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Conserved domains on  [gi|502027772|ref|WP_012698968|]
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RidA family protein [Azotobacter vinelandii]

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 ...
3-126 1.94e-70

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: 206.76  E-value: 1.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772    3 KSVINTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTD 82
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 502027772   83 LAHFAKVNEVMGRYFAQPYPARAAIGVASLPRGAQVEMDGILVL 126
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 ...
3-126 1.94e-70

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: 206.76  E-value: 1.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772    3 KSVINTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTD 82
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 502027772   83 LAHFAKVNEVMGRYFAQPYPARAAIGVASLPRGAQVEMDGILVL 126
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-127 3.02e-49

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


Pssm-ID: 223329  Cd Length: 130  Bit Score: 153.19  E-value: 3.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772   1 MSKSVINTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFL 80
Cdd:COG0251    2 RMKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGEDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502027772  81 TDLAHFAKVNEVMGRYFAQP-YPARAAIGVASLPRGAQVEMDGILVLG 127
Cdd:COG0251   82 TDMNDFAAMNEVYDEFFEVGgYPARSAVGVALLPPDALVEIEAIAALP 129
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
10-123 9.17e-48

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: 148.99  E-value: 9.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772   10 KAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDLAHFAKV 89
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 502027772   90 NEVMGRYFAQP-YPARAAIGVASLPRGAQVEMDGI 123
Cdd:pfam01042  81 NEVYAEYFDADkAPARSAVGVAALPLGALVEIEAI 115
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
18-123 4.94e-47

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: 146.93  E-value: 4.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  18 YSQAIRAGDTVYLSGQIPLDPGTmELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDLAHFAKVNEVMGRYF 97
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDG-ELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79
                         90       100
                 ....*....|....*....|....*..
gi 502027772  98 -AQPYPARAAIGVASLPRGAQVEMDGI 123
Cdd:cd00448   80 gEGPPPARTAVGVAALPPGALVEIEAI 106
PRK11401 PRK11401
enamine/imine deaminase;
3-127 5.35e-29

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 102.07  E-value: 5.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772   3 KSVINTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEgDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTD 82
Cdd:PRK11401   2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502027772  83 LAHFAKVNEVMGRYFAQ---PYPARAAIGVASLPRGAQVEMDGILVLG 127
Cdd:PRK11401  81 LNDFATINEVYKQFFDEhqaTYPTRSCVQVARLPKDVKLEIEAIAVRS 128
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
3-126 1.94e-70

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: 206.76  E-value: 1.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772    3 KSVINTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTD 82
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 502027772   83 LAHFAKVNEVMGRYFAQPYPARAAIGVASLPRGAQVEMDGILVL 126
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-127 3.02e-49

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


Pssm-ID: 223329  Cd Length: 130  Bit Score: 153.19  E-value: 3.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772   1 MSKSVINTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFL 80
Cdd:COG0251    2 RMKLIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGEDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFL 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502027772  81 TDLAHFAKVNEVMGRYFAQP-YPARAAIGVASLPRGAQVEMDGILVLG 127
Cdd:COG0251   82 TDMNDFAAMNEVYDEFFEVGgYPARSAVGVALLPPDALVEIEAIAALP 129
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
10-123 9.17e-48

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: 148.99  E-value: 9.17e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772   10 KAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDLAHFAKV 89
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 502027772   90 NEVMGRYFAQP-YPARAAIGVASLPRGAQVEMDGI 123
Cdd:pfam01042  81 NEVYAEYFDADkAPARSAVGVAALPLGALVEIEAI 115
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
18-123 4.94e-47

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: 146.93  E-value: 4.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  18 YSQAIRAGDTVYLSGQIPLDPGTmELVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDLAHFAKVNEVMGRYF 97
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDG-ELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79
                         90       100
                 ....*....|....*....|....*..
gi 502027772  98 -AQPYPARAAIGVASLPRGAQVEMDGI 123
Cdd:cd00448   80 gEGPPPARTAVGVAALPPGALVEIEAI 106
PRK11401 PRK11401
enamine/imine deaminase;
3-127 5.35e-29

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 102.07  E-value: 5.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772   3 KSVINTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELVEgDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTD 82
Cdd:PRK11401   2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 502027772  83 LAHFAKVNEVMGRYFAQ---PYPARAAIGVASLPRGAQVEMDGILVLG 127
Cdd:PRK11401  81 LNDFATINEVYKQFFDEhqaTYPTRSCVQVARLPKDVKLEIEAIAVRS 128
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
18-119 1.40e-28

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: 100.41  E-value: 1.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  18 YSQAIRAGDTVYLSGQIPLDPGTMelVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDL-AHFAKVNEVMGRY 96
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDADGS--VAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEY 80
                         90       100
                 ....*....|....*....|....
gi 502027772  97 FAQPYPARAAIGVASLPR-GAQVE 119
Cdd:cd02198   81 FKEPYPAWTAVGVAWLARpGLLVE 104
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
18-114 5.42e-24

