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Conserved domains on  [gi|19113727|ref|NP_592815|]
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glyoxylase III Hsp3102 [Schizosaccharomyces pombe]

Protein Classification

GATase1_Ydr533c_like domain-containing protein( domain architecture ID 10123554)

GATase1_Ydr533c_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_Ydr533c_like cd03147
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ...
 8-240 1.57e-135

Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains 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 Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer.


:

Pssm-ID: 153241 [Multi-domain]  Cd Length: 231  Bit Score: 380.13  E-value: 1.57e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   8 NALLVASSYYGPFYPDGKNTGVHFSELLIPYNVFKKAGFNVQFVSENGSYKFDDHSIEESKLGDFERKVFNDKNDDFWTN 87
Cdd:cd03147   1 KALIALTSYYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGFDDHSLDPDFLNGEDLEVFSNKDSDFWKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  88 LNNMKKASDIVGKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKNPQsvEGKTVVYHKHV 167
Cdd:cd03147  81 LKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAILANLKDPK--TGKPLIKGKTV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113727 168 TAFNKAGEEKMGVMDELKKRGMKSLNEIFAEAGATFIDPPNPNVNFTQIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:cd03147 159 TGFTDKGEEIMGVMEILKKRNLESIEDIAERAGANFIRPPGPWDDFTVVDGRIVTGSNPASATSTAEAAIKAL 231
 
Name Accession Description Interval E-value
GATase1_Ydr533c_like cd03147
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ...
 8-240 1.57e-135

Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains 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 Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer.


Pssm-ID: 153241 [Multi-domain]  Cd Length: 231  Bit Score: 380.13  E-value: 1.57e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   8 NALLVASSYYGPFYPDGKNTGVHFSELLIPYNVFKKAGFNVQFVSENGSYKFDDHSIEESKLGDFERKVFNDKNDDFWTN 87
Cdd:cd03147   1 KALIALTSYYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGFDDHSLDPDFLNGEDLEVFSNKDSDFWKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  88 LNNMKKASDIVGKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKNPQsvEGKTVVYHKHV 167
Cdd:cd03147  81 LKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAILANLKDPK--TGKPLIKGKTV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113727 168 TAFNKAGEEKMGVMDELKKRGMKSLNEIFAEAGATFIDPPNPNVNFTQIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:cd03147 159 TGFTDKGEEIMGVMEILKKRNLESIEDIAERAGANFIRPPGPWDDFTVVDGRIVTGSNPASATSTAEAAIKAL 231
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 6-240 1.18e-28

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: 106.34  E-value: 1.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   6 GKNALLVASSyygpfypdgkntGVHFSELLIPYNVFKKAGFNVQFVSENGSYKFddhsieESKLGDferKVFNDKnddfw 85
Cdd:COG0693   2 MKKVLILLTD------------GFEDEELTVPYDALREAGAEVDVASPEGGPPV------TSKHGI---TVTADK----- 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  86 tnlnnmkKASDIVGKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKnpqSVEGKTvvyhk 165
Cdd:COG0693  56 -------TLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAG---LLKGRK----- 120

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113727 166 hVTAFNkageekmGVMDELKkrgmkslneifaEAGATFIDPPnpnvnfTQIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:COG0693 121 -VTSFP-------NIEDDLK------------NAGATYVDEE------VVVDGNLITSRGPGDAPAFARALLELL 169
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 26-240 3.59e-09

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: 54.35  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727    26 NTGVHFSELLIPYNVFKKAGFNVQFVS-ENGSYkfddhsieeskLGDFERKVFNDKNDDfwtnlnnmkkasDIVGKDYQL 104
Cdd:TIGR01382   7 TDEFEDSELLYPLDRLREAGHEVDTVSkEAGTT-----------VGKHGYSVTVDATID------------EVNPEEYDA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   105 LFVAGGHAAMFdLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKnpqsvegktVVYHKHVTAFNkageekmGVMDEL 184
Cdd:TIGR01382  64 LVIPGGRAPEY-LRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAG---------VLRGKKLTSYP-------AIIDDV 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113727   185 KKrgmkslneifaeAGATFIDpPNPNVnftqIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:TIGR01382 127 KN------------AGAEYVD-IEVVV----VDGNLVTSRVPDDLPAFNREFLKLL 165
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 33-229 8.57e-08

