GTPB3_DICDI
ID GTPB3_DICDI Reviewed; 512 AA.
AC Q55C52;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=tRNA modification GTPase gtpbp3, mitochondrial;
DE AltName: Full=GTP-binding protein 3;
DE Flags: Precursor;
GN Name=gtpbp3; ORFNames=DDB_G0270228;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: GTPase involved in the 5-carboxymethylaminomethyl
CC modification (mnm(5)s(2)U34) of the wobble uridine base in
CC mitochondrial tRNAs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. TrmE GTPase family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72464.1; -; Genomic_DNA.
DR RefSeq; XP_646629.1; XM_641537.1.
DR AlphaFoldDB; Q55C52; -.
DR SMR; Q55C52; -.
DR STRING; 44689.DDB0267051; -.
DR PaxDb; Q55C52; -.
DR PRIDE; Q55C52; -.
DR EnsemblProtists; EAL72464; EAL72464; DDB_G0270228.
DR GeneID; 8617601; -.
DR KEGG; ddi:DDB_G0270228; -.
DR dictyBase; DDB_G0270228; gtpbp3.
DR eggNOG; KOG1191; Eukaryota.
DR HOGENOM; CLU_019624_3_1_1; -.
DR InParanoid; Q55C52; -.
DR OMA; CEIQCHG; -.
DR PhylomeDB; Q55C52; -.
DR PRO; PR:Q55C52; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; ISS:dictyBase.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central.
DR CDD; cd04164; trmE; 1.
DR Gene3D; 1.20.120.430; -; 1.
DR Gene3D; 3.30.1360.120; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00379; GTPase_MnmE; 1.
DR InterPro; IPR031168; G_TrmE.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR018948; GTP-bd_TrmE_N.
DR InterPro; IPR004520; GTPase_MnmE.
DR InterPro; IPR027368; MnmE_dom2.
DR InterPro; IPR025867; MnmE_helical.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR Pfam; PF12631; MnmE_helical; 1.
DR Pfam; PF10396; TrmE_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00450; mnmE_trmE_thdF; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51709; G_TRME; 1.
PE 3: Inferred from homology;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..512
FT /note="tRNA modification GTPase gtpbp3, mitochondrial"
FT /id="PRO_0000328465"
FT DOMAIN 246..434
FT /note="TrmE-type G"
FT BINDING 253..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 300..304
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 375..378
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
SQ SEQUENCE 512 AA; 58113 MW; CD2BB6DD75509783 CRC64;
MIKRLFCSIN KNKIINEPPK LSIIKDTIYN LSSGVGKSGV AIIRVSGPQA ETVIRKLIKK
SDVDKNEEIK SRYATLSTFY NPKTNEQLDK GMFIWFPSPN SFTGEDVVEF HIHGGRAVIY
ETMEAIGLIE GTRPSEQGEF TKRAFENGKM DLTQVEGLSD LLDASTSFQK KIALKQMQGS
ISEFYLSLRK DLIRASAYME AFIDFGDDAE LDPEIVDQSR NRIISIRDKI QQHLNDGKRG
ERLRDGANIA IVGPPNAGKS SLINLLTNRK ASIVSPIAGT TRDIVEVILD IDGYPVIIGD
TAGLRNSTND QIEIEGIEMA KDRFNNSDIK LFLFDSFNLF SQLNQNQNLN SSFNFNEEIK
NLFNFIDNET IIIFNKSDLL KQFDNLKEWE NLKLNLLDNI KKSNNLNSIQ SIEISCNNNE
NIKDLLNLLK LNLKNLFEIQ DKESPLLTRL RYKQHLSDCV ESLDRYLYYC EHDVVLASEE
LRSAILSISE ITHSVNIDDL LDIIFKDFCI GK
