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Database: UniProt
Entry: V5RHY1_SPIAP
LinkDB: V5RHY1_SPIAP
Original site: V5RHY1_SPIAP 
ID   V5RHY1_SPIAP            Unreviewed;       437 AA.
AC   V5RHY1;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 52.
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=engA {ECO:0000313|EMBL:AHB36149.1};
GN   Synonyms=der {ECO:0000256|HAMAP-Rule:MF_00195};
GN   ORFNames=SAPIS_v1c03030 {ECO:0000313|EMBL:AHB36149.1};
OS   Spiroplasma apis B31.
OC   Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=1276258 {ECO:0000313|EMBL:AHB36149.1, ECO:0000313|Proteomes:UP000018550};
RN   [1] {ECO:0000313|EMBL:AHB36149.1, ECO:0000313|Proteomes:UP000018550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B31 {ECO:0000313|EMBL:AHB36149.1};
RX   PubMed=24407648;
RA   Ku C., Lo W.S., Chen L.L., Kuo C.H.;
RT   "Complete Genome Sequence of Spiroplasma apis B31T (ATCC 33834), a
RT   Bacterium Associated with May Disease of Honeybees (Apis mellifera).";
RL   Genome Announc. 2:e01151-13(2014).
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; CP006682; AHB36149.1; -; Genomic_DNA.
DR   RefSeq; WP_023789083.1; NC_022998.1.
DR   AlphaFoldDB; V5RHY1; -.
DR   STRING; 1276258.SAPIS_v1c03030; -.
DR   KEGG; sapi:SAPIS_v1c03030; -.
DR   PATRIC; fig|1276258.3.peg.298; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_14; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000018550; 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; 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; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   SMART; SM00173; RAS; 1.
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:UP000018550};
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          5..168
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          176..352
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   BINDING         11..18
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         58..62
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         120..123
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         182..189
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         229..233
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         294..297
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   437 AA;  49509 MW;  DBF39D5778F3201C CRC64;
     MSRKGVVAIV GRPNVGKSTL FNRIIKEKKA IVEDKPGVTR DRMYGNAEWL TLPFIIVDTG
     GITLQDTAFA KEIKMQAEIA IKEADVIVFV INFREGITLE DEVVAKILYK TKKPVILAVN
     KYDKKQTYDE SYSFMTLGFG EPCLISSTHG IGVGDLLESI TAKMPKFAMN ENSDDIKISI
     VGKPNVGKSS LVNSIVGEER MIVSEVAGTT IDSVDTKIKV EGKNYTIIDT AGMRKKGKIY
     ENLEKYSYLR SLTSINKADV VILMLDASQP VTDHDTNIGG FAYEENKPII IIGNKWDLVK
     NKESNTMKKK EEEIKAYFKY LNYAKVIFIS AKENKRVHKI FEIVELVRDN IKKRIRTSLL
     NEIFNKAQLI NPAPNHNGGR LKIYYASQVE AYLPTFVLFV NNPSFVHFSY KRFLENQIRS
     QFDFSGVPIN IIFRERK
//
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