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Database: UniProt
Entry: H2AS71_KAZAF
LinkDB: H2AS71_KAZAF
Original site: H2AS71_KAZAF 
ID   H2AS71_KAZAF            Unreviewed;       167 AA.
AC   H2AS71;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   08-NOV-2023, entry version 46.
DE   RecName: Full=Ribosomal protein L7/L12 C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=KAFR0C02280 {ECO:0000313|EMBL:CCF57221.1};
GN   ORFNames=KAFR_0C02280 {ECO:0000313|EMBL:CCF57221.1};
OS   Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS   1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57221.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF57221.1, ECO:0000313|Proteomes:UP000005220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC   NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX   PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA   Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA   Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT   accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL12 family.
CC       {ECO:0000256|ARBA:ARBA00007197}.
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DR   EMBL; HE650823; CCF57221.1; -; Genomic_DNA.
DR   RefSeq; XP_003956356.1; XM_003956307.1.
DR   AlphaFoldDB; H2AS71; -.
DR   STRING; 1071382.H2AS71; -.
DR   GeneID; 13885140; -.
DR   KEGG; kaf:KAFR_0C02280; -.
DR   eggNOG; KOG1715; Eukaryota.
DR   HOGENOM; CLU_086499_0_1_1; -.
DR   InParanoid; H2AS71; -.
DR   OrthoDB; 2787370at2759; -.
DR   Proteomes; UP000005220; Chromosome 3.
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   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT   DOMAIN          35..75
FT                   /note="Large ribosomal subunit protein bL12
FT                   oligomerization"
FT                   /evidence="ECO:0000259|Pfam:PF16320"
FT   DOMAIN          100..166
FT                   /note="Large ribosomal subunit protein bL12 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00542"
SQ   SEQUENCE   167 AA;  18400 MW;  1306591D50A81866 CRC64;
     MLRLGTLRAT QMIARPVMSS VRCLTRYNST VSNEKLESIV DSISKLNILE TSNLVTLLKE
     RLNIPDINMG APMMMSNVNT ATDTNETKET SAAEEEKTTF TIKLESFDAK SKAKIIKEIK
     SLLGLSLVDA KKFVESAPKV IKDNISKDDA SSIKDTLEKL GGKISME
//
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