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Conserved domains on  [gi|1449703277|ref|WP_115872859|]
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RidA family protein [Enterococcus pseudoavium]

Protein Classification

RidA family protein( domain architecture ID 10000806)

RidA (reactive intermediate/imine deaminase A) family protein similar to Pseudomonas sp. 2-aminomuconate deaminase that hydrolyzes 2-aminomuconate to 4-oxalocrotonate, and releases ammonia in the modified meta-cleavage pathway by forming various compounds including acetaldehyde, pyruvic acid, acetyl-CoA, and succinate, that may enter the Krebs cycle

CATH:  3.30.1330.40
PubMed:  14624641|22094463|25975565
SCOP:  3001733

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 5-115 2.08e-42

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: 135.69  E-value: 2.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   5 PKSIGPYSAYRRNGNFLVTSGQLPINPETNQIEATtVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQ 84
Cdd:COG0251    11 PAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGD-IEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNE 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1449703277  85 AFEEKLAAPYPARTAIEISKLPMDALVEIEA 115
Cdd:COG0251    90 VYAEYFGEGRPARTAVGVAALPKGALVEIEA 120
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 5-115 2.08e-42

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: 135.69  E-value: 2.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   5 PKSIGPYSAYRRNGNFLVTSGQLPINPETNQIEATtVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQ 84
Cdd:COG0251    11 PAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGD-IEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNE 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1449703277  85 AFEEKLAAPYPARTAIEISKLPMDALVEIEA 115
Cdd:COG0251    90 VYAEYFGEGRPARTAVGVAALPKGALVEIEA 120
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 2-118 4.24e-40

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: 129.72  E-value: 4.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   2 KQLPKSIGPYSAYRRNGNFLVTSGQLPINPETNQIEATTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSE 81
Cdd:TIGR00004   7 DKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAE 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1449703277  82 VNQAFEEKLAAPYPARTAIEISKLPMDALVEIEALVM 118
Cdd:TIGR00004  87 VNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAV 123
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 5-117 2.27e-37

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: 122.79  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   5 PKSIGPYSAYRRNGNFLVTSGQLPINPETNQIEATTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQ 84
Cdd:pfam01042   3 PAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNE 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1449703277  85 AFEEKLAAP-YPARTAIEISKLPMDALVEIEALV 117
Cdd:pfam01042  83 VYAEYFDADkAPARSAVGVAALPLGALVEIEAIA 116
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 11-117 8.28e-36

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: 118.43  E-value: 8.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  11 YSAYRRNGNFLVTSGQLPINPETNQIEATtVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQAFEEKL 90
Cdd:cd00448     1 YSQAVRVGNLVFVSGQIPLDPDGELVPGD-IEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                          90       100
                  ....*....|....*....|....*...
gi 1449703277  91 -AAPYPARTAIEISKLPMDALVEIEALV 117
Cdd:cd00448    80 gEGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
5-121 1.78e-24

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 90.51  E-value: 1.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   5 PKSIGPYSAYRRNGNFLVTSGQLPINPETNQIeATTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVN- 83
Cdd:PRK11401   11 PGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEI-PADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINe 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1449703277  84 --QAFEEKLAAPYPARTAIEISKLPMDALVEIEALVMGGN 121
Cdd:PRK11401   90 vyKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 5-115 2.08e-42

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: 135.69  E-value: 2.08e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   5 PKSIGPYSAYRRNGNFLVTSGQLPINPETNQIEATtVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQ 84
Cdd:COG0251    11 PAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGD-IEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNE 89

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1449703277  85 AFEEKLAAPYPARTAIEISKLPMDALVEIEA 115
Cdd:COG0251    90 VYAEYFGEGRPARTAVGVAALPKGALVEIEA 120
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 2-118 4.24e-40

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: 129.72  E-value: 4.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   2 KQLPKSIGPYSAYRRNGNFLVTSGQLPINPETNQIEATTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSE 81
Cdd:TIGR00004   7 DKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAE 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1449703277  82 VNQAFEEKLAAPYPARTAIEISKLPMDALVEIEALVM 118
Cdd:TIGR00004  87 VNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAV 123
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 5-117 2.27e-37

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: 122.79  E-value: 2.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   5 PKSIGPYSAYRRNGNFLVTSGQLPINPETNQIEATTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQ 84
Cdd:pfam01042   3 PAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNE 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1449703277  85 AFEEKLAAP-YPARTAIEISKLPMDALVEIEALV 117
Cdd:pfam01042  83 VYAEYFDADkAPARSAVGVAALPLGALVEIEAIA 116
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 11-117 8.28e-36

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: 118.43  E-value: 8.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  11 YSAYRRNGNFLVTSGQLPINPETNQIEATtVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQAFEEKL 90
Cdd:cd00448     1 YSQAVRVGNLVFVSGQIPLDPDGELVPGD-IEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                          90       100
                  ....*....|....*....|....*...
gi 1449703277  91 -AAPYPARTAIEISKLPMDALVEIEALV 117
Cdd:cd00448    80 gEGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
5-121 1.78e-24

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 90.51  E-value: 1.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   5 PKSIGPYSAYRRNGNFLVTSGQLPINPETNQIeATTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVN- 83
Cdd:PRK11401   11 PGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEI-PADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINe 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1449703277  84 --QAFEEKLAAPYPARTAIEISKLPMDALVEIEALVMGGN 121
Cdd:PRK11401   90 vyKQFFDEHQATYPTRSCVQVARLPKDVKLEIEAIAVRSA 129
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 6-115 3.23e-19

