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Conserved domains on  [gi|1633269979|gb|QCJ59610|]
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imidazole glycerol phosphate synthase subunit HisH [Escherichia coli]

Protein Classification

imidazole glycerol phosphate synthase subunit HisH( domain architecture ID 10014130)

imidazole glycerol phosphate synthase subunit HisH catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the synthesis of IGP and AICAR

CATH:  3.40.50.880
EC:  4.3.2.10|3.5.1.2
Gene Ontology:  GO:0004359|GO:0000107|GO:0016829
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 1.51e-157

imidazole glycerol phosphate synthase subunit HisH; Provisional


:

Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 432.74  E-value: 1.51e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQPVLGICLGM 80
Cdd:PRK13170    1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  81 QLLGRRSEESNGVDLLGIIDEDVPKMTDFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNPWTIAQCNYG 160
Cdd:PRK13170   81 QLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTIAQCNYG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1633269979 161 EPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK13170  161 EPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
 
Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 1.51e-157

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 432.74  E-value: 1.51e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQPVLGICLGM 80
Cdd:PRK13170    1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  81 QLLGRRSEESNGVDLLGIIDEDVPKMTDFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNPWTIAQCNYG 160
Cdd:PRK13170   81 QLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTIAQCNYG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1633269979 161 EPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK13170  161 EPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-196 2.00e-106

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 303.48  E-value: 2.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERE---LFDLIKACTQPVLGICLG 79
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGldlFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNGVDLLGIIDEDVPKMTDFglPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNP-WTIAQCN 158
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR--KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEeAVLAYAD 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1633269979 159 YGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:TIGR01855 159 YGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-191 6.27e-106

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 301.96  E-value: 6.27e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIK---ACTQPVLGIC 77
Cdd:COG0118     1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIReavAGGKPVLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  78 LGMQLLGRRSEESNGVDLLGIIDEDVPKMTDFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVN--PWTIA 155
Cdd:COG0118    81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDdpEDVVA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1633269979 156 QCNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLK 191
Cdd:COG0118   161 TTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 3-194 2.92e-102

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 292.86  E-value: 2.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQ---PVLGICLG 79
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIAsgkPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNGVDLLGIIDEDVPKMT-DFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNP--WTIAQ 156
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPaSEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDpdYILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1633269979 157 CNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFL 194
Cdd:cd01748   161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
GATase pfam00117
Glutamine amidotransferase class-I;
4-194 5.31e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 83.06  E-value: 5.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   4 VILDTGCANLNSVKSAIARHGYEPKVSR--DPDVVLLADK----LFLPGVGTAQAAMDQVRE-RELFDLIKactqPVLGI 76
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPndTPAEEILEENpdgiILSGGPGSPGAAGGAIEAiREARELKI----PILGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  77 CLGMQLLgrrseesngVDLLGiidEDVPKMTDFglplPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAmpVNPWTI-- 154
Cdd:pfam00117  77 CLGHQLL---------ALAFG---GKVVKAKKF----GHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYA--VDPDTLpd 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1633269979 155 -----AQCNYGEPFTAAVQKDN-FYGVQFHPE-RSGAAGANLLKNFL 194
Cdd:pfam00117 139 glevtATSENDGTIMGIRHKKLpIFGVQFHPEsILTPHGPEILFNFF 185
 
Name Accession Description Interval E-value
hisH PRK13170
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 1.51e-157

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183877 [Multi-domain]  Cd Length: 196  Bit Score: 432.74  E-value: 1.51e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQPVLGICLGM 80
Cdd:PRK13170    1 MNVVIIDTGCANLSSVKFAIERLGYEPVVSRDPDVILAADKLFLPGVGTAQAAMDQLRERELIDLIKACTQPVLGICLGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  81 QLLGRRSEESNGVDLLGIIDEDVPKMTDFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNPWTIAQCNYG 160
Cdd:PRK13170   81 QLLGERSEESGGVDCLGIIDGPVKKMTDFGLPLPHMGWNQVTPQAGHPLFQGIEDGSYFYFVHSYAMPVNEYTIAQCNYG 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1633269979 161 EPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK13170  161 EPFSAAIQKDNFFGVQFHPERSGAAGAQLLKNFLEM 196
IMP_synth_hisH TIGR01855
imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model ...
 3-196 2.00e-106

imidazole glycerol phosphate synthase, glutamine amidotransferase subunit; This model represents the glutamine amidotransferase subunit (or domain, in eukaryotic systems) of imidazole glycerol phosphate synthase. This subunit catalyzes step 5 of histidine biosynthesis from PRPP. The other subunit, the cyclase, catalyzes step 6. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273836 [Multi-domain]  Cd Length: 196  Bit Score: 303.48  E-value: 2.00e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERE---LFDLIKACTQPVLGICLG 79
Cdd:TIGR01855   1 IVIIDYGVGNLGSVKRALKRVGAEPVVVKDSKEAELADKLILPGVGAFGAAMARLRENGldlFVELVVRLGKPVLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNGVDLLGIIDEDVPKMTDFglPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNP-WTIAQCN 158
Cdd:TIGR01855  81 MQLLFERSEEGGGVPGLGLIKGNVVKLEAR--KVPHMGWNEVHPVKESPLLNGIDEGAYFYFVHSYYAVCEEeAVLAYAD 158

