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Conserved domains on  [gi|2443687607|ref|WP_273278984|]
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MULTISPECIES: 7-cyano-7-deazaguanine synthase QueC [Methanothrix]

Protein Classification

7-cyano-7-deazaguanine synthase( domain architecture ID 10001804)

7-cyano-7-deazaguanine synthase QueC catalyzes the transformation of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ0) as part of the queuosine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-215 2.74e-105

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: 302.47  E-value: 2.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   1 MKAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVA-HHIIDLSTLAAFlGESALLG-KKE 78
Cdd:COG0603     3 KKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGeHKVIDLDFLGEI-GGSALTDdSIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  79 VPSCHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTaWNPVELQAP 158
Cdd:COG0603    82 VPEGHYAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGT-KRPVRIHTP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2443687607 159 FVHMTKADIVRMGLKLQVPYELTWSCYKGKAMPCRTCPTCIEREEAFALCGCRDPLI 215
Cdd:COG0603   161 LMHLSKAEIVKLGLELGVPYELTWSCYNGGGRACGRCDSCRLRLEAFAEAGIPDPTE 217
 
Name Accession Description Interval E-value
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-215 2.74e-105

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: 302.47  E-value: 2.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   1 MKAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVA-HHIIDLSTLAAFlGESALLG-KKE 78
Cdd:COG0603     3 KKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGeHKVIDLDFLGEI-GGSALTDdSIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  79 VPSCHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTaWNPVELQAP 158
Cdd:COG0603    82 VPEGHYAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGT-KRPVRIHTP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2443687607 159 FVHMTKADIVRMGLKLQVPYELTWSCYKGKAMPCRTCPTCIEREEAFALCGCRDPLI 215
Cdd:COG0603   161 LMHLSKAEIVKLGLELGVPYELTWSCYNGGGRACGRCDSCRLRLEAFAEAGIPDPTE 217
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 1-206 7.11e-100

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: 288.36  E-value: 7.11e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   1 MKAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSR-LDVAHHIIDLSTLAAFLGESALLGKKEV 79
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKlLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  80 PSCHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTAwNPVELQAPF 159
Cdd:cd01995    81 PDGEYDEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTA-TGVKVVAPL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2443687607 160 VHMTKADIVRMGLKLQVPYELTWSCYKGKAMPCRTCPTCIEREEAFA 206
Cdd:cd01995   160 IGLSKAEIVKLGVELGVPLELTWSCYRGGEKHCGRCESCRLRKRAFE 206
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 2-209 2.68e-90

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: 264.09  E-value: 2.68e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   2 KAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVAHHIIDLSTLAAFLGESALLGKKEVPS 81
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKILDLDFLKQIGGSALTDDSIEVPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  82 CHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTAWNPVELQAPFVH 161
Cdd:pfam06508  81 AELESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGTMGKPIEIHTPLMD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2443687607 162 MTKADIVRMGLKLQVPYELTWSCYKG--KAMPCRTCPTCIEREEAFALCG 209
Cdd:pfam06508 161 LSKAEIVKLGDELGVPYELTWSCYNGgeEGDGCGECPACRLRLKGFEEAG 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 3-201 3.05e-79

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: 235.75  E-value: 3.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   3 AVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVAHHIIDLSTLAAfLGESALLGKKEVPSC 82
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHHLLDLSLLNQ-LGGSALTREQEIPEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  83 HYTEE-AARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTaWNPVELQAPFVH 161
Cdd:TIGR00364  80 KSNEEdTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGM-LTPVEIRAPLMD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2443687607 162 MTKADIVRMGLKL---QVPYELTWSCYKGKAMPCRTCPTCIER 201
Cdd:TIGR00364 159 LTKAEIVKLADELgvlDLVIKLTYSCYAGGGEGCGKCPSCMLR 201
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 2-198 1.92e-31

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 114.79  E-value: 1.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   2 KAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDV-AHHIIDLSTLAAfLGESALLGKK-EV 79
Cdd:PRK11106    3 RAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGArAHKVLDVTLLNE-LAVSSLTRDSiPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  80 PSCHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTAwNPVELQAPF 159
Cdd:PRK11106   82 PDYEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMA-KDIRFETPL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2443687607 160 VHMTKADIVRMG---LKLQVPYELTWSCYKG-KAMPCRTCPTC 198
Cdd:PRK11106  161 MWLNKAETWALAdyyGQLDLVRHETLTCYNGiKGDGCGHCAAC 203
 
Name Accession Description Interval E-value
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-215 2.74e-105

