NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489631888|ref|WP_003536328|]
View 

MULTISPECIES: glutamine amidotransferase family protein [Sinorhizobium]

Protein Classification

class II glutamine amidotransferase( domain architecture ID 10112366)

class II glutamine amidotransferase hydrolyzes ammonia from glutamine and transfers the amino group to the appropriate substrate; similar to Sinorhizobium meliloti glutamine amidotransferase-like protein GlxB

CATH:  3.60.20.10
EC:  2.4.2.-
Gene Ontology:  GO:0006541|GO:0016740
PubMed:  8430515|9559052
SCOP:  3000131

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-295 6.23e-100

Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


:

Pssm-ID: 238888 [Multi-domain]  Cd Length: 249  Bit Score: 293.41  E-value: 6.23e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888   2 CGIVGLFLKDSrlEPQLGQLLSDMLITMTDRGP-DSAGLAIYGSategkakvtiqsakpeidfadlerdlaeagvparva 80
Cdd:cd01907    1 CGIFGIMSKDG--EPFVGALLVEMLDAMQERGPgDGAGFALYGD------------------------------------ 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  81 vksthavvaiaaarladvravlaairPDVRIMGAGDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLG 160
Cdd:cd01907   43 --------------------------PDAFVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWIAHTRQPTNSAVWWYG 96

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 161 AHPFSTGsDQCLVHNGSLSNHNNLRRELIREGIAFETQNDTEVAAAYLTAEMAKGKD-------------------LGQA 221
Cdd:cd01907   97 AHPFSIG-DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLpleyykhiirmpeeerellLALR 175

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631888 222 LTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMAETDRYVAFGSEYRALVNLPDIESARIWEPEPATVYFW 295
Cdd:cd01907  176 LTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKVWEPRPGEYVIW 249
 
Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-295 6.23e-100

Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238888 [Multi-domain]  Cd Length: 249  Bit Score: 293.41  E-value: 6.23e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888   2 CGIVGLFLKDSrlEPQLGQLLSDMLITMTDRGP-DSAGLAIYGSategkakvtiqsakpeidfadlerdlaeagvparva 80
Cdd:cd01907    1 CGIFGIMSKDG--EPFVGALLVEMLDAMQERGPgDGAGFALYGD------------------------------------ 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  81 vksthavvaiaaarladvravlaairPDVRIMGAGDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLG 160
Cdd:cd01907   43 --------------------------PDAFVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWIAHTRQPTNSAVWWYG 96

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 161 AHPFSTGsDQCLVHNGSLSNHNNLRRELIREGIAFETQNDTEVAAAYLTAEMAKGKD-------------------LGQA 221
Cdd:cd01907   97 AHPFSIG-DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLpleyykhiirmpeeerellLALR 175

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631888 222 LTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMAETDRYVAFGSEYRALVNLPDIESARIWEPEPATVYFW 295
Cdd:cd01907  176 LTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKVWEPRPGEYVIW 249
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 115-237 1.55e-23

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 100.47  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGI 193
Cdd:COG0449   39 DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAPSDENAHPHTSCSGRiAVVHNGIIENYAELREELEAKGH 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489631888 194 AFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVV 237
Cdd:COG0449  119 TFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYALAV 162
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
115-237 8.28e-23

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 98.19  E-value: 8.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHP-FSTGSDQCLVHNGSLSNHNNLRRELIREGI 193
Cdd:PRK00331  39 DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKPTERNAHPhTDCSGRIAVVHNGIIENYAELKEELLAKGH 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489631888 194 AFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVV 237
Cdd:PRK00331 119 VFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYALAV 162
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 115-237 1.06e-20

glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 273462 [Multi-domain]  Cd Length: 607  Bit Score: 91.93  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHP-FSTGSDQCLVHNGSLSNHNNLRRELIREGI 193
Cdd:TIGR01135  38 EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPTDENAHPhTDEGGRIAVVHNGIIENYAELREELEARGH 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489631888  194 AFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVV 237
Cdd:TIGR01135 118 VFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYALAV 161
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 144-269 3.74e-20

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.


