NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1490961336|gb|RLE82982|]
View 

MAG: GMP synthase (glutamine-hydrolyzing), partial [Thermoprotei archaeon]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
guaA super family cl35057
GMP synthase; Reviewed
 9-85 6.52e-26

GMP synthase; Reviewed


The actual alignment was detected with superfamily member PRK00074:

Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 98.58  E-value: 6.52e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490961336   9 LKHDTVAVVNFGGQYAHLIARRIRELGVYSELVDYeQVCEDYMRRVRLKAVVLSGSPMSASSAN-YSVVSEILKLGVP 85
Cdd:PRK00074    1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPY-DISAEEIRAFNPKGIILSGGPASVYEEGaPRADPEIFELGVP 77
 
Name Accession Description Interval E-value
guaA PRK00074
GMP synthase; Reviewed
 9-85 6.52e-26

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 98.58  E-value: 6.52e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490961336   9 LKHDTVAVVNFGGQYAHLIARRIRELGVYSELVDYeQVCEDYMRRVRLKAVVLSGSPMSASSAN-YSVVSEILKLGVP 85
Cdd:PRK00074    1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPY-DISAEEIRAFNPKGIILSGGPASVYEEGaPRADPEIFELGVP 77
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 14-85 5.98e-23

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 86.44  E-value: 5.98e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490961336  14 VAVVNFGGQYAHLIARRIRELGVYSELVDYEQVCEDyMRRVRLKAVVLSGSPMSASSAN-YSVVSEILKLGVP 85
Cdd:cd01742     1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEE-IKLKNPKGIILSGGPSSVYEEDaPRVDPEIFELGVP 72
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 14-85 1.61e-19

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 77.74  E-value: 1.61e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490961336  14 VAVVNFGGQYAHLIARRIRELGVYSELVDYEQVCEDyMRRVRLKAVVLSGSPMSASSAN-YSVVSEILKLGVP 85
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEE-IREKNPKGIILSGGPSSVYAENaPRADEKIFELGVP 72
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 17-85 8.47e-10

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 52.64  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490961336  17 VNFGGQYAHLIARRIRELG-------VY-SELVDYEQVCEDYmrrvrlKAVVLSGSPMSA------SSANYSVVSEILKL 82
Cdd:COG0518     8 DPFGGQYPGLIARRLREAGieldvlrVYaGEILPYDPDLEDP------DGLILSGGPMSVydedpwLEDEPALIREAFEL 81


                  ...
gi 1490961336  83 GVP 85
Cdd:COG0518    82 GKP 84
GATase pfam00117
Glutamine amidotransferase class-I;
15-85 3.37e-06

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 42.61  E-value: 3.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490961336  15 AVVNFGGQYAHLIARRIRELGVYSELV----DYEQVCEDYMrrvrlKAVVLSGSPMSASSANYSV--VSEILKLGVP 85
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVpndtPAEEILEENP-----DGIILSGGPGSPGAAGGAIeaIREARELKIP 72
 
Name Accession Description Interval E-value
guaA PRK00074
GMP synthase; Reviewed
 9-85 6.52e-26

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 98.58  E-value: 6.52e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1490961336   9 LKHDTVAVVNFGGQYAHLIARRIRELGVYSELVDYeQVCEDYMRRVRLKAVVLSGSPMSASSAN-YSVVSEILKLGVP 85
Cdd:PRK00074    1 IHHDKILILDFGSQYTQLIARRVRELGVYSEIVPY-DISAEEIRAFNPKGIILSGGPASVYEEGaPRADPEIFELGVP 77
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 14-85 5.98e-23

Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase. GMP synthetase is a glutamine amidotransferase from the de novo purine biosynthetic pathway. Glutamine amidotransferase (GATase) activity catalyse the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. GMP synthetase catalyses the amination of the nucleotide precursor xanthosine 5'-monophosphate to form GMP. GMP synthetase belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153213 [Multi-domain]  Cd Length: 181  Bit Score: 86.44  E-value: 5.98e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490961336  14 VAVVNFGGQYAHLIARRIRELGVYSELVDYEQVCEDyMRRVRLKAVVLSGSPMSASSAN-YSVVSEILKLGVP 85
Cdd:cd01742     1 ILILDFGSQYTHLIARRVRELGVYSEILPNTTPLEE-IKLKNPKGIILSGGPSSVYEEDaPRVDPEIFELGVP 72
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 14-85 1.61e-19

GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine de novo biosynthesis is well-conserved. However, it appears to split into two separate polypeptide chains in most of the Archaea. This N-terminal region would be the smaller subunit. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 129966 [Multi-domain]  Cd Length: 188  Bit Score: 77.74  E-value: 1.61e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1490961336  14 VAVVNFGGQYAHLIARRIRELGVYSELVDYEQVCEDyMRRVRLKAVVLSGSPMSASSAN-YSVVSEILKLGVP 85
Cdd:TIGR00888   1 ILVLDFGSQYTQLIARRLRELGVYSELVPNTTPLEE-IREKNPKGIILSGGPSSVYAENaPRADEKIFELGVP 72
PLN02347 PLN02347
GMP synthetase
 10-78 1.69e-14

GMP synthetase


Pssm-ID: 215197 [Multi-domain]  Cd Length: 536  Bit Score: 66.63  E-value: 1.69e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490961336  10 KHDTVAVVNFGGQYAHLIARRIRELGVYSELVDyEQVCEDYMRRVRLKAVVLSGSPMSASSANYSVVSE 78
Cdd:PLN02347    9 YLDVVLILDYGSQYTHLITRRVRELGVYSLLLS-GTASLDRIASLNPRVVILSGGPHSVHVEGAPTVPE 76
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 17-85 8.47e-10

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 52.64  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490961336  17 VNFGGQYAHLIARRIRELG-------VY-SELVDYEQVCEDYmrrvrlKAVVLSGSPMSA------SSANYSVVSEILKL 82
Cdd:COG0518     8 DPFGGQYPGLIARRLREAGieldvlrVYaGEILPYDPDLEDP------DGLILSGGPMSVydedpwLEDEPALIREAFEL 81


                  ...
gi 1490961336  83 GVP 85
Cdd:COG0518    82 GKP 84
PRK00758 PRK00758
GMP synthase subunit A; Validated
 14-85 6.34e-09

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 49.85  E-value: 6.34e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490961336  14 VAVVNFGGQYAHLIARRIRELGVYSELVDYEQVCEDYmrRVRLKAVVLSGSP---MSASSANYsvvseILKLGVP 85
Cdd:PRK00758    2 IVVVDNGGQYNHLIHRTLRYLGVDAKIIPNTTPVEEI--KAFEDGLILSGGPdieRAGNCPEY-----LKELDVP 69
GATase pfam00117
Glutamine amidotransferase class-I;
15-85 3.37e-06

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 42.61  E-value: 3.37e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1490961336  15 AVVNFGGQYAHLIARRIRELGVYSELV----DYEQVCEDYMrrvrlKAVVLSGSPMSASSANYSV--VSEILKLGVP 85
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVpndtPAEEILEENP-----DGIILSGGPGSPGAAGGAIeaIREARELKIP 72
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH