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Conserved domains on  [gi|54400374|ref|NP_001005938|]
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Parkinson disease protein 7 homolog [Danio rerio]

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 ...
 5-184 1.22e-74

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 TIGR01383:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 179  Bit Score: 222.19  E-value: 1.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374     5 RALVILAKGAEEMETVIPVDVMRRAGIAVTV--AGLAGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNL 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDV-DLEKFDVIVLPGGMPGAENL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    83 SESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAGDHYKysEARVQKDGNVITSRGPGTSF 162
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLNGNYSV--NKTVVVDGNLITSRGPGTAI 157

                         170       180
                  ....*....|....*....|..
gi 54400374   163 EFALTIVEELMGAEVAAQVKAP 184
Cdd:TIGR01383 158 EFALELVELLAGKEKAQEVAAG 179
 
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 ...
 5-184 1.22e-74

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: 222.19  E-value: 1.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374     5 RALVILAKGAEEMETVIPVDVMRRAGIAVTV--AGLAGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNL 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDV-DLEKFDVIVLPGGMPGAENL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    83 SESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAGDHYKysEARVQKDGNVITSRGPGTSF 162
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLNGNYSV--NKTVVVDGNLITSRGPGTAI 157

                         170       180
                  ....*....|....*....|..
gi 54400374   163 EFALTIVEELMGAEVAAQVKAP 184
Cdd:TIGR01383 158 EFALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 6-172 8.99e-72

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: 214.34  E-value: 8.99e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   6 ALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNLSES 85
Cdd:cd03135   1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDV-NLDDYDAIVIPGGLPGAQNLADN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  86 PAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMagdHYKYSEARVQKDGNVITSRGPGTSFEFA 165
Cdd:cd03135  80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLG---GANYVDEPVVVDGNIITSRGPGTAFEFA 156


                ....*..
gi 54400374 166 LTIVEEL 172
Cdd:cd03135 157 LKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-171 8.38e-62

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: 189.00  E-value: 8.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374     4 KRALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLaGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNLS 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSV-DGGEVKGSRGVKVTVDASLDDV-KPDDYDALVLPGGRAGPERLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    84 ESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAGdHYKYSEARVQKDGNVITSRGPGTSFE 163
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINA-GATYVDKPVVVDGNLVTSRGPGDAPE 157


                  ....*...
gi 54400374   164 FALTIVEE 171
Cdd:pfam01965 158 FALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 3-172 3.73e-49

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: 157.19  E-value: 3.73e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   3 GKRALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNL 82
Cdd:COG0693   2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDV-DPDDYDALVLPGGHGAPDDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  83 SESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKM-MAGDHykYSEARVQKDGNVITSRGPGTS 161
Cdd:COG0693  81 REDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLkNAGAT--YVDEEVVVDGNLITSRGPGDA 158

                       170
                ....*....|.
gi 54400374 162 FEFALTIVEEL 172
Cdd:COG0693 159 PAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
6-187 4.05e-37

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 127.20  E-value: 4.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    6 ALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLA--GKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNLS 83
Cdd:PRK11574   5 ALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVAsdGNLEITCSRGVKLLADAPLVEV-ADGDFDVIVLPGGIKGAECFR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   84 ESPAVKEVLKD--QEGRkgLIAAICAGP-TALLAHGIAYGSTVTTHPGAKDKMMAGdhyKYSEARVQKDG--NVITSRGP 158
Cdd:PRK11574  84 DSPLLVETVRQfhRSGR--IVAAICAAPaTVLVPHDLFPIGNMTGFPTLKDKIPAE---QWQDKRVVWDArvNLLTSQGP 158

                        170       180
                 ....*....|....*....|....*....
gi 54400374  159 GTSFEFALTIVEELMGAEVAAQVKAPLIL 187
Cdd:PRK11574 159 GTAIDFALKIIDLLVGREKAHEVASQLVM 187
 
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 ...
 5-184 1.22e-74

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: 222.19  E-value: 1.22e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374     5 RALVILAKGAEEMETVIPVDVMRRAGIAVTV--AGLAGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNL 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDV-DLEKFDVIVLPGGMPGAENL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    83 SESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAGDHYKysEARVQKDGNVITSRGPGTSF 162
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLNGNYSV--NKTVVVDGNLITSRGPGTAI 157

                         170       180
                  ....*....|....*....|..
gi 54400374   163 EFALTIVEELMGAEVAAQVKAP 184
Cdd:TIGR01383 158 EFALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 6-172 8.99e-72

