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Conserved domains on  [gi|499191597|ref|WP_010889137|]
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RidA family protein [Deinococcus radiodurans]

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

CATH:  3.30.1330.40
PubMed:  14624641

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 ...
2-124 3.51e-67

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: 198.29  E-value: 3.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597    2 KDIVQTADAPAAIGPYSQAVTFGNLVVTSGQIPLTAQ-GELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLAD 80
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499191597   81 MNEFTAMNAVYEQHFTAPYPARSTVQVARLPRDVRVEIEVLAER 124
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 ...
2-124 3.51e-67

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: 198.29  E-value: 3.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597    2 KDIVQTADAPAAIGPYSQAVTFGNLVVTSGQIPLTAQ-GELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLAD 80
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499191597   81 MNEFTAMNAVYEQHFTAPYPARSTVQVARLPRDVRVEIEVLAER 124
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-124 1.89e-52

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: 161.11  E-value: 1.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597   1 MKDIVQTaDAPAAIGPYSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLAD 80
Cdd:COG0251    2 TRELINP-PAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499191597  81 MNEFTAMNAVYEQHFTAPYPARSTVQVARLPRDVRVEIEVLAER 124
Cdd:COG0251   81 MADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
9-123 8.97e-49

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


Pssm-ID: 426010  Cd Length: 117  Bit Score: 151.68  E-value: 8.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597    9 DAPAAIGPYSQAVTFGNLVVTSGQIPLTAQ-GELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADMNEFTAM 87
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDtGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499191597   88 NAVYEQHFTAP-YPARSTVQVARLPRDVRVEIEVLAE 123
Cdd:pfam01042  81 NEVYAEYFDADkAPARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
17-122 2.69e-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 [Multi-domain]  Cd Length: 107  Bit Score: 142.31  E-value: 2.69e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  17 YSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADMNEFTAMNAVYEQHFT 96
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80
                         90       100
                 ....*....|....*....|....*..
gi 499191597  97 -APYPARSTVQVARLPRDVRVEIEVLA 122
Cdd:cd00448   81 eGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
1-124 5.40e-37

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 122.48  E-value: 5.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597   1 MKDIVQTADAPAAIGPYSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLAD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499191597  81 MNEFTAMNAVYEQHF---TAPYPARSTVQVARLPRDVRVEIEVLAER 124
Cdd:PRK11401  81 LNDFATINEVYKQFFdehQATYPTRSCVQVARLPKDVKLEIEAIAVR 127
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
2-124 3.51e-67

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: 198.29  E-value: 3.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597    2 KDIVQTADAPAAIGPYSQAVTFGNLVVTSGQIPLTAQ-GELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLAD 80
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 499191597   81 MNEFTAMNAVYEQHFTAPYPARSTVQVARLPRDVRVEIEVLAER 124
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-124 1.89e-52

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: 161.11  E-value: 1.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597   1 MKDIVQTaDAPAAIGPYSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLAD 80
Cdd:COG0251    2 TRELINP-PAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 499191597  81 MNEFTAMNAVYEQHFTAPYPARSTVQVARLPRDVRVEIEVLAER 124
Cdd:COG0251   81 MADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
9-123 8.97e-49

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


Pssm-ID: 426010  Cd Length: 117  Bit Score: 151.68  E-value: 8.97e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597    9 DAPAAIGPYSQAVTFGNLVVTSGQIPLTAQ-GELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADMNEFTAM 87
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDtGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 499191597   88 NAVYEQHFTAP-YPARSTVQVARLPRDVRVEIEVLAE 123
Cdd:pfam01042  81 NEVYAEYFDADkAPARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
17-122 2.69e-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 [Multi-domain]  Cd Length: 107  Bit Score: 142.31  E-value: 2.69e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  17 YSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADMNEFTAMNAVYEQHFT 96
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80
                         90       100
                 ....*....|....*....|....*..
gi 499191597  97 -APYPARSTVQVARLPRDVRVEIEVLA 122
Cdd:cd00448   81 eGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
1-124 5.40e-37

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 122.48  E-value: 5.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597   1 MKDIVQTADAPAAIGPYSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLAD 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 499191597  81 MNEFTAMNAVYEQHF---TAPYPARSTVQVARLPRDVRVEIEVLAER 124
Cdd:PRK11401  81 LNDFATINEVYKQFFdehQATYPTRSCVQVARLPKDVKLEIEAIAVR 127
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 8.42e-29

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: 100.69  E-value: 8.42e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  17 YSQAVTFGNLVVTSGQIPltaqgELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADMNEFTAMNAVYEQHFT 96
Cdd:cd06150    3 MSQAVVHNGTVYLAGQVA-----DDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVP 77
                         90       100
                 ....*....|....*....|....*..
gi 499191597  97 APY-PARSTVQVARLPRDVRVEIEVLA 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 ...
17-122 4.89e-21

