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Conserved domains on  [gi|736049980|ref|WP_034195625|]
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MULTISPECIES: RidA family protein [Burkholderia]

Protein Classification

RidA family protein( domain architecture ID 10000806)

RidA (reactive intermediate/imine deaminase A) family protein similar to Pseudomonas sp. 2-aminomuconate deaminase that hydrolyzes 2-aminomuconate to 4-oxalocrotonate, and releases ammonia in the modified meta-cleavage pathway by forming various compounds including acetaldehyde, pyruvic acid, acetyl-CoA, and succinate, that may enter the Krebs cycle

CATH:  3.30.1330.40
PubMed:  14624641|22094463|25975565
SCOP:  3001733

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 28-137 1.84e-34

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: 116.82  E-value: 1.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  28 CQAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:COG0251   18 SQAVRVGNLVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFG 96

                         90       100       110
                 ....*....|....*....|....*....|
gi 736049980 108 GVYPISTGLVVSALGQpQWLMEIDVIAVIP 137
Cdd:COG0251   97 EGRPARTAVGVAALPK-GALVEIEAIAALP 125
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 28-137 1.84e-34

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: 116.82  E-value: 1.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  28 CQAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:COG0251   18 SQAVRVGNLVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFG 96

                         90       100       110
                 ....*....|....*....|....*....|
gi 736049980 108 GVYPISTGLVVSALGQpQWLMEIDVIAVIP 137
Cdd:COG0251   97 EGRPARTAVGVAALPK-GALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 28-134 1.22e-31

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: 109.19  E-value: 1.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  28 CQAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:cd00448    2 SQAVRVGNLVFVSGQIPLDPDGELVP-GDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                         90       100
                 ....*....|....*....|....*...
gi 736049980 108 -GVYPISTGLVVSALGqPQWLMEIDVIA 134
Cdd:cd00448   81 eGPPPARTAVGVAALP-PGALVEIEAIA 107
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 29-135 1.29e-24

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: 91.59  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980   29 QAVRAGNTVYVRGQVGTDFDGNLVGLGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLID-PRYREpvYREV-GKWL 106
Cdd:pfam01042  11 QAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADmNDFAE--VNEVyAEYF 88

                          90       100       110
                  ....*....|....*....|....*....|
gi 736049980  107 KGV-YPISTGLVVSALGqPQWLMEIDVIAV 135
Cdd:pfam01042  89 DADkAPARSAVGVAALP-LGALVEIEAIAV 117
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 29-135 6.00e-22

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: 84.65  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980   29 QAVRAGNTVYVRGQVGTDFD-GNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:TIGR00004  18 QAVKVGNTVYVSGQIPLDPStGELVG-GDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQYFD 96

                          90       100
                  ....*....|....*....|....*....
gi 736049980  108 GVYPISTGLVVSALgqPQ-WLMEIDVIAV 135
Cdd:TIGR00004  97 EHYPARSAVQVAAL--PKgVLVEIEAIAV 123
PRK11401 PRK11401
enamine/imine deaminase;
29-135 2.00e-03

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 36.20  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  29 QAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPR---YREPVYREVGKW 105
Cdd:PRK11401  19 QGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNdfaTINEVYKQFFDE 97

                         90       100       110
                 ....*....|....*....|....*....|
gi 736049980 106 LKGVYPISTGLVVSALGQPQWLmEIDVIAV 135
Cdd:PRK11401  98 HQATYPTRSCVQVARLPKDVKL-EIEAIAV 126
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 28-137 1.84e-34

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: 116.82  E-value: 1.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  28 CQAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:COG0251   18 SQAVRVGNLVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTDMADFAAVNEVYAEYFG 96

                         90       100       110
                 ....*....|....*....|....*....|
gi 736049980 108 GVYPISTGLVVSALGQpQWLMEIDVIAVIP 137
Cdd:COG0251   97 EGRPARTAVGVAALPK-GALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 28-134 1.22e-31

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: 109.19  E-value: 1.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  28 CQAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:cd00448    2 SQAVRVGNLVFVSGQIPLDPDGELVP-GDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80

                         90       100
                 ....*....|....*....|....*...
gi 736049980 108 -GVYPISTGLVVSALGqPQWLMEIDVIA 134
Cdd:cd00448   81 eGPPPARTAVGVAALP-PGALVEIEAIA 107
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 28-134 1.37e-27

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: 99.17  E-value: 1.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  28 CQAVRAGNTVYVRGQVGTDFDGNlVGLGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:cd06154   14 SRAVRVGNWVFVSGTTGYDYDGM-VMPGDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAHGEVFG 92

                         90       100
                 ....*....|....*....|....*..
gi 736049980 108 GVYPISTGLVVSALGQPQWLMEIDVIA 134
Cdd:cd06154   93 DIRPAATMVVVSLLVDPEMLVEIEVTA 119
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 28-136 9.43e-26

