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Conserved domains on  [gi|238861569|gb|ACR63567|]
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ketoacid-binding protein [Escherichia coli BW2952]

Protein Classification

RidA family protein( domain architecture ID 817)

RidA (reactive intermediate/imine deaminase A) family protein

PubMed:  25975565

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YjgF_YER057c_UK114_family super family cl10015
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 1-127 6.80e-67

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


The actual alignment was detected with superfamily member PRK11401:

Pssm-ID: 447879  Cd Length: 129  Bit Score: 197.98  E-value: 6.80e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569   1 MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 238861569  81 LNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVR 127
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVR 127
 
Name Accession Description Interval E-value
PRK11401 PRK11401
enamine/imine deaminase;
1-127 6.80e-67

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 197.98  E-value: 6.80e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569   1 MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 238861569  81 LNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVR 127
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVR 127
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 3-127 3.08e-65

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 193.67  E-value: 3.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569    3 KTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGE-VPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDL 81
Cdd:TIGR00004   2 KIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGElVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 238861569   82 NDFATVNATYEAFFTEHnatFPARSCVEVARLPKDVKIEIEAIAVR 127
Cdd:TIGR00004  82 NDFAEVNEVYGQYFDEH---YPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-128 3.27e-54

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 165.74  E-value: 3.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569   1 MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKD 80
Cdd:COG0251    1 MTRELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 238861569  81 LNDFATVNATYEAFFTEHnatFPARSCVEVARLPKDVKIEIEAIAVRR 128
Cdd:COG0251   81 MADFAAVNEVYAEYFGEG---RPARTAVGVAALPKGALVEIEAIAALP 125
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 9-126 1.36e-49

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 153.99  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569    9 NAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGE-VPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATV 87
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKlVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 238861569   88 NATYEAFFTEHNAtfPARSCVEVARLPKDVKIEIEAIAV 126
Cdd:pfam01042  81 NEVYAEYFDADKA--PARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-125 1.20e-44

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 141.16  E-value: 1.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  17 YVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFT 96
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                         90       100
                 ....*....|....*....|....*....
gi 238861569  97 EHNatFPARSCVEVARLPKDVKIEIEAIA 125
Cdd:cd00448   81 EGP--PPARTAVGVAALPPGALVEIEAIA 107
 
Name Accession Description Interval E-value
PRK11401 PRK11401
enamine/imine deaminase;
1-127 6.80e-67

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 197.98  E-value: 6.80e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569   1 MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 238861569  81 LNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIEIEAIAVR 127
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVR 127
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 3-127 3.08e-65

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 193.67  E-value: 3.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569    3 KTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGE-VPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDL 81
Cdd:TIGR00004   2 KIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGElVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDL 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 238861569   82 NDFATVNATYEAFFTEHnatFPARSCVEVARLPKDVKIEIEAIAVR 127
Cdd:TIGR00004  82 NDFAEVNEVYGQYFDEH---YPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-128 3.27e-54

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms]; Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440021  Cd Length: 125  Bit Score: 165.74  E-value: 3.27e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569   1 MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKD 80
Cdd:COG0251    1 MTRELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 238861569  81 LNDFATVNATYEAFFTEHnatFPARSCVEVARLPKDVKIEIEAIAVRR 128
Cdd:COG0251   81 MADFAAVNEVYAEYFGEG---RPARTAVGVAALPKGALVEIEAIAALP 125
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 9-126 1.36e-49

Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein synthesis by cleavage of mRNA. Previously thought to inhibit protein synthesis initiation. This protein may also be involved in the regulation of purine biosynthesis. YjgF (renamed RidA) family members are enamine/imine deaminases. They hydrolyze reactive intermediates released by PLP-dependent enzymes, including threonine dehydratase. YjgF also prevents inhibition of transaminase B (IlvE) in Salmonella.


Pssm-ID: 426010  Cd Length: 117  Bit Score: 153.99  E-value: 1.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569    9 NAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGE-VPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATV 87
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKlVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 238861569   88 NATYEAFFTEHNAtfPARSCVEVARLPKDVKIEIEAIAV 126
Cdd:pfam01042  81 NEVYAEYFDADKA--PARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-125 1.20e-44

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 141.16  E-value: 1.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  17 YVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFT 96
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                         90       100
                 ....*....|....*....|....*....
gi 238861569  97 EHNatFPARSCVEVARLPKDVKIEIEAIA 125
Cdd:cd00448   81 EGP--PPARTAVGVAALPPGALVEIEAIA 107
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 24-126 9.60e-21

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100007  Cd Length: 105  Bit Score: 80.27  E-value: 9.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  24 GNMIITSGQIPvnpktGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNAtfP 103
Cdd:cd06150   10 NGTVYLAGQVA-----DDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPGHA--P 82

                         90       100
                 ....*....|....*....|...
gi 238861569 104 ARSCVEVARLPKDVKIEIEAIAV 126
Cdd:cd06150   83 ARACVEAKLADPGYLVEIVVTAA 105
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 17-125 1.15e-20

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100011  Cd Length: 119  Bit Score: 80.29  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  17 YVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFT 96
Cdd:cd06154   13 YSRAVRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFG 92

