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STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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ACX72014.1TIGRFAM: methyl-coenzyme M reductase operon protein D; PFAM: Methyl-coenzyme M reductase, protein D; KEGG: mja:MJ0843 methyl coenzyme M reductase I, operon protein D (McrD). (162 aa)    
Predicted Functional Partners:
ACX72013.1
KEGG: mja:MJ0842 methyl coenzyme M reductase I, subunit beta (McrB); TIGRFAM: methyl-coenzyme M reductase, beta subunit; PFAM: Methyl-coenzyme M reductase, beta subunit.
 
 
 0.999
ACX72015.1
TIGRFAM: methyl-coenzyme M reductase I operon protein C; PFAM: Methyl-coenzyme M reductase protein C; KEGG: mja:MJ0844 methyl coenzyme M reductase I, operon protein C (McrC).
 
  
 0.999
ACX72016.1
KEGG: mfe:Mefer_0937 methyl-coenzyme M reductase, gamma subunit; TIGRFAM: methyl-coenzyme M reductase, gamma subunit; PFAM: Methyl-coenzyme M reductase, gamma subunit.
 
 
 0.999
ACX72017.1
Methyl-coenzyme M reductase, alpha subunit; Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.
 
 
 0.999
ACX73052.1
Methyl-coenzyme M reductase, alpha subunit; Component of the methyl-coenzyme M reductase (MCR) I that catalyzes the reductive cleavage of methyl-coenzyme M (CoM-S-CH3 or 2- (methylthio)ethanesulfonate) using coenzyme B (CoB or 7- mercaptoheptanoylthreonine phosphate) as reductant which results in the production of methane and the mixed heterodisulfide of CoB and CoM (CoM-S-S-CoB). This is the final step in methanogenesis.
 
 
 0.993
ACX73051.1
KEGG: mja:MJ0082 methyl coenzyme M reductase II, subunit gamma (MtrG); TIGRFAM: methyl-coenzyme M reductase, gamma subunit; PFAM: Methyl-coenzyme M reductase, gamma subunit.
 
 
 0.991
ACX73050.1
KEGG: mja:MJ0081 methyl coenzyme M reductase II, subunit beta (MrtB); TIGRFAM: methyl-coenzyme M reductase, beta subunit; PFAM: Methyl-coenzyme M reductase, beta subunit.
 
 
 0.990
mtrE
Tetrahydromethanopterin S-methyltransferase, subunit E; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
 
 
  0.953
mtrD
Tetrahydromethanopterin S-methyltransferase, subunit D; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step.
 
 
  0.952
mtrA
Tetrahydromethanopterin S-methyltransferase, subunit A; Part of a complex that catalyzes the formation of methyl- coenzyme M and tetrahydromethanopterin from coenzyme M and methyl- tetrahydromethanopterin. This is an energy-conserving, sodium-ion translocating step; Belongs to the MtrA family.
 
 
 0.951
Your Current Organism:
Methanocaldococcus vulcanius
NCBI taxonomy Id: 579137
Other names: M. vulcanius M7, Methanocaldococcus vulcanius M7, Methanocaldococcus vulcanius str. M7, Methanocaldococcus vulcanius strain M7
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.