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RBGA_ANOFW
ID   RBGA_ANOFW              Reviewed;         284 AA.
AC   B7GGD6;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Ribosome biogenesis GTPase A {ECO:0000250|UniProtKB:O31743};
GN   Name=rbgA {ECO:0000250|UniProtKB:O31743}; OrderedLocusNames=Aflv_1757;
OS   Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX   NCBI_TaxID=491915;
RN   [1] {ECO:0000312|EMBL:ACJ34118.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21510 / WK1 {ECO:0000312|EMBL:ACJ34118.1};
RX   PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA   Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA   Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA   Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT   "Encapsulated in silica: genome, proteome and physiology of the
RT   thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL   Genome Biol. 9:R161.1-R161.16(2008).
CC   -!- FUNCTION: Required for a late step of 50S ribosomal subunit assembly.
CC       Has GTPase activity. Binds to the 23S rRNA (By similarity).
CC       {ECO:0000250|UniProtKB:O31743}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O31743,
CC       ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. MTG1
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU01058}.
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DR   EMBL; CP000922; ACJ34118.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7GGD6; -.
DR   SMR; B7GGD6; -.
DR   STRING; 491915.Aflv_1757; -.
DR   EnsemblBacteria; ACJ34118; ACJ34118; Aflv_1757.
DR   KEGG; afl:Aflv_1757; -.
DR   eggNOG; COG1161; Bacteria.
DR   HOGENOM; CLU_011106_1_0_9; -.
DR   OMA; GVLWPKF; -.
DR   Proteomes; UP000000742; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1580.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030378; G_CP_dom.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle_sf.
DR   InterPro; IPR019991; GTP-bd_ribosome_bgen.
DR   InterPro; IPR016478; GTPase_MTG1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   PIRSF; PIRSF006230; MG442; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03596; GTPase_YlqF; 1.
DR   PROSITE; PS51721; G_CP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; GTP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW   Ribosome biogenesis; RNA-binding.
FT   CHAIN           1..284
FT                   /note="Ribosome biogenesis GTPase A"
FT                   /id="PRO_0000409879"
FT   DOMAIN          17..182
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   BINDING         61..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O31743"
FT   BINDING         134..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O31743"
FT   BINDING         178
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:O31743"
SQ   SEQUENCE   284 AA;  31752 MW;  FD09A9899FA584AB CRC64;
     MATMTIQWFP GHMAKAKREV TEKLKLIDIV FELVDARIPM SSRNPLIDEI VANKPRIILL
     NKADMADPDV TKQWVDFFAA QQIDAIAIDS QSGTGVKQMV AVAKEKLRSK FEKMMAKGMK
     RPRAMRALIV GIPNVGKSTL INRLAGKHIA KTGDTPGVTK AQQWIKVGKE LELLDTPGIL
     WPKFEDEEVG YKLATTGAIK DTILNLQDVA VYALRFLAAY YPDRLKERYA LADIPEDIVQ
     LFDDIGKKRG CLAAGGVVDY DKVAELVLRD IRTEKLGRLS FDRL
 
 
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