NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|494018428|ref|WP_006960749|]
View 

MULTISPECIES: isoprenoid biosynthesis glyoxalase ElbB [Vibrio]

Protein Classification

isoprenoid biosynthesis glyoxalase ElbB( domain architecture ID 10793611)

isoprenoid biosynthesis glyoxalase ElbB displays glyoxalase activity, catalyzing the conversion of glyoxal to glycolate

CATH:  3.40.50.880
EC:  4.2.1.-
Gene Ontology:  GO:0016829
MEROPS:  C56
PubMed:  10387030
SCOP:  3001405

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
1-216 2.05e-145

isoprenoid biosynthesis glyoxalase ElbB;


:

Pssm-ID: 236980  Cd Length: 217  Bit Score: 403.78  E-value: 2.05e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   1 MKKVAVILSGSGVFDGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINHITGEEMAETRNVLTEAARIARGNIEDVAK 80
Cdd:PRK11780   1 MKKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMGETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  81 LNAEEFDAILLPGGFGAAKNLTDFAVNGAECSINTHVASACRAFAQARKPAGYLCIAPAIIPMIYDNGVKGTIGNDDATA 160
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILGAGVKLTIGNDEDTA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494018428 161 SAFNALGGEHITCEVDDIVFDEEHKVLSTPAYMLAGNISQAASGIEKLVSKLVEIA 216
Cdd:PRK11780 161 AAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLAQSIAEAASGIEKLVSRVLELA 216
 
Name Accession Description Interval E-value
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
1-216 2.05e-145

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 403.78  E-value: 2.05e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   1 MKKVAVILSGSGVFDGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINHITGEEMAETRNVLTEAARIARGNIEDVAK 80
Cdd:PRK11780   1 MKKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMGETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  81 LNAEEFDAILLPGGFGAAKNLTDFAVNGAECSINTHVASACRAFAQARKPAGYLCIAPAIIPMIYDNGVKGTIGNDDATA 160
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILGAGVKLTIGNDEDTA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494018428 161 SAFNALGGEHITCEVDDIVFDEEHKVLSTPAYMLAGNISQAASGIEKLVSKLVEIA 216
Cdd:PRK11780 161 AAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLAQSIAEAASGIEKLVSRVLELA 216
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
2-216 1.15e-142

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 396.46  E-value: 1.15e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   2 KKVAVILSGSGVFDGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINHITGEEMAETRNVLTEAARIARGNIEDVAKL 81
Cdd:COG3155    1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEEMGEKRNVLVESARIARGNIKPLAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  82 NAEEFDAILLPGGFGAAKNLTDFAVNGAECSINTHVASACRAFAQARKPAGYLCIAPAIIPMIYDNGVKGTIGNDDATAS 161
Cdd:COG3155   81 NAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLGAGVKLTIGNDADTAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494018428 162 AFNALGGEHITCEVDDIVFDEEHKVLSTPAYMLAGNISQAASGIEKLVSKLVEIA 216
Cdd:COG3155  161 AIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAASISEAAEGIEKLVKKVLELA 215
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 4-216 6.49e-118

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


Pssm-ID: 153227  Cd Length: 213  Bit Score: 333.82  E-value: 6.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   4 VAVILSGSGVFDGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINHITGEEMAETRNVLTEAARIARGNIEDVAKLNA 83
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGEAEGESRNVLVESARIARGNIKDLAKLKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  84 EEFDAILLPGGFGAAKNLTDFAVNGAECSINTHVASACRAFAQARKPAGYLCIAPAIIPMIYDNGVKGTIGNDDATASAF 163
Cdd:cd03133   81 ADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILGEGVEVTIGNDAGTAAAI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494018428 164 NALGGEHITCEVDDIVFDEEHKVLSTPAYMLAGNISQAASGIEKLVSKLVEIA 216
Cdd:cd03133  161 EKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVLKLA 213
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 80-141 8.06e-03

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: 35.86  E-value: 8.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494018428   80 KLNAEEFDAILLPGGFGAAKNLTdfavngaecsiNTHVASACRAFAQARKPAGYLCIAPAII 141
Cdd:TIGR01382  55 EVNPEEYDALVIPGGRAPEYLRL-----------NNKAVRLVREFVEKGKPVAAICHGPQLL 105
 
Name Accession Description Interval E-value
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
1-216 2.05e-145

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 403.78  E-value: 2.05e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   1 MKKVAVILSGSGVFDGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINHITGEEMAETRNVLTEAARIARGNIEDVAK 80
Cdd:PRK11780   1 MKKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMGETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  81 LNAEEFDAILLPGGFGAAKNLTDFAVNGAECSINTHVASACRAFAQARKPAGYLCIAPAIIPMIYDNGVKGTIGNDDATA 160
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILGAGVKLTIGNDEDTA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494018428 161 SAFNALGGEHITCEVDDIVFDEEHKVLSTPAYMLAGNISQAASGIEKLVSKLVEIA 216
Cdd:PRK11780 161 AAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLAQSIAEAASGIEKLVSRVLELA 216
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
2-216 1.15e-142

