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Conserved domains on  [gi|134254462|ref|NP_065785|]
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beta-citrylglutamate synthase B [Homo sapiens]

Protein Classification

RimK family alpha-L-glutamate ligase( domain architecture ID 11489658)

RimK family protein alpha-L-glutamate ligase, similar to Methanosarcina jannaschii tetrahydromethanopterin:alpha-L-glutamate ligase (MJ0620 MptN) which catalyzes the ATP or GTP-dependent addition of one L-glutamate molecule to tetrahydromethanopterin, and to human N-acetylaspartylglutamate (NAAG) synthetase (NAAGS-II) which in addition to synthesizing NAAG is capable of condensing a second glutamate residue to generate NAAG2

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
8-303 3.77e-110

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


:

Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 323.53  E-value: 3.77e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462    8 KLWFLTDRRiredypqKEILRALKAKCCEEELDFRAVVMDEVVLTIEQGNLglringelITAYPQVVVVRVptpwVQSDS 87
Cdd:TIGR00768   1 KIAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPR--------ALAELDVVIVRI----VSMFR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462   88 DITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEaevLEFPMVVKNTRGHRGKA 167
Cdd:TIGR00768  62 GLAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  168 VFLARDKHHLADLSHLIRHEAP----YLFQKYVKESHGRDVRVIVVGGRVVGTMLRCsTDGRMQSNCSLGGVGMMCSLSE 243
Cdd:TIGR00768 139 VSLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTE 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  244 QGKQLAIQVSNILGMDVCGIDLLMKDDGsFCVCEANANVGFIAFDKACNLDVAGIIADYA 303
Cdd:TIGR00768 218 EIEELAIKAAKALGLDVAGVDLLESEDG-LLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
8-303 3.77e-110

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 323.53  E-value: 3.77e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462    8 KLWFLTDRRiredypqKEILRALKAKCCEEELDFRAVVMDEVVLTIEQGNLglringelITAYPQVVVVRVptpwVQSDS 87
Cdd:TIGR00768   1 KIAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPR--------ALAELDVVIVRI----VSMFR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462   88 DITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEaevLEFPMVVKNTRGHRGKA 167
Cdd:TIGR00768  62 GLAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  168 VFLARDKHHLADLSHLIRHEAP----YLFQKYVKESHGRDVRVIVVGGRVVGTMLRCsTDGRMQSNCSLGGVGMMCSLSE 243
Cdd:TIGR00768 139 VSLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTE 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  244 QGKQLAIQVSNILGMDVCGIDLLMKDDGsFCVCEANANVGFIAFDKACNLDVAGIIADYA 303
Cdd:TIGR00768 218 EIEELAIKAAKALGLDVAGVDLLESEDG-LLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
8-309 7.48e-45

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 156.25  E-value: 7.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462   8 KLWFLTDRRIRedYPQKEILRALkakcceEELDFRAVVMDEVVLTIEQGNLGLRINGELITAYpQVVVVRVPTPWVQsds 87
Cdd:COG0189    3 KIAILTDPPDK--DSTKALIEAA------QRRGHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  88 dITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEaevLEFPMVVKNTRGHRGKA 167
Cdd:COG0189   71 -LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462 168 VFLARDKHHLAD-LSHLIRHE-APYLFQKYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQG 245
Cdd:COG0189  147 VFLVEDEDALESiLEALTELGsEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEE 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134254462 246 KQLAIQVSNILGMDVCGIDLLMKDDGsFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPS 309
Cdd:COG0189  227 RELALRAAPALGLDFAGVDLIEDDDG-PLVLEVNVTPGFRGLERATGVDIAEAIADYLEARAAR 289
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
114-302 1.66e-32

RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.


Pssm-ID: 369879 [Multi-domain]  Cd Length: 188  Bit Score: 120.68  E-value: 1.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  114 NKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEvLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRheAPYLFQ 193
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATN--EQILVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  194 KYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGMDVCGIDLLMKDDGsF 273
Cdd:pfam08443  80 EFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG-L 158
                         170       180
                  ....*....|....*....|....*....
gi 134254462  274 CVCEANANVGFIAFDKACNLDVAGIIADY 302
Cdd:pfam08443 159 LVCEVNSSPGLEGIEKTLGINIAIKIIAS 187
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
91-297 2.32e-21

30S ribosomal protein S6--L-glutamate ligase;


