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Conserved domains on  [gi|2781192751|ref|XP_066608752|]
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uncharacterized protein I312_104854 [Cryptococcus bacillisporus CA1280]

Protein Classification

RraA family protein( domain architecture ID 10002149)

RraA family protein such as Saccharomyces cerevisiae 4-hydroxy-4-methyl-2-oxoglutarate (HMG) aldolase, which catalyzes the aldol cleavage of HMG into 2 molecules of pyruvate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
4-218 6.44e-44

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


:

Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 146.47  E-value: 6.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751   4 SKNILSRLAPYGACDVADALAKLkhPAGGFLSGLKLRGPDQntKIIGRAHTVLFRANSVAPQKkgfkgHYIDSVTPGSVL 83
Cdd:COG0684     4 DAELLERLAAVSTATVSDALDRL--LRGALDPGIRPLHPGA--RLVGPAVTVRYRPGDNLMLH-----EAIDLAPPGDVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  84 FMSAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVGITAGQEVCYSSEINVPVPLRsahqpD 163
Cdd:COG0684    75 VIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVGPGEINVPVSIG-----G 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2781192751 164 VWINPGDIIVGDENGVACIPQELEDEVADLIPLLAERDRLSMEDLMAGMKAEDVF 218
Cdd:COG0684   150 VTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
 
Name Accession Description Interval E-value
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
4-218 6.44e-44

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 146.47  E-value: 6.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751   4 SKNILSRLAPYGACDVADALAKLkhPAGGFLSGLKLRGPDQntKIIGRAHTVLFRANSVAPQKkgfkgHYIDSVTPGSVL 83
Cdd:COG0684     4 DAELLERLAAVSTATVSDALDRL--LRGALDPGIRPLHPGA--RLVGPAVTVRYRPGDNLMLH-----EAIDLAPPGDVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  84 FMSAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVGITAGQEVCYSSEINVPVPLRsahqpD 163
Cdd:COG0684    75 VIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVGPGEINVPVSIG-----G 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2781192751 164 VWINPGDIIVGDENGVACIPQELEDEVADLIPLLAERDRLSMEDLMAGMKAEDVF 218
Cdd:COG0684   150 VTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
17-182 1.90e-37

ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.


Pssm-ID: 319245 [Multi-domain]  Cd Length: 150  Bit Score: 127.96  E-value: 1.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  17 CDVADALAKLkhpaGGFLSGLkLRGPDQNTKIIGRAHTVLFRansvaPQKKGFKGHYIDSVTPGSVLFMSAPAHLPNAIY 96
Cdd:cd16841     1 ADLSDALDRL----GGVLPGI-IRPLGGGARFVGPAVTVKCF-----PDDNLLVREALDEAGPGDVLVVDGGGSLRCALW 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  97 GGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVgITAGQEVCYSSEINVPVPLrsahqPDVWINPGDIIVGDE 176
Cdd:cd16841    71 GDLLATLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGT-TPRGSKKVGPGEVNVPVTI-----GGVTVNPGDIIVADE 144

                  ....*.
gi 2781192751 177 NGVACI 182
Cdd:cd16841   145 DGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
17-179 1.62e-31

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 112.60  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  17 CDVADALAKLKHPAGGfLSGLKlrgPDQNTKIIGRAHTVLFRansvaPQKKGFKGHYIDSVTPGSVLFMSAPaHLPNAIY 96
Cdd:pfam03737   1 ADLSDALGSYGGRLGA-MPGIR---PLNPGPFVGPAVTVKCF-----PEDNLLVHEALDEAGPGDVLVVDGG-GGSRAAL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  97 GGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDV----GITAGQEvcyssEINVPVPLrsahqPDVWINPGDII 172
Cdd:pfam03737  71 GDLLATLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTtprgSVKRGPG-----EVNVPVTI-----GGVTVRPGDII 140

                  ....*..
gi 2781192751 173 VGDENGV 179
Cdd:pfam03737 141 VADEDGV 147
PRK06201 PRK06201
hypothetical protein; Validated
7-211 1.68e-22