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1633269979 159 YGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:TIGR01855 159 YGEKFPAAVQKGNIFGTQFHPEKSGKTGLKLLENFLEL 196
HisH COG0118
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ...
 1-191 6.27e-106

Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439888 [Multi-domain]  Cd Length: 196  Bit Score: 301.96  E-value: 6.27e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIK---ACTQPVLGIC 77
Cdd:COG0118     1 MMIAIIDYGMGNLRSVAKALERLGAEVVVTSDPDEIRAADRLVLPGVGAFGDAMENLRERGLDEAIReavAGGKPVLGIC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  78 LGMQLLGRRSEESNGVDLLGIIDEDVPKMTDFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVN--PWTIA 155
Cdd:COG0118    81 LGMQLLFERSEENGDTEGLGLIPGEVVRFPASDLKVPHMGWNTVEIAKDHPLFAGIPDGEYFYFVHSYYVPPDdpEDVVA 160

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1633269979 156 QCNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLK 191
Cdd:COG0118   161 TTDYGVPFTAAVERGNVFGTQFHPEKSGAAGLRLLK 196
GATase1_IGP_Synthase cd01748
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ...
 3-194 2.92e-102

Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153219 [Multi-domain]  Cd Length: 198  Bit Score: 292.86  E-value: 2.92e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQ---PVLGICLG 79
Cdd:cd01748     1 IAIIDYGMGNLRSVANALERLGAEVIITSDPEEILSADKLILPGVGAFGDAMANLRERGLIEALKEAIAsgkPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNGVDLLGIIDEDVPKMT-DFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNP--WTIAQ 156
Cdd:cd01748    81 MQLLFESSEEGGGTKGLGLIPGKVVRFPaSEGLKVPHMGWNQLEITKESPLFKGIPDGSYFYFVHSYYAPPDDpdYILAT 160

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1633269979 157 CNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFL 194
Cdd:cd01748   161 TDYGGKFPAAVEKDNIFGTQFHPEKSGKAGLKLLKNFL 198
hisH PRK13141
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 9.70e-90

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237288 [Multi-domain]  Cd Length: 205  Bit Score: 261.60  E-value: 9.70e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIK---ACTQPVLGICLG 79
Cdd:PRK13141    2 IAIIDYGMGNLRSVEKALERLGAEAVITSDPEEILAADGVILPGVGAFPDAMANLRERGLDEVIKeavASGKPLLGICLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNGVDLLGIIDEDVPKMTDF-GLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSY-AMPVNP-WTIAQ 156
Cdd:PRK13141   82 MQLLFESSEEFGETEGLGLLPGRVRRFPPEeGLKVPHMGWNQLELKKESPLLKGIPDGAYVYFVHSYyADPCDEeYVAAT 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1633269979 157 CNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK13141  162 TDYGVEFPAAVGKDNVFGAQFHPEKSGDVGLKILKNFVEM 201
hisH PRK13181
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 1.86e-88

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 183878 [Multi-domain]  Cd Length: 199  Bit Score: 257.87  E-value: 1.86e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACT---QPVLGICLG 79
Cdd:PRK13181    2 IAIIDYGAGNLRSVANALKRLGVEAVVSSDPEEIAGADKVILPGVGAFGQAMRSLRESGLDEALKEHVekkQPVLGICLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEEsNGVDLLGIIDEDVPKMTDFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNPW--TIAQC 157
Cdd:PRK13181   82 MQLLFESSEE-GNVKGLGLIPGDVKRFRSEPLKVPQMGWNSVKPLKESPLFKGIEEGSYFYFVHSYYVPCEDPedVLATT 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1633269979 158 NYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK13181  161 EYGVPFCSAVAKDNIYAVQFHPEKSGKAGLKLLKNFAEL 199
hisH PRK13146
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-195 1.01e-74

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237290 [Multi-domain]  Cd Length: 209  Bit Score: 223.51  E-value: 1.01e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIAR--HGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQ----PVL 74
Cdd:PRK13146    2 MTVAIIDYGSGNLRSAAKALERagAGADVVVTADPDAVAAADRVVLPGVGAFADCMRGLRAVGLGEAVIEAVLaagrPFL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  75 GICLGMQLLGRRSEESNGVDLLGIIDEDVPKMTDFG--LPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYA-MPVNP 151
Cdd:PRK13146   82 GICVGMQLLFERGLEHGDTPGLGLIPGEVVRFQPDGpaLKVPHMGWNTVDQTRDHPLFAGIPDGARFYFVHSYYaQPANP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1633269979 152 W-TIAQCNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLE 195
Cdd:PRK13146  162 AdVVAWTDYGGPFTAAVARDNLFATQFHPEKSQDAGLALLRNFLA 206
hisH PRK13143
imidazole glycerol phosphate synthase subunit HisH; Provisional
 1-196 2.49e-69

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 237289 [Multi-domain]  Cd Length: 200  Bit Score: 209.72  E-value: 2.49e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRE-RELFDLIKACTQPVLGICLG 79
Cdd:PRK13143    1 MMIVIIDYGVGNLRSVSKALERAGAEVVITSDPEEILDADGIVLPGVGAFGAAMENLSPlRDVILEAARSGKPFLGICLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNGVDLLGIIDEDVPKMTDfGLPLPHMGWNRVYPQAGNRLFQGIeDGAYFYFVHSY-AMPVNP-WTIAQC 157
Cdd:PRK13143   81 MQLLFESSEEGGGVRGLGLFPGRVVRFPA-GVKVPHMGWNTVKVVKDCPLFEGI-DGEYVYFVHSYyAYPDDEdYVVATT 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1633269979 158 NYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK13143  159 DYGIEFPAAVCNDNVFGTQFHPEKSGETGLKILENFVEL 197
PLN02617 PLN02617
imidazole glycerol phosphate synthase hisHF
 3-195 4.16e-57

imidazole glycerol phosphate synthase hisHF


Pssm-ID: 178226 [Multi-domain]  Cd Length: 538  Bit Score: 188.00  E-value: 4.16e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQ---PVLGICLG 79
Cdd:PLN02617    9 VTLLDYGAGNVRSVRNAIRHLGFTIKDVQTPEDILNADRLIFPGVGAFGSAMDVLNNRGMAEALREYIQndrPFLGICLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNGVDLLGIIDEDVPKM-TDFGLPLPHMGWNRVYPQAGNRLFQGIeDGAYFYFVHSY-AMPVNP---WTI 154
Cdd:PLN02617   89 LQLLFESSEENGPVEGLGVIPGVVGRFdSSNGLRVPHIGWNALQITKDSELLDGV-GGRHVYFVHSYrATPSDEnkdWVL 167

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1633269979 155 AQCNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLE 195
Cdd:PLN02617  168 ATCNYGGEFIASVRKGNVHAVQFHPEKSGATGLSILRRFLE 208
hisH PRK13152
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 3.79e-49

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171876 [Multi-domain]  Cd Length: 201  Bit Score: 158.46  E-value: 3.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACT----QPVLGICL 78
Cdd:PRK13152    2 IALIDYKAGNLNSVAKAFEKIGAINFIAKNPKDLQKADKLLLPGVGSFKEAMKNLKELGFIEALKEQVlvqkKPILGICL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  79 GMQLLGRRSEESNGVDLLGIIDEDVPKM-TDFGLPLPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAMPVNPWTI-AQ 156
Cdd:PRK13152   82 GMQLFLERGYEGGVCEGLGFIEGEVVKFeEDLNLKIPHMGWNELEILKQSPLYQGIPEKSDFYFVHSFYVKCKDEFVsAK 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1633269979 157 CNYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK13152  162 AQYGHKFVASLQKDNIFATQFHPEKSQNLGLKLLENFARL 201
hisH PRK13142
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-195 8.98e-44

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 171871 [Multi-domain]  Cd Length: 192  Bit Score: 144.58  E-value: 8.98e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACT-QPVLGICLGMQ 81
Cdd:PRK13142    2 IVIVDYGLGNISNVKRAIEHLGYEVVVSNTSKIIDQAETIILPGVGHFKDAMSEIKRLNLNAILAKNTdKKMIGICLGMQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  82 LLGRRSEESNgVDLLGIID-EDVPKMTDFglPLPHMGWNRV---YPQagnrLFQGIedgayfYFVHSYAMPVNPWTIAQC 157
Cdd:PRK13142   82 LMYEHSDEGD-ASGLGFIPgNISRIQTEY--PVPHLGWNNLvskHPM----LNQDV------YFVHSYQAPMSENVIAYA 148

