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Conserved domains on  [gi|887386798|emb|CKR55356|]
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Cytotoxin / haemolysin homologue TlyA [Mycobacterium tuberculosis]

Protein Classification

TlyA family RNA methyltransferase( domain architecture ID 11439687)

TlyA family RNA methyltransferase similar to Mycobacterium tuberculosis 16S/23S rRNA (cytidine-2'-O)-methyltransferase and Bacillus subtilis rRNA methyltransferase YqxC

CATH:  3.40.50.150
Gene Ontology:  GO:0008168|GO:0032259|GO:0003723
PubMed:  12826405|12504684

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 6-244 7.58e-136

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 382.87  E-value: 7.58e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798   6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVTDSERaWVSRGAHKLVGALEAFAIAVAGRR 85
Cdd:COG1189    2 RLDVLLVERGLAESREKAQRLIMAGRVLVNGQVVDKPGTKVPEDAEIEVKGEELP-YVSRGGLKLEGALDAFGIDVAGKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798  86 CLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIGGRVDLVVADLSFISLATVLP 165
Cdd:COG1189   81 CLDIGASTGGFTDCLLQRGAAKVYAVDVGYGQLAWKLRQDPRVVVLERTNARYLTPEDLPEPPDLVVIDVSFISLTLVLP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887386798 166 ALVGCASRDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVEYFLWLR 244
Cdd:COG1189  161 ALLALLKPGGELVALVKPQFEVGRERVGKGGVVRDPALHAEVIEKVLAAAAELGLRVLGLTPSPITGPDGNIEFLLWLR 239
 
Name Accession Description Interval E-value
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 6-244 7.58e-136

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 382.87  E-value: 7.58e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798   6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVTDSERaWVSRGAHKLVGALEAFAIAVAGRR 85
Cdd:COG1189    2 RLDVLLVERGLAESREKAQRLIMAGRVLVNGQVVDKPGTKVPEDAEIEVKGEELP-YVSRGGLKLEGALDAFGIDVAGKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798  86 CLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIGGRVDLVVADLSFISLATVLP 165
Cdd:COG1189   81 CLDIGASTGGFTDCLLQRGAAKVYAVDVGYGQLAWKLRQDPRVVVLERTNARYLTPEDLPEPPDLVVIDVSFISLTLVLP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887386798 166 ALVGCASRDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVEYFLWLR 244
Cdd:COG1189  161 ALLALLKPGGELVALVKPQFEVGRERVGKGGVVRDPALHAEVIEKVLAAAAELGLRVLGLTPSPITGPDGNIEFLLWLR 239
tly TIGR00478
TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA ...
 6-238 7.22e-67

TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA from Mycobacterium tuberculosis, an rRNA methylase whose modifications are necessary to confer sensitivity to ribosome-targeting antibiotics capreomycin and viomycin. Homology supports identification as a methyltransferase. However, a parallel literature persists in calling some members hemolysins. Hemolysins are exotoxins that attack blood cell membranes and cause cell rupture, often by forming a pore in the membrane. A recent study (2013) on SCO1782 from Streptomyces coelicolor shows hemolysin activity as earlier described for a homolog from the spirochete Serpula (Treponema) hyodysenteriae and one from Mycobacterium tuberculosis. [Unknown function, General]


Pssm-ID: 129570 [Multi-domain]  Cd Length: 228  Bit Score: 207.35  E-value: 7.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798    6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVtdSERAWVSRGAHKLVGALEAFAIAVAGRR 85
Cdd:TIGR00478   1 RLDILLVRRGLFESREKAKRLILKGFVLVNGKKVDKPSALVDFDAKIELL--QNPLFVSRGGEKLKEALEEFNIDVKNKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798   86 CLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIggRVDLVVADLSFISLATVLP 165
Cdd:TIGR00478  79 VLDVGSSTGGFTDCALQKGAKEVYGVDVGYNQLAEKLRQDERVKVLERTNIRYVTPADI--FPDFATFDVSFISLISILP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 887386798  166 ALVGCASrDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVE 238
Cdd:TIGR00478 157 ELDLLLN-PNDLTLLFKPQFEAGREKKNKKGVVRDKEAIALALHKVIDKGESPDFQEKKIIFSLTKGKRGNVE 228
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 62-244 6.41e-53

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 170.08  E-value: 6.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798   62 WVSRGAHKLVGALEAFAIAVAGRRCLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLaWSLRNDPRVVVLeRTNARGLTP 141
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQL-WKPRNDPGVTFI-QGDIRDPET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798  142 -----EAIGGRVDLVVADLS-FISLATVLPAlvgcasrdADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRA 215
Cdd:pfam01728  79 ldlleELLGRKVDLVLSDGSpFISGNKVLDH--------LRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLL 150

