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Database: UniProt
Entry: A0A2T2YKI4_9BACT
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ID   A0A2T2YKI4_9BACT        Unreviewed;       436 AA.
AC   A0A2T2YKI4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
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=AHMF7605_22160 {ECO:0000313|EMBL:PSR56008.1};
OS   Adhaeribacter arboris.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Adhaeribacter.
OX   NCBI_TaxID=2072846 {ECO:0000313|EMBL:PSR56008.1, ECO:0000313|Proteomes:UP000240357};
RN   [1] {ECO:0000313|EMBL:PSR56008.1, ECO:0000313|Proteomes:UP000240357}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HMF7605 {ECO:0000313|EMBL:PSR56008.1,
RC   ECO:0000313|Proteomes:UP000240357};
RA   Kang H., Kang J., Cha I., Kim H., Joh K.;
RT   "Adhaeribacter sp. HMF7605 Genome sequencing and assembly.";
RL   Submitted (MAR-2018) 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:PSR56008.1}.
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DR   EMBL; PYFT01000001; PSR56008.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2YKI4; -.
DR   OrthoDB; 9805918at2; -.
DR   Proteomes; UP000240357; Unassembled WGS sequence.
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; 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..168
FT                   /note="EngA-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51712"
FT   DOMAIN          177..352
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         183..190
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         230..234
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
FT   BINDING         295..298
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   436 AA;  49206 MW;  645C34A115AD1E70 CRC64;
     MSNIVAIVGR PNVGKSTLFN RLVGERKAIM DNQSGVTRDR HYGYGEWIGK NFTVVDTGGY
     VHGSDDIFEG EIRKQVELAI KEATVILFMV DVEEGLHSLD EEFAAVLRRS DKPIYIVANK
     ADTNLKSQFI GDFYALGLGE EIFPVSSASG SGTGDLLDEV VKHFQTEDAE NPDEGIPRLA
     VVGRPNVGKS SFVNLLLGEE RNIVTDVAGT TRDSINSRYN AFGMEFIITD TAGLRRKTKV
     HEDIEFYSVL RSIKAIEESD VCIVMLDATR GLEAQDMNII GLADKNRKGI VILVNKWDLV
     EKETNTMKEY EEQLREKMAP LTYMPIIFTS VLTKQRVHKA IETAYQVYKN KTQKISTSKL
     NDVILKEIEA YPPPAIKGKF VKIKYITQLP THNPTFAFFC NLPQYIKESY TRFLENKIRK
     HFGFEGVPIN IVFRKK
//
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