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 91.17  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751   7 ILSRLAPYGACDVADALAKLKHPAGGflsglkLRGPDQNTKIIGRAHTVLFRA-NSVAPQKKgfkghyIDSVTPGSVLFM 85
Cdd:PRK06201   18 LVEAFRELPVANISDSMNRMTAGGAG------LRPMHRGGRLAGTALTVRTRPgDNLMIHRA------LDLARPGDVIVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  86 SAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVgITAGQEVCYSSEINVPVPLRSahqpdVW 165
Cdd:PRK06201   86 DGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGV-THRGPYKDGPGEINVPVAIGG-----MV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2781192751 166 INPGDIIVGDENGVACIPQELEDEVADLIPLLAERDRLSMEDLMAG 211
Cdd:PRK06201  160 IEPGDLIVGDDDGLVAVPPADAEALLEAARAKHAAEAKQLEAIRAG 205
 
Name Accession Description Interval E-value
RraA COG0684
RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal ...
4-218 6.44e-44

RNA degradosome component RraA (regulator of RNase E activity) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440448 [Multi-domain]  Cd Length: 204  Bit Score: 146.47  E-value: 6.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751   4 SKNILSRLAPYGACDVADALAKLkhPAGGFLSGLKLRGPDQntKIIGRAHTVLFRANSVAPQKkgfkgHYIDSVTPGSVL 83
Cdd:COG0684     4 DAELLERLAAVSTATVSDALDRL--LRGALDPGIRPLHPGA--RLVGPAVTVRYRPGDNLMLH-----EAIDLAPPGDVL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  84 FMSAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVGITAGQEVCYSSEINVPVPLRsahqpD 163
Cdd:COG0684    75 VIDAGGDTDAALWGELLATAAKARGVAGVVIDGAVRDVAEIRELGFPVFARGVTPRGTKKRVGPGEINVPVSIG-----G 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2781192751 164 VWINPGDIIVGDENGVACIPQELEDEVADLIPLLAERDRLSMEDLMAGMKAEDVF 218
Cdd:COG0684   150 VTVRPGDLVVADDDGVVVIPAELAEEVLEAAEAIEAREEFIRERIRAGESLADLY 204
RraA_family cd16841
ribonuclease activity regulator RraA family; RraA protein family is named after the regulator ...
17-182 1.90e-37

ribonuclease activity regulator RraA family; RraA protein family is named after the regulator of ribonuclease activity A (RraA), a protein that binds to RNase E and inhibits RNase E endonucleolytic cleavages. Members also include proteins with other functions, like a 4-hydroxy-4-methyl-2-oxoglutarate/4-carboxy-4-hydroxy-2-oxoadipate (HMG/CHA) aldolase from Pseudomonas putida, which catalyzes the last step of the bacterial protocatechuate 4,5-cleavage pathway and the uncharacterized YER010Cp protein from yeast, an organism lacking RNAse E.


Pssm-ID: 319245 [Multi-domain]  Cd Length: 150  Bit Score: 127.96  E-value: 1.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  17 CDVADALAKLkhpaGGFLSGLkLRGPDQNTKIIGRAHTVLFRansvaPQKKGFKGHYIDSVTPGSVLFMSAPAHLPNAIY 96
Cdd:cd16841     1 ADLSDALDRL----GGVLPGI-IRPLGGGARFVGPAVTVKCF-----PDDNLLVREALDEAGPGDVLVVDGGGSLRCALW 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  97 GGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVgITAGQEVCYSSEINVPVPLrsahqPDVWINPGDIIVGDE 176
Cdd:cd16841    71 GDLLATLAKARGWAGIVIDGAVRDVDEIRELDFPVFARGT-TPRGSKKVGPGEVNVPVTI-----GGVTVNPGDIIVADE 144

                  ....*.
gi 2781192751 177 NGVACI 182
Cdd:cd16841   145 DGVVVI 150
RraA-like pfam03737
Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) ...
17-179 1.62e-31

