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Conserved domains on  [gi|489319394|ref|WP_003226738|]
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MULTISPECIES: RidA family protein [Bacillaceae]

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 ...
3-124 5.23e-73

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: 212.93  E-value: 5.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394    3 KAVHTKHAPAAIGPYSQGIIVNNMFYSSGQIPLTPS-GEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADM 81
Cdd:TIGR00004   2 KIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489319394   82 EQFAEVNEVYGQYFDTHKPARSCVEVARLPKDALVEIEVIALV 124
Cdd:TIGR00004  82 NDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
3-124 5.23e-73

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: 212.93  E-value: 5.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394    3 KAVHTKHAPAAIGPYSQGIIVNNMFYSSGQIPLTPS-GEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADM 81
Cdd:TIGR00004   2 KIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489319394   82 EQFAEVNEVYGQYFDTHKPARSCVEVARLPKDALVEIEVIALV 124
Cdd:TIGR00004  82 NDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
9-122 1.85e-58

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: 175.93  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394    9 HAPAAIGPYSQGIIVNNMFYSSGQIPLTPS-GEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQFAEV 87
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLLYVSGQIPLDPKtGELVEGDVAEQTRQVLENIDAVLAAAGASLSDVVKTTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489319394   88 NEVYGQYFDTHK-PARSCVEVARLPKDALVEIEVIA 122
Cdd:pfam01042  81 NEVYAEYFDADKaPARSAVEVAALPPGALVEIEAIA 116
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-125 2.18e-56

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


Pssm-ID: 223329  Cd Length: 130  Bit Score: 171.29  E-value: 2.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394   1 MTKAVHTKHAPAAIGPYSQGIIVNNMFYSSGQIPLTPSGEMVNG-DIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIA 79
Cdd:COG0251    3 MKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGeDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFLT 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489319394  80 DMEQFAEVNEVYGQYFDT-HKPARSCVEVARLPKDALVEIEVIALVK 125
Cdd:COG0251   83 DMNDFAAMNEVYDEFFEVgGYPARSAVGVALLPPDALVEIEAIAALP 129
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
17-122 4.45e-52

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: 159.65  E-value: 4.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  17 YSQGIIVNNMFYSSGQIPLTPSGEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQFAEVNEVYGQYF- 95
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFg 80
                         90       100
                 ....*....|....*....|....*..
gi 489319394  96 DTHKPARSCVEVARLPKDALVEIEVIA 122
Cdd:cd00448   81 EGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
1-123 3.03e-40

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 130.57  E-value: 3.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394   1 MTKAVHTKHAPAAIGPYSQGIIVNNMFYSSGQIPLTPSGEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIAD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489319394  81 MEQFAEVNEVYGQYFDTHK---PARSCVEVARLPKDALVEIEVIAL 123
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIAV 126
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
3-124 5.23e-73

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: 212.93  E-value: 5.23e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394    3 KAVHTKHAPAAIGPYSQGIIVNNMFYSSGQIPLTPS-GEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADM 81
Cdd:TIGR00004   2 KIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDL 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 489319394   82 EQFAEVNEVYGQYFDTHKPARSCVEVARLPKDALVEIEVIALV 124
Cdd:TIGR00004  82 NDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
9-122 1.85e-58

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: 175.93  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394    9 HAPAAIGPYSQGIIVNNMFYSSGQIPLTPS-GEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQFAEV 87
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLLYVSGQIPLDPKtGELVEGDVAEQTRQVLENIDAVLAAAGASLSDVVKTTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 489319394   88 NEVYGQYFDTHK-PARSCVEVARLPKDALVEIEVIA 122
Cdd:pfam01042  81 NEVYAEYFDADKaPARSAVEVAALPPGALVEIEAIA 116
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-125 2.18e-56

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


Pssm-ID: 223329  Cd Length: 130  Bit Score: 171.29  E-value: 2.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394   1 MTKAVHTKHAPAAIGPYSQGIIVNNMFYSSGQIPLTPSGEMVNG-DIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIA 79
Cdd:COG0251    3 MKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGeDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFLT 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 489319394  80 DMEQFAEVNEVYGQYFDT-HKPARSCVEVARLPKDALVEIEVIALVK 125
Cdd:COG0251   83 DMNDFAAMNEVYDEFFEVgGYPARSAVGVALLPPDALVEIEAIAALP 129
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
17-122 4.45e-52

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: 159.65  E-value: 4.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  17 YSQGIIVNNMFYSSGQIPLTPSGEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQFAEVNEVYGQYF- 95
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFg 80
                         90       100
                 ....*....|....*....|....*..
gi 489319394  96 DTHKPARSCVEVARLPKDALVEIEVIA 122
Cdd:cd00448   81 EGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
1-123 3.03e-40

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 130.57  E-value: 3.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394   1 MTKAVHTKHAPAAIGPYSQGIIVNNMFYSSGQIPLTPSGEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIAD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 489319394  81 MEQFAEVNEVYGQYFDTHK---PARSCVEVARLPKDALVEIEVIAL 123
Cdd:PRK11401  81 LNDFATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIAV 126
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
17-122 3.15e-28

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: 99.15  E-value: 3.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  17 YSQGIIVNNMFYSSGQIPLTPSGemvngDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQFAEVNEVYGQYFD 96
Cdd:cd06150    3 MSQAVVHNGTVYLAGQVADDTSA-----DITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVP 77
                         90       100
                 ....*....|....*....|....*..
gi 489319394  97 T-HKPARSCVEVARLPKDALVEIEVIA 122
Cdd:cd06150   78 PgHAPARACVEAKLADPGYLVEIVVTA 104
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
12-122 9.73e-26

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: 93.39  E-value: 9.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  12 AAIGpYSQGIIVNNMFYSSGQIPLTPSGEMVNGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQFAEVNEVY 91
Cdd:cd06154    9 EQAG-YSRAVRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAH 87
                         90       100       110
                 ....*....|....*....|....*....|..
gi 489319394  92 GQYFDTHKPARSCVEVARLPKD-ALVEIEVIA 122
Cdd:cd06154   88 GEVFGDIRPAATMVVVSLLVDPeMLVEIEVTA 119
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
17-122 3.24e-23

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: 86.55  E-value: 3.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  17 YSQGIIVNNMFYSSGQIPLTPSGEMVnGDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADM-EQFAEVNEVYGQYF 95
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDADGSVA-EDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEYF 81
                         90       100
                 ....*....|....*....|....*...
gi 489319394  96 DTHKPARSCVEVARLPKDA-LVEIEVIA 122
Cdd:cd02198   82 KEPYPAWTAVGVAWLARPGlLVEIKVVA 109
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
23-123 2.91e-21

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: 81.15  E-value: 2.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  23 VNNMFYSSGQIPLTPSGemvngDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQFAEVNEVYGQYFDTHKP-A 101
Cdd:cd06155    6 TGGLLWISNVTASESDE-----TVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPpS 80
                         90       100
                 ....*....|....*....|..
gi 489319394 102 RSCVEvARLPKDALVEIEVIAL 123
Cdd:cd06155   81 RVCVE-CGLPEGCDVQLSCVAA 101
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
26-122 2.42e-15

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: 66.96  E-value: 2.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  26 MFYSSGQIP--LTPSGEMVN----GDIKEQTHQVFSNLKAVLEEAGASFETVVKATVFIADMEQ------FAEVNEVYGQ 93
Cdd:cd06151   13 TIYLSGTVPavVNASAPKGSparyGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLVADPAldgkmdFAGFMKAYRQ 92
                         90       100       110
                 ....*....|....*....|....*....|....
gi 489319394  94 YFDT----HKPARSCVEVARLPK-DALVEIEVIA 122
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, ...
17-122 1.20e-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: 62.32  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  17 YSQGIIVNNMFYSSGQIPLTPSGEMVNGDIKEQTHQVFSNLKAVLEEAG-ASFETVVKATVF---IADMEQFAEVNEVYG 92
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVELALKAAGgKGWEQVYKVNSYhvdIKNEEAFGLMVENFK 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 489319394  93 QYFDTHKPARSCVEVARLPKDAL-VEIEVIA 122
Cdd:cd06152   83 KWMPNHQPIWTCVGVTALGLPGMrVEIEVDA 113
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
17-122 1.91e-10

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: 53.87  E-value: 1.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  17 YSQGIIVNNMFYSSGQIPLTP-SGEMVNGDIKEQTHQVFSNLKAVLEEAGASfeTVVKATVFIADMEQFAEVNEVYGQYF 95
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPaTMTLLEGGITLQAVLSLQHLERVAKAMNVQ--WVLAAVCYVTDESSVPIARSAWSKYC 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 489319394  96 DTHKPARS-------------CVEVARLPKDALVEIEVIA 122
Cdd:cd06156   79 SELDLEDEsrnesddvnpplvIVVVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
10-122 2.91e-10

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: 54.00  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  10 APAAIGPYSQGIIVNNMFYSSGQIPLTPSGEMVNG---------DIKEQTHQVFSNLKAVLEEAGASF---ETVVKATVF 77
Cdd:cd02199    9 APAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTGkvgadlsveEGQEAARLCALNALAALKAALGDLdrvKRVVRLTGF 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489319394  78 IADMEQFAE-----------VNEVYGqyfDTHKPARSCVEVARLPKDALVEIEVIA 122
Cdd:cd02199   89 VNSAPDFTEqpkvangasdlLVEVFG---EAGRHARSAVGVASLPLNAAVEVEAIV 141
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
26-122 2.09e-07

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: 46.10  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489319394  26 MFYSSGQIPLTPSGEMVNGDIKEQTHQVFSNLKAVLEEAGAS-----FETVVKATVFIADMEQFAEVNEVYGQYFDTHKP 100
Cdd:cd06153   14 HLFISGTASIVGHGTVHPGDVEAQTRETLENIEALLEAAGRGggaqfLADLLRLKVYLRDREDLPAVRAILAARLGPAVP 93
                         90       100
                 ....*....|....*....|....
gi 489319394 101 ArSCV--EVARlpKDALVEIEVIA 122
Cdd:cd06153   94 A-VFLqaDVCR--PDLLVEIEAVA 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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