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 396.46  E-value: 1.15e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   2 KKVAVILSGSGVFDGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINHITGEEMAETRNVLTEAARIARGNIEDVAKL 81
Cdd:COG3155    1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEEMGEKRNVLVESARIARGNIKPLAEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  82 NAEEFDAILLPGGFGAAKNLTDFAVNGAECSINTHVASACRAFAQARKPAGYLCIAPAIIPMIYDNGVKGTIGNDDATAS 161
Cdd:COG3155   81 NAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLGAGVKLTIGNDADTAA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 494018428 162 AFNALGGEHITCEVDDIVFDEEHKVLSTPAYMLAGNISQAASGIEKLVSKLVEIA 216
Cdd:COG3155  161 AIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAASISEAAEGIEKLVKKVLELA 215
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 4-216 6.49e-118

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


Pssm-ID: 153227  Cd Length: 213  Bit Score: 333.82  E-value: 6.49e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   4 VAVILSGSGVFDGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINHITGEEMAETRNVLTEAARIARGNIEDVAKLNA 83
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGEAEGESRNVLVESARIARGNIKDLAKLKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  84 EEFDAILLPGGFGAAKNLTDFAVNGAECSINTHVASACRAFAQARKPAGYLCIAPAIIPMIYDNGVKGTIGNDDATASAF 163
Cdd:cd03133   81 ADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILGEGVEVTIGNDAGTAAAI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 494018428 164 NALGGEHITCEVDDIVFDEEHKVLSTPAYMLAGNISQAASGIEKLVSKLVEIA 216
Cdd:cd03133  161 EKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVLKLA 213
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-140 2.54e-08

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: 51.64  E-value: 2.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   1 MKKVAVILSgsgvfDGAEIHESVLALHAIEKQGAswhcfapnieQLHVINHITGEEMAETRNVLTEAARiargnieDVAK 80
Cdd:COG0693    2 MKKVLILLT-----DGFEDEELTVPYDALREAGA----------EVDVASPEGGPPVTSKHGITVTADK-------TLDD 59

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  81 LNAEEFDAILLPGGFGAAKNLTDfavngaecsiNTHVASACRAFAQARKPAGYLCIAPAI 140
Cdd:COG0693   60 VDPDDYDALVLPGGHGAPDDLRE----------DPDVVALVREFYEAGKPVAAICHGPAV 109
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 78-141 6.43e-04

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: 39.07  E-value: 6.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494018428  78 VAKLNAEEFDAILLPGGFGAAKNLTDfavngaecsiNTHVASACRAFAQARKPAGYLCIAPAII 141
Cdd:cd03135   53 LSDVNLDDYDAIVIPGGLPGAQNLAD----------NEKLIKLLKEFNAKGKLIAAICAAPAVL 106
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 74-140 3.85e-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: 37.15  E-value: 3.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494018428  74 NIEDVAKLNAEEFDAILLPGGFGAaknLTDFAVngaecsiNTHVASACRAFAQARKPAGYLCIAPAI 140
Cdd:cd03141   79 NTKKLSDVDPSDYDAIFIPGGHGP---MFDLPD-------NPDLQDLLREFYENGKVVAAVCHGPAA 135
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 3-138 6.07e-03

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: 35.98  E-value: 6.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428   3 KVAVILSgsgvfDGAEIHESVLALHAIEKQGASwhcfapnieqLHVINHITGEEMAETRNVLTEAARIArgniedVAKLN 82
Cdd:cd03134    1 KVAILAA-----DGFEDVELTYPLYRLREAGAE----------VVVAGPEAGGEIQGKHGYDTVTVDLT------IADVD 59

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 494018428  83 AEEFDAILLPGGFGAAKNLTDfavngaecsinTHVASACRAFAQARKPAGYLCIAP 138
Cdd:cd03134   60 ADDYDALVIPGGTNPDKLRRD-----------PDAVAFVRAFAEAGKPVAAICHGP 104
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 15-140 6.79e-03

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: 36.09  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494018428  15 DGAEIHESVLALHAIEKQGASWHCFAPNIEQLHVINH-ITGEEMAETRNVLTEAARIARGNIEDVaklNAEEFDAILLPG 93
Cdd:cd03169    8 DFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTaIHDFPGWQTYTEKPGHRFAVTADFDEV---DPDDYDALVIPG 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 494018428  94 GfGAAKNLtdfavngaecSINTHVASACRAFAQARKPAGYLCIAPAI 140
Cdd:cd03169   85 G-RAPEYL----------RLDEKVLAIVRHFAEANKPVAAICHGPQI 120
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 80-141 8.06e-03

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: 35.86  E-value: 8.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 494018428   80 KLNAEEFDAILLPGGFGAAKNLTdfavngaecsiNTHVASACRAFAQARKPAGYLCIAPAII 141
Cdd:TIGR01382  55 EVNPEEYDALVIPGGRAPEYLRL-----------NNKAVRLVREFVEKGKPVAAICHGPQLL 105
 
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