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Conserved domains on  [gi|1432804887|gb|RCR26378|]
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RidA family protein [Escherichia coli]

Protein Classification

RidA family protein( domain architecture ID 10150280)

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
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
10-113 1.87e-47

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: 147.30  E-value: 1.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  10 ARWSDVVIHNNTLYYTG-VPENLDADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWVVAGH 88
Cdd:cd06150     1 ARMSQAVVHNGTVYLAGqVADDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPGH 80
                          90       100
                  ....*....|....*....|....*
gi 1432804887  89 APVRCTVQAGLMNPKYKVEIKIVAA 113
Cdd:cd06150    81 APARACVEAKLADPGYLVEIVVTAA 105
 
Name Accession Description Interval E-value
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
10-113 1.87e-47

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: 147.30  E-value: 1.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  10 ARWSDVVIHNNTLYYTG-VPENLDADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWVVAGH 88
Cdd:cd06150     1 ARMSQAVVHNGTVYLAGqVADDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPGH 80
                          90       100
                  ....*....|....*....|....*
gi 1432804887  89 APVRCTVQAGLMNPKYKVEIKIVAA 113
Cdd:cd06150    81 APARACVEAKLADPGYLVEIVVTAA 105
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
4-113 2.66e-35

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: 117.01  E-value: 2.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887   4 VRIDAEARWSDVVIHNNTLYYTG-VPENLD------ADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVM 76
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGqIPLDPDtgklveGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1432804887  77 NKAWDAWVVAGHAPVRCTVQAGLMNPKYKVEIKIVAA 113
Cdd:pfam01042  81 NEVYAEYFDADKAPARSAVGVAALPLGALVEIEAIAV 117
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-114 1.03e-23

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: 87.93  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887   1 MTIVRIDAEA-----RWSDVVIHNNTLYYTG-VPEN-----LDADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLAD 69
Cdd:COG0251     1 MTRELINPPApapigPYSQAVRVGNLVFVSGqVPLDpdtgeLGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1432804887  70 KNDFAVMNKAWDAWvVAGHAPVRCTVQAGLMNPKYKVEIKIVAAV 114
Cdd:COG0251    81 MADFAAVNEVYAEY-FGEGRPARTAVGVAALPKGALVEIEAIAAL 124
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
12-114 1.13e-11

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: 56.92  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  12 WSDVVIHNNTLYYTG----VPENLD---ADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWv 84
Cdd:TIGR00004  16 YSQAVKVGNTVYVSGqiplDPSTGElvgGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQY- 94
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1432804887  85 VAGHAPVRCTVQ-AGLmnPK-YKVEIKIVAAV 114
Cdd:TIGR00004  95 FDEHYPARSAVQvAAL--PKgVLVEIEAIAVK 124
PRK11401 PRK11401
enamine/imine deaminase;
33-112 2.97e-06

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 43.13  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  33 ADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWVVAGHA--PVRCTVQAGLMNPKYKVEIKI 110
Cdd:PRK11401   44 ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQAtyPTRSCVQVARLPKDVKLEIEA 123

                  ..
gi 1432804887 111 VA 112
Cdd:PRK11401  124 IA 125
 
Name Accession Description Interval E-value
YjgF_YER057c_UK114_like_2 cd06150
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
10-113 1.87e-47

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: 147.30  E-value: 1.87e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  10 ARWSDVVIHNNTLYYTG-VPENLDADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWVVAGH 88
Cdd:cd06150     1 ARMSQAVVHNGTVYLAGqVADDTSADITGQTRQVLAKIDALLAEAGSDKSRILSATIWLADMADFAAMNAVWDAWVPPGH 80
                          90       100
                  ....*....|....*....|....*
gi 1432804887  89 APVRCTVQAGLMNPKYKVEIKIVAA 113
Cdd:cd06150    81 APARACVEAKLADPGYLVEIVVTAA 105
Ribonuc_L-PSP pfam01042
Endoribonuclease L-PSP; Endoribonuclease active on single-stranded mRNA. Inhibits protein ...
4-113 2.66e-35

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: 117.01  E-value: 2.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887   4 VRIDAEARWSDVVIHNNTLYYTG-VPENLD------ADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVM 76
Cdd:pfam01042   1 NAPAAAGPYSQAVKAGNLVYVSGqIPLDPDtgklveGDVAEQTRQVLENIKAVLAAAGASLSDVVKVTIFLADMNDFAEV 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1432804887  77 NKAWDAWVVAGHAPVRCTVQAGLMNPKYKVEIKIVAA 113
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, ...
12-112 5.64e-26

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: 93.01  E-value: 5.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  12 WSDVVIHNNTLYYTG-VPENLD-----ADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWVV 85
Cdd:cd00448     1 YSQAVRVGNLVFVSGqIPLDPDgelvpGDIEAQTRQALENLEAVLEAAGGSLDDVVKVTVYLTDMADFAAVNEVYDEFFG 80
                          90       100
                  ....*....|....*....|....*..
gi 1432804887  86 AGHAPVRCTVQAGLMNPKYKVEIKIVA 112
Cdd:cd00448    81 EGPPPARTAVGVAALPPGALVEIEAIA 107
RidA COG0251
Enamine deaminase RidA, house cleaning of reactive enamine intermediates, YjgF/YER057c/UK114 ...
1-114 1.03e-23

