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Conserved domains on  [gi|1888192145|ref|WP_182313307|]
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MULTISPECIES: RidA family protein [unclassified Streptomyces]

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 ...
 1-135 4.63e-26

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: 94.47  E-value: 4.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145   1 MAITLVNPGGLPEIDVYRHVSIASGtkLVFVAGQVAQDAEGNVVGeGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVH 80
Cdd:COG0251     1 MTRELINPPAPAPIGPYSQAVRVGN--LVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888192145  81 VVGWtadkmpALLEGISRA-AEKLGvTPAPPATLLGVAALAApEYLVEVEAVAVLD 135
Cdd:COG0251    78 LTDM------ADFAAVNEVyAEYFG-EGRPARTAVGVAALPK-GALVEIEAIAALP 125
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-135 4.63e-26

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: 94.47  E-value: 4.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145   1 MAITLVNPGGLPEIDVYRHVSIASGtkLVFVAGQVAQDAEGNVVGeGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVH 80
Cdd:COG0251     1 MTRELINPPAPAPIGPYSQAVRVGN--LVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888192145  81 VVGWtadkmpALLEGISRA-AEKLGvTPAPPATLLGVAALAApEYLVEVEAVAVLD 135
Cdd:COG0251    78 LTDM------ADFAAVNEVyAEYFG-EGRPARTAVGVAALPK-GALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 27-132 2.83e-20

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: 79.52  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  27 KLVFVAGQVAQDAEGNVVgEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVHVVGwtadkmPALLEGISRA-AEKLGV 105
Cdd:cd00448     9 NLVFVSGQIPLDPDGELV-PGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTD------MADFAAVNEVyDEFFGE 81

                          90       100
                  ....*....|....*....|....*..
gi 1888192145 106 TPAPPATLLGVAALaAPEYLVEVEAVA 132
Cdd:cd00448    82 GPPPARTAVGVAAL-PPGALVEIEAIA 107
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 28-133 1.56e-15

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: 67.32  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  28 LVFVAGQVAQDAEGNVVGEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVHVVGWtaDKMPALLEGISRAAEKLGvtp 107
Cdd:pfam01042  18 LVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADM--NDFAEVNEVYAEYFDADK--- 92

                          90       100
                  ....*....|....*....|....*.
gi 1888192145 108 APPATLLGVAALaAPEYLVEVEAVAV 133
Cdd:pfam01042  93 APARSAVGVAAL-PLGALVEIEAIAV 117
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 27-134 5.84e-10

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: 53.07  E-value: 5.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  27 KLVFVAGQVAQDAEGNVVGEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVhvvgwtadkmpaLLEGISRAAEKLGV- 105
Cdd:TIGR00004  24 NTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTV------------FLTDLNDFAEVNEVy 91

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1888192145 106 -----TPAPPATLLGVAALAApEYLVEVEAVAVL 134
Cdd:TIGR00004  92 gqyfdEHYPARSAVQVAALPK-GVLVEIEAIAVK 124
 
Name Accession Description Interval E-value
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
 1-135 4.63e-26

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: 94.47  E-value: 4.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145   1 MAITLVNPGGLPEIDVYRHVSIASGtkLVFVAGQVAQDAEGNVVGeGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVH 80
Cdd:COG0251     1 MTRELINPPAPAPIGPYSQAVRVGN--LVFVSGQVPLDPDTGELG-GDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVY 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1888192145  81 VVGWtadkmpALLEGISRA-AEKLGvTPAPPATLLGVAALAApEYLVEVEAVAVLD 135
Cdd:COG0251    78 LTDM------ADFAAVNEVyAEYFG-EGRPARTAVGVAALPK-GALVEIEAIAALP 125
YjgF_YER057c_UK114_family cd00448
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 27-132 2.83e-20

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: 79.52  E-value: 2.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  27 KLVFVAGQVAQDAEGNVVgEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVHVVGwtadkmPALLEGISRA-AEKLGV 105
Cdd:cd00448     9 NLVFVSGQIPLDPDGELV-PGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTD------MADFAAVNEVyDEFFGE 81

                          90       100
                  ....*....|....*....|....*..
gi 1888192145 106 TPAPPATLLGVAALaAPEYLVEVEAVA 132
Cdd:cd00448    82 GPPPARTAVGVAAL-PPGALVEIEAIA 107
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
 28-134 4.39e-17

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


Pssm-ID: 100005  Cd Length: 111  Bit Score: 71.14  E-value: 4.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  28 LVFVAGQVAQDAEGNVvgEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVHVVGwtadkMPALLEGISRAAEKLGVTP 107
Cdd:cd02198    12 TLFVSGQVGSDADGSV--AEDFEAQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVD-----MAAHLPAFAAVKDEYFKEP 84

                          90       100
                  ....*....|....*....|....*..
gi 1888192145 108 APPATLLGVAALAAPEYLVEVEAVAVL 134
Cdd:cd02198    85 YPAWTAVGVAWLARPGLLVEIKVVAVR 111
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 28-132 4.19e-16

