NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15232455|ref|NP_188117|]
View 

Class I glutamine amidotransferase-like superfamily protein [Arabidopsis thaliana]

Protein Classification

DJ-1/PfpI family protein( domain architecture ID 11492386)

DJ-1/PfpI family protein, similar to Escherichia coli YajL, a covalent chaperone that protects cells against protein sulfenylation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 7-185 1.47e-82

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


:

Pssm-ID: 213612 [Multi-domain]  Cd Length: 179  Bit Score: 249.93  E-value: 1.47e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455     7 TVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVG--VDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLK 84
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKlaVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455    85 NCKSLENMVKKQDSDGRLNAAICCAPALALGTWGLLeGKKATGYPVFMEKLAATCATaVESRVQIDGRIVTSRGPGTTIE 164
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLL-GKKATCYPGFKEKLLNGNYS-VNKTVVVDGNLITSRGPGTAIE 158

                         170       180
                  ....*....|....*....|.
gi 15232455   165 FSITLIEQLFGKEKADEVSSI 185
Cdd:TIGR01383 159 FALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 231-377 1.71e-57

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: 185.06  E-value: 1.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 231 VDILRRAKANVVIAAVGNSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPYG 310
Cdd:cd03135  18 VDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLADNEKLIKLLKEFNAKGKLIA 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232455 311 GICASPAYVFEPnGLLKGKKATTHPVVSDKLSDKSHIEHRVVVDGNVITSRAPGTAMEFSLAIVEKF 377
Cdd:cd03135  98 AICAAPAVLAKA-GLLKGKKATCYPGFEDKLGGANYVDEPVVVDGNIITSRGPGTAFEFALKIVEAL 163
 
Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 7-185 1.47e-82

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


Pssm-ID: 213612 [Multi-domain]  Cd Length: 179  Bit Score: 249.93  E-value: 1.47e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455     7 TVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVG--VDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLK 84
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKlaVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455    85 NCKSLENMVKKQDSDGRLNAAICCAPALALGTWGLLeGKKATGYPVFMEKLAATCATaVESRVQIDGRIVTSRGPGTTIE 164
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLL-GKKATCYPGFKEKLLNGNYS-VNKTVVVDGNLITSRGPGTAIE 158

                         170       180
                  ....*....|....*....|.
gi 15232455   165 FSITLIEQLFGKEKADEVSSI 185
Cdd:TIGR01383 159 FALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 8-173 1.83e-59

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: 190.07  E-value: 1.83e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   8 VLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVGVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLKNCK 87
Cdd:cd03135   1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  88 SLENMVKKQDSDGRLNAAICCAPAlALGTWGLLEGKKATGYPVFMEKLaaTCATAVESRVQIDGRIVTSRGPGTTIEFSI 167
Cdd:cd03135  81 KLIKLLKEFNAKGKLIAAICAAPA-VLAKAGLLKGKKATCYPGFEDKL--GGANYVDEPVVVDGNIITSRGPGTAFEFAL 157


                ....*.
gi 15232455 168 TLIEQL 173
Cdd:cd03135 158 KIVEAL 163
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 231-377 1.71e-57

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: 185.06  E-value: 1.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 231 VDILRRAKANVVIAAVGNSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPYG 310
Cdd:cd03135  18 VDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLADNEKLIKLLKEFNAKGKLIA 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232455 311 GICASPAYVFEPnGLLKGKKATTHPVVSDKLSDKSHIEHRVVVDGNVITSRAPGTAMEFSLAIVEKF 377
Cdd:cd03135  98 AICAAPAVLAKA-GLLKGKKATCYPGFEDKLGGANYVDEPVVVDGNIITSRGPGTAFEFALKIVEAL 163
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 231-389 1.16e-48

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


Pssm-ID: 213612 [Multi-domain]  Cd Length: 179  Bit Score: 162.87  E-value: 1.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   231 VDILRRAKANVVIAAVG--NSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKP 308
Cdd:TIGR01383  19 VDVLRRAGIKVTVAIAGlnGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLRNSKLLLNILKSQESKGKL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   309 YGGICASPAYVFEPNGLLkGKKATTHPVVSDKLSDKSH-IEHRVVVDGNVITSRAPGTAMEFSLAIVEKFYGREKALQLG 387
Cdd:TIGR01383  99 VAAICAAPAVLLAHGVLL-GKKATCYPGFKEKLLNGNYsVNKTVVVDGNLITSRGPGTAIEFALELVELLAGKEKAQEVA 177