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


Pssm-ID: 100011  Cd Length: 119  Bit Score: 76.44  E-value: 3.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   6 KSIGpYSAYRRNGNFLVTSGQLPINPETNQIeATTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQA 85
Cdd:cd06154     9 EQAG-YSRAVRVGNWVFVSGTTGYDYDGMVM-PGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRA 86

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1449703277  86 FEEKLAAPYPARTAIEISKLPMD-ALVEIEA 115
Cdd:cd06154    87 HGEVFGDIRPAATMVVVSLLVDPeMLVEIEV 117
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 11-115 1.73e-16

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: 69.21  E-value: 1.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  11 YSAYRRNGNFLVTSGQLPINPETNQIEatTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSK-FSEVNQAFEEK 89
Cdd:cd02198     3 YSPAVRVGDTLFVSGQVGSDADGSVAE--DFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAhLPAFAAVKDEY 80

                          90       100
                  ....*....|....*....|....*..
gi 1449703277  90 LAAPYPARTAIEISKLPMDA-LVEIEA 115
Cdd:cd02198    81 FKEPYPAWTAVGVAWLARPGlLVEIKV 107
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 3-117 1.70e-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: 54.39  E-value: 1.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277   3 QLPKSIGPYSAYRRNGNFLVTSGQLPINPETNQI-----EATTVyEQ--------VLQCLSNIEAIVSNEGfQFEDVMKL 69
Cdd:cd02199     8 PAPAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYtgkvgADLSV-EEgqeaarlcALNALAALKAALGDLD-RVKRVVRL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1449703277  70 TVYL------TDLSK----FSEV-NQAFEEklaAPYPARTAIEISKLPMDALVEIEALV 117
Cdd:cd02199    86 TGFVnsapdfTEQPKvangASDLlVEVFGE---AGRHARSAVGVASLPLNAAVEVEAIV 141
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 15-117 4.15e-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 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: 52.64  E-value: 4.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  15 RRNGNFLVTSGQLPINPETnqieatTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQAFEEKLAAPY 94
Cdd:cd06155     4 NRTGGLLWISNVTASESDE------TVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPN 77

                          90       100
                  ....*....|....*....|....
gi 1449703277  95 P-ARTAIEiSKLPMDALVEIEALV 117
Cdd:cd06155    78 PpSRVCVE-CGLPEGCDVQLSCVA 100
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 18-113 6.16e-08

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: 47.15  E-value: 6.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  18 GNFLVTSGQLPINPETnqieatTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYLTDLSKFSEVNQAFEEKLAAPY-PA 96
Cdd:cd06150    10 NGTVYLAGQVADDTSA------DITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPGHaPA 83

                          90
                  ....*....|....*..
gi 1449703277  97 RTAIEISKLPMDALVEI 113
Cdd:cd06150    84 RACVEAKLADPGYLVEI 100
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 21-115 1.81e-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: 100008  Cd Length: 126  Bit Score: 46.16  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  21 LVTSGQLP--INPE--TNQIEA-TTVYEQVLQCLSNIEAIVSNEGFQFEDVMKLTVYL------TDLSKFSEVNQAFEEK 89
Cdd:cd06151    14 IYLSGTVPavVNASapKGSPARyGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLvadpalDGKMDFAGFMKAYRQF 93

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1449703277  90 LAAP----YPARTAIEISKLPM-DALVEIEA 115
Cdd:cd06151    94 FGTAeqpnKPARSTLQVAGLVNpGWLVEIEV 124
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 11-114 3.15e-07

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: 45.38  E-value: 3.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  11 YSAYRRNGNFLVTSGQLPINPETNQIEAtTVYEQVLQCLSNIEAIVSNEGFQ-FEDVMKLTVYLTDLSKfSEVNQA---- 85
Cdd:cd06152     3 YSQAVRIGDRIEISGQGGWDPDTGKIPE-DLEEEIDQAFDNVELALKAAGGKgWEQVYKVNSYHVDIKN-EEAFGLmven 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1449703277  86 FEEKLAAPYPARTAIEISKLPMDAL-VEIE 114
Cdd:cd06152    81 FKKWMPNHQPIWTCVGVTALGLPGMrVEIE 110
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 24-116 2.00e-03

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: 35.38  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1449703277  24 SGQLPINPETNQIEATTVYEQVLQCLSNIEAIVsnEGFQFEDVMKLTVYLTDLSKFSEVNQAFEE-------------KL 90
Cdd:cd06156    14 SGQIGLIPATMTLLEGGITLQAVLSLQHLERVA--KAMNVQWVLAAVCYVTDESSVPIARSAWSKycseldledesrnES 91

                          90       100
                  ....*....|....*....|....*.
gi 1449703277  91 AAPYPARTAIEISKLPMDALVEIEAL 116
Cdd:cd06156    92 DDVNPPLVIVVVPELPRGALVEWQGI 117
YjgF_endoribonc pfam14588
YjgF/chorismate_mutase-like, putative endoribonuclease; YjgF_Endoribonuc is a putative ...
 1-33 5.89e-03

YjgF/chorismate_mutase-like, putative endoribonuclease; YjgF_Endoribonuc is a putative endoribonuclease. The structure is of beta-alpha-beta-alpha-beta(2) domains common both to bacterial chorismate mutase and to members of the YjgF family. These proteins form trimers with a three-fold symmetry with three closely-packed beta-sheets. The YjgF family is a large, widely distributed family of proteins of unknown biochemical function that are highly conserved among eubacteria, archaea and eukaryotes.


Pssm-ID: 405301  Cd Length: 148  Bit Score: 34.53  E-value: 5.89e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1449703277   1 MKQLPKSIGPYSAYRRNGNFLVTSGQLPINPET 33
Cdd:pfam14588  11 LPEPAAALGAYEPWAIVANFITTSFQFPFDGEK 43
 
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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