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


Pssm-ID: 100011  Cd Length: 119  Bit Score: 81.45  E-value: 4.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  17 YSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADMNEFTAMNAVYEQHFT 96
Cdd:cd06154   13 YSRAVRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFG 92
                         90       100
                 ....*....|....*....|....*..
gi 499191597  97 APYPARSTVQVARLPRD-VRVEIEVLA 122
Cdd:cd06154   93 DIRPAATMVVVSLLVDPeMLVEIEVTA 119
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
18-122 6.18e-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: 70.36  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  18 SQAVTFGNLVVTSGQIPLTaqgelvTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADMNEFTAMNAVYEQHFTA 97
Cdd:cd06155    2 SQNRTGGLLWISNVTASES------DETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDK 75
                         90       100
                 ....*....|....*....|....*.
gi 499191597  98 PYP-ARSTVQvARLPRDVRVEIEVLA 122
Cdd:cd06155   76 PNPpSRVCVE-CGLPEGCDVQLSCVA 100
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
17-124 8.02e-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: 70.37  E-value: 8.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  17 YSQAVTFGNLVVTSGQIPLTAQGElVTGGIAEQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLADM-NEFTAMNAVYEQHF 95
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDADGS-VAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEYF 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 499191597  96 TAPYPARSTVQVARLPRD-VRVEIEVLAER 124
Cdd:cd02198   82 KEPYPAWTAVGVAWLARPgLLVEIKVVAVR 111
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
9-123 1.18e-14

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: 65.56  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597   9 DAPAAIGPYSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQ--TEQVIQ-------NLRAVLAAAGTDLDRV---VKTTV 76
Cdd:cd02199    8 PAPAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTGKVGADlsVEEGQEaarlcalNALAALKAALGDLDRVkrvVRLTG 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499191597  77 FLADMNEFTAMNAV--------YEQHFTAPYPARSTVQVARLPRDVRVEIEVLAE 123
Cdd:cd02199   88 FVNSAPDFTEQPKVangasdllVEVFGEAGRHARSAVGVASLPLNAAVEVEAIVE 142
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
17-122 1.59e-11

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: 56.55  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  17 YSQAVTFGNLVVTSGQIPLTAQGELVTGGIAEQTEQVIQNLRAVLAAAG-TDLDRVVKTTVFLAD-MNE--FTAMNAVYE 92
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVELALKAAGgKGWEQVYKVNSYHVDiKNEeaFGLMVENFK 82
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499191597  93 QHFTAPYPARSTVQVARLPR-DVRVEIEVLA 122
Cdd:cd06152   83 KWMPNHQPIWTCVGVTALGLpGMRVEIEVDA 113
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
18-122 1.09e-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: 100008  Cd Length: 126  Bit Score: 55.02  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  18 SQAVTFG---NLVVTSGQIPLTAQGELVTGGIA------EQTEQVIQNLRAVLAAAGTDLDRVVKTTVFLA------DMN 82
Cdd:cd06151    2 AQAVEVPagaATIYLSGTVPAVVNASAPKGSPArygdteTQTISVLKRIETILQSQGLTMGDVVKMRVFLVadpaldGKM 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499191597  83 EFTAMNAVYEQHFTAP----YPARSTVQVARLPR-DVRVEIEVLA 122
Cdd:cd06151   82 DFAGFMKAYRQFFGTAeqpnKPARSTLQVAGLVNpGWLVEIEVVA 126
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
17-122 5.47e-05

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: 39.62  E-value: 5.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  17 YSQAVTFGNLVVTSGQIPLT-AQGELVTGGIAEQTEQVIQNLRAVLAAagTDLDRVVKTTVFLADMNEFTAMNAVYEQHF 95
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIpATMTLLEGGITLQAVLSLQHLERVAKA--MNVQWVLAAVCYVTDESSVPIARSAWSKYC 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499191597  96 TAPYPARST-------------VQVARLPRDVRVEIEVLA 122
Cdd:cd06156   79 SELDLEDESrnesddvnpplviVVVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
38-119 2.74e-03

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: 34.92  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499191597  38 QGELVTGGIAEQTEQVIQNLRAVLAAAG-----TDLDRVVKTTVFLADMNEFTAMNAVYEQHFTAPYPArSTVQVARLPR 112
Cdd:cd06153   26 HGTVHPGDVEAQTRETLENIEALLEAAGrgggaQFLADLLRLKVYLRDREDLPAVRAILAARLGPAVPA-VFLQADVCRP 104

                 ....*..
gi 499191597 113 DVRVEIE 119
Cdd:cd06153  105 DLLVEIE 111
 
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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