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Conserved domains on  [gi|1034627634|ref|XP_016883968|]
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glutamine amidotransferase-like class 1 domain-containing protein 3, mitochondrial isoform X1 [Homo sapiens]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

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
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 1-180 1.56e-93

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.


The actual alignment was detected with superfamily member cd03133:

Pssm-ID: 469582  Cd Length: 213  Bit Score: 271.03  E-value: 1.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634   1 MHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEF 80
Cdd:cd03133    43 MHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLKAADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  81 HQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCE 159
Cdd:cd03133   122 HQAGKPIGAICIAPALAAKILgEGVEVTIGND---------AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLA 192

                         170       180
                  ....*....|....*....|.
gi 1034627634 160 TALHYIHDGIGAMVRKVLELT 180
Cdd:cd03133   193 DSIHEIADGIEKLVAKVLKLA 213
 
Name Accession Description Interval E-value
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 1-180 1.56e-93

Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1. This group includes, proteins similar to ES1, Escherichia coli enhancing lycopene biosynthesis protein 2, Azospirillum brasilense iaaC and, human HES1. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Zebrafish ES1 is expressed specifically in adult photoreceptor cells and appears to be a cytoplasmic protein. A. brasilense iaaC is involved in controlling IAA biosynthesis.


Pssm-ID: 153227  Cd Length: 213  Bit Score: 271.03  E-value: 1.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634   1 MHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEF 80
Cdd:cd03133    43 MHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLKAADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  81 HQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCE 159
Cdd:cd03133   122 HQAGKPIGAICIAPALAAKILgEGVEVTIGND---------AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLA 192

                         170       180
                  ....*....|....*....|.
gi 1034627634 160 TALHYIHDGIGAMVRKVLELT 180
Cdd:cd03133   193 DSIHEIADGIEKLVAKVLKLA 213
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
1-180 2.30e-85

Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];


Pssm-ID: 442389  Cd Length: 215  Bit Score: 250.08  E-value: 2.30e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634   1 MHVIDHTKGQPsEGESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEF 80
Cdd:COG3155    45 HHVINHLTGEE-MGEKRNVLVESARIARGNIKPLAELNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAF 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  81 HQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCE 159
Cdd:COG3155   124 HEAGKPIGAICIAPALLAKLLgAGVKLTIGND---------ADTAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLA 194

                         170       180
                  ....*....|....*....|.
gi 1034627634 160 TALHYIHDGIGAMVRKVLELT 180
Cdd:COG3155   195 ASISEAAEGIEKLVKKVLELA 215
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
1-181 2.16e-82

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 242.77  E-value: 2.16e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634   1 MHVIDHTKGQPSEgESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEF 80
Cdd:PRK11780   46 LHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAEADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  81 HQAGKPIGLCCIAPVLAAKVLR-GVEVTVGHEqeeggkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCE 159
Cdd:PRK11780  125 HQAGKPIGFICIAPAMLPKILGaGVKLTIGND---------EDTAAAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLA 195

                         170       180
                  ....*....|....*....|..
gi 1034627634 160 TALHYIHDGIGAMVRKVLELTG 181
Cdd:PRK11780  196 QSIAEAASGIEKLVSRVLELAE 217
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 34-107 3.76e-05

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: 41.86  E-value: 3.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034627634  34 LANLSAANHDAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVT 107
Cdd:pfam01965  54 LDDVKPDDYDALVLPGGRAGPERLRD----------NEKLVEFVKDFYEKGKPVAAICHGPQVlaAAGVLKGRKVT 119
 
Name Accession Description Interval E-value
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 1-180 1.56e-93

Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1. This group includes, proteins similar to ES1, Escherichia coli enhancing lycopene biosynthesis protein 2, Azospirillum brasilense iaaC and, human HES1. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Zebrafish ES1 is expressed specifically in adult photoreceptor cells and appears to be a cytoplasmic protein. A. brasilense iaaC is involved in controlling IAA biosynthesis.


Pssm-ID: 153227  Cd Length: 213  Bit Score: 271.03  E-value: 1.56e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634   1 MHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEF 80
Cdd:cd03133    43 MHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLKAADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREF 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  81 HQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCE 159
Cdd:cd03133   122 HQAGKPIGAICIAPALAAKILgEGVEVTIGND---------AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLA 192

                         170       180
                  ....*....|....*....|.
gi 1034627634 160 TALHYIHDGIGAMVRKVLELT 180
Cdd:cd03133   193 DSIHEIADGIEKLVAKVLKLA 213
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
1-180 2.30e-85

Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];


