(data stored in ACNUC7421 zone)

SWISSPROT: Q3IFN2_PSEHT

ID   Q3IFN2_PSEHT            Unreviewed;       352 AA.
AC   Q3IFN2;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 90.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA {ECO:0000256|HAMAP-Rule:MF_01820};
DE            EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_01820};
GN   Name=rsgA {ECO:0000256|HAMAP-Rule:MF_01820};
GN   OrderedLocusNames=PSHAa0487 {ECO:0000313|EMBL:CAI85583.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85583.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85583.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: One of several proteins that assist in the late
CC       maturation steps of the functional core of the 30S ribosomal
CC       subunit. Helps release RbfA from mature subunits. May play a role
CC       in the assembly of ribosomal proteins into the subunit. Circularly
CC       permuted GTPase that catalyzes slow GTP hydrolysis, GTPase
CC       activity is stimulated by the 30S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00828801}.
CC   -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC       rRNA. {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00828796}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
CC       ECO:0000256|SAAS:SAAS00820346}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC       RsgA subfamily. {ECO:0000256|SAAS:SAAS00720088}.
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DR   EMBL; CR954246; CAI85583.1; -; Genomic_DNA.
DR   RefSeq; WP_011327196.1; NC_007481.1.
DR   ProteinModelPortal; Q3IFN2; -.
DR   STRING; 326442.PSHAa0487; -.
DR   EnsemblBacteria; CAI85583; CAI85583; PSHAa0487.
DR   GeneID; 32566240; -.
DR   KEGG; pha:PSHAa0487; -.
DR   eggNOG; ENOG4105E06; Bacteria.
DR   eggNOG; COG1162; LUCA.
DR   HOGENOM; HOG000006957; -.
DR   KO; K06949; -.
DR   OMA; FRDCKHL; -.
DR   OrthoDB; POG091H01WX; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-HAMAP.
DR   CDD; cd01854; YjeQ_EngC; 1.
DR   HAMAP; MF_01820; GTPase_RsgA; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004881; Ribosome_biogen_GTPase_RsgA.
DR   InterPro; IPR010914; RsgA_GTPase_dom.
DR   PANTHER; PTHR32120; PTHR32120; 1.
DR   Pfam; PF03193; RsgA_GTPase; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00157; TIGR00157; 1.
DR   PROSITE; PS50936; ENGC_GTPASE; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3IFN2.
DR   SWISS-2DPAGE; Q3IFN2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00820338};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698892};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720101, ECO:0000313|EMBL:CAI85583.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720208};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00698882};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720213};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720223};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_01820,
KW   ECO:0000256|SAAS:SAAS00720235};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_01820, ECO:0000256|SAAS:SAAS00720226}.
FT   DOMAIN      109    277       CP-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51721}.
FT   DOMAIN      126    275       EngC GTPase. {ECO:0000259|PROSITE:
FT                                PS50936}.
FT   NP_BIND     165    168       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   NP_BIND     219    227       GTP. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       301    301       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       306    306       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       308    308       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
FT   METAL       314    314       Zinc. {ECO:0000256|HAMAP-Rule:MF_01820}.
SQ   SEQUENCE   352 AA;  39048 MW;  DA92CDE79F59955B CRC64;
     MAKQKKLSKG QSRQIKANHQ KRISSADARP AKKGAQEWQT DNLGQVESAI VISRFGQHAD
     VEVESGEVLR CNIRRTVSNL VCGDEVLFRR AKVSEGDLAG VIEATQERRS QLTRPDFYDG
     VKVIAANIDQ ILMVSAVLPE FTPSIIDRYL IACEDMGIEP ILVLNKIDLI DAQGLSEIQK
     VLDVYRKLDY KVLLVSNIST DGIDELKDVL VGKNNIFVGQ SGVGKSTLVN TVLPDAEILT
     KEVSENSGLG QHTTTVSRLH HLPSGGNLID SPGIREFGLW HLEVDRVTWC FKEFREFIGG
     CRFRDCKHLN DPGCIIKEAV ADGKISQLRF DSYHRILETM ADGRAGSRAP RV
//

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