Pssm-ID: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 84.28  E-value: 3.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  144 GIGHTRMATeSAVTTLGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGIAFETQNDTEV-AAAYltaeMAKGKDlgqa 221
Cdd:pfam13522  13 ALGHVRLAI-VDLPDAGNQPMLSRDGRlVLVHNGEIYNYGELREELADLGHAFRSRSDTEVlLALY----EEWGED---- 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489631888  222 ltgALDDLDGFFTFVV--GTKSGFGVVRDPIACKPAVMAETDRYVAFGSE 269
Cdd:pfam13522  84 ---CLERLRGMFAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
 
Name Accession Description Interval E-value
GlxB cd01907
Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine ...
 2-295 6.23e-100

Glutamine amidotransferases class-II (Gn-AT)_GlxB-type. GlxB is a glutamine amidotransferase-like protein of unknown function found in bacteria and archaea. GlxB has a structural fold similar to that of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The GlxB fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238888 [Multi-domain]  Cd Length: 249  Bit Score: 293.41  E-value: 6.23e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888   2 CGIVGLFLKDSrlEPQLGQLLSDMLITMTDRGP-DSAGLAIYGSategkakvtiqsakpeidfadlerdlaeagvparva 80
Cdd:cd01907    1 CGIFGIMSKDG--EPFVGALLVEMLDAMQERGPgDGAGFALYGD------------------------------------ 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  81 vksthavvaiaaarladvravlaairPDVRIMGAGDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLG 160
Cdd:cd01907   43 --------------------------PDAFVYSSGKDMEVFKGVGYPEDIARRYDLEEYKGYHWIAHTRQPTNSAVWWYG 96

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 161 AHPFSTGsDQCLVHNGSLSNHNNLRRELIREGIAFETQNDTEVAAAYLTAEMAKGKD-------------------LGQA 221
Cdd:cd01907   97 AHPFSIG-DIAVVHNGEISNYGSNREYLERFGYKFETETDTEVIAYYLDLLLRKGGLpleyykhiirmpeeerellLALR 175

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489631888 222 LTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMAETDRYVAFGSEYRALVNLPDIESARIWEPEPATVYFW 295
Cdd:cd01907  176 LTYRLADLDGPFTIIVGTPDGFIVIRDRIKLRPAVVAETDDYVAIASEECAIREIPDRDNAKVWEPRPGEYVIW 249
Gn_AT_II cd00352
Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide ...
 2-293 1.12e-41

Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to members of the Ntn (N-terminal nucleophile) hydrolase superfamily and is found at the N-terminus of enzymes such as glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). GLMS catalyzes the formation of glucosamine 6-phosphate from fructose 6-phosphate and glutamine in amino sugar synthesis. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. Asparagine synthetase B synthesizes asparagine from aspartate and glutamine. Beta-LS catalyzes the formation of the beta-lactam ring in the beta-lactamase inhibitor clavulanic acid. GltS synthesizes L-glutamate from 2-oxoglutarate and L-glutamine. These enzymes are generally dimers, but GPATase also exists as a homotetramer.


Pssm-ID: 238212 [Multi-domain]  Cd Length: 220  Bit Score: 143.36  E-value: 1.12e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888   2 CGIVGLFLKDSRLEPQLgQLLSDMLITMTDRGPDSAGLAIYGsategkakvtiqsakpeidfadlerdlaeagvparvav 81
Cdd:cd00352    1 CGIFGIVGADGAASLLL-LLLLRGLAALEHRGPDGAGIAVYD-------------------------------------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  82 ksthavvaiaaarladvravlaairpdvrimgaGDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGA 161
Cdd:cd00352   42 ---------------------------------GDGLFVEKRAGPVSDVALDLLDEPLKSGVALGHVRLATNGLPSEANA 88