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1633269979 158 NYGEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLE 195
Cdd:PRK13142  149 QYGADIPAIVQFNNYIGIQFHPEKSGTYGLQILRQAIQ 186
hisH CHL00188
imidazole glycerol phosphate synthase subunit hisH; Provisional
 1-195 7.26e-43

imidazole glycerol phosphate synthase subunit hisH; Provisional


Pssm-ID: 214389 [Multi-domain]  Cd Length: 210  Bit Score: 142.72  E-value: 7.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIKACTQ---PVLGIC 77
Cdd:CHL00188    2 MKIGIIDYSMGNLHSVSRAIQQAGQQPCIINSESELAQVHALVLPGVGSFDLAMKKLEKKGLITPIKKWIAegnPFIGIC 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  78 LGMQLLGRRSEESNGvDLLGIIDEDVPKMTDFGL-PLPHMGWNRVYPQAGN------RLFQGIEDGAYFYFVHSY-AMPV 149
Cdd:CHL00188   82 LGLHLLFETSEEGKE-EGLGIYKGQVKRLKHSPVkVIPHMGWNRLECQNSEcqnsewVNWKAWPLNPWAYFVHSYgVMPK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1633269979 150 NPWTI-AQCNYG-EPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLE 195
Cdd:CHL00188  161 SQACAtTTTFYGkQQMVAAIEYDNIFAMQFHPEKSGEFGLWLLREFMK 208
hisH PRK14004
imidazole glycerol phosphate synthase subunit HisH; Provisional
 3-196 1.11e-39

imidazole glycerol phosphate synthase subunit HisH; Provisional


Pssm-ID: 172505 [Multi-domain]  Cd Length: 210  Bit Score: 134.65  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKSAIARHGYEPKVSRDPDVVLLADKLFLPGVGTAQAAMDQVRERELFDLIK---ACTQPVLGICLG 79
Cdd:PRK14004    2 IAILDYGMGNIHSCLKAVSLYTKDFVFTSDPETIENSKALILPGDGHFDKAMENLNSTGLRSTIDkhvESGKPLFGICIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  80 MQLLGRRSEESNG------VDLLGIIDEDVPKMTDFGLPLPHMGWNRVY--PQAGNRLFQGIEDGAYFYFVHSYaMPV-- 149
Cdd:PRK14004   82 FQILFESSEETNQgtkkeqIEGLGYIKGKIKKFEGKDFKVPHIGWNRLQirRKDKSKLLKGIGDQSFFYFIHSY-RPTga 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1633269979 150 --NPWTiAQCNY-GEPFTAAVQKDNFYGVQFHPERSGAAGANLLKNFLEM 196
Cdd:PRK14004  161 egNAIT-GLCDYyQEKFPAVVEKENIFGTQFHPEKSHTHGLKLLENFIEF 209
GATase pfam00117
Glutamine amidotransferase class-I;
4-194 5.31e-20

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 83.06  E-value: 5.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   4 VILDTGCANLNSVKSAIARHGYEPKVSR--DPDVVLLADK----LFLPGVGTAQAAMDQVRE-RELFDLIKactqPVLGI 76
Cdd:pfam00117   1 LLIDNGDSFTYNLARALRELGVEVTVVPndTPAEEILEENpdgiILSGGPGSPGAAGGAIEAiREARELKI----PILGI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  77 CLGMQLLgrrseesngVDLLGiidEDVPKMTDFglplPHMGWNRVYPQAGNRLFQGIEDGAYFYFVHSYAmpVNPWTI-- 154
Cdd:pfam00117  77 CLGHQLL---------ALAFG---GKVVKAKKF----GHHGKNSPVGDDGCGLFYGLPNVFIVRRYHSYA--VDPDTLpd 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1633269979 155 -----AQCNYGEPFTAAVQKDN-FYGVQFHPE-RSGAAGANLLKNFL 194
Cdd:pfam00117 139 glevtATSENDGTIMGIRHKKLpIFGVQFHPEsILTPHGPEILFNFF 185
GATase1_Anthranilate_Synthase cd01743
Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 ...
 20-194 1.65e-11

Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase; Type 1 glutamine amidotransferase (GATase1) domain found in Anthranilate synthase (ASase). This group contains proteins similar to para-aminobenzoate (PABA) synthase and ASase. These enzymes catalyze similar reactions and produce similar products, PABA and ortho-aminobenzoate (anthranilate). Each enzyme is composed of non-identical subunits: a glutamine amidotransferase subunit (component II) and a subunit that produces an aminobenzoate products (component I). ASase catalyses the synthesis of anthranilate from chorismate and glutamine and is a tetrameric protein comprising two copies each of components I and II. Component II of ASase belongs to the family of triad GTases which hydrolyze glutamine and transfer nascent ammonia between the active sites. In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. PRTase catalyses the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. In E.coli, the first step in the conversion of chorismate to PABA involves two proteins: PabA and PabB which co-operate to transfer the amide nitrogen of glutamine to chorismate forming 4-amino-4 deoxychorismate (ADC). PabA acts as a glutamine amidotransferase, supplying an amino group to PabB, which carries out the amination reaction. A third protein PabC then mediates elimination of pyruvate and aromatization to give PABA. Several organisms have bipartite proteins containing fused domains homologous to PabA and PabB commonly called PABA synthases. These hybrid PABA synthases may produce ADC and not PABA.


