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Conserved domains on  [gi|1000904551|ref|WP_061155548|]
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MULTISPECIES: 7-cyano-7-deazaguanine synthase QueC [Klebsiella]

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
 1-231 0e+00

queuosine biosynthesis protein QueC; Provisional


:

Pssm-ID: 182967  Cd Length: 231  Bit Score: 530.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   1 MKRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLDVTLLNELAVSSLTRDNIP 80
Cdd:PRK11106    1 MKRAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  81 VPDYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPL 160
Cdd:PRK11106   81 VPDYEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETPL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1000904551 161 MWLNKAETWALADYWGQLDLVRQETLTCYNGIKGDGCGQCAACNLRANGLNQYLGDKVGVMAVMKQKTGLA 231
Cdd:PRK11106  161 MWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYLANKPAVMAALKQKTGLA 231
 
Name Accession Description Interval E-value
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 1-231 0e+00

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 530.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   1 MKRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLDVTLLNELAVSSLTRDNIP 80
Cdd:PRK11106    1 MKRAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  81 VPDYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPL 160
Cdd:PRK11106   81 VPDYEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETPL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1000904551 161 MWLNKAETWALADYWGQLDLVRQETLTCYNGIKGDGCGQCAACNLRANGLNQYLGDKVGVMAVMKQKTGLA 231
Cdd:PRK11106  161 MWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYLANKPAVMAALKQKTGLA 231
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-213 1.65e-120

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: 341.76  E-value: 1.65e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   1 MKRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLDVTLLNELAVSSLTRDNIP 80
Cdd:COG0603     2 MKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGEHKVIDLDFLGEIGGSALTDDSIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  81 VPDYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPL 160
Cdd:COG0603    82 VPEGHYAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTPL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1000904551 161 MWLNKAETWALADywgQLDLVRQETLTCYNGIkGDGCGQCAACNLRANGLNQY 213
Cdd:COG0603   162 MHLSKAEIVKLGL---ELGVPYELTWSCYNGG-GRACGRCDSCRLRLEAFAEA 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 4-206 1.97e-115

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: 328.20  E-value: 1.97e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   4 AVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGaVAHKVLDVTLLNELAVSSLTRDNIPVPD 83
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALG-IEHHLLDLSLLNQLGGSALTREQEIPEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  84 YQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPLMWL 163
Cdd:TIGR00364  80 KSNEEDTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1000904551 164 NKAETWALADYWGQLDLVRQETLTCYNGIkGDGCGQCAACNLR 206
Cdd:TIGR00364 160 TKAEIVKLADELGVLDLVIKLTYSCYAGG-GEGCGKCPSCMLR 201
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 3-214 2.97e-112

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: 320.33  E-value: 2.97e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   3 RAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGaVAHKVLDVTLLNELAVSSLTRDNIPVP 82
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALG-VEHKILDLDFLKQIGGSALTDDSIEVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  83 DYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLG-MAKDIRFETPLM 161
Cdd:pfam06508  80 KAELESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGtMGKPIEIHTPLM 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1000904551 162 WLNKAETWALADywgQLDLVRQETLTCYNG-IKGDGCGQCAACNLRANGLNQYL 214
Cdd:pfam06508 160 DLSKAEIVKLGD---ELGVPYELTWSCYNGgEEGDGCGECPACRLRLKGFEEAG 210
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 2-213 2.33e-98

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: 284.89  E-value: 2.33e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   2 KRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLDVTLLNELAVSSLTRDNIPV 81
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  82 PDYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPLM 161
Cdd:cd01995    81 PDGEYDEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPLI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1000904551 162 WLNKAETWALAdywGQLDLVRQETLTCYNGIKgDGCGQCAACNLRANGLNQY 213
Cdd:cd01995   161 GLSKAEIVKLG---VELGVPLELTWSCYRGGE-KHCGRCESCRLRKRAFEEA 208
 