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 93.04  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  91 VLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEaeVLEFPMVVKNTRGHRGKAVFL 170
Cdd:PRK10446  76 ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDM--VGGAPLVVKLVEGTQGIGVVL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462 171 ARDKHHLADLSHLIRH-EAPYLFQKYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLA 249
Cdd:PRK10446 154 AETRQAAESVIDAFRGlNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIA 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 134254462 250 IQVSNILGMDVCGIDLLMKDDGSFcVCEANANVGFIAFDKACNLDVAG 297
Cdd:PRK10446 234 IKAARTMALDVAGVDILRANRGPL-VMEVNASPGLEGIEKTTGIDIAG 280
 
Name Accession Description Interval E-value
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
8-303 3.77e-110

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 323.53  E-value: 3.77e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462    8 KLWFLTDRRiredypqKEILRALKAKCCEEELDFRAVVMDEVVLTIEQGNLglringelITAYPQVVVVRVptpwVQSDS 87
Cdd:TIGR00768   1 KIAILYDRI-------RLDEKMLKEAAEELGIDYKVVTPPAINLTFNEGPR--------ALAELDVVIVRI----VSMFR 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462   88 DITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEaevLEFPMVVKNTRGHRGKA 167
Cdd:TIGR00768  62 GLAVLRYLESLGVPVINSSDAILNAGDKFLSHQLLAKAGIPLPRTGLAGSPEEALKLIEE---IGFPVVLKPVFGSWGRG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  168 VFLARDKHHLADLSHLIRHEAP----YLFQKYVKESHGRDVRVIVVGGRVVGTMLRCsTDGRMQSNCSLGGVGMMCSLSE 243
Cdd:TIGR00768 139 VSLARDRQAAESLLEHFEQLNGpqnlFLVQEYIKKPGGRDIRVFVVGDEVVAAIYRI-TSGHWRSNLARGGKAEPCSLTE 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  244 QGKQLAIQVSNILGMDVCGIDLLMKDDGsFCVCEANANVGFIAFDKACNLDVAGIIADYA 303
Cdd:TIGR00768 218 EIEELAIKAAKALGLDVAGVDLLESEDG-LLVNEVNANPEFKNSVKTTGVNIAGKLLDYI 276
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
8-309 7.48e-45

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 156.25  E-value: 7.48e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462   8 KLWFLTDRRIRedYPQKEILRALkakcceEELDFRAVVMDEVVLTIEQGNLGLRINGELITAYpQVVVVRVPTPWVQsds 87
Cdd:COG0189    3 KIAILTDPPDK--DSTKALIEAA------QRRGHEVEVIDPDDLTLDLGRAPELYRGEDLSEF-DAVLPRIDPPFYG--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  88 dITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEaevLEFPMVVKNTRGHRGKA 167
Cdd:COG0189   71 -LALLRQLEAAGVPVVNDPEAIRRARDKLFTLQLLARAGIPVPPTLVTRDPDDLRAFLEE---LGGPVVLKPLDGSGGRG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462 168 VFLARDKHHLAD-LSHLIRHE-APYLFQKYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQG 245
Cdd:COG0189  147 VFLVEDEDALESiLEALTELGsEPVLVQEFIPEEDGRDIRVLVVGGEPVAAIRRIPAEGEFRTNLARGGRAEPVELTDEE 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 134254462 246 KQLAIQVSNILGMDVCGIDLLMKDDGsFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPS 309
Cdd:COG0189  227 RELALRAAPALGLDFAGVDLIEDDDG-PLVLEVNVTPGFRGLERATGVDIAEAIADYLEARAAR 289
RimK pfam08443
RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification ...
114-302 1.66e-32

RimK-like ATP-grasp domain; This ATP-grasp domain is found in the ribosomal S6 modification enzyme RimK.


Pssm-ID: 369879 [Multi-domain]  Cd Length: 188  Bit Score: 120.68  E-value: 1.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  114 NKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEvLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRheAPYLFQ 193
Cdd:pfam08443   3 DKAKSHQLLAKHGIGPPNTRLAWYPEDAEQFIEQIK-RQFPVIVKSIYGSQGIGVFLAEDEQKLRQTLSATN--EQILVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  194 KYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGMDVCGIDLLMKDDGsF 273
Cdd:pfam08443  80 EFIAEANNEDIRCLVVGDQVVGALHRQSNEGDFRSNLHRGGVGEKYQLSQEETELAIKAAQAMQLDVAGVDLLRQKRG-L 158
                         170       180
                  ....*....|....*....|....*....
gi 134254462  274 CVCEANANVGFIAFDKACNLDVAGIIADY 302
Cdd:pfam08443 159 LVCEVNSSPGLEGIEKTLGINIAIKIIAS 187
PRK10446 PRK10446
30S ribosomal protein S6--L-glutamate ligase;
91-297 2.32e-21