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 162 HPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGIAFETQNDTEVAAAYLTAEMAKGkDLGQALTGALDDLDGFFTFVVGTK 240
Cdd:cd00352   89 QPFRSEDGRiALVHNGEIYNYRELREELEARGYRFEGESDSEVILHLLERLGREG-GLFEAVEDALKRLDGPFAFALWDG 167

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489631888 241 SGFGVV--RDPIACKPAVMAET-DRYVAFGSEYRALVNLPDiesARIWEPEPATVY 293
Cdd:cd00352  168 KPDRLFaaRDRFGIRPLYYGITkDGGLVFASEPKALLALPF---KGVRRLPPGELL 220
GFAT cd00714
Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus ...
 114-237 1.49e-24

Glutamine amidotransferases class-II (Gn-AT)_GFAT-type. This domain is found at the N-terminus of glucosamine-6P synthase (GlmS, or GFAT in humans). The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. In humans, GFAT catalyzes the first and rate-limiting step of hexosamine metabolism, the conversion of D-fructose-6P (Fru6P) into D-glucosamine-6P using L-glutamine as a nitrogen source. The end product of this pathway, UDP-N-acetyl glucosamine, is a major building block of the bacterial peptidoglycan and fungal chitin.


Pssm-ID: 238366 [Multi-domain]  Cd Length: 215  Bit Score: 98.29  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 114 AGDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHP-FSTGSDQCLVHNGSLSNHNNLRRELIREG 192
Cdd:cd00714   37 GDGSLEVVKAVGKVANLEEKLAEKPLSGHVGIGHTRWATHGEPTDVNAHPhRSCDGEIAVVHNGIIENYAELKEELEAKG 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489631888 193 IAFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVV 237
Cdd:cd00714  117 YKFESETDTEVIAHLIEYYYDGGLDLLEAVKKALKRLEGAYALAV 161
GlmS COG0449
Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase ...
 115-237 1.55e-23

Glucosamine 6-phosphate synthetase, contains amidotransferase and phosphosugar isomerase domains [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440218 [Multi-domain]  Cd Length: 610  Bit Score: 100.47  E-value: 1.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGI 193
Cdd:COG0449   39 DGGLEVRKAVGKLANLEEKLAEEPLSGTIGIGHTRWATHGAPSDENAHPHTSCSGRiAVVHNGIIENYAELREELEAKGH 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489631888 194 AFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVV 237
Cdd:COG0449  119 TFKSETDTEVIAHLIEEYLKGGGDLLEAVRKALKRLEGAYALAV 162
PRK00331 PRK00331
isomerizing glutamine--fructose-6-phosphate transaminase;
115-237 8.28e-23

isomerizing glutamine--fructose-6-phosphate transaminase;


Pssm-ID: 234729 [Multi-domain]  Cd Length: 604  Bit Score: 98.19  E-value: 8.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHP-FSTGSDQCLVHNGSLSNHNNLRRELIREGI 193
Cdd:PRK00331  39 DGGLEVRKAVGKVANLEAKLEEEPLPGTTGIGHTRWATHGKPTERNAHPhTDCSGRIAVVHNGIIENYAELKEELLAKGH 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 489631888 194 AFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVV 237
Cdd:PRK00331 119 VFKSETDTEVIAHLIEEELKEGGDLLEAVRKALKRLEGAYALAV 162
GPATase_N cd00715
Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the ...
 115-269 2.78e-22

Glutamine amidotransferases class-II (GN-AT)_GPAT- type. This domain is found at the N-terminus of glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase) . The glutaminase domain catalyzes amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. GPATase catalyzes the first step in purine biosynthesis, an amide transfer from glutamine to PRPP, resulting in phosphoribosylamine, pyrophosphate and glutamate. GPATase crystalizes as a homotetramer, but can also exist as a homdimer.


