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Conserved domains on  [gi|587244938|gb|EWV27891|]
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TdcF protein [Staphylococcus aureus T67319]

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 ...
 1-120 1.66e-63

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: 189.04  E-value: 1.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938    1 MKIINTTRLPEALGPYSHATVVNGMVYTSGQIPLNID-GHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKD 79
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 587244938   80 MNDFQKINEVYGQYFNEHKPARSCVEVARLPKDVKVEIELV 120
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAI 121
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 1-120 1.66e-63

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: 189.04  E-value: 1.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938    1 MKIINTTRLPEALGPYSHATVVNGMVYTSGQIPLNID-GHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKD 79
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 587244938   80 MNDFQKINEVYGQYFNEHKPARSCVEVARLPKDVKVEIELV 120
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAI 121
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-120 7.62e-57

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: 172.28  E-value: 7.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938   1 MKIINTTRLPEALGPYSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDM 80
Cdd:COG0251    2 TRELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDM 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 587244938  81 NDFQKINEVYGQYFNEHKPARSCVEVARLPKDVKVEIELV 120
Cdd:COG0251   82 ADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAI 121
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 10-120 1.49e-51

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: 158.62  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938   10 PEALGPYSHATVVNGMVYTSGQIPLNID-GHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMNDFQKINE 88
Cdd:pfam01042   3 PAAAGPYSQAVKAGNLVYVSGQIPLDPDtGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNE 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 587244938   89 VYGQYFNEHK-PARSCVEVARLPKDVKVEIELV 120
Cdd:pfam01042  83 VYAEYFDADKaPARSAVGVAALPLGALVEIEAI 115
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 16-120 1.51e-49

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: 153.48  E-value: 1.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  16 YSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMNDFQKINEVYGQYFN 95
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                         90       100
                 ....*....|....*....|....*.
gi 587244938  96 E-HKPARSCVEVARLPKDVKVEIELV 120
Cdd:cd00448   81 EgPPPARTAVGVAALPPGALVEIEAI 106
PRK11401 PRK11401
enamine/imine deaminase;
2-121 7.57e-39

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 127.10  E-value: 7.57e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938   2 KIINTTRLPEALGPYSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMN 81
Cdd:PRK11401   3 KIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLN 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 587244938  82 DFQKINEVYGQYFNEHK---PARSCVEVARLPKDVKVEIELVS 121
Cdd:PRK11401  83 DFATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIA 125
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 1-120 1.66e-63

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: 189.04  E-value: 1.66e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938    1 MKIINTTRLPEALGPYSHATVVNGMVYTSGQIPLNID-GHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKD 79
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPStGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 587244938   80 MNDFQKINEVYGQYFNEHKPARSCVEVARLPKDVKVEIELV 120
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAI 121
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-120 7.62e-57

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: 172.28  E-value: 7.62e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938   1 MKIINTTRLPEALGPYSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDM 80
Cdd:COG0251    2 TRELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDM 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 587244938  81 NDFQKINEVYGQYFNEHKPARSCVEVARLPKDVKVEIELV 120
Cdd:COG0251   82 ADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAI 121
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 10-120 1.49e-51

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: 158.62  E-value: 1.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938   10 PEALGPYSHATVVNGMVYTSGQIPLNID-GHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMNDFQKINE 88
Cdd:pfam01042   3 PAAAGPYSQAVKAGNLVYVSGQIPLDPDtGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNE 82

                          90       100       110
                  ....*....|....*....|....*....|...
gi 587244938   89 VYGQYFNEHK-PARSCVEVARLPKDVKVEIELV 120
Cdd:pfam01042  83 VYAEYFDADKaPARSAVGVAALPLGALVEIEAI 115
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 16-120 1.51e-49

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: 153.48  E-value: 1.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  16 YSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMNDFQKINEVYGQYFN 95
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                         90       100
                 ....*....|....*....|....*.
gi 587244938  96 E-HKPARSCVEVARLPKDVKVEIELV 120
Cdd:cd00448   81 EgPPPARTAVGVAALPPGALVEIEAI 106
PRK11401 PRK11401
enamine/imine deaminase;
2-121 7.57e-39

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 127.10  E-value: 7.57e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938   2 KIINTTRLPEALGPYSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMN 81
Cdd:PRK11401   3 KIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLN 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 587244938  82 DFQKINEVYGQYFNEHK---PARSCVEVARLPKDVKVEIELVS 121
Cdd:PRK11401  83 DFATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIA 125
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 16-117 2.82e-32

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: 109.55  E-value: 2.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  16 YSHATVVNGMVYTSGQIPLNidghiVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMNDFQKINEVYGQYF- 94
Cdd:cd06150    3 MSQAVVHNGTVYLAGQVADD-----TSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVp 77

                         90       100
                 ....*....|....*....|...
gi 587244938  95 NEHKPARSCVEVARLPKDVKVEI 117
Cdd:cd06150   78 PGHAPARACVEAKLADPGYLVEI 100
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 11-119 7.71e-25