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: 214.34  E-value: 8.99e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   6 ALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNLSES 85
Cdd:cd03135   1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDV-NLDDYDAIVIPGGLPGAQNLADN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  86 PAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMagdHYKYSEARVQKDGNVITSRGPGTSFEFA 165
Cdd:cd03135  80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLG---GANYVDEPVVVDGNIITSRGPGTAFEFA 156


                ....*..
gi 54400374 166 LTIVEEL 172
Cdd:cd03135 157 LKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-171 8.38e-62

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: 189.00  E-value: 8.38e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374     4 KRALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLaGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNLS 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSV-DGGEVKGSRGVKVTVDASLDDV-KPDDYDALVLPGGRAGPERLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    84 ESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAGdHYKYSEARVQKDGNVITSRGPGTSFE 163
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINA-GATYVDKPVVVDGNLVTSRGPGDAPE 157


                  ....*...
gi 54400374   164 FALTIVEE 171
Cdd:pfam01965 158 FALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 3-172 3.73e-49

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: 157.19  E-value: 3.73e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   3 GKRALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNL 82
Cdd:COG0693   2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDV-DPDDYDALVLPGGHGAPDDL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  83 SESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKM-MAGDHykYSEARVQKDGNVITSRGPGTS 161
Cdd:COG0693  81 REDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLkNAGAT--YVDEEVVVDGNLITSRGPGDA 158

                       170
                ....*....|.
gi 54400374 162 FEFALTIVEEL 172
Cdd:COG0693 159 PAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
6-187 4.05e-37

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 127.20  E-value: 4.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    6 ALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLA--GKEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNLS 83
Cdd:PRK11574   5 ALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVAsdGNLEITCSRGVKLLADAPLVEV-ADGDFDVIVLPGGIKGAECFR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   84 ESPAVKEVLKD--QEGRkgLIAAICAGP-TALLAHGIAYGSTVTTHPGAKDKMMAGdhyKYSEARVQKDG--NVITSRGP 158
Cdd:PRK11574  84 DSPLLVETVRQfhRSGR--IVAAICAAPaTVLVPHDLFPIGNMTGFPTLKDKIPAE---QWQDKRVVWDArvNLLTSQGP 158

                        170       180
                 ....*....|....*....|....*....
gi 54400374  159 GTSFEFALTIVEELMGAEVAAQVKAPLIL 187
Cdd:PRK11574 159 GTAIDFALKIIDLLVGREKAHEVASQLVM 187
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 5-159 2.38e-25

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: 96.07  E-value: 2.38e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   5 RALVILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGKEPVQCSREVMIC-PDSSLEDAhKQGPYDVVLLPGGlLGAQNLS 83
Cdd:cd03134   1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVtVDLTIADV-DADDYDALVIPGG-TNPDKLR 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 54400374  84 ESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMM-AGDHYKYSEarVQKDGNVITSRGPG 159
Cdd:cd03134  79 RDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLInAGANWVDEE--VVVDGNLITSRNPD 153
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 4-181 1.78e-19

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: 83.67  E-value: 1.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   4 KRALVILAKGAEEMETVIPVDVMRRA-------GIAVTVAGLAGkEPVQCSREVMICPDSSLEDAhkqGPYDVVLLPGGL 76
Cdd:COG4977   1 LRVAFLLLPGFSLLDLAGPLEVFRLAnrlagrpLYRWRLVSLDG-GPVRSSSGLTVAPDHGLADL---AAADTLIVPGGL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  77 lgAQNLSESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAgdhyKYSEARVQ------KDG 150
Cdd:COG4977  77 --DPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAE----RFPDVRVDpdrlyvDDG 150

                       170       180       190
                ....*....|....*....|....*....|.
gi 54400374 151 NVITSRGPGTSFEFALTIVEELMGAEVAAQV 181
Cdd:COG4977 151 DILTSAGGTAGIDLALHLVERDHGAELANAV 181
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 8-181 6.44e-18

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: 77.20  E-value: 6.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   8 VILAKGAEEMETVIPVDV---MRRAGIAVTVAgLAGKE--PVQCSREVMICPDSSLEDAhkqGPYDVVLLPGGLlGAQNL 82
Cdd:cd03139   3 ILLFPGVEVLDVIGPYEVfgrAPRLAAPFEVF-LVSETggPVSSRSGLTVLPDTSFADP---PDLDVLLVPGGG-GTRAL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  83 SESPAVKEVLKDQEGRKGLIAAICAGpTALLAH-GIAYGSTVTTHPGAKDKM-MAGDHYKySEARVQKDGNVITSRGPGT 160
Cdd:cd03139  78 VNDPALLDFIRRQAARAKYVTSVCTG-ALLLAAaGLLDGRRATTHWAAIDWLkEFGAIVV-VDARWVVDGNIWTSGGVSA 155

