ID A0A1Z9PZC7_9CYAN Unreviewed; 561 AA.
AC A0A1Z9PZC7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=GTPase HflX {ECO:0000256|HAMAP-Rule:MF_00900};
DE AltName: Full=GTP-binding protein HflX {ECO:0000256|HAMAP-Rule:MF_00900};
GN Name=hflX {ECO:0000256|HAMAP-Rule:MF_00900};
GN ORFNames=CBD89_05465 {ECO:0000313|EMBL:OUW97341.1};
OS Cyanobacteria bacterium TMED229.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=1986679 {ECO:0000313|EMBL:OUW97341.1, ECO:0000313|Proteomes:UP000196226};
RN [1] {ECO:0000313|EMBL:OUW97341.1, ECO:0000313|Proteomes:UP000196226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED229 {ECO:0000313|EMBL:OUW97341.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit and may
CC have a role during protein synthesis or ribosome biogenesis.
CC {ECO:0000256|HAMAP-Rule:MF_00900}.
CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit.
CC {ECO:0000256|HAMAP-Rule:MF_00900}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900}.
CC Note=May associate with membranes. {ECO:0000256|HAMAP-Rule:MF_00900}.
CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase
CC superfamily. HflX GTPase family. {ECO:0000256|HAMAP-Rule:MF_00900}.
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:OUW97341.1}.
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DR EMBL; NHKA01000024; OUW97341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9PZC7; -.
DR Proteomes; UP000196226; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01878; HflX; 1.
DR Gene3D; 6.10.250.2860; -; 1.
DR Gene3D; 3.40.50.11060; GTPase HflX, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00900; GTPase_HflX; 1.
DR InterPro; IPR030394; G_HFLX_dom.
DR InterPro; IPR006073; GTP-bd.
DR InterPro; IPR032305; GTP-bd_M.
DR InterPro; IPR016496; GTPase_HflX.
DR InterPro; IPR025121; GTPase_HflX_N.
DR InterPro; IPR042108; GTPase_HflX_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03156; GTP_HflX; 1.
DR PANTHER; PTHR10229:SF0; GTP-BINDING PROTEIN 6-RELATED; 1.
DR PANTHER; PTHR10229; GTP-BINDING PROTEIN HFLX; 1.
DR Pfam; PF16360; GTP-bdg_M; 1.
DR Pfam; PF13167; GTP-bdg_N; 1.
DR Pfam; PF01926; MMR_HSR1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51705; G_HFLX; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00900};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00900}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00900}.
FT DOMAIN 373..545
FT /note="Hflx-type G"
FT /evidence="ECO:0000259|PROSITE:PS51705"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 341..368
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 561 AA; 62665 MW; FB02F8B923CD262E CRC64;
MKQAHLAGRT RGLRPSQQRQ LERLSHRRHP DSSGADLFTL ERLAELAKEL EQPLHLVLDG
RGLCRVLWVG PLSGSEPLLQ HLPVARRRQS GGWRLISCSQ RQALEPDRHV AVMALDLNPN
TWLIFNTQPS PDGHRHAALF QPDRDAANGW ALIERRHLFE LCAWHPGRHD TVSLPPPTGP
DKGLERVLLL TLPTRDPVGS ERDLSELEGL VRSAGGTPVA VIRQRPGHAN PQTLWGTGKL
QEAALQVRRS QASLVITDRE LTPVQARNLE RLLDCPVMDR SELILDIFAQ RAGSAAGRLQ
VELAQLRYRL PRLLGRGRSL SRQGGGIGTR GPGETQLEKD RRAIARRIDR LLRDLKQLRQ
HRSRLRDQRR DLPRVALVGY TNAGKSSLLN SLCGRREQDR VLAENKLFAT LDPTTRRLEL
PCHGAPPRTV LLTDTVGFIR DLPGPLVEAF SATLEETLDA DVLLLVVDLA DPNWSGQLST
VHQLLDSLGC HALRQVVANQ IDRCRLDAIE AIREREPNSL FLSAMRGDGL CGLRQWLLKQ
FFDQASESGA PLTGFIPEWP S
//
