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Conserved domains on  [gi|517491066|ref|WP_018661643|]
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7-cyano-7-deazaguanine synthase QueC [Heyndrickxia acidiproducens]

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 ...
 1-213 8.34e-129

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 PRK11106:

Pssm-ID: 469708  Cd Length: 231  Bit Score: 362.47  E-value: 8.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   1 MKKekALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVK-HYILDMSLLNQLAPNALTRDG 79
Cdd:PRK11106   1 MKR--AVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARaHKVLDVTLLNELAVSSLTRDS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066  80 IAVK--EGEDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHT 157
Cdd:PRK11106  79 IPVPdyEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFET 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517491066 158 PLMWLNKAETWKLADELNAFDFVREKTLTCYNGIIADGCGECPACKLRKRGLEEYL 213
Cdd:PRK11106 159 PLMWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYL 214
 
Name Accession Description Interval E-value
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 1-213 8.34e-129

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 362.47  E-value: 8.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   1 MKKekALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVK-HYILDMSLLNQLAPNALTRDG 79
Cdd:PRK11106   1 MKR--AVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARaHKVLDVTLLNELAVSSLTRDS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066  80 IAVK--EGEDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHT 157
Cdd:PRK11106  79 IPVPdyEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFET 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517491066 158 PLMWLNKAETWKLADELNAFDFVREKTLTCYNGIIADGCGECPACKLRKRGLEEYL 213
Cdd:PRK11106 159 PLMWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYL 214
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 5-213 1.77e-122

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: 345.37  E-value: 1.77e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066    5 KALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMSLLNQLAPNALTRDGIAV-- 82
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKILDLDFLKQIGGSALTDDSIEVpk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   83 KEGEDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNL-SMDQQFVIHTPLMW 161
Cdd:pfam06508  81 AELESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLgTMGKPIEIHTPLMD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517491066  162 LNKAETWKLADELNAfdfVREKTLTCYNG-IIADGCGECPACKLRKRGLEEYL 213
Cdd:pfam06508 161 LSKAEIVKLGDELGV---PYELTWSCYNGgEEGDGCGECPACRLRLKGFEEAG 210
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 2-212 2.21e-121

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: 343.30  E-value: 2.21e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   2 KKEKALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVK-HYILDMSLLNQLAPNALTRDGI 80
Cdd:COG0603    1 MMKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGeHKVIDLDFLGEIGGSALTDDSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066  81 AVKEG--EDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHTP 158
Cdd:COG0603   81 EVPEGhyAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517491066 159 LMWLNKAETWKLADELNAfdfVREKTLTCYNGiIADGCGECPACKLRKRGLEEY 212
Cdd:COG0603  161 LMHLSKAEIVKLGLELGV---PYELTWSCYNG-GGRACGRCDSCRLRLEAFAEA 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 6-205 4.75e-110

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: 313.56  E-value: 4.75e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066    6 ALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMSLLNQLAPNALTRDG--IAVK 83
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHHLLDLSLLNQLGGSALTREQeiPEQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   84 EGEDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHTPLMWLN 163
Cdd:TIGR00364  81 SNEEDTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDLT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 517491066  164 KAETWKLADELNAFDFVREKTLTCYNGiIADGCGECPACKLR 205
Cdd:TIGR00364 161 KAEIVKLADELGVLDLVIKLTYSCYAG-GGEGCGKCPSCMLR 201
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 4-212 2.21e-94

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: 274.49  E-value: 2.21e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   4 EKALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCA-RNIAEELGVKHYILDMSLLNQLAPNALTRDGIAV 82
Cdd:cd01995    1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAaKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066  83 KEGE--DGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHTPLM 160
Cdd:cd01995   81 PDGEydEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPLI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517491066 161 WLNKAETWKLADELnafDFVREKTLTCYNGIIaDGCGECPACKLRKRGLEEY 212
Cdd:cd01995  161 GLSKAEIVKLGVEL---GVPLELTWSCYRGGE-KHCGRCESCRLRKRAFEEA 208
 
Name Accession Description Interval E-value
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 1-213 8.34e-129

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 362.47  E-value: 8.34e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   1 MKKekALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVK-HYILDMSLLNQLAPNALTRDG 79
Cdd:PRK11106   1 MKR--AVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARaHKVLDVTLLNELAVSSLTRDS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066  80 IAVK--EGEDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHT 157
Cdd:PRK11106  79 IPVPdyEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFET 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517491066 158 PLMWLNKAETWKLADELNAFDFVREKTLTCYNGIIADGCGECPACKLRKRGLEEYL 213
Cdd:PRK11106 159 PLMWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYL 214
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 5-213 1.77e-122

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: 345.37  E-value: 1.77e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066    5 KALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMSLLNQLAPNALTRDGIAV-- 82
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKILDLDFLKQIGGSALTDDSIEVpk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   83 KEGEDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNL-SMDQQFVIHTPLMW 161
Cdd:pfam06508  81 AELESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLgTMGKPIEIHTPLMD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517491066  162 LNKAETWKLADELNAfdfVREKTLTCYNG-IIADGCGECPACKLRKRGLEEYL 213
Cdd:pfam06508 161 LSKAEIVKLGDELGV---PYELTWSCYNGgEEGDGCGECPACRLRLKGFEEAG 210
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 2-212 2.21e-121

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: 343.30  E-value: 2.21e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   2 KKEKALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVK-HYILDMSLLNQLAPNALTRDGI 80
Cdd:COG0603    1 MMKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGeHKVIDLDFLGEIGGSALTDDSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066  81 AVKEG--EDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHTP 158
Cdd:COG0603   81 EVPEGhyAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 517491066 159 LMWLNKAETWKLADELNAfdfVREKTLTCYNGiIADGCGECPACKLRKRGLEEY 212
Cdd:COG0603  161 LMHLSKAEIVKLGLELGV---PYELTWSCYNG-GGRACGRCDSCRLRLEAFAEA 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 6-205 4.75e-110

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: 313.56  E-value: 4.75e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066    6 ALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMSLLNQLAPNALTRDG--IAVK 83
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHHLLDLSLLNQLGGSALTREQeiPEQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   84 EGEDGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHTPLMWLN 163
Cdd:TIGR00364  81 SNEEDTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDLT 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 517491066  164 KAETWKLADELNAFDFVREKTLTCYNGiIADGCGECPACKLR 205
Cdd:TIGR00364 161 KAEIVKLADELGVLDLVIKLTYSCYAG-GGEGCGKCPSCMLR 201
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 4-212 2.21e-94

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: 274.49  E-value: 2.21e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   4 EKALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCA-RNIAEELGVKHYILDMSLLNQLAPNALTRDGIAV 82
Cdd:cd01995    1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAaKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066  83 KEGE--DGGLPSTFVPGRNLLFLSFAGVLASQIGARHIVTGVCETDFSGYPDCRDIFVKSLNVTLNLSMDQQFVIHTPLM 160
Cdd:cd01995   81 PDGEydEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPLI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517491066 161 WLNKAETWKLADELnafDFVREKTLTCYNGIIaDGCGECPACKLRKRGLEEY 212
Cdd:cd01995  161 GLSKAEIVKLGVEL---GVPLELTWSCYRGGE-KHCGRCESCRLRKRAFEEA 208
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 5-68 4.75e-09

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 54.57  E-value: 4.75e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517491066   5 KALVVFSGGQDSTTCLFWARERF-EEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMSLLN 68
Cdd:cd01990    1 KVVVAFSGGVDSSLLAKLAKEVLgDNVVAVTADSPLVPREELEEAKRIAEEIGIRHEIIKTDELD 65
PRK13820 PRK13820
argininosuccinate synthase; Provisional
 3-63 7.45e-08

argininosuccinate synthase; Provisional


Pssm-ID: 237521  Cd Length: 394  Bit Score: 51.85  E-value: 7.45e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517491066   3 KEKALVVFSGGQDSTTCLFWARER--FEEVAAVTFDYHQRhRLEIDCARNIAEELGVKHYILD 63
Cdd:PRK13820   2 MKKVVLAYSGGLDTSVCVPLLKEKygYDEVITVTVDVGQP-EEEIKEAEEKAKKLGDKHYTID 63
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
3-68 9.21e-08

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


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 50.88  E-value: 9.21e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517491066   3 KEKALVVFSGGQDSTTCLFWARERF-EEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMSLLN 68
Cdd:COG1606   15 LGSVLVAFSGGVDSTLLAKVAHDVLgDRVLAVTADSPSLPERELEEAKELAKEIGIRHEVIETDELE 81
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 8-137 4.98e-07

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: 48.81  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   8 VVFSGGQDST--TCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMS---LLNQLAPNALTRDGIav 82
Cdd:cd01991    7 VLLSGGLDSSliAALAARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTEHHEVEVTieeLLDALPDVILIYPTD-- 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517491066  83 kegedgglpsTFVPGRNLLFLSFAGVLASQIGARHIVTGVCeTD--FSGYPDCRDIF 137
Cdd:cd01991   85 ----------TPMDLSIAIPLYFASRLAGKLGAKVVLSGEG-ADelFGGYSRHRDAP 130
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 7-62 2.84e-06

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: 46.05  E-value: 2.84e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517491066   7 LVVFSGGQDSTTCLF----WARERFEEVAAVTFDYHQRH--RLEIDCARNIAEELGVKHYIL 62
Cdd:cd01992    3 LVAVSGGPDSMALLHllkeLRPKLGLKLVAVHVDHGLREesAEEAQFVAKLCKKLGIPLHIL 64
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-63 3.09e-05

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: 43.28  E-value: 3.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517491066   2 KKEKALVVFSGGQDSTT----CLFWARERFEEVAAVTFDYHQRH--RLEIDCARNIAEELGVKHYILD 63
Cdd:COG0037   14 PGDRILVAVSGGKDSLAllhlLAKLRRRLGFELVAVHVDHGLREesDEDAEFVAELCEELGIPLHVVR 81
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
2-68 1.60e-04

Predicted ATPase, PP-loop superfamily [General function prediction only];


Pssm-ID: 440976  Cd Length: 256  Bit Score: 41.58  E-value: 1.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517491066   2 KKEKALVVFSGGQDSTTCLFWARERFEEVAAVTFDY------HQRHRLEidcarNIAEELGVKHYILDMSLLN 68
Cdd:COG1365   59 KNPKVVVAFSGGVDSSASLIIAKWIGFDVEAVTVKStiilpqMFKKNIK-----ELCKKLNVKHEFIEIDLGE 126
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 5-62 2.52e-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: 40.31  E-value: 2.52e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517491066    5 KALVVFSGGQDSTT---CLFWARERF-EEVAAVTFDYHQRH--RLEIDCARNIAEELGVKHYIL 62
Cdd:TIGR02432   1 RILVAVSGGVDSMAllhLLLKLQPKIkIKLIAAHVDHGLRPesDEEAEFVQQFCRKLNIPLEIK 64
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 6-59 5.59e-04

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: 37.43  E-value: 5.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517491066   6 ALVVFSGGQDSTTCLFWARERFE--EVAAVTFDYHQRH--------RLEIDCARNIAEELGVKH 59
Cdd:cd01986    1 VVVGYSGGKDSSVALHLASRLGRkaEVAVVHIDHGIGFkeeaesvaSIARRSILKKLAEKGARA 64
ASS cd01999
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ...
 4-63 6.48e-04

argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle enzyme that catalyzes the penultimate step in arginine biosynthesis: the ATP-dependent ligation of citrulline to aspartate to form argininosuccinate, AMP and pyrophosphate. In humans, a defect in the ASS gene causes citrullinemia, a genetic disease characterized by severe vomiting spells and mental retardation. ASS is a homotetrameric enzyme of about 400 amino-acid residues. An arginine residue seems to be important for the enzyme's catalytic mechanism. The sequences of ASS from various prokaryotes, archaeabacteria and eukaryotes show significant similarity.


