ID A0A066ZX94_HYDMR Unreviewed; 480 AA.
AC A0A066ZX94;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=EI16_11800 {ECO:0000313|EMBL:KDN96909.1};
OS Hydrogenovibrio marinus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Hydrogenovibrio.
OX NCBI_TaxID=28885 {ECO:0000313|EMBL:KDN96909.1, ECO:0000313|Proteomes:UP000027341};
RN [1] {ECO:0000313|EMBL:KDN96909.1, ECO:0000313|Proteomes:UP000027341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-110 {ECO:0000313|EMBL:KDN96909.1,
RC ECO:0000313|Proteomes:UP000027341};
RA Cha H.J., Jo B.H., Hwang B.H.;
RT "Draft genome sequence of Hydrogenovibrio marinus MH-110, a model organism
RT for aerobic H2 metabolism.";
RL Submitted (APR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN96909.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JMIU01000001; KDN96909.1; -; Genomic_DNA.
DR RefSeq; WP_029908111.1; NZ_JMIU01000001.1.
DR AlphaFoldDB; A0A066ZX94; -.
DR STRING; 28885.EI16_11800; -.
DR Proteomes; UP000027341; 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:UP000027341};
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..167
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT DOMAIN 181..354
FT /note="EngA-type G"
FT /evidence="ECO:0000259|PROSITE:PS51712"
FT REGION 445..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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 187..194
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 234..238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT BINDING 299..302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ SEQUENCE 480 AA; 53627 MW; E47A981DC78AB5B1 CRC64;
MSKPVIALVG RPNVGKSTLF NRLTRTRDAI VADYPGLTRD RQYGTGRTGN HPYIVVDTGG
LSGEQEGVDP LMAGQVRSAI EESDAILFLV DGRAGLIPAD EAIANYIRQF NKPTYLLVNK
AEGHSHQLIS ADFFQMGLGQ PFVISSAHGD NVKETIDHIL DEVVTEEEEE KAFDLDEHPG
IRVAVVGRPN VGKSTLINRM IGEERVVAFD MPGTTRDSIF VPFERDGQAY TLIDTAGVRR
RKNIKEKIEK FSIVKAIEAM ESCNVVVLVI DGSEGITDQD LTLLGLALES GRGLVIAINK
WDNLTEDQRN KIKHELEFKL HFVDYAKKHL ISALHGSGVG DLFKTIRGVY QAVMKKVSTS
DLNRVLEQAV LDHQPPLIGG RRVKLRYAHL GGSNPPRVII HGTQVDKLPQ AYTKYLMNVF
RKAFKWQGTP VFIEYKVTVN PYENRKSSFS SRRGKSESQS ENLAVKRRKK KNTQQKRRTN
//
