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DRG2_BOVIN
ID   DRG2_BOVIN              Reviewed;         364 AA.
AC   Q58D56;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Developmentally-regulated GTP-binding protein 2;
DE            Short=DRG-2;
DE   AltName: Full=Translation factor GTPase DRG2;
DE            Short=TRAFAC GTPase DRG2;
DE            EC=3.6.5.-;
GN   Name=DRG2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
CC   -!- FUNCTION: Catalyzes the conversion of GTP to GDP through hydrolysis of
CC       the gamma-phosphate bond in GTP. When hydroxylated at C-3 of 'Lys-21'
CC       by JMJD7, may bind to RNA and play a role in translation.
CC       {ECO:0000250|UniProtKB:P55039}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000250|UniProtKB:P55039};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P55039};
CC   -!- SUBUNIT: Interacts with RWDD1; this interaction confers protection to
CC       polyubiquitination and proteolytic degradation (By similarity).
CC       Interacts with JMJD7; this interaction is direct (By similarity).
CC       {ECO:0000250, ECO:0000250|UniProtKB:P55039,
CC       ECO:0000250|UniProtKB:Q9QXB9}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P55039}. Cytoplasm
CC       {ECO:0000250|UniProtKB:P55039}.
CC   -!- PTM: Polyubiquitinated. {ECO:0000250|UniProtKB:Q9QXB9}.
CC   -!- PTM: Hydroxylated (with S stereochemistry) at C-3 of Lys-21 by JMJD7.
CC       {ECO:0000250|UniProtKB:P55039}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC       superfamily. OBG GTPase family. {ECO:0000255|PROSITE-ProRule:PRU01047}.
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DR   EMBL; BT021741; AAX46588.1; -; mRNA.
DR   RefSeq; NP_001014865.1; NM_001014865.1.
DR   AlphaFoldDB; Q58D56; -.
DR   SMR; Q58D56; -.
DR   STRING; 9913.ENSBTAP00000008544; -.
DR   PaxDb; Q58D56; -.
DR   PRIDE; Q58D56; -.
DR   Ensembl; ENSBTAT00000008544; ENSBTAP00000008544; ENSBTAG00000006517.
DR   GeneID; 507472; -.
DR   KEGG; bta:507472; -.
DR   CTD; 1819; -.
DR   VEuPathDB; HostDB:ENSBTAG00000006517; -.
DR   VGNC; VGNC:28209; DRG2.
DR   eggNOG; KOG1486; Eukaryota.
DR   GeneTree; ENSGT00940000153340; -.
DR   HOGENOM; CLU_044997_0_0_1; -.
DR   InParanoid; Q58D56; -.
DR   OMA; VCDQVHR; -.
DR   OrthoDB; 754662at2759; -.
DR   TreeFam; TF105706; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000006517; Expressed in laryngeal cartilage and 105 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR   GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   CDD; cd01896; DRG; 1.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR045001; DRG.
DR   InterPro; IPR031167; G_OBG.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR031662; GTP-binding_2.
DR   InterPro; IPR006074; GTP1-OBG_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR004095; TGS.
DR   InterPro; IPR012676; TGS-like.
DR   PANTHER; PTHR43127; PTHR43127; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   Pfam; PF16897; MMR_HSR1_Xtn; 1.
DR   Pfam; PF02824; TGS; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF81271; SSF81271; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51710; G_OBG; 1.
DR   PROSITE; PS00905; GTP1_OBG; 1.
DR   PROSITE; PS51880; TGS; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Hydrolase; Hydroxylation; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation.
FT   CHAIN           1..364
FT                   /note="Developmentally-regulated GTP-binding protein 2"
FT                   /id="PRO_0000261588"
FT   DOMAIN          63..288
FT                   /note="OBG-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   DOMAIN          288..363
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   BINDING         69..76
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         76
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         94..98
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         96
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         115..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         246..249
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   BINDING         269..271
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01047"
FT   MOD_RES         21
FT                   /note="(3S)-3-hydroxylysine"
FT                   /evidence="ECO:0000250|UniProtKB:P55039"
SQ   SEQUENCE   364 AA;  40749 MW;  CBE113D597264737 CRC64;
     MGILEKISEI EKEIARTQKN KATEYHLGLL KAKLAKYRAQ LLEPSKSSSS KGEGFDVMKS
     GDARVALIGF PSVGKSTFLS LMTSTASEAA SYEFTTLTCI PGVIEYKGAN IQLLDLPGII
     EGAAQGKGRG RQVIAVARTA DVVIMMLDAT KGEVQRSLLE KELESVGIRL NKHKPNIYFK
     PKKGGGISFN STVTLTQCSE KLVQLILHEY KIFNAEVLFR EDCSPDEFID VIVGNRVYMP
     CLYVYNKIDQ ISMEEVDRLA RKPDSVVISC GMKLNLDYLL EMLWEYLALT CIYTKKRGQR
     PDFTDAIILR KGASVEHVCH RIHRSLASQF KYALVWGTST KYSPQRVGLT HTMEHEDVIQ
     IVKK
 
 
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