Pssm-ID: 238367 [Multi-domain]  Cd Length: 252  Bit Score: 93.29  E-value: 2.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHPFSTGSDQ---CLVHNGSLSNHNNLRRELIRE 191
Cdd:cd00715   38 GKRFHTHKGMGLVSDVFDEEKLRRLPGNIAIGHVRYSTAGSSSLENAQPFVVNSPLggiALAHNGNLVNAKELREELEEE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 192 GIAFETQNDTEVAAAyLTAEMAKGKDLGQALTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMA--ETDRYVaFGSE 269
Cdd:cd00715  118 GRIFQTTSDSEVILH-LIARSLAKDDLFEAIIDALERVKGAYSLVIMTADGLIAVRDPHGIRPLVLGklEGDGYV-VASE 195
PurF COG0034
Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; ...
 115-269 8.63e-22

Glutamine phosphoribosylpyrophosphate amidotransferase [Nucleotide transport and metabolism]; Glutamine phosphoribosylpyrophosphate amidotransferase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439804 [Multi-domain]  Cd Length: 464  Bit Score: 94.70  E-value: 8.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHPFSTGSDQ---CLVHNGSLSNHNNLRRELIRE 191
Cdd:COG0034   45 GGRFHLHKGMGLVSDVFDEEDLERLKGNIAIGHVRYSTTGSSSLENAQPFYVNSPFgsiALAHNGNLTNAEELREELEEE 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631888 192 GIAFETQNDTEVAAAYLTAEMaKGKDLGQALTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMAETDRYVAFGSE 269
Cdd:COG0034  125 GAIFQTTSDTEVILHLIAREL-TKEDLEEAIKEALRRVKGAYSLVILTGDGLIAARDPNGIRPLVLGKLEDGYVVASE 201
glmS TIGR01135
glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from ...
 115-237 1.06e-20

glucosamine--fructose-6-phosphate aminotransferase (isomerizing); The member from Methanococcus jannaschii contains an intein. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 273462 [Multi-domain]  Cd Length: 607  Bit Score: 91.93  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHP-FSTGSDQCLVHNGSLSNHNNLRRELIREGI 193
Cdd:TIGR01135  38 EGKLFVRKAVGKVAELANKLGEKPLPGGVGIGHTRWATHGKPTDENAHPhTDEGGRIAVVHNGIIENYAELREELEARGH 117

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 489631888  194 AFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVV 237
Cdd:TIGR01135 118 VFSSDTDTEVIAHLIEEELREGGDLLEAVQKALKQLRGAYALAV 161
GATase_6 pfam13522
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 144-269 3.74e-20

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes, such as asparagine synthetase and glutamine--fructose-6-phosphate transaminase.


Pssm-ID: 433279 [Multi-domain]  Cd Length: 130  Bit Score: 84.28  E-value: 3.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  144 GIGHTRMATeSAVTTLGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGIAFETQNDTEV-AAAYltaeMAKGKDlgqa 221
Cdd:pfam13522  13 ALGHVRLAI-VDLPDAGNQPMLSRDGRlVLVHNGEIYNYGELREELADLGHAFRSRSDTEVlLALY----EEWGED---- 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 489631888  222 ltgALDDLDGFFTFVV--GTKSGFGVVRDPIACKPAVMAETDRYVAFGSE 269
Cdd:pfam13522  84 ---CLERLRGMFAFAIwdRRRRTLFLARDRLGIKPLYYGILGGGFVFASE 130
purF TIGR01134
amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) ...
 115-273 3.76e-19

amidophosphoribosyltransferase; Alternate name: glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273461 [Multi-domain]  Cd Length: 442  Bit Score: 86.99  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHPFSTGS---DQCLVHNGSLSNHNNLRRELIRE 191
Cdd:TIGR01134  39 GNRFRLHKGNGLVSDVFNEEHLQRLKGNVGIGHVRYSTAGSSGLENAQPFVVNSpygGLALAHNGNLVNADELRRELEEE 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  192 GIAFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMAETDRYVAFGSEYR 271
Cdd:TIGR01134 119 GRHFNTTSDSEVLLHLLAHNDESKDDLFDAVARVLERVRGAYALVLMTEDGLVAVRDPHGIRPLVLGRRGDGYVVASESC 198