                  ..
gi 15232455   388 KA 389
Cdd:TIGR01383 178 AG 179
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 5-173 5.55e-44

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: 150.25  E-value: 5.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   5 TKTVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVGVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLK 84
Cdd:COG0693   2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPDDLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  85 NCKSLENMVKKQDSDGRLNAAICCAPAlALGTWGLLEGKKATGYPVFMEKLAATCATAVESRVQIDGRIVTSRGPGTTIE 164
Cdd:COG0693  82 EDPDVVALVREFYEAGKPVAAICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGNLITSRGPGDAPA 160


                ....*....
gi 15232455 165 FSITLIEQL 173
Cdd:COG0693 161 FARALLELL 169
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 6-172 6.02e-44

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: 150.10  E-value: 6.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455     6 KTVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVgVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLKN 85
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGE-VKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455    86 CKSLENMVKKQDSDGRLNAAICCAPaLALGTWGLLEGKKATGYPVFMEKLAATCATAVESRVQIDGRIVTSRGPGTTIEF 165
Cdd:pfam01965  80 NEKLVEFVKDFYEKGKPVAAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPEF 158


                  ....*..
gi 15232455   166 SITLIEQ 172
Cdd:pfam01965 159 ALEILEQ 165
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 230-376 4.63e-40

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: 140.08  E-value: 4.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   230 LVDILRRAKANVVIAAVGNSlEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPY 309
Cdd:pfam01965  19 PADVLRRAGIKVTVVSVDGG-EVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERLRDNEKLVEFVKDFYEKGKPV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232455   310 GGICASPaYVFEPNGLLKGKKATTHPVVSDKLSDK--SHIEHRVVVDGNVITSRAPGTAMEFSLAIVEK 376
Cdd:pfam01965  98 AAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLINAgaTYVDKPVVVDGNLVTSRGPGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 231-377 1.72e-39

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: 138.70  E-value: 1.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 231 VDILRRAKANVVIAAVGNSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPYG 310
Cdd:COG0693  22 YDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVA 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232455 311 GICASPAyVFEPNGLLKGKKATTHPVVSDKLSDK--SHIEHRVVVDGNVITSRAPGTAMEFSLAIVEKF 377
Cdd:COG0693 102 AICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAgaTYVDEEVVVDGNLITSRGPGDAPAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
5-190 3.34e-38

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 136.06  E-value: 3.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455    5 TKTVLIPIAHGTEPLEAVAMITVLRRGGADVTVASV--ETQVGVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGET 82
Cdd:PRK11574   2 SASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAEC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   83 LKNCKSLENMVKKQDSDGRLNAAICCAPALALGTWGLLEGKKATGYPVFMEKLAATcaTAVESRVQIDGRI--VTSRGPG 160
Cdd:PRK11574  82 FRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAE--QWQDKRVVWDARVnlLTSQGPG 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 15232455  161 TTIEFSITLIEQLFGKEKADEVSSILLLRP 190
Cdd:PRK11574 160 TAIDFALKIIDLLVGREKAHEVASQLVMAA 189
PRK11574 PRK11574
protein deglycase YajL;
231-392 1.08e-30

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 116.03  E-value: 1.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  231 VDILRRAKANVVIAAVGN--SLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKP 308
Cdd:PRK11574  22 IDLLVRGGIKVTTASVASdgNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAECFRDSPLLVETVRQFHRSGRI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  309 YGGICASPAYVFEPNGLLKGKKATTHPVVSDKLSDKSHIEHRVVVDG--NVITSRAPGTAMEFSLAIVEKFYGREKALQL 386
Cdd:PRK11574 102 VAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQDKRVVWDArvNLLTSQGPGTAIDFALKIIDLLVGREKAHEV 181


                 ....*.
gi 15232455  387 GkATLV 392
Cdd:PRK11574 182 A-SQLV 186
 
Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 7-185 1.47e-82

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


Pssm-ID: 213612 [Multi-domain]  Cd Length: 179  Bit Score: 249.93  E-value: 1.47e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455     7 TVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVG--VDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLK 84
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKlaVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455    85 NCKSLENMVKKQDSDGRLNAAICCAPALALGTWGLLeGKKATGYPVFMEKLAATCATaVESRVQIDGRIVTSRGPGTTIE 164
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLL-GKKATCYPGFKEKLLNGNYS-VNKTVVVDGNLITSRGPGTAIE 158