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: 88.76  E-value: 5.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  18 YSQAIRAGDTVYLSGQIPLDPGTMElVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDLAHFAKVNEVMGRYF 97
Cdd:cd06154   13 YSRAVRVGNWVFVSGTTGYDYDGMV-MPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVF 91
                         90
                 ....*....|....*..
gi 502027772  98 AQPYPARAAIGVASLPR 114
Cdd:cd06154   92 GDIRPAATMVVVSLLVD 108
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
18-120 2.02e-18

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: 74.11  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  18 YSQAIRAGDTVYLSGQIPLDPgtmelvEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDLAHFAKVNEVMGRYF 97
Cdd:cd06150    3 MSQAVVHNGTVYLAGQVADDT------SADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWV 76
                         90       100
                 ....*....|....*....|....
gi 502027772  98 AQPY-PARAAIGVASLPRGAQVEM 120
Cdd:cd06150   77 PPGHaPARACVEAKLADPGYLVEI 100
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
18-124 2.34e-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 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: 71.98  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  18 YSQAIRAGDTVYLSGQIPLDPGTMELVEGDFEAQTVRVFENLKAVVEAAG-GSFADIVklnIFLTDLAH-------FAKV 89
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNvQWVLAAV---CYVTDESSvpiarsaWSKY 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 502027772  90 NEVMGRYFAQPYPARAAIG------VASLPRGAQVEMDGIL 124
Cdd:cd06156   78 CSELDLEDESRNESDDVNPplvivvVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
18-119 7.45e-14

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: 62.71  E-value: 7.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  18 YSQAIRAGDTVYLSGQIPLDPGTMELVEgDFEAQTVRVFENLKAVVEAAGG-SFADIVKLNIFLTDLAHfAKVNEVMGRY 96
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGWDPDTGKIPE-DLEEEIDQAFDNVELALKAAGGkGWEQVYKVNSYHVDIKN-EEAFGLMVEN 80
                         90       100
                 ....*....|....*....|....*...
gi 502027772  97 FAQPYPARA----AIGVASLPR-GAQVE 119
Cdd:cd06152   81 FKKWMPNHQpiwtCVGVTALGLpGMRVE 108
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
6-123 1.45e-11

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


Pssm-ID: 100006  Cd Length: 142  Bit Score: 57.47  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772   6 INTDKAPAAIGTYSQAIRAGDTVYLSGQIPLDPGTMELV----------EGDFEAQTVRVfeNLKAVVEAAGGSF---AD 72
Cdd:cd02199    4 LELPPAPAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTgkvgadlsveEGQEAARLCAL--NALAALKAALGDLdrvKR 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502027772  73 IVKLNIFLTDLAHF---AKV----NEVMGRYF-AQPYPARAAIGVASLPRGAQVEMDGI 123
Cdd:cd02199   82 VVRLTGFVNSAPDFteqPKVangaSDLLVEVFgEAGRHARSAVGVASLPLNAAVEVEAI 140
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
45-121 2.82e-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: 53.03  E-value: 2.82e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502027772  45 EGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFLTDLAHFAKVNEVMGRYFAQPYP-ARAAIGvASLPRGAQVEMD 121
Cdd:cd06155   21 DETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPpSRVCVE-CGLPEGCDVQLS 97
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
21-121 2.86e-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: 100008  Cd Length: 126  Bit Score: 51.17  E-value: 2.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  21 AIRAG-DTVYLSGQIP------LDPGTMElVEGDFEAQTVRVFENLKAVVEAAGGSFADIVKLNIFL------TDLAHFA 87
Cdd:cd06151    6 EVPAGaATIYLSGTVPavvnasAPKGSPA-RYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLvadpalDGKMDFA 84
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 502027772  88 KVNEVMGRYF---AQP-YPARAAIGVASLPR-GAQVEMD 121
Cdd:cd06151   85 GFMKAYRQFFgtaEQPnKPARSTLQVAGLVNpGWLVEIE 123
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
21-123 2.74e-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: 45.71  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502027772  21 AIRAGDTVYLSGQIPLDpGTMELVEGDFEAQTVRVFENLKAVVEAAGGS-----FADIVKLNIFLTDLAHFAKVNEVMGR 95
Cdd:cd06153    8 AAGGRTHLFISGTASIV-GHGTVHPGDVEAQTRETLENIEALLEAAGRGggaqfLADLLRLKVYLRDREDLPAVRAILAA 86
                         90       100
                 ....*....|....*....|....*....
gi 502027772  96 YFaqPYPARAAIGVASLPR-GAQVEMDGI 123
Cdd:cd06153   87 RL--GPAVPAVFLQADVCRpDLLVEIEAV 113
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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