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: 87.93  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887   1 MTIVRIDAEA-----RWSDVVIHNNTLYYTG-VPEN-----LDADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLAD 69
Cdd:COG0251     1 MTRELINPPApapigPYSQAVRVGNLVFVSGqVPLDpdtgeLGGDIEAQTRQVLENILAVLAAAGGSLDDVVKVTVYLTD 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1432804887  70 KNDFAVMNKAWDAWvVAGHAPVRCTVQAGLMNPKYKVEIKIVAAV 114
Cdd:COG0251    81 MADFAAVNEVYAEY-FGEGRPARTAVGVAALPKGALVEIEAIAAL 124
TIGR00004 TIGR00004
reactive intermediate/imine deaminase; This protein was described initially as an inhibitor of ...
12-114 1.13e-11

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: 56.92  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  12 WSDVVIHNNTLYYTG----VPENLD---ADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWv 84
Cdd:TIGR00004  16 YSQAVKVGNTVYVSGqiplDPSTGElvgGDIAEQAEQVLENLKAILEAAGLSLDDVVKTTVFLTDLNDFAEVNEVYGQY- 94
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1432804887  85 VAGHAPVRCTVQ-AGLmnPK-YKVEIKIVAAV 114
Cdd:TIGR00004  95 FDEHYPARSAVQvAAL--PKgVLVEIEAIAVK 124
YjgF_YER057c_UK114_like_6 cd06154
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
34-112 2.25e-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: 100011  Cd Length: 119  Bit Score: 51.02  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  34 DAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWdAWVVAGHAPVRCTVQAGLM-NPKYKVEIKIVA 112
Cdd:cd06154    41 DAYEQTRQCLEIIEAALAEAGASLEDVVRTRMYVTDIADFEAVGRAH-GEVFGDIRPAATMVVVSLLvDPEMLVEIEVTA 119
PRK11401 PRK11401
enamine/imine deaminase;
33-112 2.97e-06

enamine/imine deaminase;


Pssm-ID: 105214  Cd Length: 129  Bit Score: 43.13  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  33 ADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWVVAGHA--PVRCTVQAGLMNPKYKVEIKI 110
Cdd:PRK11401   44 ADVQDQARLSLENVKAIVVAAGLSVGDIIKMTVFITDLNDFATINEVYKQFFDEHQAtyPTRSCVQVARLPKDVKLEIEA 123

                  ..
gi 1432804887 111 VA 112
Cdd:PRK11401  124 IA 125
YjgF_YER057c_UK114_like_3 cd06151
This group of proteins belong to a large family of YjgF/YER057c/UK114-like proteins present in ...
34-112 1.25e-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: 41.15  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  34 DAFEQTANTLAQIDAVLEKQGSNKSSI------LDATIFLADKNDFAVMNKAWDAWVvaGHA-----PVRCTVQ-AGLMN 101
Cdd:cd06151    38 DTETQTISVLKRIETILQSQGLTMGDVvkmrvfLVADPALDGKMDFAGFMKAYRQFF--GTAeqpnkPARSTLQvAGLVN 115
                          90
                  ....*....|.
gi 1432804887 102 PKYKVEIKIVA 112
Cdd:cd06151   116 PGWLVEIEVVA 126
YjgH_like cd02198
YjgH belongs to a large family of YjgF/YER057c/UK114-like proteins present in bacteria, ...
11-114 1.75e-05

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: 40.71  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  11 RWSDVVIHNNTLYYTGV----PENLDADAFE-QTANTLAQIDAVLEKQGSNKSSILDATIFLAD-KNDFAVMNKAWDAWV 84
Cdd:cd02198     2 GYSPAVRVGDTLFVSGQvgsdADGSVAEDFEaQFRLAFQNLGAVLEAAGCSFDDVVELTTFHVDmAAHLPAFAAVKDEYF 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1432804887  85 VAGHAPVRCTVQAGLMNPKYKVEIKIVAAV 114
Cdd:cd02198    82 KEPYPAWTAVGVAWLARPGLLVEIKVVAVR 111
eu_AANH_C_1 cd06155
A group of hypothetical eukaryotic proteins, characterized by the presence of an adenine ...
30-113 6.57e-05

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: 38.78  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1432804887  30 NLDADAFEQTANTLAQIDAVLEKQGSNKSSILDATIFLADKNDFAVMNKAWDAWVVAGHAPVRCTVQAGLMnPKYKVEIK 109
Cdd:cd06155    19 ESDETVEEQMESIFSKLREILQSNGLSLSDILYVTLYLRDMSDFAEVNSVYGTFFDKPNPPSRVCVECGLP-EGCDVQLS 97

                  ....
gi 1432804887 110 IVAA 113
Cdd:cd06155    98 CVAA 101
 
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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