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Conserved domains on  [gi|164470289|gb|ABY57987|]
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CI857 [Cloning vector pFlpAB-4]

Protein Classification

LexA family protein( domain architecture ID 11449429)

LexA family protein may function as a transcriptional regulator involved in the repression of one or more genes involved in the response to DNA damage (SOS response), including recA and lexA and/or may contain a S24 peptidase domain such as in the translesion error-prone DNA polymerase V autoproteolytic subunit

Gene Ontology:  GO:0003677|GO:0045892
PubMed:  10679470|10908318

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 6-231 6.43e-43

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 143.90  E-value: 6.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289   6 KPLTQEQLEDARRLKAIYEKKKneLGLSQESVADKMGMGQSGVgalfnginalnaynAALLTKILKVSVEEFSPSIARei 85
Cdd:COG1974    2 KKLTKRQREILDFIKEYIRERG--YPPSQREIAEALGLSSSAV--------------HRHLKALEKKGYLRRDPGKSR-- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289  86 yemyeAVSMQPSLRSEYEYPVFSHVQAGMFSPKLRtftkgDAERWVSTTK---KASDSAFWLEVEGNSMTAPtgskpSFP 162
Cdd:COG1974   64 -----AIELLPASPEVVGLPLLGRVAAGFPIPAEE-----NIEEYLDLPEelvKNPGATFALRVKGDSMIDA-----GIL 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289 163 DGMLILVDPEQAVEPGDFCIARLGGdEFTFKKLIRDSGQVFLQPLNPQYPMIPCN-ESCSVVGKVIASQW 231
Cdd:COG1974  129 DGDLVIVDRQLEAENGDIVVALIDG-EATVKRLYKEGGRVRLQPENPAYPPIIIEgDDVEILGVVVGVIR 197
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 6-231 6.43e-43

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 143.90  E-value: 6.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289   6 KPLTQEQLEDARRLKAIYEKKKneLGLSQESVADKMGMGQSGVgalfnginalnaynAALLTKILKVSVEEFSPSIARei 85
Cdd:COG1974    2 KKLTKRQREILDFIKEYIRERG--YPPSQREIAEALGLSSSAV--------------HRHLKALEKKGYLRRDPGKSR-- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289  86 yemyeAVSMQPSLRSEYEYPVFSHVQAGMFSPKLRtftkgDAERWVSTTK---KASDSAFWLEVEGNSMTAPtgskpSFP 162
Cdd:COG1974   64 -----AIELLPASPEVVGLPLLGRVAAGFPIPAEE-----NIEEYLDLPEelvKNPGATFALRVKGDSMIDA-----GIL 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289 163 DGMLILVDPEQAVEPGDFCIARLGGdEFTFKKLIRDSGQVFLQPLNPQYPMIPCN-ESCSVVGKVIASQW 231
Cdd:COG1974  129 DGDLVIVDRQLEAENGDIVVALIDG-EATVKRLYKEGGRVRLQPENPAYPPIIIEgDDVEILGVVVGVIR 197
Peptidase_S24 pfam00717
Peptidase S24-like;
105-227 1.28e-34

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 120.00  E-value: 1.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289  105 PVFSHVQAGMFSPKLRTFtkGDAERWVSTTKKASDSAFWLEVEGNSMTaptgskPSFPDGMLILVDPEQAVEPGDFCIAR 184
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEI--EGYLPLPESLLSPPGNLFALRVKGDSME------PGIPDGDLVLVDPSREARNGDIVVAR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 164470289  185 LGGdEFTFKKLIRDSGQVFLQPLNPQYPMIPCN--ESCSVVGKVI 227
Cdd:pfam00717  73 LDG-EATVKRLYRDGGGIRLISLNPEYPPIELPaeDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 142-227 4.43e-22

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 86.46  E-value: 4.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289 142 FWLEVEGNSMTaptgskPSFPDGMLILVDPEQAVEPGDFCIARLGGdEFTFKKLIRDS-GQVFLQPLNPQYPMIPCN-ES 219
Cdd:cd06529    1 FALRVKGDSME------PTIPDGDLVLVDPSDTPRDGDIVVARLDG-ELTVKRLQRRGgGRLRLISDNPAYPPIEIDeEE 73


                 ....*...
gi 164470289 220 CSVVGKVI 227
Cdd:cd06529   74 LEIVGVVG 81
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
18-77 6.64e-08

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 47.90  E-value: 6.64e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289    18 RLKAIYEKKknelGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLTKILKVSVEEF 77
Cdd:smart00530   1 RLKELREEK----GLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
98-227 1.04e-05

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 44.02  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289  98 LRSEYEYPVFSH-VQAGMFSPklrtftkgdAERWVSTTKKASD-------SAFWLEVEGNSMTaptgsKPSFPDGMLILV 169
Cdd:PRK10276   9 LREIVTFPLFSDlVQCGFPSP---------AADYVEQRIDLNElliqhpsATYFVKASGDSMI-----DAGISDGDLLIV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164470289 170 DPEQAVEPGDFCIARLGGdEFTFKKL-IRDSGQvfLQPLNPQYP--MIPCNESCSVVGKVI 227
Cdd:PRK10276  75 DSAITASHGDIVIAAVDG-EFTVKKLqLRPTVQ--LIPMNSAYSpiTISSEDTLDVFGVVT 132
 
Name Accession Description Interval E-value
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 6-231 6.43e-43

