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Nmar_0049 protein (Nitrosopumilus maritimus) - STRING interaction network
"Nmar_0049" - KEGG: sso:SSO2911 phosphoadenosine phosphosulfate reductase in Nitrosopumilus maritimus
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
Nmar_0049KEGG- sso-SSO2911 phosphoadenosine phosphosulfate reductase; TIGRFAM- adenylylsulfate reductase, thioredoxin dependent; PFAM- phosphoadenosine phosphosulfate reductase (241 aa)    
Predicted Functional Partners:
Nmar_0023
Adenylyl-sulfate kinase; Catalyzes the synthesis of activated sulfate (179 aa)
 
  0.997
Nmar_0679
PFAM- nitrite/sulfite reductase hemoprotein beta-component ferrodoxin domain protein; nitrite and sulphite reductase 4Fe-4S region; KEGG- tth-TTC0313 ferredoxin-nitrite reductase (602 aa)
  0.996
sat
KEGG- hbu-Hbut_1499 sulfate adenylyltransferase; TIGRFAM- sulfate adenylyltransferase; PFAM- ATP-sulfurylase; Belongs to the sulfate adenylyltransferase family (380 aa)
   
   
  0.961
Nmar_1697
PFAM- Rhodanese domain protein; KEGG- noc-Noc_0191 thiosulfate sulfurtransferase (258 aa)
   
  0.913
Nmar_0680
PFAM- Rhodanese domain protein; KEGG- bcy-Bcer98_1310 rhodanese domain protein (265 aa)
   
  0.913
Nmar_0441
Sulfurtransferase; PFAM- Rhodanese domain protein; KEGG- ttj-TTHA1028 thiosulfate sulfurtransferase (281 aa)
   
  0.913
Nmar_0024
PFAM- inositol monophosphatase; KEGG- mca-MCA2983 3’(2’),5’-bisphosphate nucleotidase (271 aa)
         
    0.900
Nmar_0051
annotation not available (221 aa)
              0.741
rtcA
RNA 3’-terminal phosphate cyclase; Catalyzes the conversion of 3’-phosphate to a 2’,3’- cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps- (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3’P to produce RNA- N3’PP5’A; (C) and attack of the adjacent 2’-hydroxyl on the 3’- phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (338 aa)
           
  0.654
Nmar_1548
PFAM- UBA/THIF-type NAD/FAD binding protein; thiamineS protein; MoeZ/MoeB domain protein; KEGG- wsu-WS1006 molybdopterin biosynthesis protein MoeB (443 aa)
 
   
  0.653
Your Current Organism:
Nitrosopumilus maritimus
NCBI taxonomy Id: 436308
Other names: N. maritimus SCM1, Nitrosopumilus maritimus, Nitrosopumilus maritimus SCM1, Nitrosopumilus maritimus str. SCM1, Nitrosopumilus maritimus strain SCM1, Seattle Aquarium strain SCM1
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