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Conserved domains on  [gi|2086742046|ref|XP_043139895|]
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uncharacterized protein ACHE_70216A [Aspergillus chevalieri]

Protein Classification

RidA family protein( domain architecture ID 817)

RidA (reactive intermediate/imine deaminase A) family protein

PubMed:  25975565

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YjgF_YER057c_UK114_family super family cl10015
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 6-129 4.90e-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.


The actual alignment was detected with superfamily member TIGR00004:

Pssm-ID: 447879  Cd Length: 124  Bit Score: 142.43  E-value: 4.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046   6 KKEVRSEKAPQN-QLFSQALVVGDMVYVSGNTGVDPATGNFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTS 84
Cdd:TIGR00004   1 KKIISTDKAPAAiGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2086742046  85 MSDYGLMNEAYAKFFnKQPKPIRTCVAVKELPRGTDVEMEVTALL 129
Cdd:TIGR00004  81 LNDFAEVNEVYGQYF-DEHYPARSAVQVAALPKGVLVEIEAIAVK 124
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 6-129 4.90e-45

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: 142.43  E-value: 4.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046   6 KKEVRSEKAPQN-QLFSQALVVGDMVYVSGNTGVDPATGNFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTS 84
Cdd:TIGR00004   1 KKIISTDKAPAAiGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2086742046  85 MSDYGLMNEAYAKFFnKQPKPIRTCVAVKELPRGTDVEMEVTALL 129
Cdd:TIGR00004  81 LNDFAEVNEVYGQYF-DEHYPARSAVQVAALPKGVLVEIEAIAVK 124
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 20-127 7.34e-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: 131.53  E-value: 7.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGnFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSMSDYGLMNEAYAKFF 99
Cdd:cd00448     1 YSQAVRVGNLVFVSGQIPLDPDGE-LVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                          90       100
                  ....*....|....*....|....*...
gi 2086742046 100 NKQPKPIRTCVAVKELPRGTDVEMEVTA 127
Cdd:cd00448    80 GEGPPPARTAVGVAALPPGALVEIEAIA 107
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 6-129 1.12e-39

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: 129.14  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046   6 KKEVRSEKAPQNQLFSQALVVGDMVYVSGNTGVDPATGNfVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSM 85
Cdd:COG0251     3 RELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGE-LGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2086742046  86 SDYGLMNEAYAKFFnKQPKPIRTCVAVKELPRGTDVEMEVTALL 129
Cdd:COG0251    82 ADFAAVNEVYAEYF-GEGRPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 20-127 1.85e-38

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: 125.87  E-value: 1.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGNFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSMSDYGLMNEAYAKFF 99
Cdd:pfam01042   9 YSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYF 88

                          90       100
                  ....*....|....*....|....*...
gi 2086742046 100 NKQPKPIRTCVAVKELPRGTDVEMEVTA 127
Cdd:pfam01042  89 DADKAPARSAVGVAALPLGALVEIEAIA 116
PRK11401 PRK11401
enamine/imine deaminase;
5-128 1.06e-18

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 75.87  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046   5 IKKEVRSEKAPQN-QLFSQALVVGDMVYVSGNTGVDPATGNFVEgTVVSRATQILKNISNILEATGSHIDKTVKVNIFLT 83
Cdd:PRK11401    1 MKKIIETQRAPGAiGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFIT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2086742046  84 SMSDYGLMNEAYAKFFNKQPK--PIRTCVAVKELPRGTDVEMEVTAL 128
Cdd:PRK11401   80 DLNDFATINEVYKQFFDEHQAtyPTRSCVQVARLPKDVKLEIEAIAV 126
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 6-129 4.90e-45

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: 142.43  E-value: 4.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046   6 KKEVRSEKAPQN-QLFSQALVVGDMVYVSGNTGVDPATGNFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTS 84
Cdd:TIGR00004   1 KKIISTDKAPAAiGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2086742046  85 MSDYGLMNEAYAKFFnKQPKPIRTCVAVKELPRGTDVEMEVTALL 129
Cdd:TIGR00004  81 LNDFAEVNEVYGQYF-DEHYPARSAVQVAALPKGVLVEIEAIAVK 124
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 20-127 7.34e-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: 131.53  E-value: 7.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGnFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSMSDYGLMNEAYAKFF 99
Cdd:cd00448     1 YSQAVRVGNLVFVSGQIPLDPDGE-LVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                          90       100
                  ....*....|....*....|....*...
gi 2086742046 100 NKQPKPIRTCVAVKELPRGTDVEMEVTA 127
Cdd:cd00448    80 GEGPPPARTAVGVAALPPGALVEIEAIA 107
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 6-129 1.12e-39

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: 129.14  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046   6 KKEVRSEKAPQNQLFSQALVVGDMVYVSGNTGVDPATGNfVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSM 85
Cdd:COG0251     3 RELINPPAPAPIGPYSQAVRVGNLVFVSGQVPLDPDTGE-LGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDM 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2086742046  86 SDYGLMNEAYAKFFnKQPKPIRTCVAVKELPRGTDVEMEVTALL 129
Cdd:COG0251    82 ADFAAVNEVYAEYF-GEGRPARTAVGVAALPKGALVEIEAIAAL 124
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 20-127 1.85e-38

