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RSGA2_ARATH
ID   RSGA2_ARATH             Reviewed;         294 AA.
AC   F4HTL8; A0A1P8AUE0; O64799; Q1PFF7; Q5Q0E0; Q5Q0E1;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2017, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Small ribosomal subunit biogenesis GTPase RsgA 2, mitochondrial;
DE   Flags: Precursor;
GN   OrderedLocusNames=At1g67460 {ECO:0000312|Araport:AT1G67460};
GN   ORFNames=F12B7.1 {ECO:0000312|EMBL:AAG52303.1},
GN   T1F15.7 {ECO:0000312|EMBL:AAC18794.1};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=16244158; DOI=10.1104/pp.105.063479;
RA   Xiao Y.-L., Smith S.R., Ishmael N., Redman J.C., Kumar N., Monaghan E.L.,
RA   Ayele M., Haas B.J., Wu H.C., Town C.D.;
RT   "Analysis of the cDNAs of hypothetical genes on Arabidopsis chromosome 2
RT   reveals numerous transcript variants.";
RL   Plant Physiol. 139:1323-1337(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=F4HTL8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=F4HTL8-2; Sequence=VSP_058909, VSP_058910;
CC       Name=3;
CC         IsoId=F4HTL8-3; Sequence=VSP_058911;
CC   -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: This protein is shorter compared to other members of the
CC       family and lacks the C-terminal part that binds zinc. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC18794.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAG52303.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC004393; AAC18794.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC011020; AAG52303.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE34649.1; -; Genomic_DNA.
DR   EMBL; CP002684; ANM60272.1; -; Genomic_DNA.
DR   EMBL; AY800610; AAV68846.1; -; mRNA.
DR   EMBL; AY800611; AAV68847.1; -; mRNA.
DR   EMBL; DQ446406; ABE65750.1; -; mRNA.
DR   PIR; T02159; T02159.
DR   RefSeq; NP_001322570.1; NM_001334299.1. [F4HTL8-1]
DR   RefSeq; NP_176913.3; NM_105413.4. [F4HTL8-3]
DR   AlphaFoldDB; F4HTL8; -.
DR   SMR; F4HTL8; -.
DR   STRING; 3702.AT1G67460.1; -.
DR   PaxDb; F4HTL8; -.
DR   PRIDE; F4HTL8; -.
DR   ProteomicsDB; 228046; -. [F4HTL8-1]
DR   EnsemblPlants; AT1G67460.1; AT1G67460.1; AT1G67460. [F4HTL8-3]
DR   EnsemblPlants; AT1G67460.2; AT1G67460.2; AT1G67460. [F4HTL8-1]
DR   GeneID; 843067; -.
DR   Gramene; AT1G67460.1; AT1G67460.1; AT1G67460. [F4HTL8-3]
DR   Gramene; AT1G67460.2; AT1G67460.2; AT1G67460. [F4HTL8-1]
DR   KEGG; ath:AT1G67460; -.
DR   Araport; AT1G67460; -.
DR   TAIR; locus:2008788; AT1G67460.
DR   eggNOG; ENOG502QRR1; Eukaryota.
DR   HOGENOM; CLU_931723_0_0_1; -.
DR   InParanoid; F4HTL8; -.
DR   OrthoDB; 1394936at2759; -.
DR   PRO; PR:F4HTL8; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; F4HTL8; 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   Gene3D; 3.40.50.300; -; 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   Alternative splicing; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..68
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           69..294
FT                   /note="Small ribosomal subunit biogenesis GTPase RsgA 2,
FT                   mitochondrial"
FT                   /id="PRO_0000439701"
FT   DOMAIN          155..294
FT                   /note="CP-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01058"
FT   BINDING         255..263
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         126..140
FT                   /note="RTVLVGDKVLVDKVD -> SWWKLNLLEFESQLL (in isoform 2)"
FT                   /id="VSP_058909"
FT   VAR_SEQ         141..294
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_058910"
FT   VAR_SEQ         285..294
FT                   /note="VSFFLSYFIL -> AKTRRIKKSGLKIRV (in isoform 3)"
FT                   /id="VSP_058911"
FT   CONFLICT        61
FT                   /note="F -> L (in Ref. 3; AAV68846/AAV68847)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="A -> V (in Ref. 3; AAV68846/AAV68847)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  32955 MW;  3EBC0B79405C1D8E CRC64;
     MQTFSSAAAL TSILRRTTIY HGGFGTGLRI RRSFYFLSAI RQENPNVTKN PHPNKTILRS
     FLAPVLPLDE KPNLVELQAI GTIATALADY MRVIVQDVPE SDNGEDDKIG VELLCVVRKL
     LKKIGRTVLV GDKVLVDKVD WVDRRAKIIN VFDRVSEVLD PPVANVDHLV ILFSLDQPKI
     DPFTLTRFLV EAESIGIRIT VALNKCELVT QEEVESWKIR LRSWNYEPLF CSVGTKVGID
     EIAFNLRNQT SVIVGPSGVG KSSLINILRS SYGGDIKHEE VFKPVSFFLS YFIL
 
 
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