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: 69.12  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  28 LVFVAGQVAQDAEGNVVGeGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVHVVGwtadkmPALLEGISRA-AEKLG-V 105
Cdd:cd06154    22 WVFVSGTTGYDYDGMVMP-GDAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTD------IADFEAVGRAhGEVFGdI 94

                          90       100
                  ....*....|....*....|....*..
gi 1888192145 106 TPAppATLLGVAALAAPEYLVEVEAVA 132
Cdd:cd06154    95 RPA--ATMVVVSLLVDPEMLVEIEVTA 119
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
 28-133 1.56e-15

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: 67.32  E-value: 1.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  28 LVFVAGQVAQDAEGNVVGEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVHVVGWtaDKMPALLEGISRAAEKLGvtp 107
Cdd:pfam01042  18 LVYVSGQIPLDPDTGKLVEGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADM--NDFAEVNEVYAEYFDADK--- 92

                          90       100
                  ....*....|....*....|....*.
gi 1888192145 108 APPATLLGVAALaAPEYLVEVEAVAV 133
Cdd:pfam01042  93 APARSAVGVAAL-PLGALVEIEAIAV 117
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
 27-134 5.84e-10

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: 53.07  E-value: 5.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  27 KLVFVAGQVAQDAEGNVVGEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVhvvgwtadkmpaLLEGISRAAEKLGV- 105
Cdd:TIGR00004  24 NTVYVSGQIPLDPSTGELVGGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTV------------FLTDLNDFAEVNEVy 91

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1888192145 106 -----TPAPPATLLGVAALAApEYLVEVEAVAVL 134
Cdd:TIGR00004  92 gqyfdEHYPARSAVQVAALPK-GVLVEIEAIAVK 124
YjgF_YER057c_UK114_like_4 cd06152
YjgF, YER057c, and UK114 belong to a large family of proteins present in bacteria, archaea, ...
 31-133 1.69e-07

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: 46.53  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  31 VAGQVAQDAEGNVVGEgDFAAQVEQCYLNVGTALAEAGG-SFDDLAKLNV-HVVGWTADKMPALLEGISRaaeklgVTP- 107
Cdd:cd06152    15 ISGQGGWDPDTGKIPE-DLEEEIDQAFDNVELALKAAGGkGWEQVYKVNSyHVDIKNEEAFGLMVENFKK------WMPn 87

                          90       100
                  ....*....|....*....|....*..
gi 1888192145 108 -APPATLLGVAALAAPEYLVEVEAVAV 133
Cdd:cd06152    88 hQPIWTCVGVTALGLPGMRVEIEVDAI 114
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 20-132 2.04e-07

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: 46.54  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  20 VSIASGTKLVFVAGQVAQ-----DAEGNVVGEGDFAAQVEQCYLNVGTALAEAGGSFDDLAKLNVHVVG--WTADKMPal 92
Cdd:cd06151     5 VEVPAGAATIYLSGTVPAvvnasAPKGSPARYGDTETQTISVLKRIETILQSQGLTMGDVVKMRVFLVAdpALDGKMD-- 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1888192145  93 LEGISRAAEKLGVTPAPPA----TLLGVAALAAPEYLVEVEAVA 132
Cdd:cd06151    83 FAGFMKAYRQFFGTAEQPNkparSTLQVAGLVNPGWLVEIEVVA 126
YjgF_YER057c_UK114_like_5 cd06153
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 18-132 1.12e-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: 39.16  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  18 RHVSIASG-TKLVFVAGQVAQDAEGnVVGEGDFAAQVEQCYLNVGTALAEAGGS-----FDDLAKLNVHVvgwtadKMPA 91
Cdd:cd06153     3 RATLLAAGgRTHLFISGTASIVGHG-TVHPGDVEAQTRETLENIEALLEAAGRGggaqfLADLLRLKVYL------RDRE 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1888192145  92 LLEGISRAAEKLGvTPAPPATLLgVAALAAPEYLVEVEAVA 132
Cdd:cd06153    76 DLPAVRAILAARL-GPAVPAVFL-QADVCRPDLLVEIEAVA 114
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
 28-133 1.60e-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: 100007  Cd Length: 105  Bit Score: 38.29  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1888192145  28 LVFVAGQVAQDaegnvvGEGDFAAQVEQCYLNVGTALAEAGGSFDDLakLNVHVvgWTADKmpALLEGISRAAEKLGVTP 107
Cdd:cd06150    12 TVYLAGQVADD------TSADITGQTRQVLAKIDALLAEAGSDKSRI--LSATI--WLADM--ADFAAMNAVWDAWVPPG 79

                          90       100
                  ....*....|....*....|....*.
gi 1888192145 108 APPATLLGVAALAAPEYLVEVEAVAV 133
Cdd:cd06150    80 HAPARACVEAKLADPGYLVEIVVTAA 105
 
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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