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Conserved domains on  [gi|2108422621|gb|UCH79581|]
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MAG: 7-cyano-7-deazaguanine synthase QueC [Candidatus Coatesbacteria bacterium]

Protein Classification

adenine nucleotide alpha hydrolase family protein( domain architecture ID 188)

AANH (adenine nucleotide alpha hydrolase) family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
1-195 2.99e-51

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member cd01995:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 208  Bit Score: 164.71  E-value: 2.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   1 MKAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRLCRHYGVGHRRLALPWLREALPRALARPGTPL 80
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  81 PSRLGDVDA---VWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKSYTA 157
Cdd:cd01995    81 PDGEYDEESipsTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPLI 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2108422621 158 EWDKVTIVRRAVGLGVPLEYVYPCYGEGPAPCGRCASC 195
Cdd:cd01995   161 GLSKAEIVKLGVELGVPLELTWSCYRGGEKHCGRCESC 198
 
Name Accession Description Interval E-value
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
1-195 2.99e-51

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 164.71  E-value: 2.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   1 MKAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRLCRHYGVGHRRLALPWLREALPRALARPGTPL 80
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  81 PSRLGDVDA---VWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKSYTA 157
Cdd:cd01995    81 PDGEYDEESipsTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPLI 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2108422621 158 EWDKVTIVRRAVGLGVPLEYVYPCYGEGPAPCGRCASC 195
Cdd:cd01995   161 GLSKAEIVKLGVELGVPLELTWSCYRGGEKHCGRCESC 198
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
1-195 1.77e-38

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 132.59  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   1 MKAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRlCRHYGVG-HRRLALPWLREALPRALARPGTP 79
Cdd:COG0603     3 KKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRI-AKALGVGeHKVIDLDFLGEIGGSALTDDSIE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  80 LPSRLGDVD---AVWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKSYT 156
Cdd:COG0603    82 VPEGHYAEEgipSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTPL 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2108422621 157 AEWDKVTIVRRAVGLGVPLEYVYPCYGEGPAPCGRCASC 195
Cdd:COG0603   162 MHLSKAEIVKLGLELGVPYELTWSCYNGGGRACGRCDSC 200
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
2-195 1.35e-34

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 122.34  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   2 KAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRlCRHYGVGHRRLALPWLREALPRALARPGTPLP 81
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKI-AKALGVEHKILDLDFLKQIGGSALTDDSIEVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  82 S---RLGDVDAVWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGR-VQLKSYTA 157
Cdd:pfam06508  80 KaelESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGTMGKpIEIHTPLM 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2108422621 158 EWDKVTIVRRAVGLGVPLEYVYPCY--GEGPAPCGRCASC 195
Cdd:pfam06508 160 DLSKAEIVKLGDELGVPYELTWSCYngGEEGDGCGECPAC 199
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
3-195 1.14e-31

queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General]


Pssm-ID: 129461 [Multi-domain]  Cd Length: 201  Bit Score: 114.41  E-value: 1.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   3 AVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRlCRHYGVGHRRLALPWLREALPRALARPGTPLPS 82
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKI-AEALGIEHHLLDLSLLNQLGGSALTREQEIPEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  83 RLGDVD---AVWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKSYTAEW 159
Cdd:TIGR00364  80 KSNEEDtlpNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDL 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2108422621 160 DKVTIVRRAVGLG---VPLEYVYPCYGEGPAPCGRCASC 195
Cdd:TIGR00364 160 TKAEIVKLADELGvldLVIKLTYSCYAGGGEGCGKCPSC 198
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
2-195 1.65e-04

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 41.22  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   2 KAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRLCRHYGVGHRRLALPWLREALPRALARPGTPLP 81
Cdd:PRK11106    3 RAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIPVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  82 SRLGDVDAV---WVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKS---- 154
Cdd:PRK11106   83 DYEPEADGLpntFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETplmw 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2108422621 155 -YTAE-------WDKVTIVRravglgvplEYVYPCY----GEGpapCGRCASC 195
Cdd:PRK11106  163 lNKAEtwaladyYGQLDLVR---------HETLTCYngikGDG---CGHCAAC 203
 
Name Accession Description Interval E-value
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
1-195 2.99e-51

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 164.71  E-value: 2.99e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   1 MKAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRLCRHYGVGHRRLALPWLREALPRALARPGTPL 80
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  81 PSRLGDVDA---VWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKSYTA 157
Cdd:cd01995    81 PDGEYDEESipsTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPLI 160
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2108422621 158 EWDKVTIVRRAVGLGVPLEYVYPCYGEGPAPCGRCASC 195
Cdd:cd01995   161 GLSKAEIVKLGVELGVPLELTWSCYRGGEKHCGRCESC 198
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
1-195 1.77e-38

