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Conserved domains on  [gi|60416282|sp|P0A0K0|]
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RecName: Full=Uncharacterized protein SAV1875

Protein Classification

type 1 glutamine amidotransferase domain-containing protein( domain architecture ID 10123305)

type 1 glutamine amidotransferase domain-containing protein similar to Pyrococcus furiosus deglycase PfpI that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals (Probable)

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 4-169 1.11e-77

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


:

Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 228.58  E-value: 1.11e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   4 KVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTANSEVVGKHGE-KVTVDVGIAEAKPEDYDALLIPGGFSPDHLRGD 82
Cdd:cd03134   1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYdTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  83 TEGRygTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDNNIVTSRVPDDLDDF 162
Cdd:cd03134  81 PDAV--AFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGNLITSRNPDDLPAF 158


                ....*..
gi 60416282 163 NREIVKQ 169
Cdd:cd03134 159 NRAILKA 165
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 4-169 1.11e-77

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 228.58  E-value: 1.11e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   4 KVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTANSEVVGKHGE-KVTVDVGIAEAKPEDYDALLIPGGFSPDHLRGD 82
Cdd:cd03134   1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYdTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  83 TEGRygTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDNNIVTSRVPDDLDDF 162
Cdd:cd03134  81 PDAV--AFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGNLITSRNPDDLPAF 158


                ....*..
gi 60416282 163 NREIVKQ 169
Cdd:cd03134 159 NRAILKA 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-171 1.00e-68

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 206.11  E-value: 1.00e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   1 MTKKVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTANSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGF-SPDHL 79
Cdd:COG0693   1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHgAPDDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  80 RGDTegRYGTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDNNIVTSRVPDDL 159
Cdd:COG0693  81 REDP--DVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGNLITSRGPGDA 158

                       170
                ....*....|..
gi 60416282 160 DDFNREIVKQLQ 171
Cdd:COG0693 159 PAFARALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 3-169 2.17e-64

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 194.78  E-value: 2.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282     3 KKVAIILANEFEDIEYSSPKEALENAGFNTVVIGdTANSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGFS-PDHLRG 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVS-VDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAgPERLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282    82 DTegRYGTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDNNIVTSRVPDDLDD 161
Cdd:pfam01965  80 NE--KLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPE 157


                  ....*...
gi 60416282   162 FNREIVKQ 169
Cdd:pfam01965 158 FALEILEQ 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 4-171 1.34e-51

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 162.59  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282     4 KVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTAnSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGFSPDHLRGDT 83
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEA-GTTVGKHGYSVTVDATIDEVNPEEYDALVIPGGRAPEYLRLNN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282    84 EGRygTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVD-ESVVVDNNIVTSRVPDDLDDF 162
Cdd:TIGR01382  80 KAV--RLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDiEVVVVDGNLVTSRVPDDLPAF 157


                  ....*....
gi 60416282   163 NREIVKQLQ 171
Cdd:TIGR01382 158 NREFLKLLG 166
pyrG PRK05380
CTP synthetase; Validated
 18-110 7.06e-06

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 45.01  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   18 YSSPKEALENAGFNTvvigdtaNSEVVGK--HGEKVTVDVgiAEAKPEDYDALLIPGGFSpdhLRGdTEGRYGTfAKYFT 95
Cdd:PRK05380 304 YKSVIEALKHAGIAN-------DVKVNIKwiDSEDLEEEN--VAELLKGVDGILVPGGFG---ERG-IEGKILA-IRYAR 369

                         90
                 ....*....|....*
gi 60416282   96 KNDVPTFAICHGPQI 110
Cdd:PRK05380 370 ENNIPFLGICLGMQL 384
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 4-169 1.11e-77

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 228.58  E-value: 1.11e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   4 KVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTANSEVVGKHGE-KVTVDVGIAEAKPEDYDALLIPGGFSPDHLRGD 82
Cdd:cd03134   1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYdTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  83 TEGRygTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDNNIVTSRVPDDLDDF 162
Cdd:cd03134  81 PDAV--AFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGNLITSRNPDDLPAF 158


                ....*..
gi 60416282 163 NREIVKQ 169
Cdd:cd03134 159 NRAILKA 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-171 1.00e-68

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 206.11  E-value: 1.00e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   1 MTKKVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTANSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGF-SPDHL 79
Cdd:COG0693   1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHgAPDDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  80 RGDTegRYGTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDNNIVTSRVPDDL 159
Cdd:COG0693  81 REDP--DVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGNLITSRGPGDA 158

                       170
                ....*....|..
gi 60416282 160 DDFNREIVKQLQ 171
Cdd:COG0693 159 PAFARALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 3-169 2.17e-64

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 194.78  E-value: 2.17e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282     3 KKVAIILANEFEDIEYSSPKEALENAGFNTVVIGdTANSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGFS-PDHLRG 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVS-VDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAgPERLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282    82 DTegRYGTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDNNIVTSRVPDDLDD 161
Cdd:pfam01965  80 NE--KLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPE 157


                  ....*...
gi 60416282   162 FNREIVKQ 169
Cdd:pfam01965 158 FALEILEQ 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 4-171 1.34e-51

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 162.59  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282     4 KVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTAnSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGFSPDHLRGDT 83
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEA-GTTVGKHGYSVTVDATIDEVNPEEYDALVIPGGRAPEYLRLNN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282    84 EGRygTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVD-ESVVVDNNIVTSRVPDDLDDF 162
Cdd:TIGR01382  80 KAV--RLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDiEVVVVDGNLVTSRVPDDLPAF 157


                  ....*....
gi 60416282   163 NREIVKQLQ 171
Cdd:TIGR01382 158 NREFLKLLG 166
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 4-170 1.04e-33

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 117.36  E-value: 1.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   4 KVAIILANEFEDIEYSSPKEALENAGFNTVVI------GDTANSEVVGKHG-----EK----VTVDVGIAEAKPEDYDAL 68
Cdd:cd03169   1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVapgkkkGDTVVTAIHDFPGwqtytEKpghrFAVTADFDEVDPDDYDAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  69 LIPGGFSPDHLRgdTEGRYGTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHVVDESVVVDN 148
Cdd:cd03169  81 VIPGGRAPEYLR--LDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDDGVVVDG 158

                       170       180
                ....*....|....*....|..
gi 60416282 149 NIVTSRVPDDLDDFNREIVKQL 170
Cdd:cd03169 159 NLVTAQAWPDHPAFLREFLKLL 180
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 5-170 1.06e-33

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 116.88  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   5 VAIILANEFEDIEYSSPKEALENAGFNTVVIGDTANSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGFS-PDHLRGDT 83
Cdd:cd03135   1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPgAQNLADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  84 EGRygTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSnaGAHVVDESVVVDNNIVTSRVPDDLDDFN 163
Cdd:cd03135  81 KLI--KLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLG--GANYVDEPVVVDGNIITSRGPGTAFEFA 156


                ....*..
gi 60416282 164 REIVKQL 170
Cdd:cd03135 157 LKIVEAL 163
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-112 1.67e-16

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: 71.09  E-value: 1.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   5 VAIILANEFEDIEYSSPKEALENAGFNTVVIGDTAnsevvgkhgekvtvDVGIAEAKPEDYDALLIPGGFSPDHLRGDTE 84
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPDG--------------GPVESDVDLDDYDGLILPGGPGTPDDLARDE 66

                        90       100
                ....*....|....*....|....*...
gi 60416282  85 gRYGTFAKYFTKNDVPTFAICHGPQILI 112
Cdd:cd01653  67 -ALLALLREAAAAGKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-111 1.46e-14

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: 65.30  E-value: 1.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   5 VAIILANEFEDIEYSSPKEALENAGFNTVVIGDTAnsevvgkhgekvtvDVGIAEAKPEDYDALLIPGGFSPDHLRGDTE 84
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPDG--------------GPVESDVDLDDYDGLILPGGPGTPDDLAWDE 66

                        90       100
                ....*....|....*....|....*..
gi 60416282  85 GRYGTFAKYFtKNDVPTFAICHGPQIL 111
Cdd:cd03128  67 ALLALLREAA-AAGKPVLGICLGAQLL 92
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 5-152 1.50e-09

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 54.15  E-value: 1.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   5 VAIILANEFEDIEYSSPKEALENAGFNTVVIGDTANSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGGFSPDHlrGDTE 84
Cdd:cd03140   1 IAVFLTDEFADWEGAYLAALLNSYEGFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDN--PEAP 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60416282  85 GRYGtFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLT----AVLNVRKDLSNAGAHVVDESVVVDNNIVT 152
Cdd:cd03140  79 DLAG-LVRQALKQGKPVAAICGATLALARAGLLNNRKHTsnslDFLKAHAPYYGGAEYYDEPQAVSDGNLIT 149
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 57-152 3.85e-08

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.


Pssm-ID: 153235 [Multi-domain]  Cd Length: 221  Bit Score: 50.63  E-value: 3.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  57 IAEAKPEDYDALLIPGGFSP--DhLRGDTEgrYGTFAKYFTKNDVPTFAICHGPQILIDTDD------LKGRTLTA---- 124
Cdd:cd03141  83 LSDVDPSDYDAIFIPGGHGPmfD-LPDNPD--LQDLLREFYENGKVVAAVCHGPAALLNVKLsdgkslVAGKTVTGftne 159

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 60416282 125 ---VLNVRKD--------LSNAGAHVV-----DESVVVDNNIVT 152
Cdd:cd03141 160 eeeAAGLKKVvpflledeLKELGANYVkaepwAEFVVVDGRLIT 203
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 5-153 3.87e-07

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 47.54  E-value: 3.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   5 VAIILANEFEDIEYSSPKEALENAGFNTvvigdtANSEV--VGKHGEKVTVDVGI------AEAKPEDYDALLIPGGFSP 76
Cdd:cd03139   1 VGILLFPGVEVLDVIGPYEVFGRAPRLA------APFEVflVSETGGPVSSRSGLtvlpdtSFADPPDLDVLLVPGGGGT 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60416282  77 DHLRGDteGRYGTFAKYFTKNDVPTFAICHGPQILIDTDDLKGRTLTAVLNVRKDLSNAGAHV-VDESVVVDNNIVTS 153
Cdd:cd03139  75 RALVND--PALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVvVDARWVVDGNIWTS 150
GATase1_catalase cd03132
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ...
 2-73 1.43e-06

Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases; Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment.


Pssm-ID: 153226  Cd Length: 142  Bit Score: 45.33  E-value: 1.43e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60416282   2 TKKVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTAnSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGG 73
Cdd:cd03132   1 GRKVGILVADGVDAAELSALKAALKAAGANVKVVAPTL-GGVVDSDGKTLEVDQTYAGAPSVLFDAVVVPGG 71
pyrG PRK05380
CTP synthetase; Validated
 18-110 7.06e-06

CTP synthetase; Validated


Pssm-ID: 235437 [Multi-domain]  Cd Length: 533  Bit Score: 45.01  E-value: 7.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   18 YSSPKEALENAGFNTvvigdtaNSEVVGK--HGEKVTVDVgiAEAKPEDYDALLIPGGFSpdhLRGdTEGRYGTfAKYFT 95
Cdd:PRK05380 304 YKSVIEALKHAGIAN-------DVKVNIKwiDSEDLEEEN--VAELLKGVDGILVPGGFG---ERG-IEGKILA-IRYAR 369

                         90
                 ....*....|....*
gi 60416282   96 KNDVPTFAICHGPQI 110
Cdd:PRK05380 370 ENNIPFLGICLGMQL 384
PyrG COG0504
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ...
 18-110 2.27e-05

CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 440270 [Multi-domain]  Cd Length: 535  Bit Score: 43.46  E-value: 2.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  18 YSSPKEALENAGFNT---VVIgDTANSEVVGKHGekvtvdvgiAEAKPEDYDALLIPGGFSPdhlRGdTEGRYGTfAKYF 94
Cdd:COG0504 305 YKSVVEALKHAGIANgvkVNI-KWIDSEDLEEEN---------AEELLKGVDGILVPGGFGE---RG-IEGKIAA-IRYA 369

                        90
                ....*....|....*.
gi 60416282  95 TKNDVPTFAICHGPQI 110
Cdd:COG0504 370 RENKIPFLGICLGMQL 385
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 24-155 3.47e-05

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 42.60  E-value: 3.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  24 ALENAGFNT--VVIGDTANsevvgkhgekvtvdvgiAEAKPEDYDALLIPGGFS-PDHLRGdteG-------RYGTFAKY 93
Cdd:cd01740  18 AFELAGFEAedVWHNDLLA-----------------GRKDLDDYDGVVLPGGFSyGDYLRA---GaiaaaspLLMEEVKE 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 60416282  94 FTKNDVPTFAICHGPQILIDTDDLKGRtLTAVLNVRKDLSNAGAHVVDEsVVVDNNIVTSRV 155
Cdd:cd01740  78 FAERGGLVLGICNGFQILVELGLLPGA-LIRNKGLKFICRWQNRFVTLR-VENNDSPFTKGY 137
GATase1_CTP_Synthase cd01746
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ...
 12-112 5.25e-05

Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site.