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: 302.47  E-value: 2.74e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   1 MKAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVA-HHIIDLSTLAAFlGESALLG-KKE 78
Cdd:COG0603     3 KKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGeHKVIDLDFLGEI-GGSALTDdSIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  79 VPSCHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTaWNPVELQAP 158
Cdd:COG0603    82 VPEGHYAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGT-KRPVRIHTP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2443687607 159 FVHMTKADIVRMGLKLQVPYELTWSCYKGKAMPCRTCPTCIEREEAFALCGCRDPLI 215
Cdd:COG0603   161 LMHLSKAEIVKLGLELGVPYELTWSCYNGGGRACGRCDSCRLRLEAFAEAGIPDPTE 217
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 1-206 7.11e-100

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: 288.36  E-value: 7.11e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   1 MKAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSR-LDVAHHIIDLSTLAAFLGESALLGKKEV 79
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKlLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  80 PSCHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTAwNPVELQAPF 159
Cdd:cd01995    81 PDGEYDEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTA-TGVKVVAPL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2443687607 160 VHMTKADIVRMGLKLQVPYELTWSCYKGKAMPCRTCPTCIEREEAFA 206
Cdd:cd01995   160 IGLSKAEIVKLGVELGVPLELTWSCYRGGEKHCGRCESCRLRKRAFE 206
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 2-209 2.68e-90

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: 264.09  E-value: 2.68e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   2 KAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVAHHIIDLSTLAAFLGESALLGKKEVPS 81
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKILDLDFLKQIGGSALTDDSIEVPK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  82 CHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTAWNPVELQAPFVH 161
Cdd:pfam06508  81 AELESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGTMGKPIEIHTPLMD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2443687607 162 MTKADIVRMGLKLQVPYELTWSCYKG--KAMPCRTCPTCIEREEAFALCG 209
Cdd:pfam06508 161 LSKAEIVKLGDELGVPYELTWSCYNGgeEGDGCGECPACRLRLKGFEEAG 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 3-201 3.05e-79

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: 235.75  E-value: 3.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   3 AVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVAHHIIDLSTLAAfLGESALLGKKEVPSC 82
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHHLLDLSLLNQ-LGGSALTREQEIPEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  83 HYTEE-AARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTaWNPVELQAPFVH 161
Cdd:TIGR00364  80 KSNEEdTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGM-LTPVEIRAPLMD 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2443687607 162 MTKADIVRMGLKL---QVPYELTWSCYKGKAMPCRTCPTCIER 201
Cdd:TIGR00364 159 LTKAEIVKLADELgvlDLVIKLTYSCYAGGGEGCGKCPSCMLR 201
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 2-198 1.92e-31

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 114.79  E-value: 1.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   2 KAVLILSGGLDSTTLLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDV-AHHIIDLSTLAAfLGESALLGKK-EV 79
Cdd:PRK11106    3 RAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGArAHKVLDVTLLNE-LAVSSLTRDSiPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607  80 PSCHYTEEAARQTVVPNRNMIMLSVAAGYAEAHEITELFYAAHKNDQTIYPDCRPEFVEALKPAIRLGTAwNPVELQAPF 159
Cdd:PRK11106   82 PDYEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMA-KDIRFETPL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2443687607 160 VHMTKADIVRMG---LKLQVPYELTWSCYKG-KAMPCRTCPTC 198
Cdd:PRK11106  161 MWLNKAETWALAdyyGQLDLVRHETLTCYNGiKGDGCGHCAAC 203
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 3-125 2.18e-04

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: 41.11  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   3 AVLiLSGGLDSTTLLY--KLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVAHHIIDLSTLAAFlgesallgkKEVP 80
Cdd:cd01991     6 GVL-LSGGLDSSLIAAlaARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEVEVTIEELL---------DALP 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2443687607  81 SCHYTEEaaRQTVVPNRNMIMLSVAAGYAEAHEIT---------ELF--YAAHKND 125
Cdd:cd01991    76 DVILIYP--TDTPMDLSIAIPLYFASRLAGKLGAKvvlsgegadELFggYSRHRDA 129
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 2-126 4.40e-04

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 39.92  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   2 KAVLILSGGLDSTTLLYKLLADGYL----VDALTFNYG--QKHKKEIDCAIAITSRLDVAHHIIDLstlaaFLGESALLG 75
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLQPKikikLIAAHVDHGlrPESDEEAEFVQQFCRKLNIPLEIKKV-----DVKALAKGK 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2443687607  76 KKEVpschytEEAARQtvvpnrnmimlsvaAGY------AEAHEITELFYAAHKNDQ 126
Cdd:TIGR02432  76 KKNL------EEAARE--------------ARYdffeeiAKKHGADYILTAHHADDQ 112
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 4-126 5.55e-04

