR   PANTHER; PTHR31605:SF0; GLYCEROL-3-PHOSPHATE O-ACYLTRANSFERASE 1; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   Pfam; PF01667; Ribosomal_S27e; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS01168; RIBOSOMAL_S27E; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|RuleBase:RU000671};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU000671};
KW   Ribosomal protein {ECO:0000256|RuleBase:RU000671};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|RuleBase:RU000671};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000671}.
FT   TRANSMEM        321..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..167
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   555 AA;  62519 MW;  20BB93A60285B83A CRC64;
     MPFGFYHEVV CTVSRSALWS FFSDIKLEDV DNVPPESQPL IVAATHHNMI IDPAVLSVTF
     PNKRRLHYWA KDSMFKNPYA ASFLTDCGVV PVDRKTKNNS LLYAATFDVL KLGEAVAVFP
     EGTSHTLPRL GAFKDGTSFA ALEYAKINQD EGLNKCAPIL PVGIVYPEKS KYRSVVIVKY
     GKPISIEPYL PLYLQDPKKA AKQLTKATEQ AMEQLTVNAP DWESKYAADM ARWLLFPGEN
     GLMKDYIPIT QSLINAMHTL GEKDVEIAKL QKSLVIYKLE LEALLLKDAQ IAKYNEKNIT
     AISTTVQLLQ RTAASLVDLP LFLPGLVAHL PLYVAGYIAG HVEIYEEVRA QNKIFFGMAL
     VPLIYLGAFI WGWFALFGGT FFGFFTALAT LGVFVWYHVT SIDERYENFK DLQGRWRLFD
     AVVLGRGMWR RKDRILGLKK LRTESLTRVR NMITTYKSTN DDVHVVWLAL RQRLAIDLLN
     PSVEHEKRSH KLKRLVQSPN SYFMDVKCPG CLNISTVFSH AQTVVLCSSC GTVLCQPTGG
     RARLTEGCSF RRKAN
//