ID D5BGH1_ZUNPS Unreviewed; 434 AA.
AC D5BGH1;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
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 OrderedLocusNames=ZPR_0780 {ECO:0000313|EMBL:ADF51130.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF51130.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF51130.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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; CP001650; ADF51130.1; -; Genomic_DNA.
DR RefSeq; WP_013070282.1; NC_014041.1.
DR AlphaFoldDB; D5BGH1; -.
DR STRING; 655815.ZPR_0780; -.
DR KEGG; zpr:ZPR_0780; -.
DR eggNOG; COG1160; Bacteria.
DR HOGENOM; CLU_016077_6_2_10; -.
DR OMA; KFRFLEY; -.
DR OrthoDB; 9805918at2; -.
DR Proteomes; UP000001654; Chromosome.
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; 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:SF6; GTP-BINDING PROTEIN ENGA; 1.
DR PANTHER; PTHR43834; 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 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};
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..167
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT DOMAIN 175..350
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
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 119..122
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 181..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 228..232
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 293..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ SEQUENCE 434 AA; 49323 MW; 7AE8CA13AABEE161 CRC64;
MSGIVAIVGR PNVGKSTFFN RLIQRREAIV DSVSGVTRDR HYGKSDWNGR NFSLIDTGGY
VIGSDDVFEA EIDKQVELAI GEADAIIFMV DVESGITPMD EDVAILLRKV NKPVFLAVNK
VDNNKRLENA VEFYALGLGE YFPIASTNGS GTGDLLDAVI ESLPEETYKE ESELPRFAVV
GRPNAGKSSF INALIGEDRY IVTDIAGTTR DSIDTKYNRF GFEFNLVDTA GIRRKSKVKE
DLEFYSVMRS VRAIENADVC LLVLDATRGF DGQVQNIFWL AQRNRKGIVI LVNKWDLVEK
ETNTMKSYEQ MIRREIEPFT DVPVIFISVL NKQRIFKAIE TAVKVFENRS KKIKTRELND
VMLPIIENNP PPAIKGKYVK VKFCTQLPTP QPQFAFFCNL PQYVKDPYKR FIENKLREEF
DFKGVPITVY FRKK
//