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Database: UniProt
Entry: A0A1H2ZNF6_9GAMM
LinkDB: A0A1H2ZNF6_9GAMM
Original site: A0A1H2ZNF6_9GAMM 
ID   A0A1H2ZNF6_9GAMM        Unreviewed;       467 AA.
AC   A0A1H2ZNF6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   ORFNames=SAMN05443545_104192 {ECO:0000313|EMBL:SDX18518.1};
OS   Aidingimonas halophila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Aidingimonas.
OX   NCBI_TaxID=574349 {ECO:0000313|EMBL:SDX18518.1, ECO:0000313|Proteomes:UP000198500};
RN   [1] {ECO:0000313|EMBL:SDX18518.1, ECO:0000313|Proteomes:UP000198500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19219 {ECO:0000313|EMBL:SDX18518.1,
RC   ECO:0000313|Proteomes:UP000198500};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNNI01000004; SDX18518.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2ZNF6; -.
DR   STRING; 574349.SAMN05443545_104192; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000198500; Unassembled WGS sequence.
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:UP000198500};
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          3..166
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          178..351
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   REGION          431..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         9..16
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         56..60
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         118..121
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   467 AA;  52276 MW;  65434FE9A9D859F9 CRC64;
     MTPVIALVGR PNVGKSTLFN RLTRSRDALV ADHPGLTRDR KYGNGRLGGK RYIVIDTGGI
     SGDEEGINAA MAEQSLLAID EADIVFFMVD ARTGLHPADE AIANHLRVNQ KKTWLVVNKT
     DGLEEHSAMA DFWSLGLGDP HSIAASHGRN VTSLIEKVLE PFPEPEETNE PAERSNGIHI
     GVIGRPNVGK STLVNRMLGE ERVVVFDEAG TTRDAIEIPF ERRGKPYVLV DTAGVRRRKN
     VREVAEKYSI IKTLEAIKEC HVAIVVLDAR SGLVEQDLHL LDYVLNSGRA LVLAVNKWDG
     LEQEARERMR TEIKRRLGFA DYADLHFISA LHGTGVGDLY PSIERAFASA HHHWSTNRLT
     TILQDAVSEH QPPMVRGRRI KLRMAHQGGS NPPIIVVHGN QTDALPEAYK RFLTNTFRKV
     LKVRGTPMRF EFRTGQNPYD TQAGASDRDK AKQRELRRTR ESRKQRR
//
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