                  ..
gi 489631888  272 AL 273
Cdd:TIGR01134 199 AL 200
PRK05793 PRK05793
amidophosphoribosyltransferase; Provisional
 115-273 2.41e-17

amidophosphoribosyltransferase; Provisional


Pssm-ID: 235611 [Multi-domain]  Cd Length: 469  Bit Score: 82.00  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHP----FSTGSdQCLVHNGSLSNHNNLRRELIR 190
Cdd:PRK05793  54 GEKIKVHKGMGLVSEVFSKEKLKGLKGNSAIGHVRYSTTGASDLDNAQPlvanYKLGS-IAIAHNGNLVNADVIRELLED 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 191 EGIAFETQNDTEVaAAYLTAEMAKgKDLGQALTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMAET-DRYVaFGSE 269
Cdd:PRK05793 133 GGRIFQTSIDSEV-ILNLIARSAK-KGLEKALVDAIQAIKGSYALVILTEDKLIGVRDPHGIRPLCLGKLgDDYI-LSSE 209


                 ....
gi 489631888 270 YRAL 273
Cdd:PRK05793 210 SCAL 213
AsnB cd00712
Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine ...
 144-294 4.02e-17

Glutamine amidotransferases class-II (GATase) asparagine synthase_B type. Asparagine synthetase B catalyses the ATP-dependent conversion of aspartate to asparagine. This enzyme is a homodimer, with each monomer composed of a glutaminase domain and a synthetase domain. The N-terminal glutaminase domain hydrolyzes glutamine to glutamic acid and ammonia.


Pssm-ID: 238364 [Multi-domain]  Cd Length: 220  Bit Score: 78.37  E-value: 4.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 144 GIGHTRMAT--ESAvttlGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGIAFETQNDTEVA-AAYLtaemAKGKDlg 219
Cdd:cd00712   43 ALGHRRLSIidLSG----GAQPMVSEDGRlVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVIlHLYE----EWGED-- 112

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489631888 220 qaltgALDDLDGFFTFVV---GTKSGFgVVRDPIACKPAVMAETDRYVAFGSEYRALVNLPDIEsaRIWEPEPATVYF 294
Cdd:cd00712  113 -----CLERLNGMFAFALwdkRKRRLF-LARDRFGIKPLYYGRDGGGLAFASELKALLALPGVP--RELDEAALAEYL 182
GATase_7 pfam13537
Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain ...
 147-275 4.08e-17

Glutamine amidotransferase domain; This domain is a class-II glutamine amidotransferase domain found in a variety of enzymes such as asparagine synthetase and glutamine-fructose-6-phosphate transaminase.


Pssm-ID: 433289 [Multi-domain]  Cd Length: 123  Bit Score: 75.63  E-value: 4.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  147 HTRMATEsaVTTLGAHPFSTGSDQ--CLVHNGSLSNHNNLRRELIREGIAFETQNDTEVAAAYLTAEmaKGKDlgqaltg 224
Cdd:pfam13537   1 HRRLSII--DLEGGAQPMVSSEDGryVIVFNGEIYNYRELRAELEAKGYRFRTHSDTEVILHLYEAE--WGED------- 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489631888  225 ALDDLDGFFTFVVGTKSG--FGVVRDPIACKPAVMAETD-RYVAFGSEYRALVN 275
Cdd:pfam13537  70 CVDRLNGMFAFAIWDRRRqrLFLARDRFGIKPLYYGRDDgGRLLFASELKALLA 123
asn_synth_AEB TIGR01536
asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing ...
 144-296 4.26e-17

asparagine synthase (glutamine-hydrolyzing); This model describes the glutamine-hydrolysing asparagine synthase. A poorly conserved C-terminal extension was removed from the model. Bacterial members of the family tend to have a long, poorly conserved insert lacking from archaeal and eukaryotic sequences. Multiple isozymes have been demonstrated, such as in Bacillus subtilis. Long-branch members of the phylogenetic tree (which typically were also second or third candidate members from their genomes) were removed from the seed alignment and score below trusted cutoff. [Amino acid biosynthesis, Aspartate family]