                         170       180
                  ....*....|....*....|....*....
gi 887386798  216 QeLGWHSVGVKASPLPGPSGNVEYFLWLR 244
Cdd:pfam01728 151 K-LGFEKVGVFKPPASRPESSEEYLVCLG 178
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 6-54 2.18e-07

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 47.24  E-value: 2.18e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 887386798   6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTV 54
Cdd:cd00165    2 RLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVIEV 50
S4 smart00363
S4 RNA-binding domain;
6-54 3.00e-07

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 46.43  E-value: 3.00e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 887386798     6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTV 54
Cdd:smart00363   2 RLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISV 50
 
Name Accession Description Interval E-value
YqxC COG1189
Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure ...
 6-244 7.58e-136

Predicted rRNA methylase YqxC, contains S4 and FtsJ domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440802 [Multi-domain]  Cd Length: 248  Bit Score: 382.87  E-value: 7.58e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798   6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVTDSERaWVSRGAHKLVGALEAFAIAVAGRR 85
Cdd:COG1189    2 RLDVLLVERGLAESREKAQRLIMAGRVLVNGQVVDKPGTKVPEDAEIEVKGEELP-YVSRGGLKLEGALDAFGIDVAGKV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798  86 CLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIGGRVDLVVADLSFISLATVLP 165
Cdd:COG1189   81 CLDIGASTGGFTDCLLQRGAAKVYAVDVGYGQLAWKLRQDPRVVVLERTNARYLTPEDLPEPPDLVVIDVSFISLTLVLP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 887386798 166 ALVGCASRDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVEYFLWLR 244
Cdd:COG1189  161 ALLALLKPGGELVALVKPQFEVGRERVGKGGVVRDPALHAEVIEKVLAAAAELGLRVLGLTPSPITGPDGNIEFLLWLR 239
tly TIGR00478
TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA ...
 6-238 7.22e-67

TlyA family rRNA methyltransferase/putative hemolysin; Members of this family include TlyA from Mycobacterium tuberculosis, an rRNA methylase whose modifications are necessary to confer sensitivity to ribosome-targeting antibiotics capreomycin and viomycin. Homology supports identification as a methyltransferase. However, a parallel literature persists in calling some members hemolysins. Hemolysins are exotoxins that attack blood cell membranes and cause cell rupture, often by forming a pore in the membrane. A recent study (2013) on SCO1782 from Streptomyces coelicolor shows hemolysin activity as earlier described for a homolog from the spirochete Serpula (Treponema) hyodysenteriae and one from Mycobacterium tuberculosis. [Unknown function, General]


Pssm-ID: 129570 [Multi-domain]  Cd Length: 228  Bit Score: 207.35  E-value: 7.22e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798    6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTVVtdSERAWVSRGAHKLVGALEAFAIAVAGRR 85
Cdd:TIGR00478   1 RLDILLVRRGLFESREKAKRLILKGFVLVNGKKVDKPSALVDFDAKIELL--QNPLFVSRGGEKLKEALEEFNIDVKNKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798   86 CLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLAWSLRNDPRVVVLERTNARGLTPEAIggRVDLVVADLSFISLATVLP 165
Cdd:TIGR00478  79 VLDVGSSTGGFTDCALQKGAKEVYGVDVGYNQLAEKLRQDERVKVLERTNIRYVTPADI--FPDFATFDVSFISLISILP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 887386798  166 ALVGCASrDADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRAQELGWHSVGVKASPLPGPSGNVE 238
Cdd:TIGR00478 157 ELDLLLN-PNDLTLLFKPQFEAGREKKNKKGVVRDKEAIALALHKVIDKGESPDFQEKKIIFSLTKGKRGNVE 228
FtsJ pfam01728
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
 62-244 6.41e-53

FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.


Pssm-ID: 426399  Cd Length: 179  Bit Score: 170.08  E-value: 6.41e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798   62 WVSRGAHKLVGALEAFAIAVAGRRCLDAGASTGGFTEVLLDRGAAHVVAADVGYGQLaWSLRNDPRVVVLeRTNARGLTP 141
Cdd:pfam01728   1 YRSRAAYKLLEIDEKFGLLKPGKTVLDLGAAPGGWSQVALQRGAGKVVGVDLGPMQL-WKPRNDPGVTFI-QGDIRDPET 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798  142 -----EAIGGRVDLVVADLS-FISLATVLPAlvgcasrdADIVPLVKPQFEVGKGQVGPGGVVHDPQLRARSVLAVARRA 215
Cdd:pfam01728  79 ldlleELLGRKVDLVLSDGSpFISGNKVLDH--------LRSLDLVKAALEVALELLRKGGNFVCKVFQGEDFSELLYLL 150

                         170       180
                  ....*....|....*....|....*....
gi 887386798  216 QeLGWHSVGVKASPLPGPSGNVEYFLWLR 244
Cdd:pfam01728 151 K-LGFEKVGVFKPPASRPESSEEYLVCLG 178
S4 cd00165
S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, ...
 6-54 2.18e-07

S4/Hsp/ tRNA synthetase RNA-binding domain; The domain surface is populated by conserved, charged residues that define a likely RNA-binding site; Found in stress proteins, ribosomal proteins and tRNA synthetases; This may imply a hitherto unrecognized functional similarity between these three protein classes.