Pssm-ID: 153214 [Multi-domain]  Cd Length: 184  Bit Score: 60.24  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  20 IARHGYEPKVSR--DPDVVLLA----DKLFL-PGVGT-AQAAMDqvrerelFDLIKACTQ--PVLGICLGMQLLGrrseE 89
Cdd:cd01743    18 LRELGAEVVVVRndEITLEELEllnpDAIVIsPGPGHpEDAGIS-------LEIIRALAGkvPILGVCLGHQAIA----E 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  90 SNGvdllGIIDEdvpkmtdfgLPLPHMGWNRVYPQAGNRLFQGIEDG--AYFYfvHSYAMPVNP-----WTIAQCNYGEP 162
Cdd:cd01743    87 AFG----GKVVR---------APEPMHGKTSEIHHDGSGLFKGLPQPftVGRY--HSLVVDPDPlpdllEVTASTEDGVI 151

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1633269979 163 FTAAVQKDNFYGVQFHPErS--GAAGANLLKNFL 194
Cdd:cd01743   152 MALRHRDLPIYGVQFHPE-SilTEYGLRLLENFL 184
PabA COG0512
Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid ...
 20-196 3.93e-09

Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Anthranilate/para-aminobenzoate synthase component II (glutamine amidotransferase) is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440278 [Multi-domain]  Cd Length: 189  Bit Score: 53.89  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  20 IARHGYEPKVSR------------DPDVVLLAdklflPGVGTAQAAmdqvreRELFDLIKAC--TQPVLGICLGMQLLGr 85
Cdd:COG0512    18 LGELGAEVVVVRndeitleeiealAPDGIVLS-----PGPGTPEEA------GISLEVIRAFagKIPILGVCLGHQAIG- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  86 rseESngvdllgiidedvpkmtdFGLPLPHMGwnRVYP-------QAGNRLFQGIEDGayFYFV--HSyampvnpWTIAQ 156
Cdd:COG0512    86 ---EA------------------FGGKVVRAP--EPMHgktspitHDGSGLFAGLPNP--FTATryHS-------LVVDR 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1633269979 157 CNYGEPF--TA--------AVQ--KDNFYGVQFHPErS--GAAGANLLKNFLEM 196
Cdd:COG0512   134 ETLPDELevTAwtedgeimGIRhrELPIEGVQFHPE-SilTEHGHQLLANFLEL 186
guaA_Nterm TIGR00888
GMP synthase (glutamine-hydrolyzing), N-terminal domain or A subunit; This protein of purine ...
 72-195 5.10e-08

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: 50.78  E-value: 5.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  72 PVLGICLGMQLL--------GRRSEESNGVDLLGIIDEDVpkmtdfglplphmgwnrvypqagnrLFQGIEDGAYFYFVH 143
Cdd:TIGR00888  72 PVLGICYGMQLMakqlggevGRAEKREYGKAELEILDEDD-------------------------LFRGLPDESTVWMSH 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1633269979 144 S---YAMPVNPWTIAQCNyGEPFTAAVQKDN-FYGVQFHPE-RSGAAGANLLKNFLE 195
Cdd:TIGR00888 127 GdkvKELPEGFKVLATSD-NCPVAAMAHEEKpIYGVQFHPEvTHTEYGNELLENFVY 182
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 60-180 9.09e-08

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: 50.33  E-value: 9.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  60 RELFDLIKACTQ---PVLGICLGMQLLGRrseesngvdLLGiidedvpkmtdfG----LPLPHMGWNRVYPQAGNRLFQG 132
Cdd:COG0518    69 EDEPALIREAFElgkPVLGICYGAQLLAH---------ALG------------GkvepGPGREIGWAPVELTEADPLFAG 127

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1633269979 133 IEDGAYFYFVHSY---AMPVNPWTIAQcNYGEPFTAAVQKDNFYGVQFHPE 180
Cdd:COG0518   128 LPDEFTVWMSHGDtvtELPEGAEVLAS-SDNCPNQAFRYGRRVYGVQFHPE 177
GATase1_GMP_Synthase cd01742
Type 1 glutamine amidotransferase (GATase1) domain found in GMP synthetase; Type 1 glutamine ...
 59-194 3.70e-07

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: 48.30  E-value: 3.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  59 ERELFDLIKactqPVLGICLGMQL----LGRRSEESN----GVDLLGIIDEDvpkmtdfglplphmgwnrvypqagnRLF 130
Cdd:cd01742    63 DPEIFELGV----PVLGICYGMQLiakaLGGKVERGDkreyGKAEIEIDDSS-------------------------PLF 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1633269979 131 QGIEDGAYFYFVHS---YAMPVNPWTIA---QCnygePFTAAVQKD-NFYGVQFHPERSGAA-GANLLKNFL 194
Cdd:cd01742   114 EGLPDEQTVWMSHGdevVKLPEGFKVIAssdNC----PVAAIANEEkKIYGVQFHPEVTHTEkGKEILKNFL 181
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 60-194 4.26e-07

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 48.01  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  60 RELFDLIKACTQ---PVLGICLGMQLLGRrseesngvdLLGiidedvpkmtdfG--LPLPH---MGWNRVYPQAGNR--- 128
Cdd:cd01741    68 KKLKELIRQALAagkPVLGICLGHQLLAR---------ALG------------GkvGRNPKgweIGWFPVTLTEAGKadp 126

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1633269979 129 LFQGIEDGAYFYFVHSYAMPVNP--WTI----AQCnygePFTAAVQKDNFYGVQFHPERSgaaganLLKNFL 194
Cdd:cd01741   127 LFAGLPDEFPVFHWHGDTVVELPpgAVLlassEAC----PNQAFRYGDRALGLQFHPEER------LLRNFL 188
guaA PRK00074
GMP synthase; Reviewed
 61-194 1.06e-06

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 48.12  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  61 ELFDLIKactqPVLGICLGMQL----LG---RRSEESngvdllgiidedvpkmtDFGLplphmgwNRVYPQAGNRLFQGI 133
Cdd:PRK00074   70 EIFELGV----PVLGICYGMQLmahqLGgkvERAGKR-----------------EYGR-------AELEVDNDSPLFKGL 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979 134 EDGAYFYFVHS---YAMPVNPWTIAQ---CNYgepftAAVQKD--NFYGVQFHPE-RSGAAGANLLKNFL 194
Cdd:PRK00074  122 PEEQDVWMSHGdkvTELPEGFKVIAStenCPI-----AAIANEerKFYGVQFHPEvTHTPQGKKLLENFV 186
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-83 5.96e-06

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 43.74  E-value: 5.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKS---AIARHGYEPK-VSRDPDVVLL------ADKLFLPGVGTAQAAMDqvRERELFDLIKACTQ- 71
Cdd:cd01653     1 VAVLLFPGFEELELASpldALREAGAEVDvVSPDGGPVESdvdlddYDGLILPGGPGTPDDLA--RDEALLALLREAAAa 78

                          90
                  ....*....|....
gi 1633269979  72 --PVLGICLGMQLL 83
Cdd:cd01653    79 gkPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-83 1.59e-05

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 41.80  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   3 VVILDTGCANLNSVKS---AIARHGYEPK-VSRDPDVVLL------ADKLFLPGVGTAQAAMDqvRERELFDLIKACTQ- 71
Cdd:cd03128     1 VAVLLFGGSEELELASpldALREAGAEVDvVSPDGGPVESdvdlddYDGLILPGGPGTPDDLA--WDEALLALLREAAAa 78

                          90
                  ....*....|....
gi 1633269979  72 --PVLGICLGMQLL 83
Cdd:cd03128    79 gkPVLGICLGAQLL 92
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 39-100 3.95e-05

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 42.62  E-value: 3.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633269979  39 ADKLFLPGVGTAQAAMDQVRERELFDLIKACTQ---PVLGICLGMQLLGRR------SEESNGVDLLGIID 100
Cdd:cd01750    38 ADLIILPGSKDTIQDLAWLRKRGLAEAIKNYARaggPVLGICGGYQMLGKYivdpegVEGPGEIEGLGLLD 108
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
25-100 1.38e-04

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 41.07  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  25 YEPKV----SRDPDVVL--LADKLFLPG----VGTAQAAMDQVRERELFDLIKACTqPVLGICLGMQLLGRRSEESNGV- 93
Cdd:pfam07685  23 YEPAVrvrfVPLPDESLgpDADLIILPGgkptIQDLALLRNSGMDEAIKEAAEDGG-PVLGICGGYQMLGETIEDPEGVr 101


                  ....*...
gi 1633269979  94 -DLLGIID 100
Cdd:pfam07685 102 iEGLGLLD 109
PRK07765 PRK07765
aminodeoxychorismate/anthranilate synthase component II;
26-84 2.05e-04

aminodeoxychorismate/anthranilate synthase component II;


Pssm-ID: 181107 [Multi-domain]  Cd Length: 214  Bit Score: 40.80  E-value: 2.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1633269979  26 EPKVSRDPDVVLLADKLFL-PGVGTAQAAMDQVrerelfDLIKACTQ---PVLGICLGMQLLG 84
Cdd:PRK07765   34 DPRLADEAAVAAQFDGVLLsPGPGTPERAGASI------DMVRACAAagtPLLGVCLGHQAIG 90
GATase1_2 cd01745
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 19-83 5.83e-04