Pssm-ID: 442389  Cd Length: 215  Bit Score: 250.08  E-value: 2.30e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634   1 MHVIDHTKGQPsEGESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEF 80
Cdd:COG3155    45 HHVINHLTGEE-MGEKRNVLVESARIARGNIKPLAELNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAF 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  81 HQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCE 159
Cdd:COG3155   124 HEAGKPIGAICIAPALLAKLLgAGVKLTIGND---------ADTAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLA 194

                         170       180
                  ....*....|....*....|.
gi 1034627634 160 TALHYIHDGIGAMVRKVLELT 180
Cdd:COG3155   195 ASISEAAEGIEKLVKKVLELA 215
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
1-181 2.16e-82

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 242.77  E-value: 2.16e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634   1 MHVIDHTKGQPSEgESRNVLTESARIARGKITDLANLSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEF 80
Cdd:PRK11780   46 LHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAEADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  81 HQAGKPIGLCCIAPVLAAKVLR-GVEVTVGHEqeeggkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCE 159
Cdd:PRK11780  125 HQAGKPIGFICIAPAMLPKILGaGVKLTIGND---------EDTAAAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLA 195

                         170       180
                  ....*....|....*....|..
gi 1034627634 160 TALHYIHDGIGAMVRKVLELTG 181
Cdd:PRK11780  196 QSIAEAASGIEKLVSRVLELAE 217
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 32-157 1.14e-12

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: 62.81  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  32 TDLANLSAANHDAAIFPGGFGAAKNLstfavdgkdcKVNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVTVg 109
Cdd:COG0693    55 KTLDDVDPDDYDALVLPGGHGAPDDL----------REDPDVVALVREFYEAGKPVAAICHGPAVlaAAGLLKGRKVTS- 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034627634 110 heqeeggkwpYAGTAEAIKALGAKHCVKEVVeahVDqkNKVVT------TPAFM 157
Cdd:COG0693   124 ----------FPNIEDDLKNAGATYVDEEVV---VD--GNLITsrgpgdAPAFA 162
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 35-152 2.10e-08

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: 51.02  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  35 ANLSAANH---DAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAP--VLAAKVLRGVEVTVG 109
Cdd:cd03135    51 KTLSDVNLddyDAIVIPGGLPGAQNLAD----------NEKLIKLLKEFNAKGKLIAAICAAPavLAKAGLLKGKKATCY 120

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034627634 110 HEQEEggkwpyagtaeaiKALGAKHCVKEVVeahVDqkNKVVT 152
Cdd:cd03135   121 PGFED-------------KLGGANYVDEPVV---VD--GNIIT 145
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 34-157 1.21e-06

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: 46.00  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  34 LANLSAANHDAAIFPGGFgAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAP-VLA-AKVLRGVEVTvghe 111
Cdd:cd03134    55 IADVDADDYDALVIPGGT-NPDKLRR----------DPDAVAFVRAFAEAGKPVAAICHGPwVLIsAGVVRGRKLT---- 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034627634 112 qeeggkwPYAGTAEAIKALGAKHCVKEVVeahVDqkNKVVTT------PAFM 157
Cdd:cd03134   120 -------SYPSIKDDLINAGANWVDEEVV---VD--GNLITSrnpddlPAFN 159
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 34-144 4.34e-06

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: 45.24  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  34 LANLSAANHDAAIFPGGFGAaknLSTFAVdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPV--LAAK------VLRGVE 105
Cdd:cd03141    83 LSDVDPSDYDAIFIPGGHGP---MFDLPD-------NPDLQDLLREFYENGKVVAAVCHGPAalLNVKlsdgksLVAGKT 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034627634 106 VTVGHEQEE-----GGKWPYaGTAEAIKALGAKHCVKEVVEAHV 144
Cdd:cd03141   153 VTGFTNEEEeaaglKKVVPF-LLEDELKELGANYVKAEPWAEFV 195
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 33-158 1.04e-05

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: 43.79  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034627634  33 DLANLSAANHDAAIFPGGfGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVTVgh 110
Cdd:cd03169    68 DFDEVDPDDYDALVIPGG-RAPEYLRL----------DEKVLAIVRHFAEANKPVAAICHGPQIlaAAGVLKGRRCTA-- 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1034627634 111 eqeeggkwpYAGTAEAIKALGAkhcvkEVVEAHVDQKNKVVTTPAFMC 158
Cdd:cd03169   135 ---------YPACKPEVELAGG-----TVVDDGVVVDGNLVTAQAWPD 168
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 34-107 3.76e-05

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: 41.86  E-value: 3.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034627634  34 LANLSAANHDAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVT 107
Cdd:pfam01965  54 LDDVKPDDYDALVLPGGRAGPERLRD----------NEKLVEFVKDFYEKGKPVAAICHGPQVlaAAGVLKGRKVT 119
 
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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