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Conserved domains on  [gi|518662923|ref|WP_019824653|]
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RidA family protein [Vibrio splendidus]

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 ...
 2-126 1.73e-61

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: 184.04  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923    2 KQIIATEQAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSD 81
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 518662923   82 MENFVAFNEVYTEVFgTENAPARSCVEAARLPKDALVEVEAIAYK 126
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 ...
 2-126 1.73e-61

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: 184.04  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923    2 KQIIATEQAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSD 81
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 518662923   82 MENFVAFNEVYTEVFgTENAPARSCVEAARLPKDALVEVEAIAYK 126
Cdd:TIGR00004  81 LNDFAEVNEVYGQYF-DEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 2.98e-54

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: 165.74  E-value: 2.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923   1 MKQIIATEqAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQfVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLS 80
Cdd:COG0251    2 TRELINPP-APAPIGPYSQAVRVGNLVFVSGQVPLDPDTGE-LGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 518662923  81 DMENFVAFNEVYTEVFGtENAPARSCVEAARLPKDALVEVEAIAYKK 127
Cdd:COG0251   80 DMADFAAVNEVYAEYFG-EGRPARTAVGVAALPKGALVEIEAIAALP 125
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 9-125 1.84e-51

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: 158.62  E-value: 1.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923    9 QAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSDMENFVAF 88
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 518662923   89 NEVYTEVFGTENAPARSCVEAARLPKDALVEVEAIAY 125
Cdd:pfam01042  81 NEVYAEYFDADKAPARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-124 3.18e-47

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


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 147.32  E-value: 3.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  17 YSQGTSYGDIVYTSGQLPLVPETMqFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSDMENFVAFNEVYTEVF 96
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGE-LVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*...
gi 518662923  97 GTENAPARSCVEAARLPKDALVEVEAIA 124
Cdd:cd00448   80 GEGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
1-126 4.44e-40

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 130.19  E-value: 4.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923   1 MKQIIATEQAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQFVEgGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLS 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFIT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518662923  81 DMENFVAFNEVYTEVFGTENA--PARSCVEAARLPKDALVEVEAIAYK 126
Cdd:PRK11401  80 DLNDFATINEVYKQFFDEHQAtyPTRSCVQVARLPKDVKLEIEAIAVR 127
 
Name Accession Description Interval E-value
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 2-126 1.73e-61

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: 184.04  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923    2 KQIIATEQAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSD 81
Cdd:TIGR00004   1 KKIISTDKAPAAIGPYSQAVKVGNTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 518662923   82 MENFVAFNEVYTEVFgTENAPARSCVEAARLPKDALVEVEAIAYK 126
Cdd:TIGR00004  81 LNDFAEVNEVYGQYF-DEHYPARSAVQVAALPKGVLVEIEAIAVK 124
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-127 2.98e-54

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: 165.74  E-value: 2.98e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923   1 MKQIIATEqAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQfVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLS 80
Cdd:COG0251    2 TRELINPP-APAPIGPYSQAVRVGNLVFVSGQVPLDPDTGE-LGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 518662923  81 DMENFVAFNEVYTEVFGtENAPARSCVEAARLPKDALVEVEAIAYKK 127
Cdd:COG0251   80 DMADFAAVNEVYAEYFG-EGRPARTAVGVAALPKGALVEIEAIAALP 125
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 9-125 1.84e-51

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: 158.62  E-value: 1.84e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923    9 QAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSDMENFVAF 88
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 518662923   89 NEVYTEVFGTENAPARSCVEAARLPKDALVEVEAIAY 125
Cdd:pfam01042  81 NEVYAEYFDADKAPARSAVGVAALPLGALVEIEAIAV 117
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-124 3.18e-47

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


Pssm-ID: 100004 [Multi-domain]  Cd Length: 107  Bit Score: 147.32  E-value: 3.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  17 YSQGTSYGDIVYTSGQLPLVPETMqFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSDMENFVAFNEVYTEVF 96
Cdd:cd00448    1 YSQAVRVGNLVFVSGQIPLDPDGE-LVPGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFF 79

                         90       100
                 ....*....|....*....|....*...
gi 518662923  97 GTENAPARSCVEAARLPKDALVEVEAIA 124
Cdd:cd00448   80 GEGPPPARTAVGVAALPPGALVEIEAIA 107
PRK11401 PRK11401
enamine/imine deaminase;
1-126 4.44e-40

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 130.19  E-value: 4.44e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923   1 MKQIIATEQAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQFVEgGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLS 80
Cdd:PRK11401   1 MKKIIETQRAPGAIGPYVQGVDLGSMVFTSGQIPVCPQTGEIPA-DVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFIT 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 518662923  81 DMENFVAFNEVYTEVFGTENA--PARSCVEAARLPKDALVEVEAIAYK 126
Cdd:PRK11401  80 DLNDFATINEVYKQFFDEHQAtyPTRSCVQVARLPKDVKLEIEAIAVR 127
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 17-124 6.53e-25

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: 90.67  E-value: 6.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  17 YSQGTSYGDIVYTSGQlplVPETmqfVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSDMENFVAFNEVYTEVF 96
Cdd:cd06150    3 MSQAVVHNGTVYLAGQ---VADD---TSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWV 76