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 132.59  E-value: 1.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   1 MKAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRlCRHYGVG-HRRLALPWLREALPRALARPGTP 79
Cdd:COG0603     3 KKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRI-AKALGVGeHKVIDLDFLGEIGGSALTDDSIE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  80 LPSRLGDVD---AVWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKSYT 156
Cdd:COG0603    82 VPEGHYAEEgipSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTPL 161
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2108422621 157 AEWDKVTIVRRAVGLGVPLEYVYPCYGEGPAPCGRCASC 195
Cdd:COG0603   162 MHLSKAEIVKLGLELGVPYELTWSCYNGGGRACGRCDSC 200
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
2-195 1.35e-34

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 122.34  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   2 KAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRlCRHYGVGHRRLALPWLREALPRALARPGTPLP 81
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKI-AKALGVEHKILDLDFLKQIGGSALTDDSIEVP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  82 S---RLGDVDAVWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGR-VQLKSYTA 157
Cdd:pfam06508  80 KaelESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGTMGKpIEIHTPLM 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2108422621 158 EWDKVTIVRRAVGLGVPLEYVYPCY--GEGPAPCGRCASC 195
Cdd:pfam06508 160 DLSKAEIVKLGDELGVPYELTWSCYngGEEGDGCGECPAC 199
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
3-195 1.14e-31

queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General]


Pssm-ID: 129461 [Multi-domain]  Cd Length: 201  Bit Score: 114.41  E-value: 1.14e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   3 AVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRlCRHYGVGHRRLALPWLREALPRALARPGTPLPS 82
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKI-AEALGIEHHLLDLSLLNQLGGSALTREQEIPEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  83 RLGDVD---AVWVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKSYTAEW 159
Cdd:TIGR00364  80 KSNEEDtlpNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDL 159
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2108422621 160 DKVTIVRRAVGLG---VPLEYVYPCYGEGPAPCGRCASC 195
Cdd:TIGR00364 160 TKAEIVKLADELGvldLVIKLTYSCYAGGGEGCGKCPSC 198
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
2-195 1.65e-04

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 41.22  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621   2 KAVVLLSGGLDSALNLALAARYRKPLRAVTFDYGQRAARRELRAARRLCRHYGVGHRRLALPWLREALPRALARPGTPLP 81
Cdd:PRK11106    3 RAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIPVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108422621  82 SRLGDVDAV---WVPNRNGVFVAVGAAMAEAAGAAVVVAGFNAEEAAAFPDNSAAFVAASNRALRYSTRGRVQLKS---- 154
Cdd:PRK11106   83 DYEPEADGLpntFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETplmw 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2108422621 155 -YTAE-------WDKVTIVRravglgvplEYVYPCY----GEGpapCGRCASC 195
Cdd:PRK11106  163 lNKAEtwaladyYGQLDLVR---------HETLTCYngikGDG---CGHCAAC 203
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
5-34 8.16e-04

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis


Pssm-ID: 440136 [Multi-domain]  Cd Length: 558  Bit Score: 39.82  E-value: 8.16e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2108422621   5 VLLSGGLDSALNLALAARY-RKPLRAVTFDY 34
Cdd:COG0367   261 AFLSGGLDSSAIAALAARLsKGPLKTFSIGF 291
Asn_synthase pfam00733
Asparagine synthase; This family is always found associated with pfam00310. Members of this ...
5-36 5.21e-03

Asparagine synthase; This family is always found associated with pfam00310. Members of this family catalyze the conversion of aspartate to asparagine.


Pssm-ID: 395594 [Multi-domain]  Cd Length: 279  Bit Score: 37.21  E-value: 5.21e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2108422621   5 VLLSGGLDSALNLALAARYRK-PLRAVTFDYGQ 36
Cdd:pfam00733  22 AFLSGGLDSSSIAALAARQSPsPLHTFSIGFEG 54
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
5-35 7.74e-03

C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or synthetase) B is always associated with an N-terminal amidotransferase domain. Family members that contain this domain catalyze the conversion of aspartate to asparagine. Asparagine synthase B catalyzes the synthesis of asparagine from aspartate, Mg(2+)ATP, and glutamine. The three-dimensional architecture of the N-terminal domain of asparagine synthetase B is similar to that observed for glutamine phosphoribosylpyrophosphate amidotransferase while the molecular motif of the C-domain is reminiscent to that observed for GMP synthetase.


Pssm-ID: 467495 [Multi-domain]  Cd Length: 224  Bit Score: 36.48  E-value: 7.74e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2108422621   5 VLLSGGLDSALNLALAARY--RKPLRAVTFDYG 35
Cdd:cd01991     7 VLLSGGLDSSLIAALAARLlpETPIDLFTVGFE 39
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
2-22 8.74e-03

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 36.75  E-value: 8.74e-03
                          10        20
                  ....*....|....*....|.
gi 2108422621   2 KAVVLLSGGLDSALNLALAAR 22
Cdd:COG0171   288 GVVLGLSGGIDSALVAALAVD 308
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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