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Conserved domains on  [gi|647613120|ref|WP_025888534|]
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MULTISPECIES: RidA family protein [Shewanella]

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 ...
 4-127 2.74e-60

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: 180.95  E-value: 2.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120    4 KIIIATDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLD 83
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 647613120   84 LGNFATVNEIMSRYFNQPYPARAAIGVKELPKGSLVEMDGVMEL 127
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 ...
 4-127 2.74e-60

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: 180.95  E-value: 2.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120    4 KIIIATDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLD 83
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 647613120   84 LGNFATVNEIMSRYFNQPYPARAAIGVKELPKGSLVEMDGVMEL 127
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 2.20e-50

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: 156.11  E-value: 2.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   1 MAEKIIiaTDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALaGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIY 80
Cdd:COG0251    1 MTRELI--NPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGEL-GGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVY 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 647613120  81 MLDLGNFATVNEIMSRYFNQPYPARAAIGVKELPKGSLVEMDGVMEL 127
Cdd:COG0251   78 LTDMADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 11-124 3.61e-42

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: 135.12  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   11 KAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDLGNFATV 90
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 647613120   91 NEIMSRYFNQP-YPARAAIGVKELPKGSLVEMDGV 124
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, ...
 19-124 5.25e-42

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: 134.22  E-value: 5.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  19 YSQAVKVGSTVYLSGQIPLDPATMaLAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDLGNFATVNEIMSRYF 98
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGE-LVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*..
gi 647613120  99 -NQPYPARAAIGVKELPKGSLVEMDGV 124
Cdd:cd00448   80 gEGPPPARTAVGVAALPPGALVEIEAI 106
PRK11401 PRK11401
enamine/imine deaminase;
4-124 1.33e-27

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 98.60  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   4 KIIIATDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAgDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLD 83
Cdd:PRK11401   2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 647613120  84 LGNFATVNEIMSRYFNQ---PYPARAAIGVKELPKGSLVEMDGV 124
Cdd:PRK11401  81 LNDFATINEVYKQFFDEhqaTYPTRSCVQVARLPKDVKLEIEAI 124
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 4-127 2.74e-60

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: 180.95  E-value: 2.74e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120    4 KIIIATDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLD 83
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 647613120   84 LGNFATVNEIMSRYFNQPYPARAAIGVKELPKGSLVEMDGVMEL 127
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 2.20e-50

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: 156.11  E-value: 2.20e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   1 MAEKIIiaTDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALaGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIY 80
Cdd:COG0251    1 MTRELI--NPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGEL-GGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVY 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 647613120  81 MLDLGNFATVNEIMSRYFNQPYPARAAIGVKELPKGSLVEMDGVMEL 127
Cdd:COG0251   78 LTDMADFAAVNEVYAEYFGEGRPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 11-124 3.61e-42

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: 135.12  E-value: 3.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   11 KAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDLGNFATV 90
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 647613120   91 NEIMSRYFNQP-YPARAAIGVKELPKGSLVEMDGV 124
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, ...
 19-124 5.25e-42

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: 134.22  E-value: 5.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  19 YSQAVKVGSTVYLSGQIPLDPATMaLAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDLGNFATVNEIMSRYF 98
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGE-LVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*..
gi 647613120  99 -NQPYPARAAIGVKELPKGSLVEMDGV 124
Cdd:cd00448   80 gEGPPPARTAVGVAALPPGALVEIEAI 106
PRK11401 PRK11401
enamine/imine deaminase;
4-124 1.33e-27

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 98.60  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   4 KIIIATDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAgDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLD 83
Cdd:PRK11401   2 KKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 647613120  84 LGNFATVNEIMSRYFNQ---PYPARAAIGVKELPKGSLVEMDGV 124
Cdd:PRK11401  81 LNDFATINEVYKQFFDEhqaTYPTRSCVQVARLPKDVKLEIEAI 124
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 19-120 6.19e-27

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: 96.18  E-value: 6.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  19 YSQAVKVGSTVYLSGQIPLDPATMAlaGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDL-GNFATVNEIMSRY 97
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDADGSV--AEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEY 80

                         90       100
                 ....*....|....*....|....
gi 647613120  98 FNQPYPARAAIGVKEL-PKGSLVE 120
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 ...
 19-120 6.28e-17

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: 70.66  E-value: 6.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  19 YSQAVKVGSTVYLSGQIPLDPATMaLAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDLGNFATVNEIMSRYF 98
Cdd:cd06154   13 YSRAVRVGNWVFVSGTTGYDYDGM-VMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVF 91

                         90       100
                 ....*....|....*....|...
gi 647613120  99 NQPYPARAAIGVKELPK-GSLVE 120
Cdd:cd06154   92 GDIRPAATMVVVSLLVDpEMLVE 114
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 19-120 1.22e-15

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: 67.35  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  19 YSQAVKVGSTVYLSGQIPLDPATMALAGDDFETQVV-------RVFDNLK------AVCEAAGGSMADIVkLNIYMLDLG 85
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVlslqhleRVAKAMNvqwvlaAVCYVTDESSVPIA-RSAWSKYCS 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 647613120  86 NFATVNEIMSRYfNQPYPARAAIGVKELPKGSLVE 120
Cdd:cd06156   80 ELDLEDESRNES-DDVNPPLVIVVVPELPRGALVE 113
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 19-121 5.75e-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: 100007  Cd Length: 105  Bit Score: 62.94  E-value: 5.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  19 YSQAVKVGSTVYLSGQIPLDPatmalaGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDLGNFATVNEIMSRYF 98
Cdd:cd06150    3 MSQAVVHNGTVYLAGQVADDT------SADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWV 76

                         90       100
                 ....*....|....*....|....
gi 647613120  99 -NQPYPARAAIGVKELPKGSLVEM 121
Cdd:cd06150   77 pPGHAPARACVEAKLADPGYLVEI 100
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 19-114 1.45e-13

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


Pssm-ID: 100009  Cd Length: 114  Bit Score: 61.94  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  19 YSQAVKVGSTVYLSGQIPLDPATMALAgDDFETQVVRVFDNLKAVCEAAGG-SMADIVKLNIYMLDLGN---FATVNEIM 94
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGWDPDTGKIP-EDLEEEIDQAFDNVELALKAAGGkGWEQVYKVNSYHVDIKNeeaFGLMVENF 81

                         90       100
                 ....*....|....*....|
gi 647613120  95 SRYFNQPYPARAAIGVKELP 114
Cdd:cd06152   82 KKWMPNHQPIWTCVGVTALG 101
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 45-122 5.52e-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: 5.52e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 647613120  45 AGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYMLDLGNFATVNEIMSRYFNQPYP-ARAAIGVKeLPKGSLVEMD 122
Cdd:cd06155   20 SDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPpSRVCVECG-LPEGCDVQLS 97
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-124 4.27e-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: 50.78  E-value: 4.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  20 SQAVKVG---STVYLSGQIP--LD---PATMALAGDDFETQVVRVFDNLKAVCEAAGGSMADIVKLNIYM------LDLG 85
Cdd:cd06151    2 AQAVEVPagaATIYLSGTVPavVNasaPKGSPARYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLvadpalDGKM 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 647613120  86 NFATVNEIMSRYFN---QP-YPARAAIGVKELPK-GSLVEMDGV 124
Cdd:cd06151   82 DFAGFMKAYRQFFGtaeQPnKPARSTLQVAGLVNpGWLVEIEVV 125
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 7-126 5.70e-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: 100006  Cd Length: 142  Bit Score: 48.23  E-value: 5.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   7 IATDKAPAAIGTYSQAVKVGSTVYLSGQIPLDPATMALAG---DDFETQ---------VVRVFDNLKAVCeaagGSM--- 71
Cdd:cd02199    4 LELPPAPAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTGkvgADLSVEegqeaarlcALNALAALKAAL----GDLdrv 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 647613120  72 ADIVKLNIYMLDLGNF----ATVN---EIMSRYF-NQPYPARAAIGVKELPKGSLVEMDGVME 126
Cdd:cd02199   80 KRVVRLTGFVNSAPDFteqpKVANgasDLLVEVFgEAGRHARSAVGVASLPLNAAVEVEAIVE 142
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 26-124 4.83e-04

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: 37.24  E-value: 4.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120  26 GSTVYLSGQIPLDPATMALAGDdFETQVVRVFDNLKAVCEAAGGSM-----ADIVKLNIYMLDLGNFATVNEIMSRYFNQ 100
Cdd:cd06153   12 RTHLFISGTASIVGHGTVHPGD-VEAQTRETLENIEALLEAAGRGGgaqflADLLRLKVYLRDREDLPAVRAILAARLGP 90

                         90       100
                 ....*....|....*....|....*..
gi 647613120 101 PYPA---RAAIGVKELpkgsLVEMDGV 124
Cdd:cd06153   91 AVPAvflQADVCRPDL----LVEIEAV 113
YjgF_endoribonc pfam14588
YjgF/chorismate_mutase-like, putative endoribonuclease; YjgF_Endoribonuc is a putative ...
 11-83 8.59e-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: 34.14  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 647613120   11 KAPAAIGTYSQAVKVGSTVYLSGQIPLDPATM---ALAGDDFETQ------VVRVFDNLKAVCEAAgGSMADIVKlnIYM 81
Cdd:pfam14588  13 EPAAALGAYEPWAIVANFITTSFQFPFDGEKLlhqGLLGADVSTQdgiaaaRLAALNAIAQLAEAA-GELANIKQ--IIR 89


                  ..
gi 647613120   82 LD 83
Cdd:pfam14588  90 LD 91
 
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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