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Conserved domains on  [gi|1009287621|ref|NP_001308403|]
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THUMP domain-containing protein 2 isoform 5 [Homo sapiens]

Protein Classification

class I SAM-dependent methyltransferase; SAM-dependent methyltransferase( domain architecture ID 1915406)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; S-adenosyl-L-methionine (SAM)-dependent methyltransferase similar to the mammalian protein RRNAD1, which is associated with periodontal disease

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdoMet_MTases super family cl17173
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 274-323 3.73e-11

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


The actual alignment was detected with superfamily member pfam01170:

Pssm-ID: 473071 [Multi-domain]  Cd Length: 184  Bit Score: 61.22  E-value: 3.73e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287621 274 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPNC 323
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANI 53
RlmL super family cl43029
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 204-317 5.03e-10

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


The actual alignment was detected with superfamily member COG0116:

Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 60.11  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621 204 DLTFRVSCRCSGTIGKA--FTAQEVGKVIGIAIMKHFGW--KADLRNPQLEIFIHL-NDIYSV----VGIPVFRvslasR 274
Cdd:COG0116    87 DGTFAVDATSVKSKLFHsqFAALRVKDAIVDRFREKYGArpSVDEDGPDVRIHVHLlKDRATLsldtSGESLHK-----R 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1009287621 275 AYIKTAG---LRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA 317
Cdd:COG0116   162 GYREAQGeapLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAA 207
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 274-323 3.73e-11

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 61.22  E-value: 3.73e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287621 274 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPNC 323
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANI 53
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 204-317 5.03e-10

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 60.11  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621 204 DLTFRVSCRCSGTIGKA--FTAQEVGKVIGIAIMKHFGW--KADLRNPQLEIFIHL-NDIYSV----VGIPVFRvslasR 274
Cdd:COG0116    87 DGTFAVDATSVKSKLFHsqFAALRVKDAIVDRFREKYGArpSVDEDGPDVRIHVHLlKDRATLsldtSGESLHK-----R 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1009287621 275 AYIKTAG---LRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA 317
Cdd:COG0116   162 GYREAQGeapLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAA 207
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 286-317 8.96e-09

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 54.18  E-value: 8.96e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1009287621 286 IAWAMASLADIKAGAFVLDPMCGLGTILLEAA 317
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAG 45
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-264 1.47e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 51.12  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621  186 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 262
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287621  263 GI 264
Cdd:smart00981  81 SI 82
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
221-317 8.19e-08

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 53.14  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621 221 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 290
Cdd:NF040721  104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                          90       100
                  ....*....|....*....|....*..
gi 1009287621 291 ASLADIKAGAFVLDPMCGLGTILLEAA 317
Cdd:NF040721  184 IYLSGWKDEESLLDPMCGSGTILIEAA 210
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 228-317 1.66e-07

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 52.05  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621 228 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 299
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90
                  ....*....|....*...
gi 1009287621 300 AFVLDPMCGLGTILLEAA 317
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAG 201
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 204-264 7.67e-07

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 47.96  E-value: 7.67e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287621 204 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 264
Cdd:cd11715    85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 243-317 6.59e-06

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 47.87  E-value: 6.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009287621 243 DLRNPQLEIFIHLNDIYSVVGIPVFRVSLASRAYIKTAG---LRSTIAWAMASLAD-IKAGAFVLDPMCGLGTILLEAA 317
Cdd:PRK11783  131 DKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGeapLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 206-255 6.91e-05

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 42.43  E-value: 6.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287621 206 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 255
Cdd:pfam02926  84 TFAVRVKRRGKNHE-FTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEI 132
 
Name Accession Description Interval E-value
UPF0020 pfam01170
Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated ...
 274-323 3.73e-11

Putative RNA methylase family UPF0020; This domain is probably a methylase. It is associated with the THUMP domain that also occurs with RNA modification domains.


