DER_SYNR3
ID DER_SYNR3 Reviewed; 452 AA.
AC A5GR60;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195};
DE AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195};
GN Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA;
GN OrderedLocusNames=SynRCC307_0466;
OS Synechococcus sp. (strain RCC307).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316278;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCC307;
RG Genoscope;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
CC -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00195}.
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DR EMBL; CT978603; CAK27369.1; -; Genomic_DNA.
DR RefSeq; WP_011934884.1; NC_009482.1.
DR AlphaFoldDB; A5GR60; -.
DR SMR; A5GR60; -.
DR STRING; 316278.SynRCC307_0466; -.
DR EnsemblBacteria; CAK27369; CAK27369; SynRCC307_0466.
DR KEGG; syr:SynRCC307_0466; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_6_2_3; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 263682at2; -.
DR Proteomes; UP000001115; Chromosome.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.20; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00195; GTPase_Der; 1.
DR InterPro; IPR031166; G_ENGA.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR016484; GTP-bd_EngA.
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 Pfam; PF14714; KH_dom-like; 1.
DR Pfam; PF01926; MMR_HSR1; 2.
DR PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 2.
DR PROSITE; PS51712; G_ENGA; 2.
PE 3: Inferred from homology;
KW GTP-binding; Nucleotide-binding; Reference proteome; Repeat;
KW Ribosome biogenesis.
FT CHAIN 1..452
FT /note="GTPase Der"
FT /id="PRO_1000011770"
FT DOMAIN 4..169
FT /note="EngA-type G 1"
FT DOMAIN 177..352
FT /note="EngA-type G 2"
FT DOMAIN 353..438
FT /note="KH-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 57..61
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 183..190
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 230..234
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT BINDING 295..298
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ SEQUENCE 452 AA; 50399 MW; 3A773154C287AA30 CRC64;
MALPVVAIIG RPNVGKSTLV NRLCRSRDAI VHDEPGVTRD RTYQEGFWGG RTFRVVDTGG
LVFDDDSEFL PEIREQASLA MAEACVALVI VDGQQGLTAA DEAIAAWLRQ QKCPVLLGVN
KCESPEQGLA MAAEFWALGL GEPKPISAIH GAGTGDLLDQ VLDFLPPQDE EEAPEPIQMA
IVGRPNVGKS SLLNTVCGEN RAIVSPIRGT TRDTIDTSIE REGQSWKLLD TAGIRRRRSV
NYGPEFFGIN RSFKAIERSD VCVLVIDAEE GVTEQDQRLA GRIEEEGRAC LVVVNKWDLV
EKDSHTMPAM EKELRSKLYF LEWAPMLFIS ALTGQRVERI FPLAVLAVEQ HRRRVTTAVV
NEVLQEALSW RSPPTTRGGR QGRLYYGTQV AVRPPSFTLF VNEPKLFGDT YRRYVERQIR
QGLGFEGSPV RLFWRGKQQR DAERDQARAA SR
