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Database: UniProt
Entry: K9VYF0_9CYAN
LinkDB: K9VYF0_9CYAN
Original site: K9VYF0_9CYAN 
ID   K9VYF0_9CYAN            Unreviewed;       137 AA.
AC   K9VYF0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Small ribosomal subunit protein uS9 {ECO:0000256|HAMAP-Rule:MF_00532};
GN   Name=rpsI {ECO:0000256|HAMAP-Rule:MF_00532};
GN   Synonyms=rps9 {ECO:0000256|HAMAP-Rule:MF_00532};
GN   ORFNames=Cri9333_2289 {ECO:0000313|EMBL:AFZ13158.1};
OS   Crinalium epipsammum PCC 9333.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC   Crinalium.
OX   NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ13158.1, ECO:0000313|Proteomes:UP000010472};
RN   [1] {ECO:0000313|EMBL:AFZ13158.1, ECO:0000313|Proteomes:UP000010472}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ13158.1,
RC   ECO:0000313|Proteomes:UP000010472};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS9 family.
CC       {ECO:0000256|ARBA:ARBA00005251, ECO:0000256|HAMAP-Rule:MF_00532,
CC       ECO:0000256|RuleBase:RU003815}.
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DR   EMBL; CP003620; AFZ13158.1; -; Genomic_DNA.
DR   RefSeq; WP_015203272.1; NC_019753.1.
DR   AlphaFoldDB; K9VYF0; -.
DR   STRING; 1173022.Cri9333_2289; -.
DR   KEGG; cep:Cri9333_2289; -.
DR   PATRIC; fig|1173022.3.peg.2477; -.
DR   eggNOG; COG0103; Bacteria.
DR   HOGENOM; CLU_046483_2_1_3; -.
DR   OrthoDB; 9803965at2; -.
DR   Proteomes; UP000010472; Chromosome.
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:UniProtKB-UniRule.
DR   Gene3D; 3.30.230.10; -; 1.
DR   HAMAP; MF_00532_B; Ribosomal_S9_B; 1.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR000754; Ribosomal_uS9.
DR   InterPro; IPR023035; Ribosomal_uS9_bac/plastid.
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:UP000010472};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW   Rule:MF_00532};
KW   Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW   Rule:MF_00532}.
FT   REGION          100..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..137
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   137 AA;  15181 MW;  D948EA68EC79ED26 CRC64;
     MQATDQSGRA VYWGTGRRKS SVARVRLVPG SGQMIINGRP GEQYFQFNSN YISAAKAPLE
     TLGLENEYDI LVNAHGGGLT GQSDSVRLGV ARALCELDPD NRKPLKTEGY LTRDPRATER
     KKYGLHKARK APQYSKR
//
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