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Conserved domains on  [gi|488981668|ref|WP_002892496|]
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MULTISPECIES: myo-inosose-2 dehydratase [Klebsiella]

Protein Classification

IolE/MocC family protein( domain architecture ID 1001934)

IolE/MocC family similar to Salmonella enterica inosose dehydratase (IolE) and Sinorhizobium meliloti rhizopine catabolism protein MocC

CATH:  3.20.20.150

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
VpdB_C super family cl30226
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
6-295 1.02e-120

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


The actual alignment was detected with superfamily member TIGR04379:

Pssm-ID: 421976  Cd Length: 290  Bit Score: 347.72  E-value: 1.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668    6 LRWGVSPLCWTNDVLEDLGGDIPLDTCLREAREAGYQGIELGRKFPRQASTLGPLLAAADLRLASGWYSGMLADRSVEAE 85
Cdd:TIGR04379   2 VKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPRDPAVLRAALEERGLELVSGWYSGLLLTRSVEEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   86 LEAVREHAQLLRQLGAKVMVYGECGQLPGETPlDEPISLSPPLSRVSLAAYCHKLNTFADLLlRDYDLQLAYHHHLMMLV 165
Cdd:TIGR04379  82 IEAFRPHLEFLKAMGAKVIVVCETGGSIQGDP-DTPLSDRPVLTDEEWERLGEGLNRLGEIA-AEQGMKLAYHHHMGTVV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668  166 EHDDELERFLSHTHDN-VGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDVRPQVLGRLYRENLSFNEAVRAGLFTIP 244
Cdd:TIGR04379 160 ETEEEIDRLMAMTDPElVGLLYDTGHATFAGGDPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFTVP 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488981668  245 GDGCIDYAPILDFVRDSDYRGWLIIEAEQDPAMAPPLATASRAYAWLAHHL 295
Cdd:TIGR04379 240 GDGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
 
Name Accession Description Interval E-value
myo_inos_iolE TIGR04379
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
6-295 1.02e-120

myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]


Pssm-ID: 275172  Cd Length: 290  Bit Score: 347.72  E-value: 1.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668    6 LRWGVSPLCWTNDVLEDLGGDIPLDTCLREAREAGYQGIELGRKFPRQASTLGPLLAAADLRLASGWYSGMLADRSVEAE 85
Cdd:TIGR04379   2 VKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPRDPAVLRAALEERGLELVSGWYSGLLLTRSVEEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   86 LEAVREHAQLLRQLGAKVMVYGECGQLPGETPlDEPISLSPPLSRVSLAAYCHKLNTFADLLlRDYDLQLAYHHHLMMLV 165
Cdd:TIGR04379  82 IEAFRPHLEFLKAMGAKVIVVCETGGSIQGDP-DTPLSDRPVLTDEEWERLGEGLNRLGEIA-AEQGMKLAYHHHMGTVV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668  166 EHDDELERFLSHTHDN-VGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDVRPQVLGRLYRENLSFNEAVRAGLFTIP 244
Cdd:TIGR04379 160 ETEEEIDRLMAMTDPElVGLLYDTGHATFAGGDPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFTVP 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488981668  245 GDGCIDYAPILDFVRDSDYRGWLIIEAEQDPAMAPPLATASRAYAWLAHHL 295
Cdd:TIGR04379 240 GDGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
6-288 4.34e-42

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 145.54  E-value: 4.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   6 LRWGVSPLCWtndvledlgGDIPLDTCLREAREAGYQGIELGRKF--PRQASTLGPLLAAADLRLASGWYSG---MLADR 80
Cdd:COG1082    1 MKLGLSTYSL---------PDLDLEEALRAAAELGYDGVELAGGDldEADLAELRAALADHGLEISSLHAPGlnlAPDPE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668  81 SVEAELEAVREHAQLLRQLGAKVMVYGECGQLPGETPLDEpislspplsrvSLAAYCHKLNTFADLLlRDYDLQLAYHHH 160
Cdd:COG1082   72 VREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEE-----------AWDRLAERLRELAELA-EEAGVTLALENH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668 161 LMMLVEHDDELERFLSHT-HDNVGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDvrpqvlgrlyrenlsfneaVRAG 239
Cdd:COG1082  140 EGTFVNTPEEALRLLEAVdSPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKD-------------------ADGD 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488981668 240 LFTIPGDGCIDYAPILDFVRDSDYRGWLIIEAEQDPAMAPPLATASRAY 288
Cdd:COG1082  201 QHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDPDDPEEAARESLEY 249
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
33-291 1.19e-20

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 88.58  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   33 LREAREAGYQGIELG--------------RKFPRQASTLGPLLAAADLRLASGWYSgmLADRSVEAELEAVREHAQLLRQ 98
Cdd:pfam01261   1 LAAAAELGFDGVELFtrrwfrpplsdeeaEELKAALKEHGLEIVVHAPYLGDNLAS--PDEEEREKAIDRLKRAIELAAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   99 LGAKVMVygecgQLPGetpldepiSLSPPLSRVSLAAYCHKLNTFADLLlRDYDLQLAYHHHLMMLVEHD---DELERFL 175
Cdd:pfam01261  79 LGAKLVV-----FHPG--------SDLGDDPEEALARLAESLRELADLA-EREGVRLALEPLAGKGTNVGntfEEALEII 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668  176 SHT-HDNVGLAFDTGHAFVAGvEIPRVLHKYGHR-IRHLHLKDVRPQVLGRLYRenlsfneavraglFTIPGDGCIDYAP 253
Cdd:pfam01261 145 DEVdSPNVGVCLDTGHLFAAG-DGDLFELRLGDRyIGHVHLKDSKNPLGSGPDR-------------HVPIGEGVIDFEA 210
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 488981668  254 ILDFVRDSDYRGWLIIEAEQDPamaPPLATASRAYAWL 291
Cdd:pfam01261 211 LFRALKEIGYDGPLSLETFNDG---PPEEGAREGLEWL 245
VpdB_C cd22304
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
173-281 5.22e-10

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


Pssm-ID: 408997  Cd Length: 126  Bit Score: 56.52  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668 173 RFLSHTHDNVGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDVRPQVLGRLYRENLSFNEAVRAGlfTIPGDGCIDYA 252
Cdd:cd22304    3 RQQEQSIPKTMLLLSRLQNFKQGDDWSQHVRKTIDRLMLLKGENVRPPITKDQVDLCLQWQEIKSVH--ANPAERLREFN 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488981668 253 PILDFVR----DSDYRGWLIIEAEQDPAMAPPL 281
Cdd:cd22304   81 YALLISPlvsnQQEINFSKEIRKEIDSLKRLPG 113
 
Name Accession Description Interval E-value
myo_inos_iolE TIGR04379
myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, ...
6-295 1.02e-120

myo-inosose-2 dehydratase; Members of this family include the enzyme myo-inosose-2 dehydratase, product of the gene iolE, as found in inositol utilization cassettes in many species. [Energy metabolism, Sugars]


Pssm-ID: 275172  Cd Length: 290  Bit Score: 347.72  E-value: 1.02e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668    6 LRWGVSPLCWTNDVLEDLGGDIPLDTCLREAREAGYQGIELGRKFPRQASTLGPLLAAADLRLASGWYSGMLADRSVEAE 85
Cdd:TIGR04379   2 VKLGIAPIAWTNDDLPELGGDTTLEQCLSEMALAGFTGTELGNKFPRDPAVLRAALEERGLELVSGWYSGLLLTRSVEEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   86 LEAVREHAQLLRQLGAKVMVYGECGQLPGETPlDEPISLSPPLSRVSLAAYCHKLNTFADLLlRDYDLQLAYHHHLMMLV 165
Cdd:TIGR04379  82 IEAFRPHLEFLKAMGAKVIVVCETGGSIQGDP-DTPLSDRPVLTDEEWERLGEGLNRLGEIA-AEQGMKLAYHHHMGTVV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668  166 EHDDELERFLSHTHDN-VGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDVRPQVLGRLYRENLSFNEAVRAGLFTIP 244
Cdd:TIGR04379 160 ETEEEIDRLMAMTDPElVGLLYDTGHATFAGGDPLAVLEKHGDRIVHVHLKDVRPEVLERVRNEDLSFLDAVLKGVFTVP 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488981668  245 GDGCIDYAPILDFVRDSDYRGWLIIEAEQDPAMAPPLATASRAYAWLAHHL 295
Cdd:TIGR04379 240 GDGCIDFAPIFAALAARDYEGWIVVEAEQDPAKAHPLEYAKKAYKYLSALA 290
YcjR COG1082
Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];
6-288 4.34e-42

