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Database: UniProt
Entry: D3R0T0_MAGIU
LinkDB: D3R0T0_MAGIU
Original site: D3R0T0_MAGIU 
ID   D3R0T0_MAGIU            Unreviewed;       441 AA.
AC   D3R0T0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=GTPase Der {ECO:0000256|ARBA:ARBA00020953, ECO:0000256|HAMAP-Rule:MF_00195};
DE   AltName: Full=GTP-binding protein EngA {ECO:0000256|HAMAP-Rule:MF_00195};
GN   Name=der {ECO:0000256|HAMAP-Rule:MF_00195,
GN   ECO:0000313|EMBL:ADC90670.1};
GN   OrderedLocusNames=HMPREF0868_0455 {ECO:0000313|EMBL:ADC90670.1};
OS   Mageeibacillus indolicus (strain UPII9-5) (Clostridiales genomosp. BVAB3
OS   (strain UPII9-5)).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Mageeibacillus.
OX   NCBI_TaxID=699246 {ECO:0000313|EMBL:ADC90670.1, ECO:0000313|Proteomes:UP000008234};
RN   [1] {ECO:0000313|Proteomes:UP000008234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UPII9-5 {ECO:0000313|Proteomes:UP000008234};
RA   Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA   Strausberg R.L., Nelson K.E.;
RT   "Sequence of Clostridiales genomosp. BVAB3 str. UPII9-5.";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000256|HAMAP-Rule:MF_00195,
CC       ECO:0000256|RuleBase:RU004481}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00195}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. EngA (Der) GTPase family.
CC       {ECO:0000256|ARBA:ARBA00008279, ECO:0000256|HAMAP-Rule:MF_00195,
CC       ECO:0000256|PROSITE-ProRule:PRU01049, ECO:0000256|RuleBase:RU004481}.
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DR   EMBL; CP001850; ADC90670.1; -; Genomic_DNA.
DR   RefSeq; WP_012993829.1; NC_013895.2.
DR   AlphaFoldDB; D3R0T0; -.
DR   STRING; 699246.HMPREF0868_0455; -.
DR   KEGG; clo:HMPREF0868_0455; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_9; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000008234; Chromosome.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   CDD; cd01894; EngA1; 1.
DR   CDD; cd01895; EngA2; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   HAMAP; MF_00195; GTPase_Der; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031166; G_ENGA.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR016484; GTPase_Der.
DR   InterPro; IPR032859; KH_dom-like.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   NCBIfam; TIGR03594; GTPase_EngA; 1.
DR   NCBIfam; TIGR00231; small_GTP; 2.
DR   PANTHER; PTHR43834; GTPASE DER; 1.
DR   PANTHER; PTHR43834:SF6; GTPASE DER; 1.
DR   Pfam; PF14714; KH_dom-like; 1.
DR   Pfam; PF01926; MMR_HSR1; 2.
DR   PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51712; G_ENGA; 2.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00195};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00195}; Reference proteome {ECO:0000313|Proteomes:UP000008234};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU004481};
KW   Ribosome biogenesis {ECO:0000256|ARBA:ARBA00022517, ECO:0000256|HAMAP-
KW   Rule:MF_00195}.
FT   DOMAIN          4..169
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          178..353
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   BINDING         10..17
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         120..123
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         184..191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         231..235
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         296..299
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   441 AA;  49368 MW;  13AD27F5E0099959 CRC64;
     MANSFVAVVG RPNVGKSTFF NFLAGERISI VDDTPGVTRD RIYAEVEWLG RKFSLIDTGG
     IEPRTDDVLL QQMRIQAELA IETADVILFM VDLKAGLHAA DADIANMLRK TKKPVILAVN
     KCDHVGDTPP EAYEFYNLGL GDFFPISAVH GLGMGELLDA IVENLPEPET DDPANHRVKI
     CLIGKPNAGK SSLTNRLLGQ NRSIVSSISG TTRDSLDTPL TNEFGNYVLI DTAGLRKKSR
     IDDQVERYSM IRALAAIERS DVCLILIDAI DGITEQDTKV AGYAHNAGKA SIFVVNKWDI
     VNKETGTMEE YTRSIRERFS YMPYAQVLFL SALTGARCDK VFPMVNHVYE QACRKLTTGV
     LNDFIAEIQA MVPAPQDKGR RLKIRYATQV GICPPEFVLF CNDKELMHFS YERYIENRLR
     QNFGFDGTPV RFILRSRERK K
//
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