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: 94.25  E-value: 9.43e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  28 CQAVRAGNTVYVRGQVGTDFDGNLVGlgDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREV-GKWL 106
Cdd:cd02198    4 SPAVRVGDTLFVSGQVGSDADGSVAE--DFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDMAAHLPAFAAVkDEYF 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 736049980 107 KGVYPISTGLVVSALGQPQWLMEIDVIAVI 136
Cdd:cd02198   82 KEPYPAWTAVGVAWLARPGLLVEIKVVAVR 111
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 29-135 1.29e-24

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: 91.59  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980   29 QAVRAGNTVYVRGQVGTDFDGNLVGLGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLID-PRYREpvYREV-GKWL 106
Cdd:pfam01042  11 QAVKAGNLVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADmNDFAE--VNEVyAEYF 88

                          90       100       110
                  ....*....|....*....|....*....|
gi 736049980  107 KGV-YPISTGLVVSALGqPQWLMEIDVIAV 135
Cdd:pfam01042  89 DADkAPARSAVGVAALP-LGALVEIEAIAV 117
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 29-135 6.00e-22

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: 84.65  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980   29 QAVRAGNTVYVRGQVGTDFD-GNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWLK 107
Cdd:TIGR00004  18 QAVKVGNTVYVSGQIPLDPStGELVG-GDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQYFD 96

                          90       100
                  ....*....|....*....|....*....
gi 736049980  108 GVYPISTGLVVSALgqPQ-WLMEIDVIAV 135
Cdd:TIGR00004  97 EHYPARSAVQVAAL--PKgVLVEIEAIAV 123
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 27-135 1.80e-13

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


Pssm-ID: 100007  Cd Length: 105  Bit Score: 62.55  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  27 LCQAVRAGNTVYVRGQVGTDfdgnlvGLGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPRYREPVYREVGKWL 106
Cdd:cd06150    3 MSQAVVHNGTVYLAGQVADD------TSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWV 76

                         90       100
                 ....*....|....*....|....*....
gi 736049980 107 KGVYPISTGLVVSALGQPQWLMEIDVIAV 135
Cdd:cd06150   77 PPGHAPARACVEAKLADPGYLVEIVVTAA 105
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 29-135 1.64e-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: 57.70  E-value: 1.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  29 QAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAG-SDLTHIVKTTTYLID---PRYREPVYREVGK 104
Cdd:cd06152    5 QAVRIGDRIEISGQGGWDPDTGKIP-EDLEEEIDQAFDNVELALKAAGgKGWEQVYKVNSYHVDiknEEAFGLMVENFKK 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 736049980 105 WLKGVYPISTGLVVSALGQPQWLMEIDVIAV 135
Cdd:cd06152   84 WMPNHQPIWTCVGVTALGLPGMRVEIEVDAI 114
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 30-134 7.19e-05

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: 40.00  E-value: 7.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  30 AVRAG-NTVYVRGQVGTDFD-----GNLVGLGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLI-DPRYREPV---- 98
Cdd:cd06151    6 EVPAGaATIYLSGTVPAVVNasapkGSPARYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLVaDPALDGKMdfag 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 736049980  99 ----YRE-VGKWLKGVYPISTGLVVSALGQPQWLMEIDVIA 134
Cdd:cd06151   86 fmkaYRQfFGTAEQPNKPARSTLQVAGLVNPGWLVEIEVVA 126
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 52-134 3.73e-04

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


Pssm-ID: 100010  Cd Length: 114  Bit Score: 38.01  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  52 VGLGDPRAQAEQAMRNVKQLLEEAG-----SDLTHIVKTTTYLIDPRYREPVYREVGKWLKGVYPIStgLVVSALGQPQW 126
Cdd:cd06153   29 VHPGDVEAQTRETLENIEALLEAAGrgggaQFLADLLRLKVYLRDREDLPAVRAILAARLGPAVPAV--FLQADVCRPDL 106


                 ....*...
gi 736049980 127 LMEIDVIA 134
Cdd:cd06153  107 LVEIEAVA 114
PRK11401 PRK11401
enamine/imine deaminase;
29-135 2.00e-03

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 36.20  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736049980  29 QAVRAGNTVYVRGQVGTDFDGNLVGlGDPRAQAEQAMRNVKQLLEEAGSDLTHIVKTTTYLIDPR---YREPVYREVGKW 105
Cdd:PRK11401  19 QGVDLGSMVFTSGQIPVCPQTGEIP-ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNdfaTINEVYKQFFDE 97

                         90       100       110
                 ....*....|....*....|....*....|
gi 736049980 106 LKGVYPISTGLVVSALGQPQWLmEIDVIAV 135
Cdd:PRK11401  98 HQATYPTRSCVQVARLPKDVKL-EIEAIAV 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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