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Database: UniProt
Entry: H2AP51_KAZAF
LinkDB: H2AP51_KAZAF
Original site: H2AP51_KAZAF 
ID   H2AP51_KAZAF            Unreviewed;       230 AA.
AC   H2AP51;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=37S ribosomal protein S17, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   Name=KAFR0A07170 {ECO:0000313|EMBL:CCF56151.1};
GN   ORFNames=KAFR_0A07170 {ECO:0000313|EMBL:CCF56151.1};
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:CCF56151.1, ECO:0000313|Proteomes:UP000005220};
RN   [1] {ECO:0000313|EMBL:CCF56151.1, 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 universal ribosomal protein uS17 family.
CC       {ECO:0000256|ARBA:ARBA00010254}.
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DR   EMBL; HE650821; CCF56151.1; -; Genomic_DNA.
DR   RefSeq; XP_003955286.1; XM_003955237.1.
DR   AlphaFoldDB; H2AP51; -.
DR   STRING; 1071382.H2AP51; -.
DR   GeneID; 13886283; -.
DR   KEGG; kaf:KAFR_0A07170; -.
DR   eggNOG; KOG1740; Eukaryota.
DR   HOGENOM; CLU_1246209_0_0_1; -.
DR   InParanoid; H2AP51; -.
DR   OrthoDB; 297148at2759; -.
DR   Proteomes; UP000005220; Chromosome 1.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000266; Ribosomal_uS17.
DR   PANTHER; PTHR10744:SF1; 37S RIBOSOMAL PROTEIN S17, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10744; 40S RIBOSOMAL PROTEIN S11 FAMILY MEMBER; 1.
DR   Pfam; PF00366; Ribosomal_S17; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980}.
FT   COILED          160..194
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   230 AA;  27051 MW;  CD38E1846DC22028 CRC64;
     MARQNLIGMV VSQGKMQKTV KVRVESKLFN KKINKELFHR KDYLVHDEGE VSREGDLVRI
     EATRPISKRK FFSIAEILRN KGQQFAQYQY QVKSDVAKEE ALKTQQFLER RSHTEAQDNS
     ILLKDVRMIQ NALSKGQSVE ELEEIKKRYG ITEFSQDTLK EILKLNVSDL QEKLTQQRSK
     IDSLHEKLDE FMNDDNKAID YLKKHGIEDP TLLQKNIKRN ILRKHLLQEL
//
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