Aldolase/RraA; Members of this family include regulator of ribonuclease E activity A (RraA) and 4-hydroxy-4-methyl-2-oxoglutarate (HMG)/4-carboxy- 4-hydroxy-2-oxoadipate (CHA) aldolase, also known as RraA-like protein. RraA acts as a trans-acting modulator of RNA turnover, binding essential endonuclease RNase E and inhibiting RNA processing. RraA-like proteins seem to contain aldolase and/or decarboxylase activity either in place of or in addition to the RNase E inhibitor functions.


Pssm-ID: 427475 [Multi-domain]  Cd Length: 148  Bit Score: 112.60  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  17 CDVADALAKLKHPAGGfLSGLKlrgPDQNTKIIGRAHTVLFRansvaPQKKGFKGHYIDSVTPGSVLFMSAPaHLPNAIY 96
Cdd:pfam03737   1 ADLSDALGSYGGRLGA-MPGIR---PLNPGPFVGPAVTVKCF-----PEDNLLVHEALDEAGPGDVLVVDGG-GGSRAAL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  97 GGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDV----GITAGQEvcyssEINVPVPLrsahqPDVWINPGDII 172
Cdd:pfam03737  71 GDLLATLAKANGWAGIVIDGAVRDVDELRELDFPVFARGTtprgSVKRGPG-----EVNVPVTI-----GGVTVRPGDII 140

                  ....*..
gi 2781192751 173 VGDENGV 179
Cdd:pfam03737 141 VADEDGV 147
PRK06201 PRK06201
hypothetical protein; Validated
7-211 1.68e-22

hypothetical protein; Validated


Pssm-ID: 180465 [Multi-domain]  Cd Length: 221  Bit Score: 91.17  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751   7 ILSRLAPYGACDVADALAKLKHPAGGflsglkLRGPDQNTKIIGRAHTVLFRA-NSVAPQKKgfkghyIDSVTPGSVLFM 85
Cdd:PRK06201   18 LVEAFRELPVANISDSMNRMTAGGAG------LRPMHRGGRLAGTALTVRTRPgDNLMIHRA------LDLARPGDVIVV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  86 SAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVgITAGQEVCYSSEINVPVPLRSahqpdVW 165
Cdd:PRK06201   86 DGGGDLTNALVGEIMLAIAARRGVAGVVIDGAVRDVAALREMGFPVFARGV-THRGPYKDGPGEINVPVAIGG-----MV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2781192751 166 INPGDIIVGDENGVACIPQELEDEVADLIPLLAERDRLSMEDLMAG 211
Cdd:PRK06201  160 IEPGDLIVGDDDGLVAVPPADAEALLEAARAKHAAEAKQLEAIRAG 205
PRK08245 PRK08245
hypothetical protein; Validated
72-211 1.12e-18

hypothetical protein; Validated


Pssm-ID: 236200  Cd Length: 240  Bit Score: 81.49  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  72 HYIDSVTPGSVLFMSAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRdvGITAGQEVC--YSSE 149
Cdd:PRK08245   80 AAIETCPPGCVLVVDARGDARAGSFGDILCTRLKKRGVAGLVTDGGVRDSPGIAALGLPVWCA--GPSAPTNLTglTAVD 157
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2781192751 150 INVPVPLrsahqPDVWINPGDIIVGDENGVACIPQELEDEVADLIPLLAERDRLSMEDLMAG 211
Cdd:PRK08245  158 INVPIGC-----GGVAVFPGDIIVADDDGVVVIPAALADEVAAEAVEQERWEDFIREEVAAG 214
PRK07028 PRK07028
bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated
18-191 6.15e-17