30S ribosomal protein S6--L-glutamate ligase;


Pssm-ID: 182468 [Multi-domain]  Cd Length: 300  Bit Score: 93.04  E-value: 2.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  91 VLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEaeVLEFPMVVKNTRGHRGKAVFL 170
Cdd:PRK10446  76 ALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDM--VGGAPLVVKLVEGTQGIGVVL 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462 171 ARDKHHLADLSHLIRH-EAPYLFQKYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLA 249
Cdd:PRK10446 154 AETRQAAESVIDAFRGlNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIA 233
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 134254462 250 IQVSNILGMDVCGIDLLMKDDGSFcVCEANANVGFIAFDKACNLDVAG 297
Cdd:PRK10446 234 IKAARTMALDVAGVDILRANRGPL-VMEVNASPGLEGIEKTTGIDIAG 280
PRK12767 PRK12767
carbamoyl phosphate synthase-like protein; Provisional
95-198 7.44e-13

carbamoyl phosphate synthase-like protein; Provisional


Pssm-ID: 237195 [Multi-domain]  Cd Length: 326  Bit Score: 68.76  E-value: 7.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  95 LEKMGCRLM-NRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEvLEFPMVVKNTRGHRGKAVFLARD 173
Cdd:PRK12767  91 FEEIGVKVLvSSKEVIEICNDKWLTYEFLKENGIPTPKSYLPESLEDFKAALAKGE-LQFPLFVKPRDGSASIGVFKVND 169
                         90       100
                 ....*....|....*....|....*
gi 134254462 174 KhhlADLSHLIRHEAPYLFQKYVKE 198
Cdd:PRK12767 170 K---EELEFLLEYVPNLIIQEFIEG 191
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
96-196 1.99e-07

Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440208 [Multi-domain]  Cd Length: 263  Bit Score: 51.80  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  96 EKMGCRlMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYgghENFAKMIDEAEVLEFPMVVKNTRGHRGKAVFLARDKH 175
Cdd:COG0439   37 EELGLP-GPSPEAIRAMRDKVLMREALAAAGVPVPGFALV---DSPEEALAFAEEIGYPVVVKPADGAGSRGVRVVRDEE 112
                         90       100
                 ....*....|....*....|....*...
gi 134254462 176 HLADLSHLIRHEA-------PYLFQKYV 196
Cdd:COG0439  113 ELEAALAEARAEAkagspngEVLVEEFL 140
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
112-279 9.99e-04

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 39.29  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  112 CVNKFWTFQELAGHGVPLPDTFSygghenfakmIDEAEVLEFPMVVKNTRGHRGKAVFLARDKHHL-ADLSHLIrheapy 190
Cdd:pfam02655   1 ASDKLKTYKALKNAGVPTPETLQ----------AEELLREEKKYVVKPRDGCGGEGVRKVENGREDeAFIENVL------ 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  191 lFQKYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVG-MMCSLSEQGKQLAIQV----SNILGMDvcGIDL 265
Cdd:pfam02655  65 -VQEFIEGEPLSVSLLSDGEKALPLSVNRQYIDNGGSGFVYAGNVTpSRTELKEEIIELAEEVveclPGLRGYV--GVDL 141
                         170
                  ....*....|....
gi 134254462  266 LMKDDGSfCVCEAN 279
Cdd:pfam02655 142 VLKDNEP-YVIEVN 154
PLN02948 PLN02948
phosphoribosylaminoimidazole carboxylase
88-179 2.19e-03

phosphoribosylaminoimidazole carboxylase


Pssm-ID: 178534 [Multi-domain]  Cd Length: 577  Bit Score: 40.04  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 134254462  88 DITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDtfsYGGHENFAKMIDEAEVLEFPMVVKNTRGH---R 164
Cdd:PLN02948  95 DVDTLEALEKQGVDVQPKSSTIRIIQDKYAQKVHFSKHGIPLPE---FMEIDDLESAEKAGDLFGYPLMLKSRRLAydgR 171
                         90
                 ....*....|....*
gi 134254462 165 GKAVflARDKHHLAD 179
Cdd:PLN02948 172 GNAV--AKTEEDLSS 184
 
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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