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Conserved domains on  [gi|490365417|ref|WP_004245081|]
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MULTISPECIES: 7-cyano-7-deazaguanine synthase QueC [Proteus]

Protein Classification

7-cyano-7-deazaguanine synthase( domain architecture ID 10793532)

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
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 1-232 0e+00

queuosine biosynthesis protein QueC; Provisional


:

Pssm-ID: 182967  Cd Length: 231  Bit Score: 516.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   1 MKKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLDVSLLNELAISSLTRDNIP 80
Cdd:PRK11106   1 MKRAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  81 VPDFKQSEQSdIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITP 160
Cdd:PRK11106  81 VPDYEPEADG-LPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490365417 161 LMWLDKAQTWALADYYGKLDFVRHNTLTCYNGIQGDGCGQCAACHLRERGLHGYLQDKNAVMDAMKNKVGLK 232
Cdd:PRK11106 160 LMWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYLANKPAVMAALKQKTGLA 231
 
Name Accession Description Interval E-value
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 1-232 0e+00

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 516.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   1 MKKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLDVSLLNELAISSLTRDNIP 80
Cdd:PRK11106   1 MKRAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  81 VPDFKQSEQSdIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITP 160
Cdd:PRK11106  81 VPDYEPEADG-LPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490365417 161 LMWLDKAQTWALADYYGKLDFVRHNTLTCYNGIQGDGCGQCAACHLRERGLHGYLQDKNAVMDAMKNKVGLK 232
Cdd:PRK11106 160 LMWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYLANKPAVMAALKQKTGLA 231
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-214 1.07e-119

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: 339.44  E-value: 1.07e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   1 MKKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLDVSLLNELAISSLTRDNIP 80
Cdd:COG0603    2 MKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGEHKVIDLDFLGEIGGSALTDDSIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  81 VPDFKQSEQSdIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITP 160
Cdd:COG0603   82 VPEGHYAEEG-IPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490365417 161 LMWLDKAQTWALADyygKLDFVRHNTLTCYNGIqGDGCGQCAACHLRERGLHGY 214
Cdd:COG0603  161 LMHLSKAEIVKLGL---ELGVPYELTWSCYNGG-GRACGRCDSCRLRLEAFAEA 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 5-207 1.28e-113

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: 323.58  E-value: 1.28e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417    5 VVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHkVLDVSLLNELAISSLTRDNIPVPDf 84
Cdd:TIGR00364   2 IVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHH-LLDLSLLNQLGGSALTREQEIPEQ- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   85 KQSEQSDIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITPLMWL 164
Cdd:TIGR00364  80 KSNEEDTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 490365417  165 DKAQTWALADYYGKLDFVRHNTLTCYNGIqGDGCGQCAACHLR 207
Cdd:TIGR00364 160 TKAEIVKLADELGVLDLVIKLTYSCYAGG-GEGCGKCPSCMLR 201
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 3-215 3.83e-111

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: 317.64  E-value: 3.83e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417    3 KTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGAtAHKVLDVSLLNELAISSLTRDNIPVP 82
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGV-EHKILDLDFLKQIGGSALTDDSIEVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   83 DFKQSEQsDIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLG-IARDIQFITPL 161
Cdd:pfam06508  80 KAELESE-EIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGtMGKPIEIHTPL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490365417  162 MWLDKAQTWALADyygKLDFVRHNTLTCYNG-IQGDGCGQCAACHLRERGLHGYL 215
Cdd:pfam06508 159 MDLSKAEIVKLGD---ELGVPYELTWSCYNGgEEGDGCGECPACRLRLKGFEEAG 210
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 2-212 2.36e-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: 289.90  E-value: 2.36e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   2 KKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLDVSLLNELAISSLTRDNIPV 81
Cdd:cd01995    1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  82 PDFKQSEQSdIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITPL 161
Cdd:cd01995   81 PDGEYDEES-IPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490365417 162 MWLDKAQTWALAdyyGKLDFVRHNTLTCYNGIQgDGCGQCAACHLRERGLH 212
Cdd:cd01995  160 IGLSKAEIVKLG---VELGVPLELTWSCYRGGE-KHCGRCESCRLRKRAFE 206
 
Name Accession Description Interval E-value
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 1-232 0e+00

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 516.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   1 MKKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLDVSLLNELAISSLTRDNIP 80
Cdd:PRK11106   1 MKRAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  81 VPDFKQSEQSdIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITP 160
Cdd:PRK11106  81 VPDYEPEADG-LPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490365417 161 LMWLDKAQTWALADYYGKLDFVRHNTLTCYNGIQGDGCGQCAACHLRERGLHGYLQDKNAVMDAMKNKVGLK 232
Cdd:PRK11106 160 LMWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYLANKPAVMAALKQKTGLA 231
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-214 1.07e-119