bifunctional hexulose-6-phosphate synthase/ribonuclease regulator; Validated


Pssm-ID: 235912 [Multi-domain]  Cd Length: 430  Bit Score: 78.91  E-value: 6.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  18 DVADALaklkHPAGGfLSGLKLRGPDqnTKIIGRAHTVlfransvapqkKGFKGHY------IDSVTPGSVLFMSAPA-H 90
Cdd:PRK07028  240 NISDAM----HRKGA-MKGIKPLVRG--TKMVGKAVTV-----------QTFAGDWakpveaIDVAKPGDVIVIYNSSkD 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  91 LpnAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSRDVGITAGQEVCYsSEINVPVPLRSahqpdVWINPGD 170
Cdd:PRK07028  302 I--APWGELATLSCLNKGIAGVVIDGAVRDVDEIRKLGFPVFARAIVPNAGEPKGF-GEINAEIVCGG-----QTVRPGD 373
                         170       180
                  ....*....|....*....|.
gi 2781192751 171 IIVGDENGVACIPQELEDEVA 191
Cdd:PRK07028  374 WIIGDENGVVVVPKERAYEIA 394
PRK12764 PRK12764
fumarylacetoacetate hydrolase family protein;
11-192 1.69e-15

fumarylacetoacetate hydrolase family protein;


Pssm-ID: 237193 [Multi-domain]  Cd Length: 500  Bit Score: 74.79  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  11 LAPYGACDVADAL-AKL-KHPAGGFLSGLKLRGPDQ-----------NTKIIGRAHTVLFRAN----------SVAPQKK 67
Cdd:PRK12764  259 LAPQAAGPLSPELkAKLaSVATATLSAQLRKRGLNNvsidgltptrpGRRMVGRARTLRYVPNredlfkehggGFNAQKR 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  68 GFkghyiDSVTPGSVLFMSAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFsrdvgiTAGQEvcys 147
Cdd:PRK12764  339 AF-----DSVNPGEVLVIEARGEKGTGTLGDILALRAQVRGAAGVVTDGGVRDYAAVAELGLPVF------FAGPH---- 403
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2781192751 148 seinvPVPLRSAHQP---DVWI-------NPGDIIVGDENGVACIPQELEDEVAD 192
Cdd:PRK12764  404 -----PAVLGRRHVPwdvDITVacggatvQPGDVIVGDDDGVVVIPPALAEEVAD 453
PRK09262 PRK09262
hypothetical protein; Provisional
74-221 4.19e-15

hypothetical protein; Provisional


Pssm-ID: 181735  Cd Length: 225  Bit Score: 71.50  E-value: 4.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  74 IDSVTPGSVLFMSAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFSR------DVGITAGQevcys 147
Cdd:PRK09262   72 VEQCQPGDVLVVAPTSPCTDGFFGDLLATSLQARGVRGLVIDAGVRDVRTLTEMGFPVWSRaisaqgTVKATLGS----- 146
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2781192751 148 seINVPVPLRSAhqpdvWINPGDIIVGDENGVACIPQELEDEVADlipllAERDRLSMED-----LMAGMKAEDVFRNR 221
Cdd:PRK09262  147 --VNVPVVCAGA-----LVNPGDVVVADDDGVVVVPRAQAAAVAD-----AAEAREANEEskrerLAAGELGLDIYKMR 213
PRK12487 PRK12487
putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;
80-186 2.28e-05

putative 4-hydroxy-4-methyl-2-oxoglutarate aldolase;


Pssm-ID: 183553  Cd Length: 163  Bit Score: 43.41  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2781192751  80 GSVLFMSAPAHLPNAIYGGLMSMRAKTLGAVGTIVDGRLRDLAEHRHMKYPVFS----------RDVGitagqevcyssE 149
Cdd:PRK12487   58 GKVLVVDGGGSCRRALLGDQIAQSALDNGWEGIVINGCVRDVGALSTMDLGVKAlgaspiktekRGQG-----------E 126
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2781192751 150 INVPVPLRSahqpdVWINPGDIIVGDENGVACIPQEL 186
Cdd:PRK12487  127 VNVTLTMGN-----VIIEPGDMLYADENGIAVSKEAL 158
 
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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