Detailed information of ANN22756-RA in Montipora grisea

Genomic Location: Scaffold_22__1_contigs__length_3165292:1708430...1709041
NR annotation: MCE2394988.1, septum formation inhibitor Maf [Candidatus Poribacteria bacterium]
Species Montipora grisea · all data for this species · gene families


 Gene Structure
More details in JBrowse  Sequence
CDS
Transcript
Protein
 UniProt (Swiss-Prot top hit)
UniProt accessionDescription
A5D426dTTP/UTP pyrophosphatase OS=Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) OX=370438 GN=PTH_0815 PE=3 SV=1
A4J7K7dTTP/UTP pyrophosphatase OS=Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1) OX=349161 GN=Dred_2550 PE=3 SV=1
B8I6Q1dTTP/UTP pyrophosphatase OS=Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10) OX=394503 GN=Ccel_2565 PE=3 SV=1
 Gene family
Family typeMembership / link
Orthogroup (gene family)OG0005066 (this species only)

 Pfam domain
Pfam accessionPfam nameDescriptionTypeSource
PF02545
all species →
MafMaf-like proteinDomainInterproscan

 InterPro
InterPro termTypeDescriptionSource
IPR003697
all species →
FamilyNucleoside triphosphate pyrophosphatase Maf-like proteinInterproscan
IPR029001
all species →
Homologous_superfamilyInosine triphosphate pyrophosphatase-likeInterproscan

 PANTHER
PANTHER termDescriptionSource
PTHR43213
all species →
BIFUNCTIONAL DTTP/UTP PYROPHOSPHATASE/METHYLTRANSFERASE PROTEIN-RELATEDInterproscan

 Gene Ontology
GO termCategoryDescriptionSource
GO:0047429
all species →
Molecular Functionnucleoside triphosphate diphosphatase activityInterproscan

Search by domain instead of by gene. Any accession above (InterPro, Pfam, PANTHER, GO, KEGG) can be used as a query on the Functional Domain Search page, which searches all 148 annotated genomes at once.
 KEGG pathway
KOEnzymeEnzyme IDPathwayMap IDSource
K06287yhdE; nucleoside triphosphate pyrophosphataseEC:3.6.1.-
Pyrimidine metabolismko00240deepkoala

Searching by KO or pathway ID across all species is available on the KEGG Pathway page.
TOP