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153216 [Multi-domain]  Cd Length: 189  Bit Score: 39.10  E-value: 5.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  19 AIARHG-------YEPKVSRDPDVVLLADKLFLPGVGT----------AQAAMDQVRERELFD--LIKACTQ---PVLGI 76
Cdd:cd01745    27 AVRKAGglpvllpPVDDEEDLEQYLELLDGLLLTGGGDvdpplygeepHPELGPIDPERDAFElaLLRAALErgkPILGI 106


                  ....*..
gi 1633269979  77 CLGMQLL 83
Cdd:cd01745   107 CRGMQLL 113
PRK12838 PRK12838
carbamoyl phosphate synthase small subunit; Reviewed
 1-196 7.58e-04

carbamoyl phosphate synthase small subunit; Reviewed


Pssm-ID: 183784 [Multi-domain]  Cd Length: 354  Bit Score: 39.49  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   1 MNVVILDTGCanlnsvKSAIARHgyepKVSRDPDVVLL-------------ADKLFLP-GVGTAQAAMDQVRE-RELFDl 65
Cdd:PRK12838  168 KHVALIDFGY------KKSILRS----LSKRGCKVTVLpydtsleeiknlnPDGIVLSnGPGDPKELQPYLPEiKKLIS- 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  66 ikacTQPVLGICLGMQLLGRrseeSNGVDLlgiidedvpkmtdFGLPLPHMGWNR-VYPQAGNRLFQGIEDgayfyfvHS 144
Cdd:PRK12838  237 ----SYPILGICLGHQLIAL----ALGADT-------------EKLPFGHRGANHpVIDLTTGRVWMTSQN-------HG 288

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1633269979 145 YAmpVNPWTIAQCNYGEPFT----AAVQ-----KDNFYGVQFHPErsGAAG----ANLLKNFLEM 196
Cdd:PRK12838  289 YV--VDEDSLDGTPLSVRFFnvndGSIEglrhkKKPVLSVQFHPE--AHPGphdaEYIFDEFLEM 349
PRK06895 PRK06895
anthranilate synthase component II;
61-195 7.92e-04

anthranilate synthase component II;


Pssm-ID: 235882 [Multi-domain]  Cd Length: 190  Bit Score: 38.56  E-value: 7.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  61 ELFDLIKACTQ--PVLGICLGMQLLGrrseESNGVDLlgiidedvpkmtdFGLPLPHMGWNR-VYPQAGNRLFQGIEDGA 137
Cdd:PRK06895   61 QLFAMLERYHQhkSILGVCLGHQTLC----EFFGGEL-------------YNLNNVRHGQQRpLKVRSNSPLFDGLPEEF 123

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1633269979 138 YFYFVHSyampvnpWTIAQCNYGEPFTAAVQKDN------------FYGVQFHPERS-GAAGANLLKNFLE 195
Cdd:PRK06895  124 NIGLYHS-------WAVSEENFPTPLEITAVCDEnvvmamqhktlpIYGVQFHPESYiSEFGEQILRNWLA 187
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
 19-100 8.71e-04

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 38.66  E-value: 8.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  19 AIARHGYEPKVSRDPDVVLLADKLFLPGvGTAQAAMDQVRERELFDLIK---ACTQPVLGICLGMQLLGRRSEESNGVDL 95
Cdd:cd01749    16 ALERLGVEVIEVRTPEDLEGIDGLIIPG-GESTTIGKLLRRTGLLDPLRefiRAGKPVFGTCAGLILLAKEVEDQGGQPL 94


                  ....*
gi 1633269979  96 LGIID 100
Cdd:cd01749    95 LGLLD 99
PuuD COG2071
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ...
 58-83 9.29e-04

Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism];


Pssm-ID: 441674 [Multi-domain]  Cd Length: 231  Bit Score: 38.61  E-value: 9.29e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1633269979  58 RERELFD--LIKACTQ---PVLGICLGMQLL 83
Cdd:COG2071    79 PERDAFElaLIRAALErgkPVLGICRGMQLL 109
PRK00784 PRK00784
cobyric acid synthase;
32-93 1.11e-03

cobyric acid synthase;


Pssm-ID: 234838 [Multi-domain]  Cd Length: 488  Bit Score: 38.91  E-value: 1.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1633269979  32 DPDVVLLadklflPGVGTAQAAMDQVRERELFDLIKACTQ---PVLGICLGMQLLGRRSEESNGV 93
Cdd:PRK00784  290 DADLVIL------PGSKNTIADLAWLRESGWDEAIRAHARrggPVLGICGGYQMLGRRIADPDGV 348
PRK05670 PRK05670
anthranilate synthase component II; Provisional
 173-196 1.99e-03

anthranilate synthase component II; Provisional


Pssm-ID: 235552 [Multi-domain]  Cd Length: 189  Bit Score: 37.42  E-value: 1.99e-03
                          10        20
                  ....*....|....*....|....*
gi 1633269979 173 YGVQFHPERSG-AAGANLLKNFLEM 196
Cdd:PRK05670  163 YGVQFHPESILtEHGHKLLENFLEL 187
carA CHL00197
carbamoyl-phosphate synthase arginine-specific small subunit; Provisional
 72-196 2.18e-03