                         170       180
                  ....*....|....*....|.
gi 15232455   165 FSITLIEQLFGKEKADEVSSI 185
Cdd:TIGR01383 159 FALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 8-173 1.83e-59

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: 190.07  E-value: 1.83e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   8 VLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVGVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLKNCK 87
Cdd:cd03135   1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLADNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  88 SLENMVKKQDSDGRLNAAICCAPAlALGTWGLLEGKKATGYPVFMEKLaaTCATAVESRVQIDGRIVTSRGPGTTIEFSI 167
Cdd:cd03135  81 KLIKLLKEFNAKGKLIAAICAAPA-VLAKAGLLKGKKATCYPGFEDKL--GGANYVDEPVVVDGNIITSRGPGTAFEFAL 157


                ....*.
gi 15232455 168 TLIEQL 173
Cdd:cd03135 158 KIVEAL 163
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 231-377 1.71e-57

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: 185.06  E-value: 1.71e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 231 VDILRRAKANVVIAAVGNSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPYG 310
Cdd:cd03135  18 VDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLADNEKLIKLLKEFNAKGKLIA 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232455 311 GICASPAYVFEPnGLLKGKKATTHPVVSDKLSDKSHIEHRVVVDGNVITSRAPGTAMEFSLAIVEKF 377
Cdd:cd03135  98 AICAAPAVLAKA-GLLKGKKATCYPGFEDKLGGANYVDEPVVVDGNIITSRGPGTAFEFALKIVEAL 163
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 231-389 1.16e-48

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


Pssm-ID: 213612 [Multi-domain]  Cd Length: 179  Bit Score: 162.87  E-value: 1.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   231 VDILRRAKANVVIAAVG--NSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKP 308
Cdd:TIGR01383  19 VDVLRRAGIKVTVAIAGlnGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLRNSKLLLNILKSQESKGKL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   309 YGGICASPAYVFEPNGLLkGKKATTHPVVSDKLSDKSH-IEHRVVVDGNVITSRAPGTAMEFSLAIVEKFYGREKALQLG 387
Cdd:TIGR01383  99 VAAICAAPAVLLAHGVLL-GKKATCYPGFKEKLLNGNYsVNKTVVVDGNLITSRGPGTAIEFALELVELLAGKEKAQEVA 177


                  ..
gi 15232455   388 KA 389
Cdd:TIGR01383 178 AG 179
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 5-173 5.55e-44

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: 150.25  E-value: 5.55e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   5 TKTVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVGVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLK 84
Cdd:COG0693   2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPDDLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  85 NCKSLENMVKKQDSDGRLNAAICCAPAlALGTWGLLEGKKATGYPVFMEKLAATCATAVESRVQIDGRIVTSRGPGTTIE 164
Cdd:COG0693  82 EDPDVVALVREFYEAGKPVAAICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGNLITSRGPGDAPA 160


                ....*....
gi 15232455 165 FSITLIEQL 173
Cdd:COG0693 161 FARALLELL 169
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 6-172 6.02e-44

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: 150.10  E-value: 6.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455     6 KTVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVgVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGETLKN 85
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGE-VKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455    86 CKSLENMVKKQDSDGRLNAAICCAPaLALGTWGLLEGKKATGYPVFMEKLAATCATAVESRVQIDGRIVTSRGPGTTIEF 165
Cdd:pfam01965  80 NEKLVEFVKDFYEKGKPVAAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPEF 158


                  ....*..
gi 15232455   166 SITLIEQ 172
Cdd:pfam01965 159 ALEILEQ 165
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 230-376 4.63e-40

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: 140.08  E-value: 4.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   230 LVDILRRAKANVVIAAVGNSlEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPY 309
Cdd:pfam01965  19 PADVLRRAGIKVTVVSVDGG-EVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERLRDNEKLVEFVKDFYEKGKPV 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232455   310 GGICASPaYVFEPNGLLKGKKATTHPVVSDKLSDK--SHIEHRVVVDGNVITSRAPGTAMEFSLAIVEK 376
Cdd:pfam01965  98 AAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLINAgaTYVDKPVVVDGNLVTSRGPGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 231-377 1.72e-39

