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Conserved domains on  [gi|398364461|ref|NP_010978|]
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putative isoleucine biosynthesis protein HMF1 [Saccharomyces cerevisiae S288C]

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 ...
24-127 5.17e-56

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: 170.55  E-value: 5.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461   24 MKVNNLIFLSGQIPVTPDN-KLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHK 102
Cdd:TIGR00004  20 VKVGNTVYVSGQIPLDPSTgELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQYFDEHY 99
                          90       100
                  ....*....|....*....|....*
gi 398364461  103 PARSCVAVAALPLGVDMEMEAIAAE 127
Cdd:TIGR00004 100 PARSAVQVAALPKGVLVEIEAIAVK 124
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
24-127 5.17e-56

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: 170.55  E-value: 5.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461   24 MKVNNLIFLSGQIPVTPDN-KLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHK 102
Cdd:TIGR00004  20 VKVGNTVYVSGQIPLDPSTgELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQYFDEHY 99
                          90       100
                  ....*....|....*....|....*
gi 398364461  103 PARSCVAVAALPLGVDMEMEAIAAE 127
Cdd:TIGR00004 100 PARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
24-126 7.02e-44

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: 139.36  E-value: 7.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461   24 MKVNNLIFLSGQIPVTPDN-KLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHK 102
Cdd:pfam01042  13 VKAGNLVYVSGQIPLDPDTgKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYFDADK 92
                          90       100
                  ....*....|....*....|....*
gi 398364461  103 -PARSCVAVAALPLGVDMEMEAIAA 126
Cdd:pfam01042  93 aPARSAVGVAALPLGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
24-126 7.05e-43

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: 137.23  E-value: 7.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  24 MKVNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHKP 103
Cdd:COG0251   21 VRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFGEGRP 100
                         90       100
                 ....*....|....*....|...
gi 398364461 104 ARSCVAVAALPLGVDMEMEAIAA 126
Cdd:COG0251  101 ARTAVGVAALPKGALVEIEAIAA 123
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
24-125 4.44e-41

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: 131.91  E-value: 4.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  24 MKVNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYF-NTHK 102
Cdd:cd00448    5 VRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFgEGPP 84
                         90       100
                 ....*....|....*....|...
gi 398364461 103 PARSCVAVAALPLGVDMEMEAIA 125
Cdd:cd00448   85 PARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
26-129 1.28e-24

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 90.90  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  26 VNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHK--- 102
Cdd:PRK11401  23 LGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQaty 102
                         90       100
                 ....*....|....*....|....*..
gi 398364461 103 PARSCVAVAALPLGVDMEMEAIAAERD 129
Cdd:PRK11401 103 PTRSCVQVARLPKDVKLEIEAIAVRSA 129
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
24-127 5.17e-56

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: 170.55  E-value: 5.17e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461   24 MKVNNLIFLSGQIPVTPDN-KLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHK 102
Cdd:TIGR00004  20 VKVGNTVYVSGQIPLDPSTgELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQYFDEHY 99
                          90       100
                  ....*....|....*....|....*
gi 398364461  103 PARSCVAVAALPLGVDMEMEAIAAE 127
Cdd:TIGR00004 100 PARSAVQVAALPKGVLVEIEAIAVK 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
24-126 7.02e-44

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: 139.36  E-value: 7.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461   24 MKVNNLIFLSGQIPVTPDN-KLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHK 102
Cdd:pfam01042  13 VKAGNLVYVSGQIPLDPDTgKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYFDADK 92
                          90       100
                  ....*....|....*....|....*
gi 398364461  103 -PARSCVAVAALPLGVDMEMEAIAA 126
Cdd:pfam01042  93 aPARSAVGVAALPLGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
24-126 7.05e-43

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: 137.23  E-value: 7.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  24 MKVNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHKP 103
Cdd:COG0251   21 VRVGNLVFVSGQVPLDPDTGELGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFGEGRP 100
                         90       100
                 ....*....|....*....|...
gi 398364461 104 ARSCVAVAALPLGVDMEMEAIAA 126
Cdd:COG0251  101 ARTAVGVAALPKGALVEIEAIAA 123
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
24-125 4.44e-41

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: 131.91  E-value: 4.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  24 MKVNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYF-NTHK 102
Cdd:cd00448    5 VRVGNLVFVSGQIPLDPDGELVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFgEGPP 84
                         90       100
                 ....*....|....*....|...
gi 398364461 103 PARSCVAVAALPLGVDMEMEAIA 125
Cdd:cd00448   85 PARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
26-129 1.28e-24