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 39.50  E-value: 5.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   4 VLI-LSGGLDSTTLLYkLLAD-----GYLVDALTFNYGQKH--KKEIDCAIAITSRLDVAHHIIDLsTLAAFLGESallg 75
Cdd:cd01992     2 ILVaVSGGPDSMALLH-LLKElrpklGLKLVAVHVDHGLREesAEEAQFVAKLCKKLGIPLHILTV-TEAPKSGGN---- 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2443687607  76 kkevpschyTEEAARQtvvpnrnmIMLSVAAGYAEAHEITELFYAAHKNDQ 126
Cdd:cd01992    76 ---------LEAAARE--------ARYAFLERAAKEHGIDVLLTAHHLDDQ 109
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 4-91 6.16e-04

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 39.82  E-value: 6.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   4 VLI-LSGGLDSTTLLYkLLAD-----GYLVDALTFNYGQKH--KKEIDCAIAITSRLDVAHHIIDLSTLAAFLGESallg 75
Cdd:COG0037    18 ILVaVSGGKDSLALLH-LLAKlrrrlGFELVAVHVDHGLREesDEDAEFVAELCEELGIPLHVVRVDVPAIAKKEG---- 92

                          90
                  ....*....|....*.
gi 2443687607  76 kkevpscHYTEEAARQ 91
Cdd:COG0037    93 -------KSPEAAARR 101
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 2-62 2.17e-03

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 37.92  E-value: 2.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443687607   2 KAVLILSGGLDSTT--LLYKLLADGYLVDALTFNYGQKHKKEIDCAIAITSRLDVAHHIIDLS 62
Cdd:cd00553    25 GFVLGLSGGIDSAVvaALAVRALGAENVLALIMPSRYSSKETRDDAKALAENLGIEYRTIDID 87
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
1-65 4.47e-03

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 37.01  E-value: 4.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2443687607   1 MKAVLI-LSGGLDSTTLLY---KLLADGYLvdALTFNYGQKHKKEIDCAIAITSRLDVAHHIIDLSTLA 65
Cdd:COG1606    15 LGSVLVaFSGGVDSTLLAKvahDVLGDRVL--AVTADSPSLPERELEEAKELAKEIGIRHEVIETDELE 81
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 3-43 4.51e-03

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 34.74  E-value: 4.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2443687607   3 AVLILSGGLDSTTLLYKL--LADGYLVDALTFNYGQKHKKEID 43
Cdd:cd01986     1 VVVGYSGGKDSSVALHLAsrLGRKAEVAVVHIDHGIGFKEEAE 43
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 4-84 5.85e-03

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 36.53  E-value: 5.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   4 VLI-LSGGLDSTTLLYKLLADGYLVDALTFNYGQKH--KKEIDCAIAITSRLDVAHHIIDLSTLAAfLGESALLGKKEVP 80
Cdd:cd01993    11 ILVaVSGGKDSLALLAVLKKLGYNVEALYINLGIGEysEKSEEVVKKLAEKLNLPLHVVDLKEEYG-LGIPELAKKSRRP 89


                  ....
gi 2443687607  81 SCHY 84
Cdd:cd01993    90 PCSV 93
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 7-127 6.45e-03

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 36.07  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2443687607   7 LSGGLDSTTLLYKLLAD----GYLVDALTFNYG--QKHKKEIDCAIAITSRLDVAHHIIDLsTLAAFLGESallgkkevp 80
Cdd:pfam01171   3 VSGGPDSMALLYLLAKLkiklGIELTAAHVNHGlrEESDREAEHVQALCRQLGIPLEILRV-DVAKKSGEN--------- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2443687607  81 schyTEEAARQtvvpnrnmIMLSVAAGYAEAHEITELFYAAHKNDQT 127
Cdd:pfam01171  73 ----LEAAARE--------ARYDFFEEALKKHGADVLLTAHHLDDQL 107
PRK13820 PRK13820
argininosuccinate synthase; Provisional
 1-60 7.82e-03

argininosuccinate synthase; Provisional


Pssm-ID: 237521  Cd Length: 394  Bit Score: 36.83  E-value: 7.82e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2443687607   1 MKAVLILSGGLDsTTLLYKLLADGYLVD---ALTFNYGQKhKKEIDCAIAITSRLDVAHHIID 60
Cdd:PRK13820    3 KKVVLAYSGGLD-TSVCVPLLKEKYGYDeviTVTVDVGQP-EEEIKEAEEKAKKLGDKHYTID 63
 
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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