Name Accession Description Interval E-value
PRK11106 PRK11106
queuosine biosynthesis protein QueC; Provisional
 1-231 0e+00

queuosine biosynthesis protein QueC; Provisional


Pssm-ID: 182967  Cd Length: 231  Bit Score: 530.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   1 MKRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLDVTLLNELAVSSLTRDNIP 80
Cdd:PRK11106    1 MKRAVVVFSGGQDSTTCLIQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGARAHKVLDVTLLNELAVSSLTRDSIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  81 VPDYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPL 160
Cdd:PRK11106   81 VPDYEPEADGLPNTFVPGRNILFLTLAAIYAYQVKAEAVITGVCETDFSGYPDCRDEFVKALNHAVSLGMAKDIRFETPL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1000904551 161 MWLNKAETWALADYWGQLDLVRQETLTCYNGIKGDGCGQCAACNLRANGLNQYLGDKVGVMAVMKQKTGLA 231
Cdd:PRK11106  161 MWLNKAETWALADYYGQLDLVRHETLTCYNGIKGDGCGHCAACHLRANGLNHYLANKPAVMAALKQKTGLA 231
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-213 1.65e-120

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: 341.76  E-value: 1.65e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   1 MKRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLDVTLLNELAVSSLTRDNIP 80
Cdd:COG0603     2 MKKAVVLLSGGLDSTTCLAWALARGYEVYALSFDYGQRHRKELEAARRIAKALGVGEHKVIDLDFLGEIGGSALTDDSIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  81 VPDYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPL 160
Cdd:COG0603    82 VPEGHYAEEGIPSTYVPGRNLIFLSIAAAYAEALGAEDIFIGVNATDYSGYPDCRPEFIEAFNAALNLGTKRPVRIHTPL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1000904551 161 MWLNKAETWALADywgQLDLVRQETLTCYNGIkGDGCGQCAACNLRANGLNQY 213
Cdd:COG0603   162 MHLSKAEIVKLGL---ELGVPYELTWSCYNGG-GRACGRCDSCRLRLEAFAEA 210
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 4-206 1.97e-115

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: 328.20  E-value: 1.97e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   4 AVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGaVAHKVLDVTLLNELAVSSLTRDNIPVPD 83
Cdd:TIGR00364   1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALG-IEHHLLDLSLLNQLGGSALTREQEIPEQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  84 YQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPLMWL 163
Cdd:TIGR00364  80 KSNEEDTLPNTFVPGRNLVFLSIAASYAEAIGAEAIITGVCETDFSGYPDCRDEFVKAFNVALNLGMLTPVEIRAPLMDL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1000904551 164 NKAETWALADYWGQLDLVRQETLTCYNGIkGDGCGQCAACNLR 206
Cdd:TIGR00364 160 TKAEIVKLADELGVLDLVIKLTYSCYAGG-GEGCGKCPSCMLR 201
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 3-214 2.97e-112

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: 320.33  E-value: 2.97e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   3 RAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGaVAHKVLDVTLLNELAVSSLTRDNIPVP 82
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALG-VEHKILDLDFLKQIGGSALTDDSIEVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  83 DYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLG-MAKDIRFETPLM 161
Cdd:pfam06508  80 KAELESEEIPNTYVPGRNLIFLSIAASLAEALGAEAIFIGVNEEDYSGYPDCRPEFVKAFNVALNLGtMGKPIEIHTPLM 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1000904551 162 WLNKAETWALADywgQLDLVRQETLTCYNG-IKGDGCGQCAACNLRANGLNQYL 214
Cdd:pfam06508 160 DLSKAEIVKLGD---ELGVPYELTWSCYNGgEEGDGCGECPACRLRLKGFEEAG 210
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 2-213 2.33e-98

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: 284.89  E-value: 2.33e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   2 KRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLDVTLLNELAVSSLTRDNIPV 81
Cdd:cd01995     1 MKAVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKEELEAAKLIAKLLGIEHKVIDLSFLGELGGSSLTDEGEEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551  82 PDYQPDAEGIPNTFVPGRNILFLTLTAIYAYQVKAEAIITGVCETDFSGYPDCRDEFVKALHHAVSLGMAKDIRFETPLM 161
Cdd:cd01995    81 PDGEYDEESIPSTWVPNRNLIFLSIAAAYAESLGASAIVIGVNAEDASGYPDCRPEFVEAMNSALNLGTATGVKVVAPLI 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1000904551 162 WLNKAETWALAdywGQLDLVRQETLTCYNGIKgDGCGQCAACNLRANGLNQY 213
Cdd:cd01995   161 GLSKAEIVKLG---VELGVPLELTWSCYRGGE-KHCGRCESCRLRKRAFEEA 208
ASS cd01999
argininosuccinate_synthase (ASS); Argininosuccinate synthase (ASS; EC 6.3.4.5) is a urea cycle ...
 2-70 7.02e-09