Sugar phosphate isomerase/epimerase [Carbohydrate transport and metabolism];


Pssm-ID: 440699 [Multi-domain]  Cd Length: 254  Bit Score: 145.54  E-value: 4.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   6 LRWGVSPLCWtndvledlgGDIPLDTCLREAREAGYQGIELGRKF--PRQASTLGPLLAAADLRLASGWYSG---MLADR 80
Cdd:COG1082    1 MKLGLSTYSL---------PDLDLEEALRAAAELGYDGVELAGGDldEADLAELRAALADHGLEISSLHAPGlnlAPDPE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668  81 SVEAELEAVREHAQLLRQLGAKVMVYGECGQLPGETPLDEpislspplsrvSLAAYCHKLNTFADLLlRDYDLQLAYHHH 160
Cdd:COG1082   72 VREAALERLKRAIDLAAELGAKVVVVHPGSPPPPDLPPEE-----------AWDRLAERLRELAELA-EEAGVTLALENH 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668 161 LMMLVEHDDELERFLSHT-HDNVGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDvrpqvlgrlyrenlsfneaVRAG 239
Cdd:COG1082  140 EGTFVNTPEEALRLLEAVdSPNVGLLLDTGHALLAGEDPVELLRKLGDRIKHVHLKD-------------------ADGD 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 488981668 240 LFTIPGDGCIDYAPILDFVRDSDYRGWLIIEAEQDPAMAPPLATASRAY 288
Cdd:COG1082  201 QHLPPGEGDIDFAAILRALKEAGYDGWLSLEVESDPDDPEEAARESLEY 249
AP_endonuc_2 pfam01261
Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose ...
33-291 1.19e-20

Xylose isomerase-like TIM barrel; This TIM alpha/beta barrel structure is found in xylose isomerase and in endonuclease IV (EC:3.1.21.2). This domain is also found in the N termini of bacterial myo-inositol catabolism proteins. These are involved in the myo-inositol catabolism pathway, and is required for growth on myo-inositol in Rhizobium leguminosarum bv. viciae.


Pssm-ID: 426164 [Multi-domain]  Cd Length: 248  Bit Score: 88.58  E-value: 1.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   33 LREAREAGYQGIELG--------------RKFPRQASTLGPLLAAADLRLASGWYSgmLADRSVEAELEAVREHAQLLRQ 98
Cdd:pfam01261   1 LAAAAELGFDGVELFtrrwfrpplsdeeaEELKAALKEHGLEIVVHAPYLGDNLAS--PDEEEREKAIDRLKRAIELAAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668   99 LGAKVMVygecgQLPGetpldepiSLSPPLSRVSLAAYCHKLNTFADLLlRDYDLQLAYHHHLMMLVEHD---DELERFL 175
Cdd:pfam01261  79 LGAKLVV-----FHPG--------SDLGDDPEEALARLAESLRELADLA-EREGVRLALEPLAGKGTNVGntfEEALEII 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668  176 SHT-HDNVGLAFDTGHAFVAGvEIPRVLHKYGHR-IRHLHLKDVRPQVLGRLYRenlsfneavraglFTIPGDGCIDYAP 253
Cdd:pfam01261 145 DEVdSPNVGVCLDTGHLFAAG-DGDLFELRLGDRyIGHVHLKDSKNPLGSGPDR-------------HVPIGEGVIDFEA 210
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 488981668  254 ILDFVRDSDYRGWLIIEAEQDPamaPPLATASRAYAWL 291
Cdd:pfam01261 211 LFRALKEIGYDGPLSLETFNDG---PPEEGAREGLEWL 245
VpdB_C cd22304
C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of ...
173-281 5.22e-10