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: 138.70  E-value: 1.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 231 VDILRRAKANVVIAAVGNSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKPYG 310
Cdd:COG0693  22 YDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVA 101

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232455 311 GICASPAyVFEPNGLLKGKKATTHPVVSDKLSDK--SHIEHRVVVDGNVITSRAPGTAMEFSLAIVEKF 377
Cdd:COG0693 102 AICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAgaTYVDEEVVVDGNLITSRGPGDAPAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
5-190 3.34e-38

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 136.06  E-value: 3.34e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455    5 TKTVLIPIAHGTEPLEAVAMITVLRRGGADVTVASV--ETQVGVDACHGIKMVADTLLSDITDSVFDLIVLPGGLPGGET 82
Cdd:PRK11574   2 SASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAEC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   83 LKNCKSLENMVKKQDSDGRLNAAICCAPALALGTWGLLEGKKATGYPVFMEKLAATcaTAVESRVQIDGRI--VTSRGPG 160
Cdd:PRK11574  82 FRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAE--QWQDKRVVWDARVnlLTSQGPG 159

                        170       180       190
                 ....*....|....*....|....*....|
gi 15232455  161 TTIEFSITLIEQLFGKEKADEVSSILLLRP 190
Cdd:PRK11574 160 TAIDFALKIIDLLVGREKAHEVASQLVMAA 189
PRK11574 PRK11574
protein deglycase YajL;
231-392 1.08e-30

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 116.03  E-value: 1.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  231 VDILRRAKANVVIAAVGN--SLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCEKLVNMLRKQAEANKP 308
Cdd:PRK11574  22 IDLLVRGGIKVTTASVASdgNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAECFRDSPLLVETVRQFHRSGRI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  309 YGGICASPAYVFEPNGLLKGKKATTHPVVSDKLSDKSHIEHRVVVDG--NVITSRAPGTAMEFSLAIVEKFYGREKALQL 386
Cdd:PRK11574 102 VAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQDKRVVWDArvNLLTSQGPGTAIDFALKIIDLLVGREKAHEV 181


                 ....*.
gi 15232455  387 GkATLV 392
Cdd:PRK11574 182 A-SQLV 186
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 7-172 6.93e-20

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: 85.67  E-value: 6.93e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   7 TVLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVGVDACHGIKMV-ADTLLSDITDSVFDLIVLPGGLpGGETLKN 85
Cdd:cd03134   1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVtVDLTIADVDADDYDALVIPGGT-NPDKLRR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  86 CKSLENMVKKQDSDGRLNAAICCAPALALGTwGLLEGKKATGYPVFMEKLAATCATAVESRVQIDGRIVTSRGPGTTIEF 165
Cdd:cd03134  80 DPDAVAFVRAFAEAGKPVAAICHGPWVLISA-GVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGNLITSRNPDDLPAF 158


                ....*..
gi 15232455 166 SITLIEQ 172
Cdd:cd03134 159 NRAILKA 165
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 8-183 3.45e-19

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: 84.52  E-value: 3.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   8 VLIPIAHGTEPLEAVAMITVLRR-----GGADV-TVASVETQVGVDAchGIKMVADTLLSDITDsvFDLIVLPGGlPGGE 81
Cdd:cd03139   1 VGILLFPGVEVLDVIGPYEVFGRaprlaAPFEVfLVSETGGPVSSRS--GLTVLPDTSFADPPD--LDVLLVPGG-GGTR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  82 TLKNCKSLENMVKKQDSDGRLNAAICCApALALGTWGLLEGKKATGYPVFMEKLAATCATAVES-RVQIDGRIVTSRGPG 160
Cdd:cd03139  76 ALVNDPALLDFIRRQAARAKYVTSVCTG-ALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDaRWVVDGNIWTSGGVS 154

                       170       180
                ....*....|....*....|...
gi 15232455 161 TTIEFSITLIEQLFGKEKADEVS 183
Cdd:cd03139 155 AGIDMALALVARLFGEELAQAVA 177
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 234-376 4.65e-17

