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Conserved domains on  [gi|90111542|ref|NP_417583|]
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putative enamine/imine deaminase [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

RidA family protein( domain architecture ID 10793569)

RidA (reactive intermediate/imine deaminase A) family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11401 PRK11401
enamine/imine deaminase;
1-129 6.70e-85

enamine/imine deaminase;


:

Pssm-ID: 105214  Cd Length: 129  Bit Score: 243.82  E-value: 6.70e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542    1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 90111542   81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
 
Name Accession Description Interval E-value
PRK11401 PRK11401
enamine/imine deaminase;
1-129 6.70e-85

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 243.82  E-value: 6.70e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542    1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 90111542   81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 2-127 2.28e-68

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: 201.75  E-value: 2.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542     2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVgGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 90111542    81 LNDFATINEVYKQFFDEHqatYPTRSCVQVARLPKDVKLEIEAIAVR 127
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEH---YPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 9.96e-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: 164.58  E-value: 9.96e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542   1 MKKIIETQrAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
Cdd:COG0251   2 TRELINPP-APAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 90111542  81 LNDFATINEVYKQFFDEHqatYPTRSCVQVARLPKDVKLEIEAIAVR 127
Cdd:COG0251  81 MADFAAVNEVYAEYFGEG---RPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 10-126 1.15e-50

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: 156.69  E-value: 1.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542    10 APGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEI-PADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATIN 88
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLvEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVN 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 90111542    89 EVYKQFFDEHqaTYPTRSCVQVARLPKDVKLEIEAIAV 126
Cdd:pfam01042  82 EVYAEYFDAD--KAPARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-125 5.06e-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: 139.62  E-value: 5.06e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  17 YVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFD 96
Cdd:cd00448   1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                        90       100
                ....*....|....*....|....*....
gi 90111542  97 EhqATYPTRSCVQVARLPKDVKLEIEAIA 125
Cdd:cd00448  81 E--GPPPARTAVGVAALPPGALVEIEAIA 107
 
Name Accession Description Interval E-value
PRK11401 PRK11401
enamine/imine deaminase;
1-129 6.70e-85

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 243.82  E-value: 6.70e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542    1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 90111542   81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 2-127 2.28e-68

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: 201.75  E-value: 2.28e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542     2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVgGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 90111542    81 LNDFATINEVYKQFFDEHqatYPTRSCVQVARLPKDVKLEIEAIAVR 127
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEH---YPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 9.96e-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: 164.58  E-value: 9.96e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542   1 MKKIIETQrAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
Cdd:COG0251   2 TRELINPP-APAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 90111542  81 LNDFATINEVYKQFFDEHqatYPTRSCVQVARLPKDVKLEIEAIAVR 127
Cdd:COG0251  81 MADFAAVNEVYAEYFGEG---RPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 10-126 1.15e-50

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: 156.69  E-value: 1.15e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542    10 APGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEI-PADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATIN 88
Cdd:pfam01042   2 APAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLvEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVN 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 90111542    89 EVYKQFFDEHqaTYPTRSCVQVARLPKDVKLEIEAIAV 126
Cdd:pfam01042  82 EVYAEYFDAD--KAPARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-125 5.06e-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: 139.62  E-value: 5.06e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  17 YVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFD 96
Cdd:cd00448   1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                        90       100
                ....*....|....*....|....*....
gi 90111542  97 EhqATYPTRSCVQVARLPKDVKLEIEAIA 125
Cdd:cd00448  81 E--GPPPARTAVGVAALPPGALVEIEAIA 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 7.16e-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: 100007  Cd Length: 105  Bit Score: 77.96  E-value: 7.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  24 GSMVFTSGQIPvcpqtGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQAtyP 103
Cdd:cd06150  10 NGTVYLAGQVA-----DDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPGHA--P 82

                        90       100
                ....*....|....*....|...
gi 90111542 104 TRSCVQVARLPKDVKLEIEAIAV 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 7.23e-19

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: 76.05  E-value: 7.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  17 YVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFD 96
Cdd:cd06154  13 YSRAVRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFG 92