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 90.90  E-value: 1.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  26 VNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHK--- 102
Cdd:PRK11401  23 LGSMVFTSGQIPVCPQTGEIPADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQaty 102
                         90       100
                 ....*....|....*....|....*..
gi 398364461 103 PARSCVAVAALPLGVDMEMEAIAAERD 129
Cdd:PRK11401 103 PTRSCVQVARLPKDVKLEIEAIAVRSA 129
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
27-126 1.12e-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: 100007  Cd Length: 105  Bit Score: 77.58  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  27 NNLIFLSGQIPVtpdnkLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYF-NTHKPAR 105
Cdd:cd06150   10 NGTVYLAGQVAD-----DTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVpPGHAPAR 84
                         90       100
                 ....*....|....*....|.
gi 398364461 106 SCVAVAALPLGVDMEMEAIAA 126
Cdd:cd06150   85 ACVEAKLADPGYLVEIVVTAA 105
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
24-125 2.73e-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: 71.82  E-value: 2.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  24 MKVNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHKP 103
Cdd:cd06154   17 VRVGNWVFVSGTTGYDYDGMVMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFGDIRP 96
                         90       100
                 ....*....|....*....|....
gi 398364461 104 ARSCVaVAALPLGVDM--EMEAIA 125
Cdd:cd06154   97 AATMV-VVSLLVDPEMlvEIEVTA 119
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
46-126 8.01e-14

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: 62.27  E-value: 8.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  46 EGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYF-NTHKPARSCVAvAALPLGVDMEMEAI 124
Cdd:cd06155   21 DETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFdKPNPPSRVCVE-CGLPEGCDVQLSCV 99

                 ..
gi 398364461 125 AA 126
Cdd:cd06155  100 AA 101
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
25-126 1.83e-13

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: 61.89  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  25 KVNNLIFLSGQIPVTPDnklveGSIADKAEQVI----QNIKNVLEASNSSLDRVVKVNIFLADI-NHFAEFNSVYAKYFN 99
Cdd:cd02198    8 RVGDTLFVSGQVGSDAD-----GSVAEDFEAQFrlafQNLGAVLEAAGCSFDDVVELTTFHVDMaAHLPAFAAVKDEYFK 82
                         90       100
                 ....*....|....*....|....*....
gi 398364461 100 THKPARSCVAVAAL--PlGVDMEMEAIAA 126
Cdd:cd02198   83 EPYPAWTAVGVAWLarP-GLLVEIKVVAV 110
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
29-125 6.36e-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: 100008  Cd Length: 126  Bit Score: 55.40  E-value: 6.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  29 LIFLSGQIPVTPDNKLVEGSIA---DKAEQ---VIQNIKNVLEASNSSLDRVVKVNIFLADINH------FAEFNSVYAK 96
Cdd:cd06151   13 TIYLSGTVPAVVNASAPKGSPArygDTETQtisVLKRIETILQSQGLTMGDVVKMRVFLVADPAldgkmdFAGFMKAYRQ 92
                         90       100       110
                 ....*....|....*....|....*....|....
gi 398364461  97 YFNT----HKPARSCVAVAALPL-GVDMEMEAIA 125
Cdd:cd06151   93 FFGTaeqpNKPARSTLQVAGLVNpGWLVEIEVVA 126
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
24-125 9.35e-11

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: 55.01  E-value: 9.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  24 MKVNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLE-ASNSSLDRVVKVNIFLADIN---HFAEFNSVYAKYFN 99
Cdd:cd06152    7 VRIGDRIEISGQGGWDPDTGKIPEDLEEEIDQAFDNVELALKaAGGKGWEQVYKVNSYHVDIKneeAFGLMVENFKKWMP 86
                         90       100
                 ....*....|....*....|....*..
gi 398364461 100 THKPARSCVAVAALPL-GVDMEMEAIA 125
Cdd:cd06152   87 NHQPIWTCVGVTALGLpGMRVEIEVDA 113
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
28-126 2.05e-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: 49.38  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364461  28 NLIFLSGQIPVTPDNKLVEG------SIAD---KAEQVIQNIKNVLEASNSSLDRV---VKVNIFLADINHFAE------ 89
Cdd:cd02199   24 NLLYVSGQLPRVDGKLVYTGkvgadlSVEEgqeAARLCALNALAALKAALGDLDRVkrvVRLTGFVNSAPDFTEqpkvan 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 398364461  90 -----FNSVYAKyfnTHKPARSCVAVAALPLGVDMEMEAIAA 126
Cdd:cd02199  104 gasdlLVEVFGE---AGRHARSAVGVASLPLNAAVEVEAIVE 142
 
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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