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Database: UniProt
Entry: I2H5K4_TETBL
LinkDB: I2H5K4_TETBL
Original site: I2H5K4_TETBL 
ID   I2H5K4_TETBL            Unreviewed;       303 AA.
AC   I2H5K4;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Small ribosomal subunit protein uS9m {ECO:0000256|ARBA:ARBA00039318};
DE   AltName: Full=37S ribosomal protein S9, mitochondrial {ECO:0000256|ARBA:ARBA00042623};
GN   Name=TBLA0F01130 {ECO:0000313|EMBL:CCH61656.1};
GN   ORFNames=TBLA_0F01130 {ECO:0000313|EMBL:CCH61656.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH61656.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH61656.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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 uS9 family.
CC       {ECO:0000256|ARBA:ARBA00005251, ECO:0000256|RuleBase:RU003815}.
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DR   EMBL; HE806321; CCH61656.1; -; Genomic_DNA.
DR   RefSeq; XP_004181175.1; XM_004181127.1.
DR   AlphaFoldDB; I2H5K4; -.
DR   STRING; 1071380.I2H5K4; -.
DR   GeneID; 14496765; -.
DR   KEGG; tbl:TBLA_0F01130; -.
DR   eggNOG; KOG1697; Eukaryota.
DR   HOGENOM; CLU_036531_2_1_1; -.
DR   InParanoid; I2H5K4; -.
DR   OMA; RESAMWA; -.
DR   OrthoDB; 1408353at2759; -.
DR   Proteomes; UP000002866; Chromosome 6.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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; 3.30.230.10; -; 1.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR000754; Ribosomal_uS9.
DR   InterPro; IPR020574; Ribosomal_uS9_CS.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   PANTHER; PTHR21569:SF1; 28S RIBOSOMAL PROTEIN S9, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21569; RIBOSOMAL PROTEIN S9; 1.
DR   Pfam; PF00380; Ribosomal_S9; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS00360; RIBOSOMAL_S9; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|RuleBase:RU003815};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980,
KW   ECO:0000256|RuleBase:RU003815}.
FT   REGION          284..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..303
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  35486 MW;  58128DE6127D63E5 CRC64;
     MNICKVLNLH LKPQRFGQLR NFHICNALKY ENERRSYRQF DHSSLSRTIP ALPTFYSSNP
     PHEYRIQRLE SLIKKYAKYP TVQETIRFDQ ENGNMTINKR ERPNWISIDQ YKMIGGDTRL
     KPKQYENLIR LLNRLYQIDG QLSNLEIKEE LNKYLHKPPL SFQAENLHQQ KQLDKYGRAL
     GISHRKTARA KVYVVRGSGE VLVNGRQLNQ YFLKMKDRAN ILKPLQVTQT SGEFNLFILV
     SGGGLTGQSE AAMQAISKAL LIWNPLLKPC LRQAGLMTRD YRHVERKKPG HKKARKMPTW
     VKR
//
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