Pssm-ID: 273676 [Multi-domain]  Cd Length: 466  Bit Score: 81.23  E-value: 4.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  144 GIGHTRMAteSAVTTLGAHPFS-TGSDQCLVHNGSLSNHNNLRRELIREGIAFETQNDTEVA-AAYLTaemaKGKDlgqa 221
Cdd:TIGR01536  43 ILGHRRLA--IIDLSGGAQPMSnEGKTYVIVFNGEIYNHEELREELEAKGYTFQTDSDTEVIlHLYEE----WGEE---- 112

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489631888  222 ltgALDDLDGFFTFVV--GTKSGFGVVRDPIACKPAVMAETDRYVAFGSEYRALVNLPDIesariwEPEPATVYFWD 296
Cdd:TIGR01536 113 ---CVDRLDGMFAFALwdSEKGELFLARDRFGIKPLYYAYDGGQLYFASEIKALLAHPNI------KPFPDGAALAP 180
AsnB COG0367
Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; ...
 141-293 3.11e-16

Asparagine synthetase B (glutamine-hydrolyzing) [Amino acid transport and metabolism]; Asparagine synthetase B (glutamine-hydrolyzing) is part of the Pathway/BioSystem: Asparagine biosynthesis


Pssm-ID: 440136 [Multi-domain]  Cd Length: 558  Bit Score: 78.73  E-value: 3.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 141 GSHGIGHTRMAT--ESAvttLGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGIAFETQNDTEVA-AAYLtaemAKGK 216
Cdd:COG0367   40 GGVALGHRRLSIidLSE---GGHQPMVSEDGRyVLVFNGEIYNYRELRAELEALGHRFRTHSDTEVIlHAYE----EWGE 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 217 DlgqaltgALDDLDGFFTFVV---GTKSGFGvVRDPIACKPAVMAETDRYVAFGSEYRALVNLPDIESARIWE------- 286
Cdd:COG0367  113 D-------CLERLNGMFAFAIwdrRERRLFL-ARDRFGIKPLYYAEDGGGLAFASELKALLAHPGVDRELDPEalaeylt 184

                        170
                 ....*....|.
gi 489631888 287 ----PEPATVY 293
Cdd:COG0367  185 lgyvPAPRTIF 195
PTZ00295 PTZ00295
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 115-240 1.38e-14

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 240349 [Multi-domain]  Cd Length: 640  Bit Score: 73.90  E-value: 1.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLpkdvvarfdvRSMGGSH-GIGHTRMATESAVTTLGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREG 192
Cdd:PTZ00295  78 SDSIEILKEKLL----------DSHKNSTiGIAHTRWATHGGKTDENAHPHCDYKKRiALVHNGTIENYVELKSELIAKG 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 489631888 193 IAFETQNDTEVAAAYLTAEMAKGKDLGQALTGALDDLDGFFTFVVGTK 240
Cdd:PTZ00295 148 IKFRSETDSEVIANLIGLELDQGEDFQEAVKSAISRLQGTWGLCIIHK 195
PLN02440 PLN02440
amidophosphoribosyltransferase
 115-296 9.69e-14

amidophosphoribosyltransferase


Pssm-ID: 215241 [Multi-domain]  Cd Length: 479  Bit Score: 71.25  E-value: 9.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 115 GDSVEIYKEVGLPKDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHPFSTGSDQ---CLVHNGSLSNHNNLRRELIRE 191
Cdd:PLN02440  39 GNRLQSITGNGLVSDVFDESKLDQLPGDIAIGHVRYSTAGASSLKNVQPFVANYRFgsiGVAHNGNLVNYEELRAKLEEN 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 192 GIAFETQNDTEVaAAYLTAEmAKGKDLGQALTGALDDLDGFFTFVVGTKSGFGVVRDPIACKPAVMA--ETDRYVaFGSE 269
Cdd:PLN02440 119 GSIFNTSSDTEV-LLHLIAI-SKARPFFSRIVDACEKLKGAYSMVFLTEDKLVAVRDPHGFRPLVMGrrSNGAVV-FASE 195