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: 77.97  E-value: 4.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 234 LRRAKANVVIAAVGNSLEVEGSR-KAKLVAEVLLDEVAEKSFDLIVLPGGLNgAQRFASCEKLVNMLRKQAEANKPYGGI 312
Cdd:cd03134  22 LREAGAEVVVAGPEAGGEIQGKHgYDTVTVDLTIADVDADDYDALVIPGGTN-PDKLRRDPDAVAFVRAFAEAGKPVAAI 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232455 313 CASPaYVFEPNGLLKGKKATTHPVVSDKLS-------DKShiehrVVVDGNVITSRAPGTAMEFSLAIVEK 376
Cdd:cd03134 101 CHGP-WVLISAGVVRGRKLTSYPSIKDDLInaganwvDEE-----VVVDGNLITSRNPDDLPAFNRAILKA 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 242-375 4.95e-16

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: 75.15  E-value: 4.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   242 VIAAVGNSLEVEGSRKAKLVAEVLLDEVAEKSFDLIVLPGGlNGAQRFASCEKLVNMLRKQAEANKPYGGICASPaYVFE 321
Cdd:TIGR01382  29 VDTVSKEAGTTVGKHGYSVTVDATIDEVNPEEYDALVIPGG-RAPEYLRLNNKAVRLVREFVEKGKPVAAICHGP-QLLI 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15232455   322 PNGLLKGKKATTHPVVSDKLSDKSHIEHR---VVVDGNVITSRAPGTAMEFSLAIVE 375
Cdd:TIGR01382 107 SAGVLRGKKLTSYPAIIDDVKNAGAEYVDievVVVDGNLVTSRVPDDLPAFNREFLK 163
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 260-392 4.31e-15

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 75.19  E-value: 4.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 260 LVAEVLLDEVAEksFDLIVLPGGLNgaQRFASCEKLVNMLRKQAEANKPYGGICASpAYVFEPNGLLKGKKATTH----- 334
Cdd:COG4977  55 VAPDHGLADLAA--ADTLIVPGGLD--PAAAADPALLAWLRRAAARGARLASICTG-AFLLAAAGLLDGRRATTHwehad 129

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232455 335 ------P---VVSDKLsdkshiehrVVVDGNVITSRAPGTAMEFSLAIVEKFYGREKALQLGKATLV 392
Cdd:COG4977 130 afaerfPdvrVDPDRL---------YVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVV 187
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 233-383 3.72e-14

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: 70.26  E-value: 3.72e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 233 ILRRAKANVVIAAVGNSLE-VEGSRKAKLVAEVLLDEVAEksFDLIVLPGGLnGAQRFASCEKLVNMLRKQAEANKPYGG 311
Cdd:cd03139  23 RAPRLAAPFEVFLVSETGGpVSSRSGLTVLPDTSFADPPD--LDVLLVPGGG-GTRALVNDPALLDFIRRQAARAKYVTS 99

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232455 312 ICaSPAYVFEPNGLLKGKKATTHPVVSDKLSDKSHI---EHRVVVDGNVITSRAPGTAMEFSLAIVEKFYGREKA 383
Cdd:cd03139 100 VC-TGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIvvvDARWVVDGNIWTSGGVSAGIDMALALVARLFGEELA 173
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 259-392 8.10e-14

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153232 [Multi-domain]  Cd Length: 195  Bit Score: 69.60  E-value: 8.10e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 259 KLVAEVLLDEVAEksFDLIVLPG--GLNGAQRFASCEKLVNMLRKQAEANKPYGGICaSPAYVFEPNGLLKGKKATTH-- 334
Cdd:cd03138  57 LILPDATLADVPA--PDLVIVPGlgGDPDELLLADNPALIAWLRRQHANGATVAAAC-TGVFLLAEAGLLDGRRATTHww 133

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232455 335 ---------PVVsdklsdKSHIEHRVVVDGNVITSRAPGTAMEFSLAIVEKFYGREKALQLGKATLV 392
Cdd:cd03138 134 lapqfrrrfPKV------RLDPDRVVVTDGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 9-190 9.38e-14

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 71.34  E-value: 9.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   9 LIPIAHGTEPLEAVAmiTVLRRGGADVTVASVETQVgVDACHGIKMVADTLLSDITDsvFDLIVLPGGLpgGETLKNCKS 88
Cdd:COG4977  13 LLDLAGPLEVFRLAN--RLAGRPLYRWRLVSLDGGP-VRSSSGLTVAPDHGLADLAA--ADTLIVPGGL--DPAAAADPA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  89 LENMVKKQDSDGRLNAAICcAPALALGTWGLLEGKKATGYPVFMEKLAATC--ATAVESRVQI-DGRIVTSRGPGTTIEF 165
Cdd:COG4977  86 LLAWLRRAAARGARLASIC-TGAFLLAAAGLLDGRRATTHWEHADAFAERFpdVRVDPDRLYVdDGDILTSAGGTAGIDL 164

                       170       180
                ....*....|....*....|....*
gi 15232455 166 SITLIEQLFGKEKADEVSSILLLRP 190
Cdd:COG4977 165 ALHLVERDHGAELANAVARRLVVDP 189
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 242-385 6.39e-11

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 60.98  E-value: 6.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 242 VIAAVGNslEVEGSRKAKLVAEVLLDEVAEksFDLIVLPGGlNGAQRFASCEKLVNMLRKQAEANKPYGGICaSPAYVFE 321
Cdd:cd03137  37 VCSPEGG--PVRSSSGLSLVADAGLDALAA--ADTVIVPGG-PDVDGRPPPPALLAALRRAAARGARVASVC-TGAFVLA 110

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232455 322 PNGLLKGKKATTHPVVSDKLSD---KSHIEHRV--VVDGNVITSRAPGTAMEFSLAIVEKFYGREKALQ 385
Cdd:cd03137 111 EAGLLDGRRATTHWAYAEDLARrfpAVRVDPDVlyVDDGNVWTSAGVTAGIDLCLHLVREDLGAAVANR 179
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 51-188 1.87e-10

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153232 [Multi-domain]  Cd Length: 195  Bit Score: 59.97  E-value: 1.87e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  51 GIKMVADTLLSDITDsvFDLIVLPG--GLPGGETLKNCKSLENMVKKQDSDGRLNAAiCCAPALALGTWGLLEGKKATG- 127
Cdd:cd03138  55 GILILPDATLADVPA--PDLVIVPGlgGDPDELLLADNPALIAWLRRQHANGATVAA-ACTGVFLLAEAGLLDGRRATTh 131

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15232455 128 ---YPVFMEKLAATCATAVESRVQiDGRIVTSRGPGTTIEFSITLIEQLFGKEKADEVSSILLL 188
Cdd:cd03138 132 wwlAPQFRRRFPKVRLDPDRVVVT-DGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 51-188 2.22e-10

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153230 [Multi-domain]  Cd Length: 185  Bit Score: 59.52  E-value: 2.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  51 GIKMVADTLLSDITDsvFDLIVLPGGLPGGETLKncKSLENMVKKQDSDGRLNAAICCAPALaLGTWGLLEGKKAT---- 126
Cdd:cd03136  50 GLRVAPDAALEDAPP--LDYLFVVGGLGARRAVT--PALLAWLRRAARRGVALGGIDTGAFL-LARAGLLDGRRATvhwe 124

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232455 127 GYPVFMEKLAAtcATAVESRVQIDGRIVTSRGPGTTIEFSITLIEQLFGKEKADEVSSILLL 188
Cdd:cd03136 125 HLEAFAEAFPR--VQVTRDLFEIDGDRLTCAGGTAALDLMLELIARDHGAALAARVAEQFLH 184
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 259-378 3.68e-10

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: 58.39  E-value: 3.68e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 259 KLVAEVLLDEVAEKSFDLIVLPGGLNGAQRFAscEKLVNMLRKQAEANKPYGGICASPAYVFEpNGLLKGKKATT----- 333
Cdd:cd03140  46 RVVPDYSLDDLPPEDYDLLILPGGDSWDNPEA--PDLAGLVRQALKQGKPVAAICGATLALAR-AGLLNNRKHTSnsldf 122

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15232455 334 -HPVVSDKLSDKSHIEHRVVVDGNVITsrAPGTA-MEFSLAIVEKFY 378
Cdd:cd03140 123 lKAHAPYYGGAEYYDEPQAVSDGNLIT--ANGTApVEFAAEILRALD 167
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 267-362 3.97e-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: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 55.73  E-value: 3.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 267 DEVAEKSFDLIVLPGGlNGAQRFASCEKLVNMLRKQAEANKPYGGICASPaYVFEPNGLLKGKKATTHPVVSD--KLSDK 344
Cdd:cd03169  70 DEVDPDDYDALVIPGG-RAPEYLRLDEKVLAIVRHFAEANKPVAAICHGP-QILAAAGVLKGRRCTAYPACKPevELAGG 147