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: 55.23  E-value: 7.02e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   2 KRAVVVFSGGQDSTTCLVQALQQYD-EVHCVTFDYGQRhrAEIDVARELALKLGAVAHKVLDVTllNELA 70
Cdd:cd01999     1 KKVVLAYSGGLDTSVILKWLKEEYGyEVIAFTADLGQG--DEEEEIEEKALKLGAVKVYVVDLR--EEFA 66
PRK13820 PRK13820
argininosuccinate synthase; Provisional
 1-64 1.06e-07

argininosuccinate synthase; Provisional


Pssm-ID: 237521  Cd Length: 394  Bit Score: 51.47  E-value: 1.06e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1000904551   1 MKRAVVVFSGGQDsTTCLVQALQQ---YDEVHCVTFDYGQRhRAEIDVARELALKLGaVAHKVLDVT 64
Cdd:PRK13820    2 MKKVVLAYSGGLD-TSVCVPLLKEkygYDEVITVTVDVGQP-EEEIKEAEEKAKKLG-DKHYTIDAK 65
Arginosuc_synth pfam00764
Arginosuccinate synthase; This family contains a PP-loop motif.
 5-62 1.06e-07

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


Pssm-ID: 279148  Cd Length: 386  Bit Score: 51.58  E-value: 1.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1000904551   5 VVVFSGGQDSTTCLVQALQQY-DEVHCVTFDYGQRhRAEIDVARELALKLGAVAHKVLD 62
Cdd:pfam00764   1 VLAYSGGLDTSVCIPWLKEQGgYEVIAVAVDVGQG-GEDIDEAREKALKLGAVKHYVID 58
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
1-70 9.21e-07

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


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 48.18  E-value: 9.21e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1000904551   1 MKRAVVVFSGGQDSTTCL---VQALQqyDEVHCVTFDYGQRHRAEIDVARELALKLGaVAHKVLDVtllNELA 70
Cdd:COG1606    15 LGSVLVAFSGGVDSTLLAkvaHDVLG--DRVLAVTADSPSLPERELEEAKELAKEIG-IRHEVIET---DELE 81
PRK14561 PRK14561
hypothetical protein; Provisional
 1-80 2.75e-06

hypothetical protein; Provisional


Pssm-ID: 184745  Cd Length: 194  Bit Score: 46.36  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   1 MKrAVVVFSGGQDSTTCLVqALQQYDEVHCVTFDYGQRHraEIDVARELALKLGaVAHKV--LDVTLLNElAVSSLTRDN 78
Cdd:PRK14561    1 MK-AGVLFSGGKDSSLAAI-LLERFYDVELVTVNFGVLD--SWKHAREAAKALG-FPHRVleLDREILEK-AVDMIIEDG 74


                  ..
gi 1000904551  79 IP 80
Cdd:PRK14561   75 YP 76
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 3-67 3.77e-05

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: 43.40  E-value: 3.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1000904551   3 RAVVVFSGGQDSTTCLVQALQQ-YDEVHCVTFDYGQRHRAEIDVARELALKLGaVAHKVLDVTLLN 67
Cdd:cd01990     1 KVVVAFSGGVDSSLLAKLAKEVlGDNVVAVTADSPLVPREELEEAKRIAEEIG-IRHEIIKTDELD 65
PRK00509 PRK00509
argininosuccinate synthase; Provisional
 1-63 5.10e-05

