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Database: UniProt
Entry: D6WD98_TRICA
LinkDB: D6WD98_TRICA
Original site: D6WD98_TRICA 
ID   D6WD98_TRICA            Unreviewed;       300 AA.
AC   D6WD98;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1 {ECO:0000256|ARBA:ARBA00040793};
DE            EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
DE   AltName: Full=Metazoan SpoT homolog 1 {ECO:0000256|ARBA:ARBA00041464};
DE   AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase {ECO:0000256|ARBA:ARBA00041770};
GN   Name=AUGUSTUS-3.0.2_00063 {ECO:0000313|EMBL:EEZ99488.2};
GN   ORFNames=TcasGA2_TC000063 {ECO:0000313|EMBL:EEZ99488.2};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EEZ99488.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EEZ99488.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EEZ99488.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EEZ99488.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EEZ99488.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
CC   -!- FUNCTION: ppGpp hydrolyzing enzyme involved in starvation response.
CC       {ECO:0000256|ARBA:ARBA00037781}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC         H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00024273};
CC   -!- SIMILARITY: Belongs to the MESH1 family.
CC       {ECO:0000256|ARBA:ARBA00038354}.
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DR   EMBL; KQ971321; EEZ99488.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6WD98; -.
DR   STRING; 7070.D6WD98; -.
DR   EnsemblMetazoa; TC000063_001; TC000063_001; TC000063.
DR   eggNOG; KOG1157; Eukaryota.
DR   HOGENOM; CLU_084517_1_0_1; -.
DR   Proteomes; UP000007266; Linkage group 3.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 3.30.70.330; -; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   PANTHER; PTHR46246; GUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE MESH1; 1.
DR   PANTHER; PTHR46246:SF1; GUANOSINE-3',5'-BIS(DIPHOSPHATE) 3'-PYROPHOSPHOHYDROLASE MESH1; 1.
DR   Pfam; PF13328; HD_4; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266}.
FT   DOMAIN          32..127
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
SQ   SEQUENCE   300 AA;  34347 MW;  D3CE2D40899ABD94 CRC64;
     MTNIAGDLLK CVNFAAEKHK DQRRKNASKT PYINHPIGVA YILTHEAEID DLDVLQAALL
     HDTVEDTATT FEEIEQVFGK RVRDIVEEVT DDKSLPKEER KRLQIEHAPG ASHQAKLVKL
     ADKLYNLRDL ENSAPEGWSE QRIQEYFTWS SKVVAGLRGT NPALERSLDQ QSLCQTRPAY
     RQGRRLTAVK TYTIANESRH LFVYGVPKID LFSELKALCA KQGKLAKFHL VADHKTEIFT
     ECFHVVYDKF EVARKAKRLL DNKSFYGGIL HVCYAPEYES VDETRAKLLL RRQSILDYKG
//
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