NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2501683|sp|P97117|]
View 

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
3-130 1.89e-64

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: 191.74  E-value: 1.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683      3 KKVVSTTTAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDD 82
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2501683     83 IADFALVNDIYAQYFDttsvEEFPARSAVQVAALPKNAKLEIEITAMK 130
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFD----EHYPARSAVQVAALPKGVLVEIEAIAVK 124
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
3-130 1.89e-64

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: 191.74  E-value: 1.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683      3 KKVVSTTTAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDD 82
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2501683     83 IADFALVNDIYAQYFDttsvEEFPARSAVQVAALPKNAKLEIEITAMK 130
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFD----EHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
10-129 2.41e-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: 395828  Cd Length: 117  Bit Score: 155.90  E-value: 2.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683     10 TAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDIADFALV 89
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLLYVSGQIPLDPKTGELVEGDVAEQTRQVLENIDAVLAAAGASLSDVVKTTIFLADMNDFAEV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2501683     90 NDIYAQYFDTTSveeFPARSAVQVAALPKNAKLEIEITAM 129
Cdd:pfam01042  81 NEVYAEYFDADK---APARSAVEVAALPPGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-130 4.21e-44

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


Pssm-ID: 223329  Cd Length: 130  Bit Score: 140.47  E-value: 4.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683    1 MSKKVVSTTTAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFF 80
Cdd:COG0251   2 RMKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGEDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 2501683   81 DDIADFALVNDIYAQYFDttsVEEFPARSAVQVAALPKNAKLEIEITAMK 130
Cdd:COG0251  82 TDMNDFAAMNEVYDEFFE---VGGYPARSAVGVALLPPDALVEIEAIAAL 128
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
18-128 2.82e-39

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: 127.29  E-value: 2.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   18 YSQAILNDNTLYISGQIGIDPETDEFAGaTTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDIADFALVNDIYAQYF 97
Cdd:cd00448   1 YSQAVRVGNLVFVSGQIPLDPDGELVPG-DIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79
                        90       100       110
                ....*....|....*....|....*....|.
gi 2501683   98 DttsVEEFPARSAVQVAALPKNAKLEIEITA 128
Cdd:cd00448  80 G---EGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
3-130 1.52e-28

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 100.91  E-value: 1.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683     3 KKVVSTTTAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAgATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDD 82
Cdd:PRK11401   2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 2501683    83 IADFALVNDIYAQYFDTTSVeEFPARSAVQVAALPKNAKLEIEITAMK 130
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQA-TYPTRSCVQVARLPKDVKLEIEAIAVR 127
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
3-130 1.89e-64

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: 191.74  E-value: 1.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683      3 KKVVSTTTAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDD 82
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2501683     83 IADFALVNDIYAQYFDttsvEEFPARSAVQVAALPKNAKLEIEITAMK 130
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFD----EHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
10-129 2.41e-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: 395828  Cd Length: 117  Bit Score: 155.90  E-value: 2.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683     10 TAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDIADFALV 89
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLLYVSGQIPLDPKTGELVEGDVAEQTRQVLENIDAVLAAAGASLSDVVKTTIFLADMNDFAEV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2501683     90 NDIYAQYFDTTSveeFPARSAVQVAALPKNAKLEIEITAM 129
Cdd:pfam01042  81 NEVYAEYFDADK---APARSAVEVAALPPGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-130 4.21e-44

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


Pssm-ID: 223329  Cd Length: 130  Bit Score: 140.47  E-value: 4.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683    1 MSKKVVSTTTAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFF 80
Cdd:COG0251   2 RMKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGEDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFL 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 2501683   81 DDIADFALVNDIYAQYFDttsVEEFPARSAVQVAALPKNAKLEIEITAMK 130
Cdd:COG0251  82 TDMNDFAAMNEVYDEFFE---VGGYPARSAVGVALLPPDALVEIEAIAAL 128
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
18-128 2.82e-39

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: 127.29  E-value: 2.82e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   18 YSQAILNDNTLYISGQIGIDPETDEFAGaTTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDIADFALVNDIYAQYF 97
Cdd:cd00448   1 YSQAVRVGNLVFVSGQIPLDPDGELVPG-DIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79
                        90       100       110
                ....*....|....*....|....*....|.
gi 2501683   98 DttsVEEFPARSAVQVAALPKNAKLEIEITA 128
Cdd:cd00448  80 G---EGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
3-130 1.52e-28

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 100.91  E-value: 1.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683     3 KKVVSTTTAPKALGPYSQAILNDNTLYISGQIGIDPETDEFAgATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDD 82
Cdd:PRK11401   2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 2501683    83 IADFALVNDIYAQYFDTTSVeEFPARSAVQVAALPKNAKLEIEITAMK 130
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQA-TYPTRSCVQVARLPKDVKLEIEAIAVR 127
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
18-128 1.09e-16