                         90       100       110
                 ....*....|....*....|....*....|
gi 238861569  97 EHNatfPARSCVEVARLPKD-VKIEIEAIA 125
Cdd:cd06154   93 DIR---PAATMVVVSLLVDPeMLVEIEVTA 119
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 44-125 1.80e-16

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the first of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100012  Cd Length: 101  Bit Score: 69.21  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  44 ADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNAtfPARSCVEvARLPKDVKIEIEA 123
Cdd:cd06155   22 ETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNP--PSRVCVE-CGLPEGCDVQLSC 98


                 ..
gi 238861569 124 IA 125
Cdd:cd06155   99 VA 100
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 17-127 3.29e-14

YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100005  Cd Length: 111  Bit Score: 63.82  E-value: 3.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  17 YVQGVDLGNMIITSGQIPVNPKtGEVPADVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVF-VKDLNDFATVNATYEAFF 95
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDAD-GSVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFhVDMAAHLPAFAAVKDEYF 81

                         90       100       110
                 ....*....|....*....|....*....|...
gi 238861569  96 TEhnaTFPARSCVEVARLPKD-VKIEIEAIAVR 127
Cdd:cd02198   82 KE---PYPAWTAVGVAWLARPgLLVEIKVVAVR 111
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 26-125 3.39e-13

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100008  Cd Length: 126  Bit Score: 61.57  E-value: 3.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  26 MIITSGQIP--VNPKTGEVPA----DVAAQARQSLDNVKAIVEAAGLKVGDIVKTTVF-VKDLN-----DFATVNATYEA 93
Cdd:cd06151   13 TIYLSGTVPavVNASAPKGSParygDTETQTISVLKRIETILQSQGLTMGDVVKMRVFlVADPAldgkmDFAGFMKAYRQ 92

                         90       100       110
                 ....*....|....*....|....*....|....
gi 238861569  94 FF-TEHNATFPARSCVEVARLPK-DVKIEIEAIA 125
Cdd:cd06151   93 FFgTAEQPNKPARSTLQVAGLVNpGWLVEIEVVA 126
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-126 4.14e-13

YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100009  Cd Length: 114  Bit Score: 60.78  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  17 YVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAIVEAAGLK-VGDIVKTTVFVKDLND---FATVNATYE 92
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVELALKAAGGKgWEQVYKVNSYHVDIKNeeaFGLMVENFK 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 238861569  93 AFFTEHNATFparSCVEVARLP-KDVKIEIEAIAV 126
Cdd:cd06152   83 KWMPNHQPIW---TCVGVTALGlPGMRVEIEVDAI 114
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 10-125 9.23e-13

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100006  Cd Length: 142  Bit Score: 60.55  E-value: 9.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  10 APAAIGPYVQGVDLGNMIITSGQIPVNPK----TGEVPADV---AAQ--ARQSLDNVKAIVEAA--GL-KVGDIVKTTVF 77
Cdd:cd02199    9 APAPVGNYVPAVRTGNLLYVSGQLPRVDGklvyTGKVGADLsveEGQeaARLCALNALAALKAAlgDLdRVKRVVRLTGF 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 238861569  78 VKDLNDF----ATVNATYEAF---FTEhnATFPARSCVEVARLPKDVKIEIEAIA 125
Cdd:cd02199   89 VNSAPDFteqpKVANGASDLLvevFGE--AGRHARSAVGVASLPLNAAVEVEAIV 141
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 43-125 1.26e-08

This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100010  Cd Length: 114  Bit Score: 49.18  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  43 PADVAAQARQSLDNVKAIVEAAGLKVG-----DIVKTTVFVKDLNDFATVNATYEAFF-TEHNATFPArscVEVARlpKD 116
Cdd:cd06153   31 PGDVEAQTRETLENIEALLEAAGRGGGaqflaDLLRLKVYLRDREDLPAVRAILAARLgPAVPAVFLQ---ADVCR--PD 105


                 ....*....
gi 238861569 117 VKIEIEAIA 125
Cdd:cd06153  106 LLVEIEAVA 114
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 17-125 2.87e-07

A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine nucleotide alpha hydrolase (AANH)-like domain located N-terminal to two distinctly different YjgF-YER057c-UK114-like domains. This CD contains the second of these domains. The YjgF-YER057c-UK114 protein family is a large family of proteins present in bacteria, archaea, and eukaryotes with no definitive function. The conserved domain is similar in structure to chorismate mutase but there is no sequence similarity and no functional connection. Members of this family have been implicated in isoleucine (Yeo7, Ibm1, aldR) and purine (YjgF) biosynthesis, as well as threonine anaerobic degradation (tdcF) and mitochondrial DNA maintenance (Ibm1). This domain homotrimerizes forming a distinct intersubunit cavity that may serve as a small molecule binding site.


Pssm-ID: 100013  Cd Length: 118  Bit Score: 45.78  E-value: 2.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238861569  17 YVQGVDLGNMIITSGQIPVNPKTGE-VPADVAAQARQSLDNVKAIVEAagLKVGDIVKTTVFVKDLNDFATVNATYEAFF 95
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTlLEGGITLQAVLSLQHLERVAKA--MNVQWVLAAVCYVTDESSVPIARSAWSKYC 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 238861569  96 TEHNATFPARS----------CVEVARLPKDVKIEIEAIA 125
Cdd:cd06156   79 SELDLEDESRNesddvnpplvIVVVPELPRGALVEWQGIA 118
 
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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