Pssm-ID: 395932 [Multi-domain]  Cd Length: 184  Bit Score: 61.22  E-value: 3.73e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287621 274 RAYIKTAGLRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAAKEWPNC 323
Cdd:pfam01170   4 RPFNGPAPLKETLAAAMVNLAGWKPGDPLLDPMCGSGTILIEAALMGANI 53
RlmL COG0116
23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA ...
 204-317 5.03e-10

23S rRNA G2445 N2-methylase RlmL [Translation, ribosomal structure and biogenesis]; 23S rRNA G2445 N2-methylase RlmL is part of the Pathway/BioSystem: 23S rRNA modification


Pssm-ID: 439886 [Multi-domain]  Cd Length: 369  Bit Score: 60.11  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621 204 DLTFRVSCRCSGTIGKA--FTAQEVGKVIGIAIMKHFGW--KADLRNPQLEIFIHL-NDIYSV----VGIPVFRvslasR 274
Cdd:COG0116    87 DGTFAVDATSVKSKLFHsqFAALRVKDAIVDRFREKYGArpSVDEDGPDVRIHVHLlKDRATLsldtSGESLHK-----R 161

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1009287621 275 AYIKTAG---LRSTIAWAMASLADIKAGAFVLDPMCGLGTILLEAA 317
Cdd:COG0116   162 GYREAQGeapLKETLAAALLLLSGWDGDRPLVDPMCGSGTILIEAA 207
Trm11 COG1041
tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 ...
 286-317 8.96e-09

tRNA G10 N-methylase Trm11 [Translation, ribosomal structure and biogenesis]; tRNA G10 N-methylase Trm11 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440663 [Multi-domain]  Cd Length: 172  Bit Score: 54.18  E-value: 8.96e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1009287621 286 IAWAMASLADIKAGAFVLDPMCGLGTILLEAA 317
Cdd:COG1041    14 LARALVNLAGAKEGDTVLDPFCGTGTILIEAG 45
THUMP smart00981
The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP ...
 186-264 1.47e-08

The THUMP domain is named after after thiouridine synthases, methylases and PSUSs; The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterised RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 214952 [Multi-domain]  Cd Length: 83  Bit Score: 51.12  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621  186 EEEFQNDIEKAIDTHNQ--NDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFIHLNDIYSVV 262
Cdd:smart00981   2 LEDLYETALELIRWEKIfkEGKTFAVRAKRRGK-NHEFTSLEVKRAIGDKLLEKTGgRKVDLKNPDVVIRVELRKDKAYL 80


                   ..
gi 1009287621  263 GI 264
Cdd:smart00981  81 SI 82
Trm14_Arch NF040721
tRNA (guanine(6)-N2)-methyltransferase;
221-317 8.19e-08

tRNA (guanine(6)-N2)-methyltransferase;


Pssm-ID: 468685 [Multi-domain]  Cd Length: 370  Bit Score: 53.14  E-value: 8.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621 221 FTAQEVGKVIGIAIMKHFG------WKADLRNPQLEIFIHLNDIYSVVGIPVF-RVSLASR---AYIKTAGLRSTIAWAM 290
Cdd:NF040721  104 FTSIDIGRVAGEAVIDSYLrdkgvrLKVNLDEPDVIVRVELIFDELLVGIDTTgDEGLHKRgyrVYQHPAHLNPTIASSL 183

                          90       100
                  ....*....|....*....|....*..
gi 1009287621 291 ASLADIKAGAFVLDPMCGLGTILLEAA 317
Cdd:NF040721  184 IYLSGWKDEESLLDPMCGSGTILIEAA 210
TIGR01177 TIGR01177
putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is ...
 228-317 1.66e-07

putative methyltransferase, TIGR01177 family; This family of probable methyltransferases is found exclusively in the Archaea. [Hypothetical proteins, Conserved]


Pssm-ID: 273486 [Multi-domain]  Cd Length: 329  Bit Score: 52.05  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1009287621 228 KVIGiAIMKHFGWKADLRNPQLEIFI-HLNDIYSVVGIPVFRV-------SLASRAYIKTAGLRSTIAWAMASLADIKAG 299
Cdd:TIGR01177 105 RKIG-AILKKKGFKVSLRRPDIVVRVvITEDIFYLGRVLEERDkeqfierKPDRRPFFKPGSMDPKLARAMVNLARVTEG 183