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: 70.28  E-value: 1.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   18 YSQAILNDNTLYISGQIGIDPETDEFAGaTTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDIADFALVNDIYAQYF 97
Cdd:cd06154  13 YSRAVRVGNWVFVSGTTGYDYDGMVMPG-DAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVF 91
                        90       100       110
                ....*....|....*....|....*....|..
gi 2501683   98 DTTSveefPARSAVQVAALPK-NAKLEIEITA 128
Cdd:cd06154  92 GDIR----PAATMVVVSLLVDpEMLVEIEVTA 119
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
18-128 3.15e-16

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: 68.72  E-value: 3.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   18 YSQAILNDNTLYISGQIGIDPETDefagatTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDIADFALVNDIYAQYF 97
Cdd:cd06150   3 MSQAVVHNGTVYLAGQVADDTSAD------ITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWV 76
                        90       100       110
                ....*....|....*....|....*....|.
gi 2501683   98 DTtsvEEFPARSAVQVAALPKNAKLEIEITA 128
Cdd:cd06150  77 PP---GHAPARACVEAKLADPGYLVEIVVTA 104
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
26-128 2.48e-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: 66.13  E-value: 2.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   26 NTLYISGQigidpeTDEFAGATTAEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDIADFALVNDIYAQYFDTTSVeef 105
Cdd:cd06155   8 GLLWISNV------TASESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNP--- 78
                        90       100
                ....*....|....*....|...
gi 2501683  106 PARSAVQvAALPKNAKLEIEITA 128
Cdd:cd06155  79 PSRVCVE-CGLPEGCDVQLSCVA 100
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
18-128 7.74e-15

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: 65.36  E-value: 7.74e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   18 YSQAILNDNTLYISGQIGIDPETDEFAGATtaEQAHQIFDNIDNILHEAEFSRNDIVKAALFFDDI-ADFALVNDIYAQY 96
Cdd:cd02198   3 YSPAVRVGDTLFVSGQVGSDADGSVAEDFE--AQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEY 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 2501683   97 FDttsvEEFPARSAVQVAALPKNAKL-EIEITA 128
Cdd:cd02198  81 FK----EPYPAWTAVGVAWLARPGLLvEIKVVA 109
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
27-128 3.04e-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: 56.56  E-value: 3.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   27 TLYISGQIG--IDPETDEF---AGATTAEQAHQIFDNIDNILHEAEFSRNDIVK------AALFFDDIADFALVNDIYAQ 95
Cdd:cd06151  13 TIYLSGTVPavVNASAPKGspaRYGDTETQTISVLKRIETILQSQGLTMGDVVKmrvflvADPALDGKMDFAGFMKAYRQ 92
                        90       100       110
                ....*....|....*....|....*....|....
gi 2501683   96 YFDTTSVEEFPARSAVQVAALPKNAKL-EIEITA 128
Cdd:cd06151  93 FFGTAEQPNKPARSTLQVAGLVNPGWLvEIEVVA 126
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
18-128 5.32e-11

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: 55.41  E-value: 5.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   18 YSQAILNDNTLYISGQIGIDPET--DEFAGATT-AEQAHQifdNIDNILHeaEFSRNDIVKAALFFDDIADFALVNDIYA 94
Cdd:cd06156   1 YSQAIVVPKVAYISGQIGLIPATmtLLEGGITLqAVLSLQ---HLERVAK--AMNVQWVLAAVCYVTDESSVPIARSAWS 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 2501683   95 QYFD-TTSVEEFPARS--------AVQVAALPKNAKLEIEITA 128
Cdd:cd06156  76 KYCSeLDLEDESRNESddvnpplvIVVVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
11-128 2.73e-06

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: 43.60  E-value: 2.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   11 APKALGPYSQAILNDNTLYISGQIGIDPETDEFAG----ATTAEQAH------------QI------FDNIDNILHEAEF 68
Cdd:cd02199   9 APAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTGkvgaDLSVEEGQeaarlcalnalaALkaalgdLDRVKRVVRLTGF 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2501683   69 srndiVKAALFFDDIAdfALVN---DIYAQYFDTTSVeefPARSAVQVAALPKNAKLEIEITA 128
Cdd:cd02199  89 -----VNSAPDFTEQP--KVANgasDLLVEVFGEAGR---HARSAVGVASLPLNAAVEVEAIV 141
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
18-128 1.00e-05

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: 41.52  E-value: 1.00e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501683   18 YSQAILNDNTLYISGQIGIDPETDEFAgATTAEQAHQIFDNIDNILHEAEFSR-NDIVKAALFFDDIADfalvndiyAQY 96
Cdd:cd06152   3 YSQAVRIGDRIEISGQGGWDPDTGKIP-EDLEEEIDQAFDNVELALKAAGGKGwEQVYKVNSYHVDIKN--------EEA 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 2501683   97 FDTTsVEEF--------PARSAVQVAALP-KNAKLEIEITA 128
Cdd:cd06152  74 FGLM-VENFkkwmpnhqPIWTCVGVTALGlPGMRVEIEVDA 113
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH