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Conserved domains on  [gi|335892424]
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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

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 ...
29-151 1.88e-67

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


:

Pssm-ID: 129116  Cd Length: 124  Bit Score: 200.21  E-value: 1.88e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424   29 LTPVSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDN-KPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLAD 107
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTgELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 335892424  108 MKNFAEFNSVYAKHFHTHKPARSCVGVASLPLNVDLEMEVIAVE 151
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 ...
29-151 1.88e-67

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 200.21  E-value: 1.88e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424   29 LTPVSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDN-KPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLAD 107
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTgELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 335892424  108 MKNFAEFNSVYAKHFHTHKPARSCVGVASLPLNVDLEMEVIAVE 151
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP. Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
37-149 2.38e-52

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: 366434  Cd Length: 116  Bit Score: 161.68  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424   37 APPAAASYSQAMKANNFVYVSGQIPYTPD-NKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFN 115
Cdd:pfam01042   2 APAAIGPYSQAVRAGNLVYVSGQIPLDPDtGELVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKTTIFLADMNDFAEVN 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 335892424  116 SVYAKHFHTHK-PARSCVGVASLPLNVDLEMEVIA 149
Cdd:pfam01042  82 EVYAEYFDAPKaPARSAVGVAALPPGALVEIEAIA 116
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
30-152 9.73e-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: 9.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  30 TPVSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQG-SISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADM 108
Cdd:COG0251    5 LIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGeDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFLTDM 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 335892424 109 KNFAEFNSVYAKHF-HTHKPARSCVGVASLPLNVDLEMEVIAVEK 152
Cdd:COG0251   85 NDFAAMNEVYDEFFeVGGYPARSAVGVALLPPDALVEIEAIAALP 129
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
44-149 5.78e-45

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


Pssm-ID: 100004  Cd Length: 107  Bit Score: 142.70  E-value: 5.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  44 YSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFNSVYAKHF- 122
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFg 80
                         90       100
                 ....*....|....*....|....*..
gi 335892424 123 HTHKPARSCVGVASLPLNVDLEMEVIA 149
Cdd:cd00448   81 EGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
32-150 6.99e-26

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 95.13  E-value: 6.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  32 VSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNF 111
Cdd:PRK11401   5 IETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDF 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 335892424 112 AEFNSVYAKHFHTHK---PARSCVGVASLPLNVDLEMEVIAV 150
Cdd:PRK11401  85 ATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIAV 126
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
29-151 1.88e-67

reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of protein synthesis intiation, then as an endoribonuclease active on single-stranded mRNA, endoribonuclease L-PSP. Members of this family, conserved in all domains of life and often with several members per bacterial genome, appear to catalyze a reaction that minimizes toxic by-products from reactions catalyzed by pyridoxal phosphate-dependent enzymes. [Cellular processes, Other]


Pssm-ID: 129116  Cd Length: 124  Bit Score: 200.21  E-value: 1.88e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424   29 LTPVSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDN-KPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLAD 107
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTgELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 335892424  108 MKNFAEFNSVYAKHFHTHKPARSCVGVASLPLNVDLEMEVIAVE 151
Cdd:TIGR00004  81 LNDFAEVNEVYGQYFDEHYPARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP. Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
37-149 2.38e-52

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: 366434  Cd Length: 116  Bit Score: 161.68  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424   37 APPAAASYSQAMKANNFVYVSGQIPYTPD-NKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFN 115
Cdd:pfam01042   2 APAAIGPYSQAVRAGNLVYVSGQIPLDPDtGELVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKTTIFLADMNDFAEVN 81
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 335892424  116 SVYAKHFHTHK-PARSCVGVASLPLNVDLEMEVIA 149
Cdd:pfam01042  82 EVYAEYFDAPKaPARSAVGVAALPPGALVEIEAIA 116
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
30-152 9.73e-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: 9.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  30 TPVSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQG-SISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADM 108
Cdd:COG0251    5 LIIATPNAPAPIGPYSQAVVAGGLVFVSGQIPLDPTGELVGGeDIEAQTRQALANIKAVLEAAGSTLDDVVKVTVFLTDM 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 335892424 109 KNFAEFNSVYAKHF-HTHKPARSCVGVASLPLNVDLEMEVIAVEK 152
Cdd:COG0251   85 NDFAAMNEVYDEFFeVGGYPARSAVGVALLPPDALVEIEAIAALP 129
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
44-149 5.78e-45

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


Pssm-ID: 100004  Cd Length: 107  Bit Score: 142.70  E-value: 5.78e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  44 YSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFNSVYAKHF- 122
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFg 80
                         90       100
                 ....*....|....*....|....*..
gi 335892424 123 HTHKPARSCVGVASLPLNVDLEMEVIA 149
Cdd:cd00448   81 EGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
32-150 6.99e-26

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 95.13  E-value: 6.99e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  32 VSTKLAPPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNF 111
Cdd:PRK11401   5 IETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDF 84
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 335892424 112 AEFNSVYAKHFHTHK---PARSCVGVASLPLNVDLEMEVIAV 150
Cdd:PRK11401  85 ATINEVYKQFFDEHQatyPTRSCVQVARLPKDVKLEIEAIAV 126
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
42-150 1.40e-22

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: 85.67  E-value: 1.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  42 ASYSQAMKANNFVYVSGQIPytpdnKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFNSVYAKH 121
Cdd:cd06150    1 ARMSQAVVHNGTVYLAGQVA-----DDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAW 75
                         90       100       110
                 ....*....|....*....|....*....|
gi 335892424 122 FHT-HKPARSCVGVASLPLNVDLEMEVIAV 150
Cdd:cd06150   76 VPPgHAPARACVEAKLADPGYLVEIVVTAA 105
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
40-151 3.86e-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: 77.21  E-value: 3.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  40 AAASYSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFNSVYA 119
Cdd:cd06154    9 EQAGYSRAVRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHG 88
                         90       100       110
                 ....*....|....*....|....*....|...
gi 335892424 120 KHFHTHKPARSCVGVASLplnVDLEMEV-IAVE 151
Cdd:cd06154   89 EVFGDIRPAATMVVVSLL---VDPEMLVeIEVT 118
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
49-149 4.77e-19

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: 76.53  E-value: 4.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  49 KANNFVYVSGQIPYTPDnkpvqGSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKNFAEFNSVYAKHFHTHK-P 127
Cdd:cd06155    5 RTGGLLWISNVTASESD-----ETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNpP 79
                         90       100
                 ....*....|....*....|..
gi 335892424 128 ARSCVGvASLPLNVDLEMEVIA 149
Cdd:cd06155   80 SRVCVE-CGLPEGCDVQLSCVA 100
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
44-150 1.47e-17

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


Pssm-ID: 100005  Cd Length: 111  Bit Score: 73.06  E-value: 1.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  44 YSQAMKANNFVYVSGQIPYTPDNKPVQGsISEKAEQVFQNVKNILAESNSSLDNIVKVNVFLADMKN-FAEFNSVYAKHF 122
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDADGSVAED-FEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAhLPAFAAVKDEYF 81
                         90       100       110
                 ....*....|....*....|....*....|
gi 335892424 123 HTHKPARSCVGVASL--PlNVDLEMEVIAV 150
Cdd:cd02198   82 KEPYPAWTAVGVAWLarP-GLLVEIKVVAV 110
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
43-150 1.01e-16

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: 70.80  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  43 SYSQAMKANNFVYVSGQIPYTPDNKPVQGSISEKAEQVFQNV-KNILAESNSSLDNIVKVNVFLADMKNfAEFNSVYAKH 121
Cdd:cd06152    2 HYSQAVRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVeLALKAAGGKGWEQVYKVNSYHVDIKN-EEAFGLMVEN 80
                         90       100       110
                 ....*....|....*....|....*....|....
gi 335892424 122 FH----THKPARSCVGVASLPL-NVDLEMEVIAV 150
Cdd:cd06152   81 FKkwmpNHQPIWTCVGVTALGLpGMRVEIEVDAI 114
RutC TIGR03610
pyrimidine utilization protein C; This protein is observed in operons extremely similar to ...
27-149 9.69e-16

pyrimidine utilization protein C; This protein is observed in operons extremely similar to that characterized in E. coli K-12 responsible for the import and catabolism of pyrimidines, primarily uracil. This protein is a member of the endoribonuclease L-PSP family defined by pfam01042.


Pssm-ID: 274677  Cd Length: 127  Bit Score: 68.72  E-value: 9.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424   27 TTLTPVSTklaPPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQ-GSISEKAEQVFQNVKNILAESNSSLDNIVKVNVFL 105
Cdd:TIGR03610   4 KVIIPAGT---SKPLAPFVPGTLADGVVYVSGTLPFDKDNNVVHvGDAAAQTRHVLETIKSVIETAGGTMDDVTFNHIFI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 335892424  106 ADMKNFAEFNSVYAKHFHTHKPARSCVGVASLPLNVDLEMEVIA 149
Cdd:TIGR03610  81 RDWADYAAINEVYAEYFPGEKPARYCIQCGLVKPDALVEIASVA 124
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
37-149 2.25e-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: 57.86  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  37 APPAAASYSQAMKANNFVYVSGQIPYTPDNKPVQGSISEK---------AEQVFQNVKNILAESNSSLD---NIVKVNVF 104
Cdd:cd02199    9 APAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYTGKVGADlsveegqeaARLCALNALAALKAALGDLDrvkRVVRLTGF 88
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 335892424 105 LADMKNFAE-----------FNSVY---AKHfhthkpARSCVGVASLPLNVDLEMEVIA 149
Cdd:cd02199   89 VNSAPDFTEqpkvangasdlLVEVFgeaGRH------ARSAVGVASLPLNAAVEVEAIV 141
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
54-149 1.92e-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: 52.32  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  54 VYVSGQIPYTPDNKPVQGSIS------EKAEQVFQNVKNILAESNSSLDNIVKVNVFL-ADMKN-----FAEFNSVYAKH 121
Cdd:cd06151   14 IYLSGTVPAVVNASAPKGSPArygdteTQTISVLKRIETILQSQGLTMGDVVKMRVFLvADPALdgkmdFAGFMKAYRQF 93
                         90       100       110
                 ....*....|....*....|....*....|...
gi 335892424 122 FHT----HKPARSCVGVASLPLNVDL-EMEVIA 149
Cdd:cd06151   94 FGTaeqpNKPARSTLQVAGLVNPGWLvEIEVVA 126
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
44-149 1.60e-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: 36.15  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 335892424  44 YSQAMKANNFVYVSGQIPYTPDN-KPVQGSISEKAEQVFQNVKNILAESNSSldNIVKVNVFLADMKNFAEFNSVYAKhF 122
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATmTLLEGGITLQAVLSLQHLERVAKAMNVQ--WVLAAVCYVTDESSVPIARSAWSK-Y 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 335892424 123 HTHKPARS--------------CVGVASLPLNVDLEMEVIA 149
Cdd:cd06156   78 CSELDLEDesrnesddvnpplvIVVVPELPRGALVEWQGIA 118
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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