Pssm-ID: 467503  Cd Length: 386  Bit Score: 39.83  E-value: 6.48e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517491066   4 EKALVVFSGGQDSTTCLFWARERFE-EVAAVTFDYHQRHrlEIDCARNIAEELG-VKHYILD 63
Cdd:cd01999    1 KKVVLAYSGGLDTSVILKWLKEEYGyEVIAFTADLGQGD--EEEEIEEKALKLGaVKVYVVD 60
PRK14561 PRK14561
hypothetical protein; Provisional
 5-80 7.41e-04

hypothetical protein; Provisional


Pssm-ID: 184745  Cd Length: 194  Bit Score: 39.04  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   5 KALVVFSGGQDSTTCLfWARERFEEVAAVTFDYHQRHRLEIdcARNIAEELGVKHYI--LDMSLLNQLAPNALT----RD 78
Cdd:PRK14561   2 KAGVLFSGGKDSSLAA-ILLERFYDVELVTVNFGVLDSWKH--AREAAKALGFPHRVleLDREILEKAVDMIIEdgypNN 78


                 ..
gi 517491066  79 GI 80
Cdd:PRK14561  79 AI 80
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 2-63 1.24e-03

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 39.17  E-value: 1.24e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517491066   2 KKEKALVVFSGGQDST-TCLFwARERFEEVAAVTFDYHQRhrlEIDCARNIAEELGVKHYILD 63
Cdd:PRK14664   4 SKKRVLVGMSGGIDSTaTCLM-LQEQGYEIVGVTMRVWGD---EPQDARELAARMGIEHYVAD 62
PRK08576 PRK08576
hypothetical protein; Provisional
 6-57 2.72e-03

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 38.14  E-value: 2.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 517491066   6 ALVVFSGGQDSTTCLFWARERFEEVAAVTFDYHQRHRLEIDCARNIAEELGV 57
Cdd:PRK08576 237 VIVPWSGGKDSTAALLLAKKAFGDVTAVYVDTGYEMPLTDEYVEKVAEKLGV 288
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 8-62 4.27e-03

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


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 36.84  E-value: 4.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517491066    8 VVFSGGQDSTTCLF----WARERFEEVAAVTFDYHQRH--RLEIDCARNIAEELGVKHYIL 62
Cdd:pfam01171   1 VAVSGGPDSMALLYllakLKIKLGIELTAAHVNHGLREesDREAEHVQALCRQLGIPLEIL 61
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 11-65 5.01e-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: 36.76  E-value: 5.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 517491066  11 SGGQDSTTCLFWARE--RFEEVAAVTFDYHQRHRLEIDCARNIAEELGVKHYILDMS 65
Cdd:cd00553   31 SGGIDSAVVAALAVRalGAENVLALIMPSRYSSKETRDDAKALAENLGIEYRTIDID 87
COG2117 COG2117
Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the ...
 5-64 7.74e-03

Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441720  Cd Length: 196  Bit Score: 35.95  E-value: 7.74e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517491066   5 KALVVFSGGQDSTTCLfWARERFEEVAAVTFDYHQRHRLEIdcARNIAEELGVKHYILDM 64
Cdd:COG2117    1 KAAVLYSGGKDSSLAA-LLLERFYDVELVTANFGITDSWKH--AREAAEALGFPHRVLEL 57
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 5-61 8.52e-03

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong 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. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 36.11  E-value: 8.52e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517491066   5 KALVVFSGGQDSTTCLFWA-RERFEEVAAVTF-----DYHQRHRLEIDCARNIAEELGVKHYI 61
Cdd:cd01994    1 KVVALISGGKDSIYALLHAiRNGHEVVALANLrpedkDSYMFQTVGHELLELQAEALGLPLIR 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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