                          90
                  ....*....|....*...
gi 1009287621 300 AFVLDPMCGLGTILLEAA 317
Cdd:TIGR01177 184 DRVLDPFCGTGGFLIEAG 201
THUMP_AdoMetMT cd11715
THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of ...
 204-264 7.67e-07

THUMP domain associated with S-adenosylmethionine-dependent methyltransferases; Proteins of this family contain an N-terminal THUMP domain and a C-terminal S-adenosylmethionine-dependent methyltransferase domain. Members have been implicated in the modification of 23S RNA m2G2445, a highly conserved modification in bacteria and in the m2G6 modification of tRNA. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212584  Cd Length: 152  Bit Score: 47.96  E-value: 7.67e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1009287621 204 DLTFRVSCRCSGTigKAFTAQEVGKVIGIAIMKHFG-----WKADLRNPQLEIFIHLNDIYSVVGI 264
Cdd:cd11715    85 DGTFAVRATRVGS--KLFHSQFAALRVKDAIVDRFRekgkrPSVDLDNPDVRIRVHLSKDRATLSL 148
rlmL PRK11783
bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2)) ...
 243-317 6.59e-06

bifunctional 23S rRNA (guanine(2069)-N(7))-methyltransferase RlmK/23S rRNA (guanine(2445)-N(2))-methyltransferase RlmL;


Pssm-ID: 236981 [Multi-domain]  Cd Length: 702  Bit Score: 47.87  E-value: 6.59e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1009287621 243 DLRNPQLEIFIHLNDIYSVVGIPVFRVSLASRAYIKTAG---LRSTIAWAMASLAD-IKAGAFVLDPMCGLGTILLEAA 317
Cdd:PRK11783  131 DKEQPDIRINARLNKGEATISLDLSGESLHQRGYRQATGeapLKENLAAAILLRSGwPQEGTPLLDPMCGSGTLLIEAA 209
THUMP pfam02926
THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and ...
 206-255 6.91e-05

THUMP domain; The THUMP domain is named after after thiouridine synthases, methylases and PSUSs. The THUMP domain consists of about 110 amino acid residues. The structure of ThiI reveals that the THUMP has a fold unlike that of previously characterized RNA-binding domains. It is predicted that this domain is an RNA-binding domain The THUMP domain probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 460749  Cd Length: 143  Bit Score: 42.43  E-value: 6.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1009287621 206 TFRVSCRCSGTIGKaFTAQEVGKVIGIAIMKHFGWKADLRNPQLEIFIHL 255
Cdd:pfam02926  84 TFAVRVKRRGKNHE-FTSLEINREVGKAIVEKTGLKVDLENPDIVVHVEI 132
THUMP_ThiI cd11716
THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the ...
 191-253 1.24e-03

THUMP domain of thiamine biosynthesis protein ThiI; ThiI is an enzyme responsible for the formation of the modified base S(4)U (4-thiouridine) found at position 8 in some prokaryotic tRNAs. This modification acts as a signal for UV exposure, triggering a response that provides protection against its damaging effects. ThiI consists of an N-terminal THUMP domain, followed by an NFLD domain, and a C-terminal PP-loop pyrophosphatase domain. The N-terminal THUMP domain has been implicated in the recognition of the acceptor-stem region. The THUMP domain is named after thiouridine synthases, methylases and PSUSs. The domain consists of about 110 amino acid residues. It is predicted to be an RNA-binding domain and probably functions by delivering a variety of RNA modification enzymes to their targets.


Pssm-ID: 212585  Cd Length: 166  Bit Score: 38.97  E-value: 1.24e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1009287621 191 NDIEKA----IDTHNQNDLTFRVSCRCSGTiGKAFTAQEVGKVIGIAIMKHFG-WKADLRNPQLEIFI 253
Cdd:cd11716    82 EDIKEAalelLKEELKKGKTFKVRAKRADK-SFPFTSMEINREVGAALLENTPdLKVDLKNPDVTIRV 148
 
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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