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: 125.87  E-value: 1.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGNFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSMSDYGLMNEAYAKFF 99
Cdd:pfam01042   9 YSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEVNEVYAEYF 88

                          90       100
                  ....*....|....*....|....*...
gi 2086742046 100 NKQPKPIRTCVAVKELPRGTDVEMEVTA 127
Cdd:pfam01042  89 DADKAPARSAVGVAALPLGALVEIEAIA 116
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-127 7.73e-21

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: 80.66  E-value: 7.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPatgnfvEGTVVSRATQILKNISNILEATGShiDKT--VKVNIFLTSMSDYGLMNEAYAK 97
Cdd:cd06150     3 MSQAVVHNGTVYLAGQVADDT------SADITGQTRQVLAKIDALLAEAGS--DKSriLSATIWLADMADFAAMNAVWDA 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 2086742046  98 FFNKQPKPIRTCVAVKELPRGTDVEMEVTA 127
Cdd:cd06150    75 WVPPGHAPARACVEAKLADPGYLVEIVVTA 104
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-127 1.87e-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: 1.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGnFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSMSDYGLMNEAYAKFF 99
Cdd:cd06154    13 YSRAVRVGNWVFVSGTTGYDYDGM-VMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVF 91

                          90       100
                  ....*....|....*....|....*....
gi 2086742046 100 nKQPKPIRTCVAVKELPR-GTDVEMEVTA 127
Cdd:cd06154    92 -GDIRPAATMVVVSLLVDpEMLVEIEVTA 119
PRK11401 PRK11401
enamine/imine deaminase;
5-128 1.06e-18

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 75.87  E-value: 1.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046   5 IKKEVRSEKAPQN-QLFSQALVVGDMVYVSGNTGVDPATGNFVEgTVVSRATQILKNISNILEATGSHIDKTVKVNIFLT 83
Cdd:PRK11401    1 MKKIIETQRAPGAiGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFIT 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2086742046  84 SMSDYGLMNEAYAKFFNKQPK--PIRTCVAVKELPRGTDVEMEVTAL 128
Cdd:PRK11401   80 DLNDFATINEVYKQFFDEHQAtyPTRSCVQVARLPKDVKLEIEAIAV 126
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 20-127 4.70e-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: 68.49  E-value: 4.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGNFVEgTVVSRATQILKNISNILEATGSH-IDKTVKVNIFLTSMSD---YGLMNEAY 95
Cdd:cd06152     3 YSQAVRIGDRIEISGQGGWDPDTGKIPE-DLEEEIDQAFDNVELALKAAGGKgWEQVYKVNSYHVDIKNeeaFGLMVENF 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2086742046  96 AKFFNKQpKPIRTCVAVKELPR-GTDVEMEVTA 127
Cdd:cd06152    82 KKWMPNH-QPIWTCVGVTALGLpGMRVEIEVDA 113
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 20-127 1.26e-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: 62.28  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGnfVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLT-SMSDYGLMNEAYAKF 98
Cdd:cd02198     3 YSPAVRVGDTLFVSGQVGSDADGS--VAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVdMAAHLPAFAAVKDEY 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 2086742046  99 FnKQPKPIRTCVAVKELPR-GTDVEMEVTA 127
Cdd:cd02198    81 F-KEPYPAWTAVGVAWLARpGLLVEIKVVA 109
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 42-128 2.00e-12

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: 58.81  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  42 TGNFVEGTVVSRATQILKNISNILEATGSHIDKTVKVNIFLTSMSDYGLMNEAYAKFFNKQPKPIRTCVAVKeLPRGTDV 121
Cdd:cd06155    16 TASESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPPSRVCVECG-LPEGCDV 94


                  ....*..
gi 2086742046 122 EMEVTAL 128
Cdd:cd06155    95 QLSCVAA 101
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 20-127 3.84e-11

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: 55.80  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVGDMVYVSGNTGVDPATGNFVEGTVVSRATQILKNISNILEATGShiDKTVKVNIFLTSMSDYGLMNEAYAKFF 99
Cdd:cd06156     1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNV--QWVLAAVCYVTDESSVPIARSAWSKYC 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2086742046 100 NKQ------------PKPIRTCVAVKELPRGTDVEMEVTA 127
Cdd:cd06156    79 SELdledesrnesddVNPPLVIVVVPELPRGALVEWQGIA 118
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-127 4.45e-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: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2086742046  20 FSQALVVG---DMVYVSGnTGVDPATGNFVEGTVVSR---ATQ---ILKNISNILEATGSHIDKTVKVNIFL------TS 84
Cdd:cd06151     1 IAQAVEVPagaATIYLSG-TVPAVVNASAPKGSPARYgdtETQtisVLKRIETILQSQGLTMGDVVKMRVFLvadpalDG 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2086742046  85 MSDYGLMNEAYAKFFN--KQP-KPIRTCVAVKELPR-GTDVEMEVTA 127
Cdd:cd06151    80 KMDFAGFMKAYRQFFGtaEQPnKPARSTLQVAGLVNpGWLVEIEVVA 126
 
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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