ID   MESH1_DANRE             Reviewed;         180 AA.
AC   Q568P1;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1;
DE            EC=3.1.7.2;
DE   AltName: Full=HD domain-containing protein 3;
DE   AltName: Full=Metazoan SpoT homolog 1;
DE            Short=MESH1;
DE   AltName: Full=Penta-phosphate guanosine-3'-pyrophosphohydrolase;
DE            Short=(ppGpp)ase;
GN   Name=hddc3; Synonyms=Mesh1; ORFNames=zgc:110184;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: ppGpp hydrolyzing enzyme involved in starvation response.
CC       {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the MESH1 family. {ECO:0000305}.
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DR   EMBL; BC092780; AAH92780.1; -; mRNA.
DR   RefSeq; NP_001017835.1; NM_001017835.1.
DR   AlphaFoldDB; Q568P1; -.
DR   SMR; Q568P1; -.
DR   STRING; 7955.ENSDARP00000033279; -.
DR   PaxDb; 7955-ENSDARP00000033279; -.
DR   GeneID; 550533; -.
DR   KEGG; dre:550533; -.
DR   AGR; ZFIN:ZDB-GENE-050417-377; -.
DR   CTD; 374659; -.
DR   ZFIN; ZDB-GENE-050417-377; hddc3.
DR   eggNOG; KOG1157; Eukaryota.
DR   InParanoid; Q568P1; -.
DR   OrthoDB; 2783605at2759; -.
DR   PhylomeDB; Q568P1; -.
DR   PRO; PR:Q568P1; -.
DR   Proteomes; UP000000437; Chromosome 7.
DR   GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
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   PROSITE; PS51831; HD; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Manganese; Metal-binding; Reference proteome.
FT   CHAIN           1..180
FT                   /note="Guanosine-3',5'-bis(diphosphate) 3'-
FT                   pyrophosphohydrolase MESH1"
FT                   /id="PRO_0000263112"
FT   DOMAIN          33..128
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   ACT_SITE        66
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        67
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  20296 MW;  6CC9689FCDE3E8DE CRC64;
     MNCSSTAVLL ETVNFAAEKH RNQRHKDPEG TPYINHPIGV ARILSHEGEI TDVEVIQAAL
     LHDTVEDTDT TFEELESVFG ATVARIVQGV TDDKSLPKAE RERQQVEHAP HCSHQAKLVK
     LADKLYNLRD LNRCTPEGWS AQRVQEYFEW ASQVVKGLRG TNAAIEEKLQ QLFLERGVKL
//