C-terminal fragment of effector protein VpdB; This model represents the C-terminal fragment of the effector protein VpdB that binds the Legionella pneumophila Dot/Icm type IVB coupling protein (T4CP) complex which includes IcmS, IcmW, and LvgA. These L. pneumophila proteins are known to selectively assist the export of a subclass of effectors. The effector protein VpdB, like other L. pneumophila effectors VpdA, VpdC and VpdD, is a homolog of phospholipase A (PLA) patatin-like enzymes. However, VpdB does not appear to be involved in phospholipid metabolism. The structure reveals interactions between LvgA and a linear motif in the C-terminus of VpdB. This binding interface of LvgA also interacts with the C-terminal region of three additional L. pneumophila effectors, SidH, SetA, and PieA.


Pssm-ID: 408997  Cd Length: 126  Bit Score: 56.52  E-value: 5.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668 173 RFLSHTHDNVGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDVRPQVLGRLYRENLSFNEAVRAGlfTIPGDGCIDYA 252
Cdd:cd22304    3 RQQEQSIPKTMLLLSRLQNFKQGDDWSQHVRKTIDRLMLLKGENVRPPITKDQVDLCLQWQEIKSVH--ANPAERLREFN 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488981668 253 PILDFVR----DSDYRGWLIIEAEQDPAMAPPL 281
Cdd:cd22304   81 YALLISPlvsnQQEINFSKEIRKEIDSLKRLPG 113
Hyi COG3622
Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and ...
174-267 2.17e-06

Hydroxypyruvate/dehydroerythronate isomerase, Hyi/OtnI family [Carbohydrate transport and metabolism];


Pssm-ID: 442840  Cd Length: 260  Bit Score: 48.18  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668 174 FLSHT-----------HDNVGLAFDTGHAFVAGVEIPRVLHKYGHRIRHLHLKDVrPqvlGRlyrenlsfNEavraglft 242
Cdd:COG3622  154 FLDTTaqavaiieavgSPNLKLLYDIYHMQIMEGDLIRTIRRHLPRIGHVQIADV-P---GR--------HE-------- 213
                         90       100
                 ....*....|....*....|....*
gi 488981668 243 iPGDGCIDYAPILDFVRDSDYRGWL 267
Cdd:COG3622  214 -PGTGELNYPAIFKALDALGYDGWV 237
AP2Ec cd00019
AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester ...
175-270 5.42e-04

AP endonuclease family 2; These endonucleases play a role in DNA repair. Cleave phosphodiester bonds at apurinic or apyrimidinic sites; the alignment also contains hexulose-6-phosphate isomerases, enzymes that catalyze the epimerization of D-arabino-6-hexulose 3-phosphate to D-fructose 6-phosphate, via cleaving the phosphoesterbond with the sugar.


Pssm-ID: 237986  Cd Length: 279  Bit Score: 40.77  E-value: 5.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488981668 175 LSHTHDNVGLAFDTGHAFVAGVEIPRV--LHKYG---------HRIRHLHLKDVRPqVLGRLYRENLSFNEavraglfti 243
Cdd:cd00019  164 LIKEKPRVGVCIDTCHIFAAGYDISTVegFEKVLeefdkviglEYLKAIHLNDSKG-ELGSGKDRHEPIGE--------- 233
                         90       100
                 ....*....|....*....|....*...
gi 488981668 244 pgdGCIDYAPILDFVRDSDYR-GWLIIE 270
Cdd:cd00019  234 ---GDIDGEELFKELKKDPYQnIPLILE 258
 
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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