                        90       100       110
                ....*....|....*....|....*....|
gi 90111542  97 EHQatyPTRSCVQVARLPKD-VKLEIEAIA 125
Cdd:cd06154  93 DIR---PAATMVVVSLLVDPeMLVEIEVTA 119
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 17-127 2.93e-17

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: 71.52  E-value: 2.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  17 YVQGVDLGSMVFTSGQIPVCPQtGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDL-NDFATINEVYKQFF 95
Cdd:cd02198   3 YSPAVRVGDTLFVSGQVGSDAD-GSVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEYF 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 90111542  96 DEhqaTYPTRSCVQVARLPKDVKL-EIEAIAVR 127
Cdd:cd02198  82 KE---PYPAWTAVGVAWLARPGLLvEIKVVAVR 111
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 38-125 2.02e-15

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: 66.51  E-value: 2.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  38 QTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQAtyPTRSCVQvARLPKDV 117
Cdd:cd06155  16 TASESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNP--PSRVCVE-CGLPEGC 92


                ....*...
gi 90111542 118 KLEIEAIA 125
Cdd:cd06155  93 DVQLSCVA 100
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 5-125 1.75e-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: 62.48  E-value: 1.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542   5 IETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCP----QTGEIPADV-----QDQARLSLENVKAIVVAAglsVGD----- 70
Cdd:cd02199   4 LELPPAPAPVGNYVPAVRTGNLLYVSGQLPRVDgklvYTGKVGADLsveegQEAARLCALNALAALKAA---LGDldrvk 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111542  71 -IIKMTVFITDLNDF----ATIN---EVYKQFFDEhqATYPTRSCVQVARLPKDVKLEIEAIA 125
Cdd:cd02199  81 rVVRLTGFVNSAPDFteqpKVANgasDLLVEVFGE--AGRHARSAVGVASLPLNAAVEVEAIV 141
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 17-125 2.81e-13

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: 61.58  E-value: 2.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  17 YVQGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAagLSVGDIIKMTVFITDLNDFATINEVYKQFF 95
Cdd:cd06156   1 YSQAIVVPKVAYISGQIGLIPATMTLLeGGITLQAVLSLQHLERVAKA--MNVQWVLAAVCYVTDESSVPIARSAWSKYC 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 90111542  96 DE--HQATYPTRSC--------VQVARLPKDVKLEIEAIA 125
Cdd:cd06156  79 SEldLEDESRNESDdvnpplviVVVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 25-125 3.42e-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: 3.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  25 SMVFTSGQIP------VCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFI------TDLNDFATINEVYK 92
Cdd:cd06151  12 ATIYLSGTVPavvnasAPKGSPARYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLvadpalDGKMDFAGFMKAYR 91

                        90       100       110
                ....*....|....*....|....*....|....*
gi 90111542  93 QFF-DEHQATYPTRSCVQVARLPKDVKL-EIEAIA 125
Cdd:cd06151  92 QFFgTAEQPNKPARSTLQVAGLVNPGWLvEIEVVA 126
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-126 8.47e-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: 60.01  E-value: 8.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  17 YVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGL-SVGDIIKMTVFITDLND---FATINEVYK 92
Cdd:cd06152   3 YSQAVRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVELALKAAGGkGWEQVYKVNSYHVDIKNeeaFGLMVENFK 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 90111542  93 QFFDEHQatyPTRSCVQVARLP-KDVKLEIEAIAV 126
Cdd:cd06152  83 KWMPNHQ---PIWTCVGVTALGlPGMRVEIEVDAI 114
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 24-125 2.49e-05

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: 40.70  E-value: 2.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111542  24 GSMVFTSGqipvcpqTGEI-------PADVQDQARLSLENVKAIVVAAGLSVG-----DIIKMTVFITDLNDFATINEVY 91
Cdd:cd06153  12 RTHLFISG-------TASIvghgtvhPGDVEAQTRETLENIEALLEAAGRGGGaqflaDLLRLKVYLRDREDLPAVRAIL 84

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 90111542  92 KQFF-DEHQATYptrscVQ--VARlpKDVKLEIEAIA 125
Cdd:cd06153  85 AARLgPAVPAVF-----LQadVCR--PDLLVEIEAVA 114
 
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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