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 143.90  E-value: 6.43e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289   6 KPLTQEQLEDARRLKAIYEKKKneLGLSQESVADKMGMGQSGVgalfnginalnaynAALLTKILKVSVEEFSPSIARei 85
Cdd:COG1974    2 KKLTKRQREILDFIKEYIRERG--YPPSQREIAEALGLSSSAV--------------HRHLKALEKKGYLRRDPGKSR-- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289  86 yemyeAVSMQPSLRSEYEYPVFSHVQAGMFSPKLRtftkgDAERWVSTTK---KASDSAFWLEVEGNSMTAPtgskpSFP 162
Cdd:COG1974   64 -----AIELLPASPEVVGLPLLGRVAAGFPIPAEE-----NIEEYLDLPEelvKNPGATFALRVKGDSMIDA-----GIL 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289 163 DGMLILVDPEQAVEPGDFCIARLGGdEFTFKKLIRDSGQVFLQPLNPQYPMIPCN-ESCSVVGKVIASQW 231
Cdd:COG1974  129 DGDLVIVDRQLEAENGDIVVALIDG-EATVKRLYKEGGRVRLQPENPAYPPIIIEgDDVEILGVVVGVIR 197
Peptidase_S24 pfam00717
Peptidase S24-like;
105-227 1.28e-34

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 120.00  E-value: 1.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289  105 PVFSHVQAGMFSPKLRTFtkGDAERWVSTTKKASDSAFWLEVEGNSMTaptgskPSFPDGMLILVDPEQAVEPGDFCIAR 184
Cdd:pfam00717   1 PLIGRVAAGAPILAEEEI--EGYLPLPESLLSPPGNLFALRVKGDSME------PGIPDGDLVLVDPSREARNGDIVVAR 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 164470289  185 LGGdEFTFKKLIRDSGQVFLQPLNPQYPMIPCN--ESCSVVGKVI 227
Cdd:pfam00717  73 LDG-EATVKRLYRDGGGIRLISLNPEYPPIELPaeDDVEIIGRVV 116
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 142-227 4.43e-22

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 86.46  E-value: 4.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289 142 FWLEVEGNSMTaptgskPSFPDGMLILVDPEQAVEPGDFCIARLGGdEFTFKKLIRDS-GQVFLQPLNPQYPMIPCN-ES 219
Cdd:cd06529    1 FALRVKGDSME------PTIPDGDLVLVDPSDTPRDGDIVVARLDG-ELTVKRLQRRGgGRLRLISDNPAYPPIEIDeEE 73


                 ....*...
gi 164470289 220 CSVVGKVI 227
Cdd:cd06529   74 LEIVGVVG 81
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 142-226 7.45e-17

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 72.68  E-value: 7.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289 142 FWLEVEGNSMTaptgskPSFPDGMLILVDPEQA-VEPGDFCIARLGGDEFTFKKLIRD--SGQVFLQPLNPQYPMIPC-- 216
Cdd:cd06462    1 FALRVEGDSME------PTIPDGDLVLVDKSSYePKRGDIVVFRLPGGELTVKRVIGLpgEGHYFLLGDNPNSPDSRIdg 74

                         90
                 ....*....|
gi 164470289 217 NESCSVVGKV 226
Cdd:cd06462   75 PPELDIVGVV 84
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 138-227 5.06e-14

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 66.14  E-value: 5.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289 138 SDSAFWLEVEGNSMtAPTgskpsFPDGMLILVDPEQA-VEPGDFCIARLGGdEFTFKKLIR-DSGQVFLQPLNPQYP--M 213
Cdd:COG2932   32 PDNLFAVRVSGDSM-EPT-----IRDGDIVLVDPSDTeIRDGGIYVVRTDG-ELLVKRLQRrPDGKLRLISDNPAYPpiE 104

                         90
                 ....*....|....*.
gi 164470289 214 IPCNE--SCSVVGKVI 227
Cdd:COG2932  105 IPPEDadEIEIIGRVV 120
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 16-77 4.14e-08

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 48.70  E-value: 4.14e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164470289  16 ARRLKAIYEKKknelGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLTKILKVSVEEF 77
Cdd:cd00093    1 GERLKELRKEK----GLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 24-77 4.53e-08

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 48.31  E-value: 4.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 164470289   24 EKKKNELGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLTKILKVSVEEF 77
Cdd:pfam01381   2 KELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
18-77 6.64e-08

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 47.90  E-value: 6.64e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289    18 RLKAIYEKKknelGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLTKILKVSVEEF 77
Cdd:smart00530   1 RLKELREEK----GLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLDEL 56
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
1-77 6.51e-06

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 43.06  E-value: 6.51e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164470289   1 MSTKKKPLtqeqledARRLKAIYEKKknelGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLTKILKVSVEEF 77
Cdd:COG1396    1 MSTLKKAL-------GERLRELRKAR----GLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSLDEL 66
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
98-227 1.04e-05

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 44.02  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164470289  98 LRSEYEYPVFSH-VQAGMFSPklrtftkgdAERWVSTTKKASD-------SAFWLEVEGNSMTaptgsKPSFPDGMLILV 169
Cdd:PRK10276   9 LREIVTFPLFSDlVQCGFPSP---------AADYVEQRIDLNElliqhpsATYFVKASGDSMI-----DAGISDGDLLIV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164470289 170 DPEQAVEPGDFCIARLGGdEFTFKKL-IRDSGQvfLQPLNPQYP--MIPCNESCSVVGKVI 227
Cdd:PRK10276  75 DSAITASHGDIVIAAVDG-EFTVKKLqLRPTVQ--LIPMNSAYSpiTISSEDTLDVFGVVT 132
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 16-76 2.15e-04

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 38.38  E-value: 2.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164470289  16 ARRLKAIYEKKknelGLSQESVADKMGMGQSGVGALFNGINALNAYNAALLTKILKVSVEE 76
Cdd:COG1813   14 GERIREAREAR----GLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISLAE 70
 
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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