                       170       180
                ....*....|....*....|.
gi 54400374 161 SFEFALTIVEELMGAEVAAQV 181
Cdd:cd03139 156 GIDMALALVARLFGEELAQAV 176
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 23-181 7.85e-16

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: 71.46  E-value: 7.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  23 VDVMR-------RAGIAVTVAGLAGkEPVQCSREVMICPDSSLEDAhkqGPYDVVLLPGGLLGAQnlSESPAVKEVLKDQ 95
Cdd:cd03136  18 IEPLRaanrlagRELYRWRVLSLDG-APVTSSNGLRVAPDAALEDA---PPLDYLFVVGGLGARR--AVTPALLAWLRRA 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  96 EGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAgdhyKYSEARVQK-----DGNVITSRGPGTSFEFALTIVE 170
Cdd:cd03136  92 ARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAE----AFPRVQVTRdlfeiDGDRLTCAGGTAALDLMLELIA 167

                       170
                ....*....|.
gi 54400374 171 ELMGAEVAAQV 181
Cdd:cd03136 168 RDHGAALAARV 178
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 8-181 4.72e-13

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: 64.06  E-value: 4.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   8 VILAKGAEEMETVIPVDVMRRAGIA-------VTVAGLAGkEPVQCSREVMICPDSSLEDAHkqgPYDVVLLPGGLlGAQ 80
Cdd:cd03137   3 VLVFPGVSLLDLSGPAEVFGEANRAlgppayeLRVCSPEG-GPVRSSSGLSLVADAGLDALA---AADTVIVPGGP-DVD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  81 NLSESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAgdhyKYSEARVQ------KDGNVIT 154
Cdd:cd03137  78 GRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLAR----RFPAVRVDpdvlyvDDGNVWT 153

                       170       180
                ....*....|....*....|....*..
gi 54400374 155 SRGPGTSFEFALTIVEELMGAEVAAQV 181
Cdd:cd03137 154 SAGVTAGIDLCLHLVREDLGAAVANRV 180
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 7-136 4.20e-11

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: 57.61  E-value: 4.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   7 LVILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGKEPVqcsrevmicPDSSLEDahkqgpYDVVLLPGGLLGAQNLSESP 86
Cdd:cd01653   2 AVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVE---------SDVDLDD------YDGLILPGGPGTPDDLARDE 66

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 54400374  87 AVKEVLKDQEGRKGLIAAICAGPTALLAhgiaygsTVTTHPGAKDKMMAG 136
Cdd:cd01653  67 ALLALLREAAAAGKPILGICLGAQLLVL-------GVQFHPEAIDGAEAG 109
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 7-112 5.97e-09

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: 51.05  E-value: 5.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   7 LVILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGKEPvqcsrevmicpdsslEDAHKQGPYDVVLLPGGLLGAQNLSESP 86
Cdd:cd03128   2 AVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPV---------------ESDVDLDDYDGLILPGGPGTPDDLAWDE 66

                        90       100
                ....*....|....*....|....*.
gi 54400374  87 AVKEVLKDQEGRKGLIAAICAGPTAL 112
Cdd:cd03128  67 ALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 41-172 9.06e-09

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


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 52.22  E-value: 9.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  41 KEPVQCSREVMICPDSSLEDAhKQGPYDVVLLPGGLLGAQNlsESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGI--A 118
Cdd:cd03140  36 GEPVTSIGGLRVVPDYSLDDL-PPEDYDLLILPGGDSWDNP--EAPDLAGLVRQALKQGKPVAAICGATLALARAGLlnN 112

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 54400374 119 YGSTVTT------HPGAKdkmmAGDHYkYSEARVQKDGNVITSrgPGTSF-EFALTIVEEL 172
Cdd:cd03140 113 RKHTSNSldflkaHAPYY----GGAEY-YDEPQAVSDGNLITA--NGTAPvEFAAEILRAL 166
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 26-181 5.01e-08

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: 50.72  E-value: 5.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  26 MRRAGIAVTVAGLAGkEPVQCSREVMICPDSSLEDAhkqGPYDVVLLPG--GLLGAQNLSESPAVKEVLKDQEGRKGLIA 103
Cdd:cd03138  33 GGAPPFEVRLVSLDG-GPVLLAGGILILPDATLADV---PAPDLVIVPGlgGDPDELLLADNPALIAWLRRQHANGATVA 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374 104 AICAGPTALLAHGIAYGSTVTTH-----------PGAKDKMmagdhykysEARVQKDGNVITSRGPGTSFEFALTIVEEL 172
Cdd:cd03138 109 AACTGVFLLAEAGLLDGRRATTHwwlapqfrrrfPKVRLDP---------DRVVVTDGNLITAGGAMAWADLALHLIERL 179