                        170       180
                 ....*....|....*....|....*..
gi 489631888 270 YRAlvnLPDIESARIWEPEPATVYFWD 296
Cdd:PLN02440 196 TCA---LDLIGATYEREVNPGEVIVVD 219
asnB PRK09431
asparagine synthetase B; Provisional
 146-274 2.37e-11

asparagine synthetase B; Provisional


Pssm-ID: 236513 [Multi-domain]  Cd Length: 554  Bit Score: 64.16  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 146 GHTRMATESaVTTLGAHPFSTGSDQCLVHNGSLSNHNNLRRELIrEGIAFETQNDTEVAAA-YLTaemaKGKDLgqaltg 224
Cdd:PRK09431  47 GHERLSIVD-VNGGAQPLYNEDGTHVLAVNGEIYNHQELRAELG-DKYAFQTGSDCEVILAlYQE----KGPDF------ 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 489631888 225 aLDDLDGFFTFVV--GTKSGFGVVRDPIACKPAVMAETDR-YVAFGSEYRALV 274
Cdd:PRK09431 115 -LDDLDGMFAFALydSEKDAYLIARDPIGIIPLYYGYDEHgNLYFASEMKALV 166
PLN02981 PLN02981
glucosamine:fructose-6-phosphate aminotransferase
 144-203 7.39e-11

glucosamine:fructose-6-phosphate aminotransferase


Pssm-ID: 215531 [Multi-domain]  Cd Length: 680  Bit Score: 62.85  E-value: 7.39e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489631888 144 GIGHTRMATESAVTTLGAHPFST--GSDQCLVHNGSLSNHNNLRRELIREGIAFETQNDTEV 203
Cdd:PLN02981  89 GIAHTRWATHGPPAPRNSHPQSSgpGNEFLVVHNGIITNYEVLKETLLRHGFTFESDTDTEV 150
PTZ00077 PTZ00077
asparagine synthetase-like protein; Provisional
 143-273 1.84e-09

asparagine synthetase-like protein; Provisional


Pssm-ID: 185431 [Multi-domain]  Cd Length: 586  Bit Score: 58.19  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 143 HGIGHTRMATESAVTtlGAHPFSTGSDQ-CLVHNGSLSNHNNLRRELIREGIAFETQNDTEVAAAYLtaEMAKGKDLgqa 221
Cdd:PTZ00077  49 NILAHERLAIVDLSD--GKQPLLDDDETvALMQNGEIYNHWEIRPELEKEGYKFSSNSDCEIIGHLY--KEYGPKDF--- 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489631888 222 ltgaLDDLDGFFTFVV--GTKSGFGVVRDPIACKPAVMA-ETDRYVAFGSEYRAL 273
Cdd:PTZ00077 122 ----WNHLDGMFATVIydMKTNTFFAARDHIGIIPLYIGyAKDGSIWFSSELKAL 172
YafJ COG0121
Predicted glutamine amidotransferase YafJ [General function prediction only];
113-237 9.17e-09

Predicted glutamine amidotransferase YafJ [General function prediction only];


Pssm-ID: 439891 [Multi-domain]  Cd Length: 248  Bit Score: 54.97  E-value: 9.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 113 GAGDSVEIYKEVgLP--KDVVARFDVRSMGGSHGIGHTRMATESAVTTLGAHPFsTGSDQCLVHNGSLSNHNNLRRELIR 190
Cdd:COG0121   47 EGDGEPRLYRDP-LPawSDPNLRLLARPIKSRLVIAHVRKATVGPVSLENTHPF-RGGRWLFAHNGQLDGFDRLRRRLAE 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489631888 191 EGIAF-----ETQNDTEVAAAYLTAEMAK-GKDLGQALTGALDDLD------GFFTFVV 237
Cdd:COG0121  125 ELPDElyfqpVGTTDSELAFALLLSRLRDgGPDPAEALAEALRELAelarapGRLNLLL 183
PLN02549 PLN02549
asparagine synthase (glutamine-hydrolyzing)
 166-287 4.41e-07

asparagine synthase (glutamine-hydrolyzing)


Pssm-ID: 178164 [Multi-domain]  Cd Length: 578  Bit Score: 50.92  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 166 TGSDQCLVH---------NGSLSNHNNLRRELirEGIAFETQNDTEVAAaYLTAEMakGKDLgqaltgaLDDLDGFFTFV 236
Cdd:PLN02549  57 ESGDQPLYNedktivvtaNGEIYNHKELREKL--KLHKFRTGSDCEVIA-HLYEEH--GEEF-------VDMLDGMFSFV 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489631888 237 -VGTKSG-FGVVRDPIACKPAVMA-ETDRYVAFGSEYRALVNlpDIESARIWEP 287
Cdd:PLN02549 125 lLDTRDNsFIAARDHIGITPLYIGwGLDGSVWFASEMKALCD--DCERFEEFPP 176
YafJ cd01908
Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine ...
 145-225 4.43e-07

Glutamine amidotransferases class-II (Gn-AT)_YafJ-type. YafJ is a glutamine amidotransferase-like protein of unknown function found in prokaryotes, eukaryotes and archaea. YafJ has a conserved structural fold similar to those of other class II glutamine amidotransferases including glucosamine-fructose 6-phosphate synthase (GLMS or GFAT), glutamine phosphoribosylpyrophosphate (Prpp) amidotransferase (GPATase), asparagine synthetase B (AsnB), beta lactam synthetase (beta-LS) and glutamate synthase (GltS). The YafJ fold is also somewhat similar to the Ntn (N-terminal nucleophile) hydrolase fold of the proteasomal alpha and beta subunits.


Pssm-ID: 238889 [Multi-domain]  Cd Length: 257  Bit Score: 50.08  E-value: 4.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888 145 IGHTRMATESAVTTLGAHPFSTGSdQCLVHNGSLSNHNNLRRELIREGIAF---ETqnDTEVAAAYLTAEMAKGKDLGQA 221
Cdd:cd01908   84 LAHVRAATVGPVSLENCHPFTRGR-WLFAHNGQLDGFRLLRRRLLRLLPRLpvgTT--DSELAFALLLSRLLERDPLDPA 160


                 ....
gi 489631888 222 LTGA 225
Cdd:cd01908  161 ELLD 164
PTZ00394 PTZ00394
glucosamine-fructose-6-phosphate aminotransferase; Provisional
 1-205 6.15e-07

glucosamine-fructose-6-phosphate aminotransferase; Provisional


Pssm-ID: 173585 [Multi-domain]  Cd Length: 670  Bit Score: 50.65  E-value: 6.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888   1 MCGIVGLFLKD-SRLEPQLGQLLSDMLITMTDRGPDSAGLAI---YGSATEGKAKVTIQSAKPeidfadlerdlaeagvp 76
Cdd:PTZ00394   1 MCGIFGYANHNvPRTVEQILNVLLDGIQKVEYRGYDSAGLAIdanIGSEKEDGTAASAPTPRP----------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489631888  77 arVAVKSthaVVAIAAARLADVRAVLAAIRPDvriMGAGDSVEIykevglpkdvvarfdvrsmggshGIGHTRMATESAV 156
Cdd:PTZ00394  64 --CVVRS---VGNISQLREKVFSEAVAATLPP---MDATTSHHV-----------------------GIAHTRWATHGGV 112

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 489631888 157 TTLGAHP-FSTGSDQCLVHNGSLSNHNNLRRELIREGIAFETQNDTEVAA 205
Cdd:PTZ00394 113 CERNCHPqQSNNGEFTIVHNGIVTNYMTLKELLKEEGYHFSSDTDTEVIS 162
 
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