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Conserved domains on  [gi|40807498|ref|NP_032313|]
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2-iminobutanoate/2-iminopropanoate deaminase [Mus musculus]

Protein Classification

RidA family protein (domain architecture ID 10794411)

RidA (reactive intermediate/imine deaminase A) family protein similar to 2-iminobutanoate/2-iminopropanoate deaminase, which catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
6-129 2.60e-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: 2.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498     6 RKVISTTKAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLAD 85
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 40807498    86 MNDFGTVNEIYKTYFQGSLPARAAYQVAALPRGSRVEIEAIAVQ 129
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
6-129 2.60e-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: 2.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498     6 RKVISTTKAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLAD 85
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 40807498    86 MNDFGTVNEIYKTYFQGSLPARAAYQVAALPRGSRVEIEAIAVQ 129
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
13-128 3.33e-53

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: 395828  Cd Length: 117  Bit Score: 163.22  E-value: 3.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498    13 KAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADMNDFGTV 92
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLLYVSGQIPLDPKTGELVEGDVAEQTRQVLENIDAVLAAAGASLSDVVKTTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 40807498    93 NEIYKTYFQG-SLPARAAYQVAALPRGSRVEIEAIAV 128
Cdd:pfam01042  81 NEVYAEYFDAdKAPARSAVEVAALPPGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
4-131 1.15e-48

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms];


Pssm-ID: 223329  Cd Length: 130  Bit Score: 152.03  E-value: 1.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498   4 IIRKVISTTKAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLL 83
Cdd:COG0251   2 RMKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGEDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFL 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 40807498  84 ADMNDFGTVNEIYKTYFQ-GSLPARAAYQVAALPRGSRVEIEAIAVQGP 131
Cdd:COG0251  82 TDMNDFAAMNEVYDEFFEvGGYPARSAVGVALLPPDALVEIEAIAALPE 130
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
21-127 2.36e-45

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  Cd Length: 107  Bit Score: 143.08  E-value: 2.36e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  21 YSQAVQVDRTIYISGQVGLDPSsGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADMNDFGTVNEIYKTYF 100
Cdd:cd00448   1 YSQAVRVGNLVFVSGQIPLDPD-GELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79
                        90       100
                ....*....|....*....|....*...
gi 40807498 101 QGS-LPARAAYQVAALPRGSRVEIEAIA 127
Cdd:cd00448  80 GEGpPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
5-130 3.94e-35

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 117.86  E-value: 3.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498    5 IRKVISTTKAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQlVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLA 84
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGE-IPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFIT 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 40807498   85 DMNDFGTVNEIYKTYF---QGSLPARAAYQVAALPRGSRVEIEAIAVQG 130
Cdd:PRK11401  80 DLNDFATINEVYKQFFdehQATYPTRSCVQVARLPKDVKLEIEAIAVRS 128
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
6-129 2.60e-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: 2.60e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498     6 RKVISTTKAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLAD 85
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 40807498    86 MNDFGTVNEIYKTYFQGSLPARAAYQVAALPRGSRVEIEAIAVQ 129
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
13-128 3.33e-53

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: 395828  Cd Length: 117  Bit Score: 163.22  E-value: 3.33e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498    13 KAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADMNDFGTV 92
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLLYVSGQIPLDPKTGELVEGDVAEQTRQVLENIDAVLAAAGASLSDVVKTTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 40807498    93 NEIYKTYFQG-SLPARAAYQVAALPRGSRVEIEAIAV 128
Cdd:pfam01042  81 NEVYAEYFDAdKAPARSAVEVAALPPGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
4-131 1.15e-48

Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 family [Defense mechanisms];


Pssm-ID: 223329  Cd Length: 130  Bit Score: 152.03  E-value: 1.15e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498   4 IIRKVISTTKAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLL 83
Cdd:COG0251   2 RMKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGEDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFL 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 40807498  84 ADMNDFGTVNEIYKTYFQ-GSLPARAAYQVAALPRGSRVEIEAIAVQGP 131
Cdd:COG0251  82 TDMNDFAAMNEVYDEFFEvGGYPARSAVGVALLPPDALVEIEAIAALPE 130
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
21-127 2.36e-45

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  Cd Length: 107  Bit Score: 143.08  E-value: 2.36e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  21 YSQAVQVDRTIYISGQVGLDPSsGQLVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADMNDFGTVNEIYKTYF 100
Cdd:cd00448   1 YSQAVRVGNLVFVSGQIPLDPD-GELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79
                        90       100
                ....*....|....*....|....*...
gi 40807498 101 QGS-LPARAAYQVAALPRGSRVEIEAIA 127
Cdd:cd00448  80 GEGpPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
5-130 3.94e-35

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 117.86  E-value: 3.94e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498    5 IRKVISTTKAPAAIGPYSQAVQVDRTIYISGQVGLDPSSGQlVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLA 84
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGE-IPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFIT 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 40807498   85 DMNDFGTVNEIYKTYF---QGSLPARAAYQVAALPRGSRVEIEAIAVQG 130
Cdd:PRK11401  80 DLNDFATINEVYKQFFdehQATYPTRSCVQVARLPKDVKLEIEAIAVRS 128
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
21-127 1.32e-23