Pssm-ID: 153217 [Multi-domain]  Cd Length: 235  Bit Score: 42.16  E-value: 5.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  12 EFEDiEYSSPKEALENAGFntvvigdtansevvgKHGEKVTVD----VGIAEAKP----EDYDALLIPGGFSpdhLRGdT 83
Cdd:cd01746  11 ELPD-AYLSVLEALKHAGI---------------ALGVKLEIKwidsEDLEEENAeealKGADGILVPGGFG---IRG-V 70

                        90       100
                ....*....|....*....|....*....
gi 60416282  84 EGRYGTfAKYFTKNDVPTFAICHGPQILI 112
Cdd:cd01746  71 EGKILA-IKYARENNIPFLGICLGMQLAV 98
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 63-113 2.48e-04

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 40.13  E-value: 2.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 60416282   63 EDYDALLIPGGFSP-DHLRGDT--EGRYGTFA----KYFTKNDVPTFAICHGPQILID 113
Cdd:PRK01175  47 SDYDCLVIPGGFSAgDYIRAGAifAARLKAVLrkdiEEFIDEGYPIIGICNGFQVLVE 104
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 24-112 3.09e-04

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


Pssm-ID: 439817 [Multi-domain]  Cd Length: 236  Bit Score: 39.66  E-value: 3.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282  24 ALENAGFNTVVIgdtansevvgKHGEKVTvdvgiaeaKPEDYDALLIPGGFS-PDHLRGdteGryGTFAK--------YF 94
Cdd:COG0047  20 AFERAGAEAEDV----------WHSDLRT--------DLDDFDGLVLPGGFSyGDYLRA---G--AIAAFspimdavrEF 76

                        90
                ....*....|....*...
gi 60416282  95 TKNDVPTFAICHGPQILI 112
Cdd:COG0047  77 ARRGGLVLGICNGFQILT 94
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
58-149 7.80e-04

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 38.56  E-value: 7.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282   58 AEAKPEDYDALLIPGGFS-PDHLRGdtegryGTFAKY---------FTKNDVPTFAICHGPQILIDTDDLKGrTLTAvln 127
Cdd:PRK03619  35 KETDLDGVDAVVLPGGFSyGDYLRC------GAIAAFspimkavkeFAEKGKPVLGICNGFQILTEAGLLPG-ALTR--- 104

                         90       100
                 ....*....|....*....|....*
gi 60416282  128 vrkdlsNAGAHVVDESV---VVDNN 149
Cdd:PRK03619 105 ------NASLKFICRDVhlrVENND 123
PRK11574 PRK11574
protein deglycase YajL;
1-73 1.22e-03

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 37.84  E-value: 1.22e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60416282    1 MTKKVAIILANEFEDIEYSSPKEALENAGFN--TVVIGDTANSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGG 73
Cdd:PRK11574   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKvtTASVASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGG 75
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
57-74 1.62e-03

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 37.46  E-value: 1.62e-03
                         10
                 ....*....|....*...
gi 60416282   57 IAEAKPEDYDALLIPGGF 74
Cdd:PRK11780  78 LAEADAEDFDALIVPGGF 95
GATase pfam00117
Glutamine amidotransferase class-I;
48-113 2.31e-03

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 36.83  E-value: 2.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282    48 GEKVTV---DVGIAEAKPEDYDALLIPGGF-SPDHLRGDTEgrygtFAKYFTKNDVPTFAICHGPQILID 113
Cdd:pfam00117  21 GVEVTVvpnDTPAEEILEENPDGIILSGGPgSPGAAGGAIE-----AIREARELKIPILGICLGHQLLAL 85
katE PRK11249
hydroperoxidase II; Provisional
 2-87 2.77e-03

hydroperoxidase II; Provisional


Pssm-ID: 236886 [Multi-domain]  Cd Length: 752  Bit Score: 37.33  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60416282    2 TKKVAIILANEFEDIEYSSPKEALENAGFNTVVIGDTAnSEVVGKHGEKVTVDVGIAEAKPEDYDALLIPGG-FSPDHLR 80
Cdd:PRK11249 597 GRKVAILLNDGVDAADLLAILKALKAKGVHAKLLYPRM-GEVTADDGTVLPIAATFAGAPSLTFDAVIVPGGkANIADLA 675


                 ....*..
gi 60416282   81 GDTEGRY 87
Cdd:PRK11249 676 DNGDARY 682
 
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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