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Database: UniProt
Entry: H0GUT4_SACCK
LinkDB: H0GUT4_SACCK
Original site: H0GUT4_SACCK 
ID   H0GUT4_SACCK            Unreviewed;       180 AA.
AC   H0GUT4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   08-NOV-2023, entry version 36.
DE   SubName: Full=Mnp1p {ECO:0000313|EMBL:EHN02447.1};
GN   ORFNames=VIN7_7110 {ECO:0000313|EMBL:EHN02447.1};
OS   Saccharomyces cerevisiae x Saccharomyces kudriavzevii (strain VIN7)
OS   (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=1095631 {ECO:0000313|EMBL:EHN02447.1, ECO:0000313|Proteomes:UP000009009};
RN   [1] {ECO:0000313|EMBL:EHN02447.1, ECO:0000313|Proteomes:UP000009009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VIN7 {ECO:0000313|EMBL:EHN02447.1,
RC   ECO:0000313|Proteomes:UP000009009};
RX   PubMed=22136070; DOI=10.1111/j.1567-1364.2011.00773.x;
RA   Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA   Pretorius I.S., Egholm M., Chambers P.J.;
RT   "The genome sequence of the wine yeast VIN7 reveals an allotriploid hybrid
RT   genome with Saccharomyces cerevisiae and Saccharomyces kudriavzevii
RT   origins.";
RL   FEMS Yeast Res. 12:88-96(2012).
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000256|ARBA:ARBA00007197}.
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:EHN02447.1}.
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DR   EMBL; AGVY01000213; EHN02447.1; -; Genomic_DNA.
DR   AlphaFoldDB; H0GUT4; -.
DR   HOGENOM; CLU_086499_0_1_1; -.
DR   PhylomeDB; H0GUT4; -.
DR   Proteomes; UP000009009; 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:0006412; P:translation; IEA:InterPro.
DR   CDD; cd00387; Ribosomal_L7_L12; 1.
DR   Gene3D; 3.30.1390.10; -; 1.
DR   Gene3D; 1.20.5.710; Single helix bin; 1.
DR   HAMAP; MF_00368; Ribosomal_L7_L12; 1.
DR   InterPro; IPR000206; Ribosomal_bL12.
DR   InterPro; IPR013823; Ribosomal_bL12_C.
DR   InterPro; IPR014719; Ribosomal_bL12_C/ClpS-like.
DR   InterPro; IPR008932; Ribosomal_bL12_oligo.
DR   InterPro; IPR036235; Ribosomal_bL12_oligo_N_sf.
DR   PANTHER; PTHR45987; 39S RIBOSOMAL PROTEIN L12; 1.
DR   PANTHER; PTHR45987:SF4; 39S RIBOSOMAL PROTEIN L12, MITOCHONDRIAL; 1.
DR   Pfam; PF00542; Ribosomal_L12; 1.
DR   Pfam; PF16320; Ribosomal_L12_N; 1.
DR   SUPFAM; SSF54736; ClpS-like; 1.
DR   SUPFAM; SSF48300; Ribosomal protein L7/12, oligomerisation (N-terminal) domain; 1.
PE   3: Inferred from homology;
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT   DOMAIN          39..87
FT                   /note="Large ribosomal subunit protein bL12
FT                   oligomerization"
FT                   /evidence="ECO:0000259|Pfam:PF16320"
FT   DOMAIN          113..180
FT                   /note="Large ribosomal subunit protein bL12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00542"
FT   REGION          89..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   180 AA;  18878 MW;  7975FAE6D5CFC282 CRC64;
     MKARITPALT SPITISTRFN STTTTAPLPK DKLEPVDPKI TKIVQDISQL TLLETSSLIN
     ELKTALNIPE ISMPMGGFMA GGAGAGAGNL AGSASEAGAG DEEEAKPEAK TVFTVKLDSF
     DAKTKAKVIK EVKGLLGLSL VEAKKFVEAA PKVLKENVAK DDADKIKKTL EDLGAKVSLE
//
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