                ....*....
gi 54400374 173 MGAEVAAQV 181
Cdd:cd03138 180 AGPELAQLV 188
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 13-172 2.45e-07

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: 49.09  E-value: 2.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  13 GAEEMETVIPVDVMRRAGIAVTVAGLAGKEP--VQCSREVMICPDSSLEDAHKQG----------------PYDVVLLPG 74
Cdd:cd03141  19 GLWLEELAHPYDVFTEAGYEVDFASPKGGKVplDPRSLDAEDDDDASVFDNDEEFkkklantkklsdvdpsDYDAIFIPG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  75 GLlGA-QNLSESPAVKEVLKDQEGRKGLIAAICAGPTALL----AHG--IAYGSTVTTHP-------GAKDKMM------ 134
Cdd:cd03141  99 GH-GPmFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLnvklSDGksLVAGKTVTGFTneeeeaaGLKKVVPfllede 177

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 54400374 135 ---AGDHYKYSEA---RVQKDGNVITSRGPGTSFEFALTIVEEL 172
Cdd:cd03141 178 lkeLGANYVKAEPwaeFVVVDGRLITGQNPASAAAVAEALVKAL 221
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 67-157 5.30e-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: 41.86  E-value: 5.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374  67 YDVVLLPGGLlGAQNLSESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAK-DKMMAGDHykYSEAR 145
Cdd:cd03169  77 YDALVIPGGR-APEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKpEVELAGGT--VVDDG 153

                        90
                ....*....|..
gi 54400374 146 VQKDGNVITSRG 157
Cdd:cd03169 154 VVVDGNLVTAQA 165
PRK04155 PRK04155
protein deglycase HchA;
3-121 7.90e-05

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 41.91  E-value: 7.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374    3 GKRALVILAK--------------GAEEMETVIPVDVMRRAGIAVTVAGLAGKePVQCSREVMICPDS------------ 56
Cdd:PRK04155  49 GKKILMIAADerylpmdngklfstGNHPVETLLPMYHLHKAGFEFDVATLSGN-PVKFEYWAMPHEDEavmgfyekyksk 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 54400374   57 -----SLEDAHKQG-----PYDVVLLPGG---LLGaqnLSESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAYGS 121
Cdd:PRK04155 128 fkqpkKLADVVANLlapdsDYAAVFIPGGhgaLIG---LPESEDVAAALQWALDNDRFIITLCHGPAALLAAGVDHGD 202
ftrA PRK09393
transcriptional activator FtrA; Provisional
 90-181 3.15e-04

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 40.33  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   90 EVLKDQEGRKGLIAAICAGPTALLAHGIAYGSTVTTHPGAKDKMMAgdhyKYSEARVQKD------GNVITSRGPGTSFE 163
Cdd:PRK09393  97 EALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQA----RYPAIRVDPDvlyvdeGQILTSAGSAAGID 172

                         90
                 ....*....|....*...
gi 54400374  164 FALTIVEELMGAEVAAQV 181
Cdd:PRK09393 173 LCLHLVRRDFGSEAANRV 190
GATase1_EcHsp31_like cd03148
Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 ...
 9-132 1.20e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31); Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31). This group includes proteins similar to EcHsp31. EcHsp31 has chaperone activity. 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 GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. 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. EcHsp31 is a homodimer.


Pssm-ID: 153242 [Multi-domain]  Cd Length: 232  Bit Score: 38.31  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 54400374   9 ILAKGAEEMETVIPVDVMRRAGIAVTVAGLAGkEPVQCSREVMICPDS---SLEDAHKQ-------------------GP 66
Cdd:cd03148  18 LFSTGNHPVEMLLPLYHLHAAGFDFDVATLSG-LPVKFEYWAMPHEDEavmPFFEKHKSklrnpkkladvvaslnaddSE 96

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 54400374  67 YDVVLLPGGLLGAQNLSESPAVKEVLKDQEGRKGLIAAICAGPTALLAHGIAY------GSTVTTHPGAKDK 132
Cdd:cd03148  97 YAAVFIPGGHGALIGIPESQDVAAALQWAIKNDRFVITLCHGPAAFLAARHGGgknpleGYSVCVFPDSLDE 168
 
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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