MTG2_PONAB
ID MTG2_PONAB Reviewed; 406 AA.
AC Q5RDW1;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Mitochondrial ribosome-associated GTPase 2;
DE AltName: Full=GTP-binding protein 5;
GN Name=MTG2; Synonyms=GTPBP5;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the regulation of the mitochondrial ribosome
CC assembly and of translational activity. Displays GTPase activity.
CC Involved in the ribosome maturation process (By similarity).
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Associates with the mitochondrial ribosome large subunit; the
CC association occurs in a GTP-dependent manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. Mitochondrion inner
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Matrix side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. OBG GTPase family. {ECO:0000305}.
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DR EMBL; CR857782; CAH90046.1; -; mRNA.
DR RefSeq; NP_001124977.1; NM_001131505.1.
DR AlphaFoldDB; Q5RDW1; -.
DR SMR; Q5RDW1; -.
DR STRING; 9601.ENSPPYP00000012513; -.
DR Ensembl; ENSPPYT00000013005; ENSPPYP00000012513; ENSPPYG00000011198.
DR GeneID; 100171850; -.
DR KEGG; pon:100171850; -.
DR CTD; 26164; -.
DR eggNOG; KOG1489; Eukaryota.
DR GeneTree; ENSGT00940000157379; -.
DR HOGENOM; CLU_011747_2_3_1; -.
DR InParanoid; Q5RDW1; -.
DR OMA; VVFDWEP; -.
DR OrthoDB; 1150635at2759; -.
DR TreeFam; TF314774; -.
DR Proteomes; UP000001595; Chromosome 20.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005761; C:mitochondrial ribosome; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0070129; P:regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0044065; P:regulation of respiratory system process; ISS:UniProtKB.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR CDD; cd01898; Obg; 1.
DR Gene3D; 2.70.210.12; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01454; GTPase_Obg; 1.
DR InterPro; IPR031167; G_OBG.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR014100; GTP-bd_Obg/CgtA.
DR InterPro; IPR006169; GTP1_OBG_dom.
DR InterPro; IPR036726; GTP1_OBG_dom_sf.
DR InterPro; IPR045086; OBG_GTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR PANTHER; PTHR11702; PTHR11702; 1.
DR Pfam; PF01018; GTP1_OBG; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR PIRSF; PIRSF002401; GTP_bd_Obg/CgtA; 1.
DR PRINTS; PR00326; GTP1OBG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF82051; SSF82051; 1.
DR TIGRFAMs; TIGR02729; Obg_CgtA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51710; G_OBG; 1.
DR PROSITE; PS51883; OBG; 1.
PE 2: Evidence at transcript level;
KW GTP-binding; Magnesium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotide-binding; Reference proteome;
KW Ribosome biogenesis; Translation regulation.
FT CHAIN 1..406
FT /note="Mitochondrial ribosome-associated GTPase 2"
FT /id="PRO_0000261589"
FT DOMAIN 70..224
FT /note="Obg"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01231"
FT DOMAIN 225..390
FT /note="OBG-type G"
FT REGION 15..406
FT /note="Localized in the mitochondria"
FT /evidence="ECO:0000250"
FT REGION 30..406
FT /note="Not localized in the mitochondria"
FT /evidence="ECO:0000250"
FT BINDING 231..238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 256..260
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 258
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 278..281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 345..348
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 371..373
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 44073 MW; 22EBA83736088E5A CRC64;
MTPARHFSAR LRTVFEGVGH WALSTQAGLK PSRLLPQQAS PRLLSVSCAD LAKRQELPGK
KPLSEKKLKR YFVDYRRVLV CGGNGGAGAS CFHSEPRKEF GGPDGGDGGN GGHVILRADQ
QVKSLSSVLS RYQGFSGEDG GSKNCFGRSG AVLYIRVPMG TLVKEGGRVV ADLSRVGDEY
IAALGGAGGK GNRFFLANNN RAPVTCTPGQ PGQQRVLHLE LKTVAHAGMV GFPNAGKSSL
LRAISNARPA VASYPFTTLK PHVGIVHYEG HLQIAVADIP GIIRGAHQNR GLGSAFLRHI
ERCRFLLFVV DLSQPEPWTQ VDDLKYELEM YEKGLSERPH AIIANKIDLP EAQANLSQLR
DHLGQEVIVL SALTGENLEQ LLLHLKVLYD AYTEAELGQG RQPLRW
