RSGA1_ARATH
ID RSGA1_ARATH Reviewed; 433 AA.
AC Q4V399; O64802;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_01820};
DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_01820};
DE AltName: Full=Protein EMBRYO DEFECTIVE 1688 {ECO:0000303|PubMed:15266054};
DE Flags: Precursor;
GN Name=rsgA {ECO:0000255|HAMAP-Rule:MF_01820};
GN Synonyms=EMB1688 {ECO:0000303|PubMed:15266054};
GN OrderedLocusNames=At1g67440 {ECO:0000312|Araport:AT1G67440};
GN ORFNames=T1F15.10 {ECO:0000312|EMBL:AAC18791.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
CC -!- FUNCTION: One of several proteins that assist in the late maturation
CC steps of the functional core of the 30S ribosomal subunit. Helps
CC release RbfA from mature subunits. May play a role in the assembly of
CC ribosomal proteins into the subunit. Circularly permuted GTPase that
CC catalyzes slow GTP hydrolysis, GTPase activity is stimulated by the 30S
CC ribosomal subunit (By similarity). Required for embryo development
CC (PubMed:15266054). {ECO:0000255|HAMAP-Rule:MF_01820,
CC ECO:0000269|PubMed:15266054}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01820};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01820};
CC -!- SUBUNIT: Monomer. Associates with 30S ribosomal subunit, binds 16S
CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Embryo defective. {ECO:0000269|PubMed:15266054}.
CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. RsgA
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01820}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18791.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC004393; AAC18791.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34646.1; -; Genomic_DNA.
DR EMBL; BT023457; AAY56448.1; -; mRNA.
DR PIR; T02162; T02162.
DR RefSeq; NP_176911.2; NM_105411.3.
DR AlphaFoldDB; Q4V399; -.
DR SMR; Q4V399; -.
DR STRING; 3702.AT1G67440.1; -.
DR iPTMnet; Q4V399; -.
DR PaxDb; Q4V399; -.
DR EnsemblPlants; AT1G67440.1; AT1G67440.1; AT1G67440.
DR GeneID; 843064; -.
DR Gramene; AT1G67440.1; AT1G67440.1; AT1G67440.
DR KEGG; ath:AT1G67440; -.
DR Araport; AT1G67440; -.
DR TAIR; locus:2197618; AT1G67440.
DR eggNOG; ENOG502QRR1; Eukaryota.
DR HOGENOM; CLU_033617_4_0_1; -.
DR InParanoid; Q4V399; -.
DR PhylomeDB; Q4V399; -.
DR PRO; PR:Q4V399; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q4V399; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0009658; P:chloroplast organization; IMP:TAIR.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd01854; YjeQ_EngC; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01820; GTPase_RsgA; 1.
DR InterPro; IPR030378; G_CP_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00157; TIGR00157; 1.
DR PROSITE; PS50936; ENGC_GTPASE; 1.
DR PROSITE; PS51721; G_CP; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Hydrolase; Metal-binding; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA-binding;
KW Transit peptide; Zinc.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..433
FT /note="Small ribosomal subunit biogenesis GTPase RsgA 1,
FT mitochondrial"
FT /id="PRO_0000439700"
FT DOMAIN 113..291
FT /note="CP-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..220
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
FT BINDING 330
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01820"
SQ SEQUENCE 433 AA; 49155 MW; 278BE85FA75D628A CRC64;
MLRAKHIGKN YSSSLSPVLS PEHKPSLLES QAIGTVATAQ ANFMRVIVQD VANSVTSDDD
NDSSKTGVEL LCVVRAVLKK IRRRVLVGDK VLVGSIDWVD RRGMIENVFH RRSEILDPPV
ANVDHLLVLF SLDQPKLEPF TLTRFLVEAE STRIPLTLAL NKTELISEEE LETWKIRLRG
WNYEPLFCSV GTKDGLDDIA FVLRDQTSVI VGPSGVGKSS LINVLRSNHG GGVVEDENWF
EPMLGNKWFD DQRVGEVSSR SGRGKHTTRN VSLLPVSEGG YLADTPGFNQ PSLLKVTKHS
LAHCFPEIRN MIESEKCGFR DCLHIGEPGC VVKGDWERYP YYLQLLDEIR IREEFQLRTF
GTKREDDVRY KVGDMGVKHA EPRLMPKKHR RESRKKTKQT MISELDEFED EDSDLYIEND
PIVQAIENEN KRQ
