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DER_PROM1
ID   DER_PROM1               Reviewed;         456 AA.
AC   A2C0J7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=NATL1_04431;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(2007).
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; CP000553; ABM75007.1; -; Genomic_DNA.
DR   RefSeq; WP_011823194.1; NC_008819.1.
DR   AlphaFoldDB; A2C0J7; -.
DR   SMR; A2C0J7; -.
DR   STRING; 167555.NATL1_04431; -.
DR   EnsemblBacteria; ABM75007; ABM75007; NATL1_04431.
DR   KEGG; pme:NATL1_04431; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_3; -.
DR   OMA; KFRFLEY; -.
DR   Proteomes; UP000002592; 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; IPR003593; AAA+_ATPase.
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   PRINTS; PR00326; GTP1OBG.
DR   SMART; SM00382; AAA; 2.
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; Repeat; Ribosome biogenesis.
FT   CHAIN           1..456
FT                   /note="GTPase Der"
FT                   /id="PRO_1000011691"
FT   DOMAIN          4..169
FT                   /note="EngA-type G 1"
FT   DOMAIN          178..353
FT                   /note="EngA-type G 2"
FT   DOMAIN          354..439
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         184..191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         231..235
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         296..299
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   456 AA;  50953 MW;  E46318BEC58982DE CRC64;
     MALPVVAIIG RPNVGKSTLV NRLCQSREAI VHDEPGVTRD RTYQDGFWRD RDFKVVDTGG
     LVFDDDSEFL PEIREQANLA LEEAVVALVI VDGQEGITTA DESIAEFLRS RSCKTLVVVN
     KCESPEQGLA MAAEFWKLGL GEPYPISAIH GVGTGDLLDQ VVNLFPSKDL DEVSDSPVQL
     AIIGRPNVGK SSLLNSICGE TRAIVSSIRG TTRDTIDTRI THQGKEWKLV DTAGIRRRRS
     VNYGPEFFGI NRSFKAIERS DVCVLVIDAL DGVTEQDQRL AGRIEQEGRA CLIVINKWDA
     VEKDSHTMSA MEKDIRSKLY FLDWAQMIFT SAVTGQRVEG IFALATLAVD QSRRRVTTSV
     VNEVLTEALK WRSPPTTRGG KQGRLYYGTQ VAINPPSFTL FVNEPKLFGE TYRRYIERQI
     REGLGFEGTP IKLFWRGKQQ RDVEKDMARQ QKGVQN
 
 
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