ID   G2FF66_9GAMM            Unreviewed;       288 AA.
AC   G2FF66;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=UPF0042 nucleotide-binding protein {ECO:0000313|EMBL:EGW54613.1};
GN   ORFNames=TevJSym_ak00770 {ECO:0000313|EMBL:EGW54613.1};
OS   endosymbiont of Tevnia jerichonana (vent Tica).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX   NCBI_TaxID=1049564 {ECO:0000313|EMBL:EGW54613.1, ECO:0000313|Proteomes:UP000005167};
RN   [1] {ECO:0000313|EMBL:EGW54613.1, ECO:0000313|Proteomes:UP000005167}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Gardebrecht A., Markert S., Felbeck H., Thuermer A., Albrecht D.,
RA   Wollherr A., Kabisch J., Lehmann R., Daniel R., Liesegang H., Hecker M.,
RA   Sievert S.M., Schweder T.;
RT   "The endosymbionts of the deep-sea tubeworms Riftia pachyptila and Tevnia
RT   jerichonana share an identical physiology as revealed by proteogenomic
RT   analyses.";
RL   ISME J. 0:0-0(2011).
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:EGW54613.1}.
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DR   EMBL; AFZB01000011; EGW54613.1; -; Genomic_DNA.
DR   AlphaFoldDB; G2FF66; -.
DR   PATRIC; fig|1049564.3.peg.1548; -.
DR   eggNOG; COG1660; Bacteria.
DR   Proteomes; UP000005167; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_00636; RapZ_like; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005337; RapZ-like.
DR   PANTHER; PTHR30448:SF0; RNASE ADAPTER PROTEIN RAPZ; 1.
DR   PANTHER; PTHR30448; UNCHARACTERIZED; 1.
DR   Pfam; PF03668; ATP_bind_2; 1.
DR   PIRSF; PIRSF005052; P-loopkin; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005167}.
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00636"
FT   BINDING         64..67
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00636"
SQ   SEQUENCE   288 AA;  32702 MW;  056487CEF13E5963 CRC64;
     MATGIRLLII TGLSGSGKTI ALHTLEDLGY YCIDNLPICL LEAFSNHLVE DPEPIFRHTA
     VGIDARSQPS HIAKLPEMVA KMREQGIDCE MIFLEAQQET LIKRFSETRR KHPLSDDDHS
     LDEAIRQEQE VLEPLASTAD LRIDTTHTNL HELRDLIRGR VTGGSRQVSL LFESFGFKHG
     VPRDVDFVFD VRCLPNPHWQ TELRPLTGLD GPVANFLESS EESSQMQADL TRFLESWIPR
     FEADGRSYLT IAIGCTGGQH RSVYITDQLY RHFKQQGRNV LSRHRELS
//