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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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AEJ62095.1Glycosyl transferase family 39; PFAM: Dolichyl-phosphate-mannose-protein mannosyltransferase; COGs: COG1928 Dolichyl-phosphate-mannose--protein O-mannosyl transferase; InterPro IPR003342; KEGG: sta:STHERM_c17650 hypothetical protein; PFAM: Glycosyl transferase, family 39; SPTR: Glycosyl transferase family 39. (1218 aa)    
Predicted Functional Partners:
AEJ62096.1
PFAM: Glycosyl transferase family 2; COGs: COG0463 Glycosyltransferase involved in cell wall biogenesis; InterPro IPR001173; KEGG: sta:STHERM_c17660 glycosyltransferase; PFAM: Glycosyl transferase, family 2; SPTR: Glycosyl transferase family 2.
 
 
 0.880
AEJ62097.1
PFAM: GtrA-like protein; COGs: COG2246 membrane protein; InterPro IPR007267; KEGG: sta:STHERM_c17670 membrane spanning protein; PFAM: GtrA-like protein; SPTR: GtrA family protein.
 
     0.872
AEJ60315.1
Phosphatidate cytidylyltransferase; COGs: COG0170 Dolichol kinase; InterPro IPR000374; KEGG: sta:STHERM_c00280 phosphatidate cytidylyltransferase; PFAM: Phosphatidate cytidylyltransferase; SPTR: Phosphatidate cytidylyltransferase.
   
 
 0.673
plsY
Glycerol-3-phosphate acyltransferase; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
   
 
 0.673
AEJ62094.1
PFAM: Acyltransferase; TIGRFAM: 1-acyl-sn-glycerol-3-phosphate acyltransferases; COGs: COG0204 1-acyl-sn-glycerol-3-phosphate acyltransferase; InterPro IPR002123; KEGG: sta:STHERM_c17640 acyltransferase; PFAM: Phospholipid/glycerol acyltransferase; SMART: Phospholipid/glycerol acyltransferase; SPTR: Phospholipid/glycerol acyltransferase.
   
   0.543
dapL
LL-diaminopimelate aminotransferase; Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL- diaminopimelate.
       0.501
AEJ60650.1
PFAM: Glycosyl hydrolases family 31; COGs: COG1501 Alpha-glucosidase family 31 of glycosyl hydrolase; InterPro IPR000322; KEGG: sta:STHERM_c03990 glycoside hydrolase, family 31; PFAM: Glycoside hydrolase, family 31; SPTR: Glycoside hydrolase family 31.
    
 
 0.435
AEJ61316.1
PFAM: Glycosyl hydrolases family 31; COGs: COG1501 Alpha-glucosidase family 31 of glycosyl hydrolase; InterPro IPR000322; KEGG: sta:STHERM_c10190 alpha-glucosidase 2; PFAM: Glycoside hydrolase, family 31; SPTR: Alpha-glucosidase.
    
 
 0.435
AEJ62092.1
PFAM: Histidine kinase; Response regulator receiver domain; Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; PAS fold; TIGRFAM: PAS domain S-box; COGs: COG3920 Signal transduction histidine kinase; InterProIPR001789:IPR013767:IPR011495:IPR003594:IPR 000014; KEGG: sta:STHERM_c17620 sensor histidine kinase; PFAM: ATP-binding region, ATPase-like; PAS fold; Signal transduction response regulator, receiver region; Signal transduction histidine kinase, subgroup 2, dimerisation and phosphoacceptor region; SMART: Signal transduction response regulator, receiver region; PAS; ATP-binding [...]
     
 0.409
secY
Preprotein translocase, SecY subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
   
 
 0.407
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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