                        90
                ....*....|....*...
gi 15232455 345 SHIEHRVVVDGNVITSRA 362
Cdd:cd03169 148 TVVDDGVVVDGNLVTAQA 165
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 252-385 1.64e-08

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153230 [Multi-domain]  Cd Length: 185  Bit Score: 53.74  E-value: 1.64e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 252 VEGSRKAKLVAEVLLDEVAEksFDLIVLPGGLNgAQRFAScEKLVNMLRKQAEANKPYGGICaSPAYVFEPNGLLKGKKA 331
Cdd:cd03136  45 VTSSNGLRVAPDAALEDAPP--LDYLFVVGGLG-ARRAVT-PALLAWLRRAARRGVALGGID-TGAFLLARAGLLDGRRA 119

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15232455 332 TTHPVVSDKLS---DKSHI-EHRVVVDGNVITSRAPGTAMEFSLAIVEKFYGREKALQ 385
Cdd:cd03136 120 TVHWEHLEAFAeafPRVQVtRDLFEIDGDRLTCAGGTAALDLMLELIARDHGAALAAR 177
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 214-320 3.07e-08

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: 51.45  E-value: 3.07e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 214 ILVPIAEESEEIEAIALVDILRRAKANVVIAAVGnslevegsrkaklvAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCE 293
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPD--------------GGPVESDVDLDDYDGLILPGGPGTPDDLARDE 66

                        90       100
                ....*....|....*....|....*..
gi 15232455 294 KLVNMLRKQAEANKPYGGICASPAYVF 320
Cdd:cd01653  67 ALLALLREAAAAGKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 214-318 6.12e-08

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: 49.89  E-value: 6.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 214 ILVPIAEESEEIEAIALVDILRRAKANVVIAAVGnslevegsrkaklvAEVLLDEVAEKSFDLIVLPGGLNGAQRFASCE 293
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPD--------------GGPVESDVDLDDYDGLILPGGPGTPDDLAWDE 66

                        90       100
                ....*....|....*....|....*
gi 15232455 294 KLVNMLRKQAEANKPYGGICASPAY 318
Cdd:cd03128  67 ALLALLREAAAAGKPVLGICLGAQL 91
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 8-158 1.08e-06

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: 48.41  E-value: 1.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   8 VLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETQVGVDACH---------------GIKMVADTLLSDITDSVFDLIV 72
Cdd:cd03169   2 ILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTaihdfpgwqtytekpGHRFAVTADFDEVDPDDYDALV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  73 LPGGlPGGETLKNCKSLENMVKKQDSDGRLNAAICCAPaLALGTWGLLEGKKATGYPVFMEKLAATCATAVESRVQIDGR 152
Cdd:cd03169  82 IPGG-RAPEYLRLDEKVLAIVRHFAEANKPVAAICHGP-QILAAAGVLKGRRCTAYPACKPEVELAGGTVVDDGVVVDGN 159


                ....*.
gi 15232455 153 IVTSRG 158
Cdd:cd03169 160 LVTAQA 165
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 8-114 1.33e-06

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


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 46.82  E-value: 1.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   8 VLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETqvgvdachgikmvaDTLLSDITDSVFDLIVLPGGLPGGETLKNCK 87
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPDG--------------GPVESDVDLDDYDGLILPGGPGTPDDLARDE 66

                        90       100
                ....*....|....*....|....*..
gi 15232455  88 SLENMVKKQDSDGRLNAAICCAPALAL 114
Cdd:cd01653  67 ALLALLREAAAAGKPILGICLGAQLLV 93
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 51-173 2.04e-06

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: 47.60  E-value: 2.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  51 GIKMVADTLLSDITDSVFDLIVLPGGLPGGEtlKNCKSLENMVKKQDSDGRLNAAICCAPaLALGTWGLLEGKKATGYPV 130
Cdd:cd03140  44 GLRVVPDYSLDDLPPEDYDLLILPGGDSWDN--PEAPDLAGLVRQALKQGKPVAAICGAT-LALARAGLLNNRKHTSNSL 120

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15232455 131 FMEKLAATCATAVESRVQ----IDGRIVTSrgPGTT-IEFSITLIEQL 173
Cdd:cd03140 121 DFLKAHAPYYGGAEYYDEpqavSDGNLITA--NGTApVEFAAEILRAL 166
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 28-182 3.75e-06

