Detailed information of CAB3985860.1 in Paramuricea clavata

Genomic Location: :...
NR annotation: CAB3985860.1, 2-oxoglutarate and iron-dependent oxygenase domain-containing 2 isoform X1 [Paramuricea clavata]


 Gene Structure
More details in Jbrowse  Sequence
CDS
Transcript
Protein
 Uniprot
Uniprot termDescription
Q28C222-oxoglutarate and iron-dependent oxygenase domain-containing protein 2 OS=Xenopus tropicalis OX=8364 GN=ogfod2 PE=2 SV=1
A3KGZ22-oxoglutarate and iron-dependent oxygenase domain-containing protein 2 OS=Danio rerio OX=7955 GN=ogfod2 PE=2 SV=1
Q6N0632-oxoglutarate and iron-dependent oxygenase domain-containing protein 2 OS=Homo sapiens OX=9606 GN=OGFOD2 PE=1 SV=2

 Pfam domain
Pfam accessionPfam nameDescriptionTypeSource
PF00083Sugar_trSugar (and other) transporterFamilyInterproscan

 InterPro
InterPro termTypeDescriptionSource
IPR020846DomainMajor facilitator superfamily domainInterproscan
IPR005829Conserved_siteSugar transporter, conserved siteInterproscan
IPR036259Homologous_superfamilyMFS transporter superfamilyInterproscan
IPR006620DomainProlyl 4-hydroxylase, alpha subunitInterproscan
IPR005123DomainOxoglutarate/iron-dependent dioxygenaseInterproscan
IPR005828FamilyMajor facilitator, sugar transporter-likeInterproscan

 PANTHER
PANTHER termDescriptionSource
PTHR24064SOLUTE CARRIER FAMILY 22 MEMBERInterproscan

 Gene Ontology
GO termsCategoryDescriptionSource
GO:0022857Molecular Functiontransmembrane transporter activityInterproscan
GO:0016020Cellular ComponentmembraneInterproscan
GO:0055085Biological Processtransmembrane transportInterproscan
GO:0005506Molecular Functioniron ion bindingInterproscan
GO:0016705Molecular Functionoxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygenInterproscan
GO:0031418Molecular FunctionL-ascorbic acid bindingInterproscan

 KEGG pathway
KOEnzymeEnzyme IDpathwaymapIDSource
K08202SLC22A4_5, OCTN; MFS transporter, OCT family, solute carrier family 22 (organic cation transporter), member 4/5-Transportersko02000deepkoala

TOP