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: 87.99  E-value: 1.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  21 YSQAVQVDRTIYISGQVGLDPSSGQlVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADMNDFGTVNEIYKTYF 100
Cdd:cd06154  13 YSRAVRVGNWVFVSGTTGYDYDGMV-MPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVF 91
                        90       100
                ....*....|....*....|....*...
gi 40807498 101 QGSLPARAAYQVAALPR-GSRVEIEAIA 127
Cdd:cd06154  92 GDIRPAATMVVVSLLVDpEMLVEIEVTA 119
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
21-128 6.05e-22

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: 83.36  E-value: 6.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  21 YSQAVQVDRTIYISGQVGLDPSsgqlvpGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADMNDFGTVNEIYKTYF 100
Cdd:cd06150   3 MSQAVVHNGTVYLAGQVADDTS------ADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWV 76
                        90       100
                ....*....|....*....|....*....
gi 40807498 101 Q-GSLPARAAYQVAALPRGSRVEIEAIAV 128
Cdd:cd06150  77 PpGHAPARACVEAKLADPGYLVEIVVTAA 105
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
21-128 1.26e-20

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: 80.38  E-value: 1.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  21 YSQAVQVDRTIYISGQVGLDPSSGqlVPGGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADM-NDFGTVNEIYKTY 99
Cdd:cd02198   3 YSPAVRVGDTLFVSGQVGSDADGS--VAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEY 80
                        90       100       110
                ....*....|....*....|....*....|
gi 40807498 100 FQGSLPARAAYQVAALPR-GSRVEIEAIAV 128
Cdd:cd02198  81 FKEPYPAWTAVGVAWLARpGLLVEIKVVAV 110
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
49-127 1.10e-17

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: 72.67  E-value: 1.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  49 GGVVEEAKQALKNLGEILKAAGCDFNNVVKTTVLLADMNDFGTVNEIYKTYFQGSLP-ARAAyqVAA-LPRGSRVEIEAI 126
Cdd:cd06155  22 ETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPpSRVC--VECgLPEGCDVQLSCV 99

                .
gi 40807498 127 A 127
Cdd:cd06155 100 A 100
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
21-127 1.25e-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 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: 67.74  E-value: 1.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  21 YSQAVQVDRTIYISGQVGLDPSSGQLVPGGVVEEAKQALKNLGEILKAAGCdfNNVVKTTVLLADMNDFGTVNEIYKTYF 100
Cdd:cd06156   1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNV--QWVLAAVCYVTDESSVPIARSAWSKYC 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 40807498 101 -------------QGSLPARAAYQVAALPRGSRVEIEAIA 127
Cdd:cd06156  79 seldledesrnesDDVNPPLVIVVVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
21-128 3.74e-14

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: 63.86  E-value: 3.74e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  21 YSQAVQVDRTIYISGQVGLDPSSGQlVPGGVVEEAKQALKNLGEILKAAGCD-FNNVVKTTVLLAD-MND--FGTVNEIY 96
Cdd:cd06152   3 YSQAVRIGDRIEISGQGGWDPDTGK-IPEDLEEEIDQAFDNVELALKAAGGKgWEQVYKVNSYHVDiKNEeaFGLMVENF 81
                        90       100       110
                ....*....|....*....|....*....|...
gi 40807498  97 KTYFQGSLPARAAYQVAALPR-GSRVEIEAIAV 128
Cdd:cd06152  82 KKWMPNHQPIWTCVGVTALGLpGMRVEIEVDAI 114
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
22-127 3.84e-11

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: 56.17  E-value: 3.84e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  22 SQAVQV---DRTIYISGQVG--LDPSSGQLVPGGVVEEAKQA---LKNLGEILKAAGCDFNNVVKTTVLLA------DMN 87
Cdd:cd06151   2 AQAVEVpagAATIYLSGTVPavVNASAPKGSPARYGDTETQTisvLKRIETILQSQGLTMGDVVKMRVFLVadpaldGKM 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 40807498  88 DFGTVNEIYKTYF----QGSLPARAAYQVAALPR-GSRVEIEAIA 127
Cdd:cd06151  82 DFAGFMKAYRQFFgtaeQPNKPARSTLQVAGLVNpGWLVEIEVVA 126
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
14-127 6.81e-11

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: 55.93  E-value: 6.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  14 APAAIGPYSQAVQVDRTIYISGQVGLDPssGQLVPGGVV------EEAKQALK----NLGEILKAAGCDFN---NVVKTT 80
Cdd:cd02199   9 APAPVGNYVPAVRTGNLLYVSGQLPRVD--GKLVYTGKVgadlsvEEGQEAARlcalNALAALKAALGDLDrvkRVVRLT 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 40807498  81 VLLADMNDFG----TVN---EIYKTYF--QGsLPARAAYQVAALPRGSRVEIEAIA 127
Cdd:cd02199  87 GFVNSAPDFTeqpkVANgasDLLVEVFgeAG-RHARSAVGVASLPLNAAVEVEAIV 141
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
28-127 1.56e-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: 41.09  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 40807498  28 DRTIYISGQVGLDPSsGQLVPGGVVEEAKQALKNLGEILKAAGC-----DFNNVVKTTVLLADMNDFGTVNEIYKTYFQG 102
Cdd:cd06153  12 RTHLFISGTASIVGH-GTVHPGDVEAQTRETLENIEALLEAAGRgggaqFLADLLRLKVYLRDREDLPAVRAILAARLGP 90
                        90       100
                ....*....|....*....|....*.
gi 40807498 103 SLParAAYQVAALPR-GSRVEIEAIA 127
Cdd:cd06153  91 AVP--AVFLQADVCRpDLLVEIEAVA 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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