Pssm-ID: 238095 [Multi-domain]  Cd Length: 70  Bit Score: 47.24  E-value: 2.18e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 887386798   6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTV 54
Cdd:cd00165    2 RLDKILARLGLAPSRSEARQLIKHGHVLVNGKVVTKPSYKVKPGDVIEV 50
S4 smart00363
S4 RNA-binding domain;
6-54 3.00e-07

S4 RNA-binding domain;


Pssm-ID: 214638 [Multi-domain]  Cd Length: 60  Bit Score: 46.43  E-value: 3.00e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 887386798     6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVSDTTALTV 54
Cdd:smart00363   2 RLDKFLARLGLAPSRSQARRLIEQGRVKVNGKKVTKPSYIVKPGDVISV 50
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 85-173 4.65e-06

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.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 44.34  E-value: 4.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798  85 RCLDAGASTGGFTEVLLDRGAAHVVAAD-----VGYGQLAWSLRNDPRVVVLERtNARGLTPEAiGGRVDLVVADLSFIS 159
Cdd:cd02440    1 RVLDLGCGTGALALALASGPGARVTGVDispvaLELARKAAAALLADNVEVLKG-DAEELPPEA-DESFDVIISDPPLHH 78

                         90
                 ....*....|....
gi 887386798 160 LATVLPALVGCASR 173
Cdd:cd02440   79 LVEDLARFLEEARR 92
S4 pfam01479
S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was ...
 6-47 3.30e-05

S4 domain; The S4 domain is a small domain consisting of 60-65 amino acid residues that was detected in the bacterial ribosomal protein S4, eukaryotic ribosomal S9, two families of pseudouridine synthases, a novel family of predicted RNA methylases, a yeast protein containing a pseudouridine synthetase and a deaminase domain, bacterial tyrosyl-tRNA synthetases, and a number of uncharacterized, small proteins that may be involved in translation regulation. The S4 domain probably mediates binding to RNA.


Pssm-ID: 396182 [Multi-domain]  Cd Length: 48  Bit Score: 40.55  E-value: 3.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 887386798    6 RVDAELVRRGLARSRQQAAELIGAGKVRIDGLPAVKPATAVS 47
Cdd:pfam01479   2 RLDKVLARLGLASSRSQARQLIEHGRVLVNGKVVKDPSYRVK 43
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 78-172 2.93e-03

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 36.92  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 887386798  78 AIAVAGRRCLDAGASTGGFTEVLLDRGaAHVVAADVGYGQLAWSLRNDPRV-VVLERTNARGLTPEaiGGRVDLVVADLS 156
Cdd:COG2227   20 RLLPAGGRVLDVGCGTGRLALALARRG-ADVTGVDISPEALEIARERAAELnVDFVQGDLEDLPLE--DGSFDLVICSEV 96

                         90
                 ....*....|....*.
gi 887386798 157 FISLATVLPALVGCAS 172
Cdd:COG2227   97 LEHLPDPAALLRELAR 112
YlmH COG2302
RNA-binding protein YlmH, contains S4-like domain [General function prediction only];
19-47 7.85e-03

RNA-binding protein YlmH, contains S4-like domain [General function prediction only];


Pssm-ID: 441877  Cd Length: 260  Bit Score: 37.06  E-value: 7.85e-03
                         10        20
                 ....*....|....*....|....*....
gi 887386798  19 SRQQAAELIGAGKVRIDGLPAVKPATAVS 47
Cdd:COG2302  197 SRSKAAELIESGKVKVNWKVVDKPSFEVK 225
HslR COG1188
Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal ...
 1-46 9.29e-03

Ribosomal 50S subunit-recycling heat shock protein, contains S4 domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440801  Cd Length: 120  Bit Score: 35.19  E-value: 9.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 887386798   1 MARRARVDAEL--VRrgLARSRQQAAELIGAGKVRIDGLPAvKPATAV 46
Cdd:COG1188    1 AAERMRLDKWLwaAR--FFKTRSLAAEACDGGRVRVNGQRA-KPSREV 45
 
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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