carbamoyl-phosphate synthase arginine-specific small subunit; Provisional


Pssm-ID: 214392 [Multi-domain]  Cd Length: 382  Bit Score: 37.85  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  72 PVLGICLGMQLLGRRSEESNgvdllgiidedvpkmtdFGLPLPHMGWNrvYPQAGNRLFQgIEDGAYFYFVHSYAMPVNP 151
Cdd:CHL00197  265 PIFGICMGHQILSLALEAKT-----------------FKLKFGHRGLN--HPSGLNQQVE-ITSQNHGFAVNLESLAKNK 324

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1633269979 152 WTIAQCNYGEPFTAAVQKDNF--YGVQFHPERS-GAAGAN-LLKNFLEM 196
Cdd:CHL00197  325 FYITHFNLNDGTVAGISHSPKpyFSVQYHPEASpGPHDADyLFEYFIEI 373
CarA COG0505
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ...
 2-85 4.31e-03

Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440271 [Multi-domain]  Cd Length: 361  Bit Score: 36.92  E-value: 4.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   2 NVVILDTGcanlnsVKSAI----ARHGYEPKV-----------SRDPDVVLLADklflpGVG---TAQAAMDQVRErelf 63
Cdd:COG0505   178 HVVALDFG------VKRNIlrelAERGCRVTVvpattsaeeilALNPDGVFLSN-----GPGdpaALDYAIETIRE---- 242

                          90       100
                  ....*....|....*....|..
gi 1633269979  64 dLIKACTqPVLGICLGMQLLGR 85
Cdd:COG0505   243 -LLGKGI-PIFGICLGHQLLAL 262
PRK13527 PRK13527
glutamine amidotransferase subunit PdxT; Provisional
 15-103 5.27e-03

glutamine amidotransferase subunit PdxT; Provisional


Pssm-ID: 237412 [Multi-domain]  Cd Length: 200  Bit Score: 36.40  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  15 SVKSAIARHG--YEPKVSRDPDVVLLADKLFLPGvGTAQAAMDQVRERELFDLIKACTQ---PVLGICLGMQLLGRRSEE 89
Cdd:PRK13527   18 ALKRALDELGidGEVVEVRRPGDLPDCDALIIPG-GESTTIGRLMKREGILDEIKEKIEeglPILGTCAGLILLAKEVGD 96

                          90
                  ....*....|....*...
gi 1633269979  90 SN----GVDLLGIIDEDV 103
Cdd:PRK13527   97 DRvtktEQPLLGLMDVTV 114
PRK12564 PRK12564
carbamoyl-phosphate synthase small subunit;
2-85 5.46e-03

carbamoyl-phosphate synthase small subunit;


Pssm-ID: 237139 [Multi-domain]  Cd Length: 360  Bit Score: 36.59  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979   2 NVVILDTGcanlnsVKSAI----ARHGYEPKV-----------SRDPDVVLLADklflpGVG---TAQAAMDQVRErelf 63
Cdd:PRK12564  179 KVVAIDFG------VKRNIlrelAERGCRVTVvpatttaeeilALNPDGVFLSN-----GPGdpaALDYAIEMIRE---- 243

                          90       100
                  ....*....|....*....|..
gi 1633269979  64 dLIKACTqPVLGICLGMQLLGR 85
Cdd:PRK12564  244 -LLEKKI-PIFGICLGHQLLAL 263
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 72-100 6.35e-03

Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 36.31  E-value: 6.35e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1633269979  72 PVLGICLGMQLLGRRSEESNGVDL--LGIID 100
Cdd:COG3442    87 PVLAICGGYQLLGHYYETADGERIpgLGILD 117
PRK00758 PRK00758
GMP synthase subunit A; Validated
 72-196 6.60e-03

GMP synthase subunit A; Validated


Pssm-ID: 179112 [Multi-domain]  Cd Length: 184  Bit Score: 35.98  E-value: 6.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1633269979  72 PVLGICLGMQLL--------GRRSEESNGVDLLGIIDEDVPkmtdF-GLPLP------HMGWNRVYPQAGNRLFQ----G 132
Cdd:PRK00758   69 PILGICLGHQLIakafggevGRGEYGEYALVEVEILDEDDI----LkGLPPEirvwasHADEVKELPDGFEILARsdicE 144

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1633269979 133 IEdgayfyfvhsyAMpvnpwtiaqcnygepftaaVQKDN-FYGVQFHPERS-GAAGANLLKNFLEM 196
Cdd:PRK00758  145 VE-----------AM-------------------KHKEKpIYGVQFHPEVAhTEYGEEIFKNFLEI 180
 
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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