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: 50.33  E-value: 8.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727    33 ELLIPYNVFKKAGFNVQFVSENGS-------YKFD-DHSIEESKLGDFErkvfndknddfwtnlnnmkkasdivgkdyqL 104
Cdd:pfam01965  15 ELIYPADVLRRAGIKVTVVSVDGGevkgsrgVKVTvDASLDDVKPDDYD------------------------------A 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   105 LFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKnpqSVEGKTVVYHKhvtafnkageekmGVMDEL 184
Cdd:pfam01965  65 LVLPGGRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAG---VLKGRKVTSHP-------------AVKDDL 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 19113727   185 KKrgmkslneifaeAGATFIDPPnpnvnfTQIDGKIVTGVNPQSA 229
Cdd:pfam01965 129 IN------------AGATYVDKP------VVVDGNLVTSRGPGDA 155
PRK04155 PRK04155
protein deglycase HchA;
27-155 1.76e-06

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 47.69  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   27 TGVHFSELLIPYNVFKKAGFNVQFVSENGS-YKFDDHSI--EESKLGDFerkvFNDKNDDFwtnlNNMKKASDIV----- 98
Cdd:PRK04155  72 TGNHPVETLLPMYHLHKAGFEFDVATLSGNpVKFEYWAMphEDEAVMGF----YEKYKSKF----KQPKKLADVVanlla 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113727   99 -GKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPV-LLANVKNPQS 155
Cdd:PRK04155 144 pDSDYAAVFIPGGHGALIGLPESEDVAAALQWALDNDRFIITLCHGPAaLLAAGVDHGD 202
 
Name Accession Description Interval E-value
GATase1_Ydr533c_like cd03147
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ...
 8-240 1.57e-135

Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains 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 Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer.


Pssm-ID: 153241 [Multi-domain]  Cd Length: 231  Bit Score: 380.13  E-value: 1.57e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   8 NALLVASSYYGPFYPDGKNTGVHFSELLIPYNVFKKAGFNVQFVSENGSYKFDDHSIEESKLGDFERKVFNDKNDDFWTN 87
Cdd:cd03147   1 KALIALTSYYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGFDDHSLDPDFLNGEDLEVFSNKDSDFWKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  88 LNNMKKASDIVGKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKNPQsvEGKTVVYHKHV 167
Cdd:cd03147  81 LKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAILANLKDPK--TGKPLIKGKTV 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113727 168 TAFNKAGEEKMGVMDELKKRGMKSLNEIFAEAGATFIDPPNPNVNFTQIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:cd03147 159 TGFTDKGEEIMGVMEILKKRNLESIEDIAERAGANFIRPPGPWDDFTVVDGRIVTGSNPASATSTAEAAIKAL 231
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 9-240 1.26e-82

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: 245.93  E-value: 1.26e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   9 ALLVASSYYGPfYPDGKNTGVHFSELLIPYNVFKKAGFNVQFVSENGSY-KFDDHSIeesKLGDFERKVFNDKNDDFWTN 87
Cdd:cd03141   1 ILIVLTSADKL-GGTGRPTGLWLEELAHPYDVFTEAGYEVDFASPKGGKvPLDPRSL---DAEDDDDASVFDNDEEFKKK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  88 LNNMKKASDIVGKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKNPqsvEGKTVVYHKHV 167
Cdd:cd03141  77 LANTKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLS---DGKSLVAGKTV 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19113727 168 TAFNKAGEEKMGvmdeLKKRGMKSLNEIFAEAGATFIDPPnPNVNFTQIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:cd03141 154 TGFTNEEEEAAG----LKKVVPFLLEDELKELGANYVKAE-PWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 6-240 1.18e-28

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: 106.34  E-value: 1.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   6 GKNALLVASSyygpfypdgkntGVHFSELLIPYNVFKKAGFNVQFVSENGSYKFddhsieESKLGDferKVFNDKnddfw 85
Cdd:COG0693   2 MKKVLILLTD------------GFEDEELTVPYDALREAGAEVDVASPEGGPPV------TSKHGI---TVTADK----- 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  86 tnlnnmkKASDIVGKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKnpqSVEGKTvvyhk 165
Cdd:COG0693  56 -------TLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAG---LLKGRK----- 120