                         90       100
                 ....*....|....*....|....*...
gi 518662923  97 GTENAPARSCVEAARLPKDALVEVEAIA 124
Cdd:cd06150   77 PPGHAPARACVEAKLADPGYLVEIVVTA 104
eu_AANH_C_2 cd06156
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 17-124 9.51e-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 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: 75.44  E-value: 9.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  17 YSQGTSYGDIVYTSGQLPLVPETMQFVEGGIKEQARQSLENLKAVLEASNAGLdtVLKTTCFLSDMENFVAFNEV---YT 93
Cdd:cd06156    1 YSQAIVVPKVAYISGQIGLIPATMTLLEGGITLQAVLSLQHLERVAKAMNVQW--VLAAVCYVTDESSVPIARSAwskYC 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518662923  94 EVFGTENAPARS---------CVEAARLPKDALVEVEAIA 124
Cdd:cd06156   79 SELDLEDESRNEsddvnpplvIVVVPELPRGALVEWQGIA 118
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
 44-125 1.11e-16

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: 69.59  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  44 EGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSDMENFVAFNEVYTEVFGTENAPARSCVEaARLPKDALVEVEAI 123
Cdd:cd06155   21 DETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPPSRVCVE-CGLPEGCDVQLSCV 99


                 ..
gi 518662923 124 AY 125
Cdd:cd06155  100 AA 101
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 17-126 6.17e-16

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: 68.06  E-value: 6.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  17 YSQGTSYGDIVYTSGQLPLVPETMqfVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFLSDMEN-FVAFNEVYTEV 95
Cdd:cd02198    3 YSPAVRVGDTLFVSGQVGSDADGS--VAEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAhLPAFAAVKDEY 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 518662923  96 FGtENAPARSCVEAARLPKDA-LVEVEAIAYK 126
Cdd:cd02198   81 FK-EPYPAWTAVGVAWLARPGlLVEIKVVAVR 111
YjgF_YER057c_UK114_like_1 cd02199
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 9-124 1.13e-15

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: 68.26  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923   9 QAPAAIGPYSQGTSYGDIVYTSGQLPLVPETMQF---------VEGGiKEQARQSLENLKAVLEASNAGLDTV---LKTT 76
Cdd:cd02199    8 PAPAPVGNYVPAVRTGNLLYVSGQLPRVDGKLVYtgkvgadlsVEEG-QEAARLCALNALAALKAALGDLDRVkrvVRLT 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518662923  77 CFLSDMENF-----VA--FNEVYTEVFGTENAPARSCVEAARLPKDALVEVEAIA 124
Cdd:cd02199   87 GFVNSAPDFteqpkVAngASDLLVEVFGEAGRHARSAVGVASLPLNAAVEVEAIV 141
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 27-124 1.00e-10

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: 55.02  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  27 VYTSGQLPLV-----PETMQFVEGGIKEQARQSLENLKAVLEASNAGLDTVLKTTCFL------SDMENFVAFNEVYTEV 95
Cdd:cd06151   14 IYLSGTVPAVvnasaPKGSPARYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLvadpalDGKMDFAGFMKAYRQF 93

                         90       100       110
                 ....*....|....*....|....*....|...
gi 518662923  96 FGTE---NAPARSCVEAARLPK-DALVEVEAIA 124
Cdd:cd06151   94 FGTAeqpNKPARSTLQVAGLVNpGWLVEIEVVA 126
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 24-124 4.06e-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: 100010  Cd Length: 114  Bit Score: 48.02  E-value: 4.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  24 GDIVYTSGQLPLVP-ETMqfVEGGIKEQARQSLENLKAVLEASNAG-----LDTVLKTTCFLSDMENFVAFNEVYTEVFG 97
Cdd:cd06153   12 RTHLFISGTASIVGhGTV--HPGDVEAQTRETLENIEALLEAAGRGggaqfLADLLRLKVYLRDREDLPAVRAILAARLG 89

                         90       100
                 ....*....|....*....|....*..
gi 518662923  98 tENAPArSCVEAARLPKDALVEVEAIA 124
Cdd:cd06153   90 -PAVPA-VFLQADVCRPDLLVEIEAVA 114
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 17-125 1.68e-06

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: 43.83  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518662923  17 YSQGTSYGDIVYTSGQLPLVPETMQFVEgGIKEQARQSLENLKAVLE-ASNAGLDTVLKTTCFLSDMENFVAFnEVYTEV 95
Cdd:cd06152    3 YSQAVRIGDRIEISGQGGWDPDTGKIPE-DLEEEIDQAFDNVELALKaAGGKGWEQVYKVNSYHVDIKNEEAF-GLMVEN 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 518662923  96 FGT---ENAPARSCVEAARLPKDAL-VEVEAIAY 125
Cdd:cd06152   81 FKKwmpNHQPIWTCVGVTALGLPGMrVEIEVDAI 114
ASKHA_NBD_HSP70_HSPA4 cd11737
nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; ...
 53-123 9.43e-03

nucleotide-binding domain (NBD) of heat shock 70 kDa protein 4 (HSPA4) and similar proteins; HSPA4, also called HSP70RY, , HS24/P52, hsp70 RY, and HSPH2, or heat shock 70-related protein APG-2, responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele. HSPA4 belongs to the 105/110 kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent "client" proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD). For HSP70 chaperones, the nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. Hsp70 chaperone activity is also regulated by J-domain proteins.


Pssm-ID: 466843 [Multi-domain]  Cd Length: 381  Bit Score: 34.53  E-value: 9.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518662923  53 QSLENLKAVLEASNAglDTVLKTTCFLSDME-----NFVAFNEVYTEVFGTENAPARSCVEAARLPKDALVEVEAI 123
Cdd:cd11737  267 QECEKLKKLMSANAS--DLPLNIECFMNDIDvsgtmNRGQFEEMCADLLARVEPPLRSVLEQAKLKKEDIYAVEIV 340
 
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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