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: 91.08  E-value: 7.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  11 EALGPYSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMNDFQKINEVY 90
Cdd:cd06154    8 EEQAGYSRAVRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAH 87

                         90       100       110
                 ....*....|....*....|....*....|
gi 587244938  91 GQYFNEHKPARSCVEVARLPKD-VKVEIEL 119
Cdd:cd06154   88 GEVFGDIRPAATMVVVSLLVDPeMLVEIEV 117
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 17-120 4.32e-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: 70.75  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  17 SHATVVNGMVYTSgqiplNIDGHIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDMNDFQKINEVYGQYFNE 96
Cdd:cd06155    1 LSQNRTGGLLWIS-----NVTASESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDK 75

                         90       100
                 ....*....|....*....|....*
gi 587244938  97 HKP-ARSCVEvARLPKDVKVEIELV 120
Cdd:cd06155   76 PNPpSRVCVE-CGLPEGCDVQLSCV 99
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 16-123 2.28e-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: 66.52  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  16 YSHATVVNGMVYTSGQIPLNIDGhIVSADVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFIKDM-NDFQKINEVYGQYF 94
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDADG-SVAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEYF 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 587244938  95 NEHKPARSCVEVARLPKD-VKVEIELVSKI 123
Cdd:cd02198   82 KEPYPAWTAVGVAWLARPgLLVEIKVVAVR 111
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 25-120 3.54e-12

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: 58.87  E-value: 3.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  25 MVYTSGQIPLNIDGHIVSA------DVQAQTKQVLENLKVVLEEAGSDLNSVAKATIFI------KDMNDFQKINEVYGQ 92
Cdd:cd06151   13 TIYLSGTVPAVVNASAPKGsparygDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLvadpalDGKMDFAGFMKAYRQ 92

                         90       100       110
                 ....*....|....*....|....*....|...
gi 587244938  93 YF----NEHKPARSCVEVARLPK-DVKVEIELV 120
Cdd:cd06151   93 FFgtaeQPNKPARSTLQVAGLVNpGWLVEIEVV 125
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 10-120 4.64e-09

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: 50.92  E-value: 4.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  10 PEALGPYSHATVVNGMVYTSGQIPLnIDGHI-----VSADV-----QAQTKQVLENLKVVLEEAGSDLNSVA---KATIF 76
Cdd:cd02199   10 PAPVGNYVPAVRTGNLLYVSGQLPR-VDGKLvytgkVGADLsveegQEAARLCALNALAALKAALGDLDRVKrvvRLTGF 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 587244938  77 IKDMNDF----QKIN---EVYGQYFNEH-KPARSCVEVARLPKDVKVEIELV 120
Cdd:cd02199   89 VNSAPDFteqpKVANgasDLLVEVFGEAgRHARSAVGVASLPLNAAVEVEAI 140
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 16-120 7.84e-08

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: 47.30  E-value: 7.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  16 YSHATVVNGMVYTSGQIPLNIDGHIVSADVQAQTKQVLENLKVVLEEAG----SDLNSVAKATIFIKDMNDFQKINEVYG 91
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVELALKAAGgkgwEQVYKVNSYHVDIKNEEAFGLMVENFK 82

                         90       100       110
                 ....*....|....*....|....*....|
gi 587244938  92 QYFNEHKPARSCVEVARLP-KDVKVEIELV 120
Cdd:cd06152   83 KWMPNHQPIWTCVGVTALGlPGMRVEIEVD 112
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 16-121 1.49e-06

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: 43.86  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  16 YSHATVVNGMVYTSGQIPL---NIDghIVSADVQAQTKQVLENLKVVLEEAGSdlNSVAKATIFIKDMNDFQKINEVYGQ 92
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLipaTMT--LLEGGITLQAVLSLQHLERVAKAMNV--QWVLAAVCYVTDESSVPIARSAWSK 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 587244938  93 YFNEHKPARS-------------CVEVARLPKDVKVEIELVS 121
Cdd:cd06156   77 YCSELDLEDEsrnesddvnpplvIVVVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 24-120 1.73e-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: 100010  Cd Length: 114  Bit Score: 43.40  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 587244938  24 GMVYTSGQIplNIDGH--IVSADVQAQTKQVLENLKVVLEEAG-----SDLNSVAKATIFIKDMNDFQKINEVYGQYFNE 96
Cdd:cd06153   13 THLFISGTA--SIVGHgtVHPGDVEAQTRETLENIEALLEAAGrgggaQFLADLLRLKVYLRDREDLPAVRAILAARLGP 90

                         90       100
                 ....*....|....*....|....*.
gi 587244938  97 HKPArSCV--EVARlpKDVKVEIELV 120
Cdd:cd06153   91 AVPA-VFLqaDVCR--PDLLVEIEAV 113
 
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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