argininosuccinate synthase; Provisional


Pssm-ID: 234785  Cd Length: 399  Bit Score: 43.51  E-value: 5.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1000904551   1 MKRAVVVFSGGQDSTTCLVQALQQYD-EVHCVTFDYGQRhrAEIDVARELALKLGAVAHKVLDV 63
Cdd:PRK00509    2 KKKVVLAYSGGLDTSVIIKWLKETYGcEVIAFTADVGQG--EELEPIREKALKSGASEIYVEDL 63
Asn_synthase_B_C cd01991
C-terminal domain of asparagine synthase B; The C-terminal domain of asparagine synthase (or ...
 6-155 6.93e-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: 42.65  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   6 VVFSGGQDST--TCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVaHKVLDVTLLNELAVSSLTRDNIPVPD 83
Cdd:cd01991     7 VLLSGGLDSSliAALAARLLPETPIDLFTVGFEGSPTPDRAAARRVAEELGTE-HHEVEVTIEELLDALPDVILIYPTDT 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1000904551  84 YQPDAEGIPntfvpgrniLFLTLTAIYAYQVKaeAIITGVCeTD--FSGYPDCRDEFvKALHHAVSLGMAKDIR 155
Cdd:cd01991    86 PMDLSIAIP---------LYFASRLAGKLGAK--VVLSGEG-ADelFGGYSRHRDAP-LRGWEALEEELLRDLD 146
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 5-65 1.65e-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: 41.04  E-value: 1.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1000904551   5 VVVFSGGQDStTCLVQALQQYD-----EVHCVTFDYGQRH--RAEIDVARELALKLGaVAHKVLDVTL 65
Cdd:cd01992     3 LVAVSGGPDS-MALLHLLKELRpklglKLVAVHVDHGLREesAEEAQFVAKLCKKLG-IPLHILTVTE 68
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 2-64 1.67e-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: 41.36  E-value: 1.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1000904551   2 KRAVVVFSGGQDSTT---CLVQALQQYD-EVHCVTFDYGQRH--RAEIDVARELALKLGaVAHKVLDVT 64
Cdd:COG0037    16 DRILVAVSGGKDSLAllhLLAKLRRRLGfELVAVHVDHGLREesDEDAEFVAELCEELG-IPLHVVRVD 83
PRK04527 PRK04527
argininosuccinate synthase; Provisional
 2-62 1.81e-04

argininosuccinate synthase; Provisional


Pssm-ID: 235305  Cd Length: 400  Bit Score: 41.74  E-value: 1.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1000904551   2 KRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYGQRHRAEIDVARELALKLGAVAHKVLD 62
Cdd:PRK04527    3 KDIVLAFSGGLDTSFCIPYLQERGYAVHTVFADTGGVDAEERDFIEKRAAELGAASHVTVD 63
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 4-52 2.01e-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: 38.59  E-value: 2.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1000904551   4 AVVVFSGGQDSTTCLVQALQQY--DEVHCVTFDYGQRHRAEIDVARELALK 52
Cdd:cd01986     1 VVVGYSGGKDSSVALHLASRLGrkAEVAVVHIDHGIGFKEEAESVASIARR 51
COG2117 COG2117
Predicted subunit of tRNA(5-methylaminomethyl-2-thiouridylate) methyltransferase, contains the ...
 3-80 9.53e-04

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: 39.03  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1000904551   3 RAVVVFSGGQDSTTCLVqALQQYDEVHCVTFDYGQRHraEIDVARELALKLGaVAHKV--LDVTLLNElAVSSLTRDNIP 80
Cdd:COG2117     1 KAAVLYSGGKDSSLAAL-LLERFYDVELVTANFGITD--SWKHAREAAEALG-FPHRVleLDRGVLEE-AVDMIIEDGYP 75
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 1-64 3.04e-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: 3.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1000904551   1 MKRAVVVFSGGQDSTTCL---VQALQQYDeVHCVTFDYGQRHRAEIDVARELALKLGaVAHKVLDVT 64
Cdd:cd00553    23 AKGFVLGLSGGIDSAVVAalaVRALGAEN-VLALIMPSRYSSKETRDDAKALAENLG-IEYRTIDID 87
PRK08576 PRK08576
hypothetical protein; Provisional
 2-36 3.39e-03

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 38.14  E-value: 3.39e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1000904551   2 KRAVVVFSGGQDSTTCLVQALQQYDEVHCVTFDYG 36
Cdd:PRK08576  235 WTVIVPWSGGKDSTAALLLAKKAFGDVTAVYVDTG 269
 
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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