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 47.11  E-value: 3.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  28 LRRGGADVTVASVETQVgVDACHGIKMVADTLLSDITDsvFDLIVLPGGlPGGETLKNCKSLENMVKKQDSDGRLNAAIC 107
Cdd:cd03137  28 LGPPAYELRVCSPEGGP-VRSSSGLSLVADAGLDALAA--ADTVIVPGG-PDVDGRPPPPALLAALRRAAARGARVASVC 103

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232455 108 CApALALGTWGLLEGKKATGYPVFMEKLAATC-ATAVESRVqI---DGRIVTSRGPGTTIEFSITLIEQLFGKEKADEV 182
Cdd:cd03137 104 TG-AFVLAEAGLLDGRRATTHWAYAEDLARRFpAVRVDPDV-LyvdDGNVWTSAGVTAGIDLCLHLVREDLGAAVANRV 180
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 8-112 1.00e-05

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


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 43.73  E-value: 1.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   8 VLIPIAHGTEPLEAVAMITVLRRGGADVTVASVETqvgvdachgikmvaDTLLSDITDSVFDLIVLPGGLPGGETLKNCK 87
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPDG--------------GPVESDVDLDDYDGLILPGGPGTPDDLAWDE 66

                        90       100
                ....*....|....*....|....*
gi 15232455  88 SLENMVKKQDSDGRLNAAICCAPAL 112
Cdd:cd03128  67 ALLALLREAAAAGKPVLGICLGAQL 91
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 20-173 2.36e-05

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: 2.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  20 EAVAMITVLRRGGADVTVASVE-TQVGVDAcHGIKM------------------VADTL-LSDITDSVFDLIVLPGG--- 76
Cdd:cd03141  24 ELAHPYDVFTEAGYEVDFASPKgGKVPLDP-RSLDAeddddasvfdndeefkkkLANTKkLSDVDPSDYDAIFIPGGhgp 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455  77 ---LPGGETLknCKSLENMVKKqdsdGRLNAAICCAPA------LALGTWgLLEGKKATGYPVFMEKLAATC-------- 139
Cdd:cd03141 103 mfdLPDNPDL--QDLLREFYEN----GKVVAAVCHGPAallnvkLSDGKS-LVAGKTVTGFTNEEEEAAGLKkvvpflle 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15232455 140 ------------ATAVESRVQIDGRIVTSRGPGTTIEFSITLIEQL 173
Cdd:cd03141 176 delkelganyvkAEPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
266-317 9.57e-04

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 40.15  E-value: 9.57e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15232455  266 LDEVAEKSFDLIVLPGGL-------NGAQRFASCE---KLVNMLRKQAEANKPYGGICASPA 317
Cdd:PRK11780  78 LAEADAEDFDALIVPGGFgaaknlsNFAVKGAECTvnpDVKALVRAFHQAGKPIGFICIAPA 139
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 266-359 3.38e-03

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: 38.69  E-value: 3.38e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455 266 LDEVAEKSFDLIVLPGGLnGA-QRFASCEKLVNMLRKQAEANKPYGGICASPA---YVFEPNG--LLKGKKATTHPVVSD 339
Cdd:cd03141  83 LSDVDPSDYDAIFIPGGH-GPmFDLPDNPDLQDLLREFYENGKVVAAVCHGPAallNVKLSDGksLVAGKTVTGFTNEEE 161

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15232455 340 KLSDKSHI----------------------EHRVVVDGNVIT 359
Cdd:cd03141 162 EAAGLKKVvpflledelkelganyvkaepwAEFVVVDGRLIT 203
ftrA PRK09393
transcriptional activator FtrA; Provisional
 51-190 3.47e-03

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 39.18  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232455   51 GIKMVADTLLSDITDSvfDLIVLPG----GLPGGETLknCKSLenmvkkQDSDGRlNAAIC--CAPALALGTWGLLEGKK 124
Cdd:PRK09393  61 GITVVADGGLELLDRA--DTIVIPGwrgpDAPVPEPL--LEAL------RAAHAR-GARLCsiCSGVFVLAAAGLLDGRR 129

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15232455  125 ATGYPVFMEKLAATC-ATAVESRV--QIDGRIVTSRGPGTTIEFSITLIEQLFGKEKADEVSSILLLRP 190
Cdd:PRK09393 130 ATTHWRYAERLQARYpAIRVDPDVlyVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPP 198
 
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