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19113727 166 hVTAFNkageekmGVMDELKkrgmkslneifaEAGATFIDPPnpnvnfTQIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:COG0693 121 -VTSFP-------NIEDDLK------------NAGATYVDEE------VVVDGNLITSRGPGDAPAFARALLELL 169
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 32-226 1.51e-10

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: 57.94  E-value: 1.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  32 SELLIPYNVFKKAGFNVQFVS--ENGSYKFDDHsieesklgdfERKVFNDKNddfwtnlnnmkkASDIVGKDYQLLFVAG 109
Cdd:cd03134  13 VELTYPLYRLREAGAEVVVAGpeAGGEIQGKHG----------YDTVTVDLT------------IADVDADDYDALVIPG 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727 110 GHAAmfDL----PKAtnlQAVAREVFTNGGVLSAVCHGPVLL--ANVknpqsVEGKTvvyhkhVTAFNkageekmGVMDE 183
Cdd:cd03134  71 GTNP--DKlrrdPDA---VAFVRAFAEAGKPVAAICHGPWVLisAGV-----VRGRK------LTSYP-------SIKDD 127

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19113727 184 LKkrgmkslNeifaeAGATFIDPPNpnvnftQIDGKIVTGVNP 226
Cdd:cd03134 128 LI-------N-----AGANWVDEEV------VVDGNLITSRNP 152
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 26-240 3.59e-09

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: 54.35  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727    26 NTGVHFSELLIPYNVFKKAGFNVQFVS-ENGSYkfddhsieeskLGDFERKVFNDKNDDfwtnlnnmkkasDIVGKDYQL 104
Cdd:TIGR01382   7 TDEFEDSELLYPLDRLREAGHEVDTVSkEAGTT-----------VGKHGYSVTVDATID------------EVNPEEYDA 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   105 LFVAGGHAAMFdLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKnpqsvegktVVYHKHVTAFNkageekmGVMDEL 184
Cdd:TIGR01382  64 LVIPGGRAPEY-LRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAG---------VLRGKKLTSYP-------AIIDDV 126

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19113727   185 KKrgmkslneifaeAGATFIDpPNPNVnftqIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:TIGR01382 127 KN------------AGAEYVD-IEVVV----VDGNLVTSRVPDDLPAFNREFLKLL 165
GATase1_EcHsp31_like cd03148
Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 ...
 23-194 4.19e-09

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: 55.26  E-value: 4.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  23 DGK--NTGVHFSELLIPYNVFKKAGFNVQFVSENG-SYKFDDHSIEESklgDFERKVFNDKNDDfwtNLNNMKKASDIVG 99
Cdd:cd03148  15 NGKlfSTGNHPVEMLLPLYHLHAAGFDFDVATLSGlPVKFEYWAMPHE---DEAVMPFFEKHKS---KLRNPKKLADVVA 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727 100 K------DYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGP--VLLANV---KNPqsVEGKTVVYHKhvT 168
Cdd:cd03148  89 SlnaddsEYAAVFIPGGHGALIGIPESQDVAAALQWAIKNDRFVITLCHGPaaFLAARHgggKNP--LEGYSVCVFP--D 164

                       170       180       190
                ....*....|....*....|....*....|....*
gi 19113727 169 AFNKAGEEKMGVM---------DELKKRGMKSLNE 194
Cdd:cd03148 165 SLDEGANIEIGYMpghltwlvgEELKKMGMNIIND 199
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 33-240 7.73e-09

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: 53.33  E-value: 7.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  33 ELLIPYNVFKKAGFNVQFVSENGSykfddhsieESKLGDFERKVFNDKNddfwtnlnnmkkASDIVGKDYQLLFVAGGHA 112
Cdd:cd03135  13 EAVTPVDVLRRAGIEVTTASLEKK---------LAVGSSHGIKVKADKT------------LSDVNLDDYDAIVIPGGLP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727 113 AMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLAnvkNPQSVEGKTvvyhkhVTAFNkageekmGVMDELkkrgmksl 192
Cdd:cd03135  72 GAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLA---KAGLLKGKK------ATCYP-------GFEDKL-------- 127

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 19113727 193 neifaeAGATFIDPPnpnvnfTQIDGKIVTGVNPQSAKSTAEAAVSAL 240
Cdd:cd03135 128 ------GGANYVDEP------VVVDGNIITSRGPGTAFEFALKIVEAL 163
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 28-147 4.83e-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: 49.90  E-value: 4.83e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  28 GVHFSELLIPYNVFKKAGFNVQFVSENGSYKFDDHSIEesklgdferkvfndknddfwtnlnnmkkasdivgkDYQLLFV 107
Cdd:cd01653   8 GFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLD-----------------------------------DYDGLIL 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19113727 108 AGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLL 147
Cdd:cd01653  53 PGGPGTPDDLARDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 28-147 6.58e-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: 49.12  E-value: 6.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  28 GVHFSELLIPYNVFKKAGFNVQFVSENGSYKFDDHSIEesklgdferkvfndknddfwtnlnnmkkasdivgkDYQLLFV 107
Cdd:cd03128   8 GSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLD-----------------------------------DYDGLIL 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 19113727 108 AGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLL 147
Cdd:cd03128  53 PGGPGTPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 33-229 8.57e-08

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: 50.33  E-value: 8.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727    33 ELLIPYNVFKKAGFNVQFVSENGS-------YKFD-DHSIEESKLGDFErkvfndknddfwtnlnnmkkasdivgkdyqL 104
Cdd:pfam01965  15 ELIYPADVLRRAGIKVTVVSVDGGevkgsrgVKVTvDASLDDVKPDDYD------------------------------A 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   105 LFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKnpqSVEGKTVVYHKhvtafnkageekmGVMDEL 184
Cdd:pfam01965  65 LVLPGGRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAG---VLKGRKVTSHP-------------AVKDDL 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 19113727   185 KKrgmkslneifaeAGATFIDPPnpnvnfTQIDGKIVTGVNPQSA 229
Cdd:pfam01965 129 IN------------AGATYVDKP------VVVDGNLVTSRGPGDA 155
PRK04155 PRK04155
protein deglycase HchA;
27-155 1.76e-06

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 47.69  E-value: 1.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727   27 TGVHFSELLIPYNVFKKAGFNVQFVSENGS-YKFDDHSI--EESKLGDFerkvFNDKNDDFwtnlNNMKKASDIV----- 98
Cdd:PRK04155  72 TGNHPVETLLPMYHLHKAGFEFDVATLSGNpVKFEYWAMphEDEAVMGF----YEKYKSKF----KQPKKLADVVanlla 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 19113727   99 -GKDYQLLFVAGGHAAMFDLPKATNLQAVAREVFTNGGVLSAVCHGPV-LLANVKNPQS 155
Cdd:PRK04155 144 pDSDYAAVFIPGGHGALIGLPESEDVAAALQWALDNDRFIITLCHGPAaLLAAGVDHGD 202
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 33-223 6.02e-04

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: 39.55  E-value: 6.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727  33 ELLIPYNVFKKAGFNVQFVSEngsykfddhsieESKLGDFERKVFNDK-NDDFWT-----NLNNMKKASDIVGKDYQLLF 106
Cdd:cd03169  14 EVMVPFQALQEVGHEVDVVAP------------GKKKGDTVVTAIHDFpGWQTYTekpghRFAVTADFDEVDPDDYDALV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113727 107 VAGGHAAMFdLPKATNLQAVAREVFTNGGVLSAVCHGPVLLANVKnpqSVEGKTvvyhkhVTAFnkageEKMGVMDELkk 186
Cdd:cd03169  82 IPGGRAPEY-LRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAG---VLKGRR------CTAY-----PACKPEVEL-- 144

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 19113727 187 rgmkslneifaeAGATFIDPPnpnvnfTQIDGKIVTG 223
Cdd:cd03169 145 ------------AGGTVVDDG------VVVDGNLVTA 163
 
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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