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: 339.44  E-value: 1.07e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   1 MKKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLDVSLLNELAISSLTRDNIP 80
Cdd:COG0603    2 MKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGEHKVIDLDFLGEIGGSALTDDSIE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  81 VPDFKQSEQSdIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITP 160
Cdd:COG0603   82 VPEGHYAEEG-IPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTP 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490365417 161 LMWLDKAQTWALADyygKLDFVRHNTLTCYNGIqGDGCGQCAACHLRERGLHGY 214
Cdd:COG0603  161 LMHLSKAEIVKLGL---ELGVPYELTWSCYNGG-GRACGRCDSCRLRLEAFAEA 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 5-207 1.28e-113

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: 323.58  E-value: 1.28e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417    5 VVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHkVLDVSLLNELAISSLTRDNIPVPDf 84
Cdd:TIGR00364   2 IVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHH-LLDLSLLNQLGGSALTREQEIPEQ- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   85 KQSEQSDIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITPLMWL 164
Cdd:TIGR00364  80 KSNEEDTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 490365417  165 DKAQTWALADYYGKLDFVRHNTLTCYNGIqGDGCGQCAACHLR 207
Cdd:TIGR00364 160 TKAEIVKLADELGVLDLVIKLTYSCYAGG-GEGCGKCPSCMLR 201
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 3-215 3.83e-111

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: 317.64  E-value: 3.83e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417    3 KTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGAtAHKVLDVSLLNELAISSLTRDNIPVP 82
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGV-EHKILDLDFLKQIGGSALTDDSIEVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   83 DFKQSEQsDIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLG-IARDIQFITPL 161
Cdd:pfam06508  80 KAELESE-EIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGtMGKPIEIHTPL 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 490365417  162 MWLDKAQTWALADyygKLDFVRHNTLTCYNG-IQGDGCGQCAACHLRERGLHGYL 215
Cdd:pfam06508 159 MDLSKAEIVKLGD---ELGVPYELTWSCYNGgEEGDGCGECPACRLRLKGFEEAG 210
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 2-212 2.36e-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: 289.90  E-value: 2.36e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   2 KKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLDVSLLNELAISSLTRDNIPV 81
Cdd:cd01995    1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  82 PDFKQSEQSdIPSTFVPGRNILFLTLAAIYAYQIGAESVITGVCETDFSGYPDCRDEFVKALNHAVNLGIARDIQFITPL 161
Cdd:cd01995   81 PDGEYDEES-IPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490365417 162 MWLDKAQTWALAdyyGKLDFVRHNTLTCYNGIQgDGCGQCAACHLRERGLH 212
Cdd:cd01995  160 IGLSKAEIVKLG---VELGVPLELTWSCYRGGE-KHCGRCESCRLRKRAFE 206
PRK13820 PRK13820
argininosuccinate synthase; Provisional
 1-63 1.64e-06

argininosuccinate synthase; Provisional


Pssm-ID: 237521  Cd Length: 394  Bit Score: 48.00  E-value: 1.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490365417   1 MKKTVVVFSGGQDsTTCLIQALEQ---YDEVHCITFNYGQRhKEEIEVAQRVSQLLGAtAHKVLDV 63
Cdd:PRK13820   2 MKKVVLAYSGGLD-TSVCVPLLKEkygYDEVITVTVDVGQP-EEEIKEAEEKAKKLGD-KHYTIDA 64
PRK14561 PRK14561
hypothetical protein; Provisional
 6-80 3.66e-06

hypothetical protein; Provisional


Pssm-ID: 184745  Cd Length: 194  Bit Score: 45.97  E-value: 3.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490365417   6 VVFSGGQDSTTCLIqALEQYDEVHCITFNYGQRHkeEIEVAQRVSQLLGaTAHKV--LDVSLLNElAISSLTRDNIP 80
Cdd:PRK14561   5 VLFSGGKDSSLAAI-LLERFYDVELVTVNFGVLD--SWKHAREAAKALG-FPHRVleLDREILEK-AVDMIIEDGYP 76
ASS cd01999
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ...
 2-63 6.99e-06

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: 45.99  E-value: 6.99e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490365417   2 KKTVVVFSGGQDSTTCLIQALEQYD-EVHCITFNYGQrhKEEIEVAQRVSQLLGATAHKVLDV 63
Cdd:cd01999    1 KKVVLAYSGGLDTSVILKWLKEEYGyEVIAFTADLGQ--GDEEEEIEEKALKLGAVKVYVVDL 61
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
1-67 6.99e-05

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


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 42.79  E-value: 6.99e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   1 MKKTVVVFSGGQDSTTCL---IQALEqyDEVHCITFNYGQRHKEEIEVAQRVSQLLGATaHKVLDVSLLN 67
Cdd:COG1606   15 LGSVLVAFSGGVDSTLLAkvaHDVLG--DRVLAVTADSPSLPERELEEAKELAKEIGIR-HEVIETDELE 81
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 6-158 8.84e-05

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: 42.26  E-value: 8.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   6 VVFSGGQDST--TCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGaTAHKVLDVS---LLNELAISSLTRDNIP 80
Cdd:cd01991    7 VLLSGGLDSSliAALAARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELG-TEHHEVEVTieeLLDALPDVILIYPTDT 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417  81 VPDFkqseqsdipstfvpgRNILFLTLAAIYAYQIGAESVITGVCeTD--FSGYPDCRDEFvKALNHAVNLGIARDIQFI 158
Cdd:cd01991   86 PMDL---------------SIAIPLYFASRLAGKLGAKVVLSGEG-ADelFGGYSRHRDAP-LRGWEALEEELLRDLDRL 148
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 3-67 1.53e-04

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: 41.47  E-value: 1.53e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490365417   3 KTVVVFSGGQDSTTCLIQALEQ-YDEVHCITFNYGQRHKEEIEVAQRVSQLLGATaHKVLDVSLLN 67
Cdd:cd01990    1 KVVVAFSGGVDSSLLAKLAKEVlGDNVVAVTADSPLVPREELEEAKRIAEEIGIR-HEIIKTDELD 65
Arginosuc_synth pfam00764
Arginosuccinate synthase; This family contains a PP-loop motif.
 5-62 3.85e-04

Arginosuccinate synthase; This family contains a PP-loop motif.


Pssm-ID: 279148  Cd Length: 386  Bit Score: 40.79  E-value: 3.85e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490365417    5 VVVFSGGQDSTTCLIQALEQY-DEVHCITFNYGQRhKEEIEVAQRVSQLLGATAHKVLD 62
Cdd:pfam00764   1 VLAYSGGLDTSVCIPWLKEQGgYEVIAVAVDVGQG-GEDIDEAREKALKLGAVKHYVID 58
PRK08576 PRK08576
hypothetical protein; Provisional
 3-54 6.00e-04

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 40.45  E-value: 6.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490365417   3 KTVVV-FSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLG 54
Cdd:PRK08576 235 WTVIVpWSGGKDSTAALLLAKKAFGDVTAVYVDTGYEMPLTDEYVEKVAEKLG 287
COG2117 COG2117
Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the ...
 3-80 1.38e-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: 38.65  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490365417   3 KTVVVFSGGQDST-TCLIqaLEQYDEVHCITFNYGQRHKeeIEVAQRVSQLLGaTAHKV--LDVSLLNElAISSLTRDNI 79
Cdd:COG2117    1 KAAVLYSGGKDSSlAALL--LERFYDVELVTANFGITDS--WKHAREAAEALG-FPHRVleLDRGVLEE-AVDMIIEDGY 74


                 .
gi 490365417  80 P 80
Cdd:COG2117   75 P 75
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 4-48 1.46e-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: 36.28  E-value: 1.46e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490365417   4 TVVVFSGGQDSTTCLIQALEQY--DEVHCITFNYGQRHKEEIEVAQR 48
Cdd:cd01986    1 VVVGYSGGKDSSVALHLASRLGrkAEVAVVHIDHGIGFKEEAESVAS 47
PRK04527 PRK04527
argininosuccinate synthase; Provisional
 2-62 2.21e-03

argininosuccinate synthase; Provisional


Pssm-ID: 235305  Cd Length: 400  Bit Score: 38.66  E-value: 2.21e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490365417   2 KKTVVVFSGGQDSTTCLIQALEQYDEVHCITFNYGQRHKEEIEVAQRVSQLLGATAHKVLD 62
Cdd:PRK04527   3 KDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADTGGVDAEERDFIEKRAAELGAASHVTVD 63
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 3-52 2.36e-03

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: 37.57  E-value: 2.36e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490365417   3 KTVVVFSGGQDStTCLIQALEQYD-----EVHCITFNYGQRH---KEEIEVAQRVSQL 52
Cdd:cd01992    1 KILVAVSGGPDS-MALLHLLKELRpklglKLVAVHVDHGLREesaEEAQFVAKLCKKL 57
PAPS_reductase-like_YbdN cd23947
uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to ...
 2-54 3.33e-03

uncharacterized phosphoadenosine phosphosulfate reductase-like proteins, similar to Escherichia coli YbdN; This subgroup contains Escherichia coli YbdN and other phosphoadenosine phosphosulfate (PAPS) reductase (or PAPS sulfotransferase EC 1.8.4.8)-like proteins. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N-type ATP PPases and ATP sulfurylases. A highly modified version of the P loop, the fingerprint peptide of mononucleotide-binding proteins, is present in the active site of the protein, which appears to be a positively charged cleft containing a number of conserved arginine and lysine residues. Although PAPS reductase has no ATPase activity, it shows a striking similarity to the structure of the ATP pyrophosphatase (ATP PPase) domain of GMP synthetase, indicating that both enzyme families have evolved from a common ancestral nucleotide-binding fold. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP).


Pssm-ID: 467512 [Multi-domain]  Cd Length: 206  Bit Score: 37.37  E-value: 3.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490365417   2 KKTVVV-FSGGQDSTTCLIQALEQYDEV---HCITFN-YGQRHKEEIEVAQRVSQLLG 54
Cdd:cd23947   12 FDPVIVsFSGGKDSLVLLHLALEALRRLrkdVYVVFIdTGIEFPETIDFVEKLAETLG 69
 
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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