node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACX96965.1 | glnD | Hneap_2148 | Hneap_2147 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | UTP-GlnB uridylyltransferase, GlnD; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | 0.773 |
ACX96965.1 | map | Hneap_2148 | Hneap_2146 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.752 |
ACX96965.1 | mnmE | Hneap_2148 | Hneap_2410 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | tRNA modification GTPase TrmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family. | 0.757 |
ACX96965.1 | rlmB | Hneap_2148 | Hneap_0352 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | RNA methyltransferase, TrmH family, group 3; Specifically methylates the ribose of guanosine 2251 in 23S rRNA. | 0.734 |
ACX96965.1 | rplC | Hneap_2148 | Hneap_0323 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | 50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | 0.767 |
ACX96965.1 | rplM | Hneap_2148 | Hneap_2044 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.726 |
ACX96965.1 | rplQ | Hneap_2148 | Hneap_0348 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | TIGRFAM: ribosomal protein L17; PFAM: ribosomal protein L17; KEGG: msu:MS2022 50S ribosomal protein L17. | 0.730 |
ACX96965.1 | rplU | Hneap_2148 | Hneap_0270 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.730 |
ACX96965.1 | rsfS | Hneap_2148 | Hneap_1739 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | Iojap-like protein; Functions as a ribosomal silencing factor. Interacts with ribosomal protein L14 (rplN), blocking formation of intersubunit bridge B8. Prevents association of the 30S and 50S ribosomal subunits and the formation of functional ribosomes, thus repressing translation. | 0.750 |
ACX96965.1 | truD | Hneap_2148 | Hneap_1148 | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | tRNA pseudouridine synthase D TruD; Responsible for synthesis of pseudouridine from uracil-13 in transfer RNAs; Belongs to the pseudouridine synthase TruD family. | 0.753 |
glnD | ACX96965.1 | Hneap_2147 | Hneap_2148 | UTP-GlnB uridylyltransferase, GlnD; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | 0.773 |
glnD | map | Hneap_2147 | Hneap_2146 | UTP-GlnB uridylyltransferase, GlnD; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 0.834 |
map | ACX96965.1 | Hneap_2146 | Hneap_2148 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | 0.752 |
map | glnD | Hneap_2146 | Hneap_2147 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | UTP-GlnB uridylyltransferase, GlnD; Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen assimilation and metabolism. | 0.834 |
map | rplC | Hneap_2146 | Hneap_0323 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | 50S ribosomal protein L3; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. | 0.987 |
map | rplM | Hneap_2146 | Hneap_2044 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.977 |
map | rplQ | Hneap_2146 | Hneap_0348 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | TIGRFAM: ribosomal protein L17; PFAM: ribosomal protein L17; KEGG: msu:MS2022 50S ribosomal protein L17. | 0.825 |
map | rplU | Hneap_2146 | Hneap_0270 | Methionine aminopeptidase, type I; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. | Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family. | 0.846 |
mnmE | ACX96965.1 | Hneap_2410 | Hneap_2148 | tRNA modification GTPase TrmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family. | PFAM: pseudouridine synthase; KEGG: pen:PSEEN1443 ribosomal large subunit pseudouridine synthase A. | 0.757 |
mnmE | rlmB | Hneap_2410 | Hneap_0352 | tRNA modification GTPase TrmE; Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA- cmnm(5)s(2)U34; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family. | RNA methyltransferase, TrmH family, group 3; Specifically methylates the ribose of guanosine 2251 in 23S rRNA. | 0.883 |