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Conserved domains on  [gi|1063743330|ref|NP_001330820|]
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Haloacid dehalogenase-like hydrolase (HAD) superfamily protein [Arabidopsis thaliana]

Protein Classification

HAD family hydrolase( domain architecture ID 229399)

HAD (haloacid dehalogenase) family hydrolase; the HAD family includes phosphoesterases, ATPases, phosphonatases, dehalogenases, and sugar phosphomutases acting on a remarkably diverse set of substrates

EC:  3.6.3.-
Gene Ontology:  GO:0005524|GO:0016887|GO:0005215

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
1-324 0e+00

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member PLN03017:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 366  Bit Score: 630.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330   1 MVSQNVVVSDAKTGIITVSTVSNSSvfTPTAQKPPtaPGYISVSKKKLLKNLEINGAdQSQRLNSWVDSMRASSPTHLKS 80
Cdd:PLN03017    1 SASQNVVVSETTTSSIIPNNVSNSS--NSSSQKLP--PGLISISKKKLLKNIDIING-GGQRINAWVDSMRASSPTHLKS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330  81 -LSSFSSEEEHNSWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVT 159
Cdd:PLN03017   76 lPSSISSQQQLNSWIMQHPSALEMFEQIMEASRGKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKCFPTAIVT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 160 GRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFC 239
Cdd:PLN03017  156 GRCIDKVYNFVKLAELYYAGSHGMDIKGPAKGFSRHKRVKQSLLYQPANDYLPMIDEVYRQLLEKTKSTPGAKVENHKFC 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 240 LSVHFRCVDEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDE 319
Cdd:PLN03017  236 ASVHFRCVDEKKWSELVLQVRSVLKNFPTLKLTQGRKVFEIRPMIEWDKGKALEFLLESLGFGNTNNVFPVYIGDDRTDE 315

                  ....*
gi 1063743330 320 DAFKV 324
Cdd:PLN03017  316 DAFKM 320
 
Name Accession Description Interval E-value
PLN03017 PLN03017
trehalose-phosphatase
1-324 0e+00

trehalose-phosphatase


Pssm-ID: 178591 [Multi-domain]  Cd Length: 366  Bit Score: 630.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330   1 MVSQNVVVSDAKTGIITVSTVSNSSvfTPTAQKPPtaPGYISVSKKKLLKNLEINGAdQSQRLNSWVDSMRASSPTHLKS 80
Cdd:PLN03017    1 SASQNVVVSETTTSSIIPNNVSNSS--NSSSQKLP--PGLISISKKKLLKNIDIING-GGQRINAWVDSMRASSPTHLKS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330  81 -LSSFSSEEEHNSWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVT 159
Cdd:PLN03017   76 lPSSISSQQQLNSWIMQHPSALEMFEQIMEASRGKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKCFPTAIVT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 160 GRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFC 239
Cdd:PLN03017  156 GRCIDKVYNFVKLAELYYAGSHGMDIKGPAKGFSRHKRVKQSLLYQPANDYLPMIDEVYRQLLEKTKSTPGAKVENHKFC 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 240 LSVHFRCVDEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDE 319
Cdd:PLN03017  236 ASVHFRCVDEKKWSELVLQVRSVLKNFPTLKLTQGRKVFEIRPMIEWDKGKALEFLLESLGFGNTNNVFPVYIGDDRTDE 315

                  ....*
gi 1063743330 320 DAFKV 324
Cdd:PLN03017  316 DAFKM 320
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
119-324 5.99e-78

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 238.00  E-value: 5.99e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 119 FLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTS--IVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGfSRYN 196
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPNTvaIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGG-DWYN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 197 kdkpsvlyQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEK----KWSELASKVRSVVKNYPTLKLS 272
Cdd:pfam02358  80 --------QAEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDfgsfQAKELAEHLESVLQDNPPLRVT 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063743330 273 QGRKVFEIRPIIKWnKGKALEFLLESLGFENCNDVFPIYIGDDKTDEDAFKV 324
Cdd:pfam02358 152 QGKKVVEVRPVGVS-KGKAVEFILEELGSAGSLPDFPLCIGDDRTDEDMFSV 202
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
117-324 7.31e-58

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 186.34  E-value: 7.31e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 117 VMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAK--CFPTSIVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSR 194
Cdd:cd01627     1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAAdpKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 195 YNKDKPSvlyqpagdfLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVD---EKKWSELASKVRSVVKNYPTLKl 271
Cdd:cd01627    81 TLAPKAD---------LEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADpegARAALELALHLASDLLKALEVV- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063743330 272 sQGRKVFEIRPiIKWNKGKALEFLLESLGFEncnDVFPIYIGDDKTDEDAFKV 324
Cdd:cd01627   151 -PGKKVVEVRP-VGVNKGEAVERILGELPFA---GDFVLCAGDDVTDEDAFRA 198
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
113-324 1.90e-52

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 173.07  E-value: 1.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 113 GKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTS--IVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPtk 190
Cdd:COG1877     1 APRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPGGAvaIVSGRDLADLDRLLGPLGLPLAGSHGAERRLP-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 191 gfsrynkDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEKKWSELASKVRSVVKNY-PTL 269
Cdd:COG1877    79 -------GGEWEVLPLAAEAPEWLDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLgPGL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063743330 270 KLSQGRKVFEIRPiIKWNKGKALEFLLESLGFencnDVFPIYIGDDKTDEDAFKV 324
Cdd:COG1877   152 EVLPGKKVVELRP-AGVDKGRAVRALLAELPF----GRAPVFIGDDVTDEDAFAA 201
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
113-330 2.70e-33

trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273219 [Multi-domain]  Cd Length: 244  Bit Score: 123.02  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 113 GKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFP--TSIVTGRCIDKVYSFVKLAELYYAGSHG--MDIKGP 188
Cdd:TIGR00685   1 ARKRAFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHnaIWIISGRKFLEKWLGVKLPGLGLAGEHGceMKDNGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 189 TKGFSRynkdkpsvlyqpAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFR-CVD----EKKWSELASKVRSvv 263
Cdd:TIGR00685  81 CQDWVN------------LTEKIPSWKVRANELREEITTRPGVFIERKGVALAWHYRqAPVpelaRFRAKELKEKILS-- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063743330 264 knYPTLKLSQGRKVFEIRPiIKWNKGKALEFLLESLGFENCNdvfPIYIGDDKTDEDAFKVYITNEN 330
Cdd:TIGR00685 147 --FTDLEVMDGKAVVELKP-RFVNKGEIVKRLLWHQPGSGIS---PVYLGDDITDEDAFRVVNNQWG 207
 
Name Accession Description Interval E-value
PLN03017 PLN03017
trehalose-phosphatase
1-324 0e+00

trehalose-phosphatase


Pssm-ID: 178591 [Multi-domain]  Cd Length: 366  Bit Score: 630.14  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330   1 MVSQNVVVSDAKTGIITVSTVSNSSvfTPTAQKPPtaPGYISVSKKKLLKNLEINGAdQSQRLNSWVDSMRASSPTHLKS 80
Cdd:PLN03017    1 SASQNVVVSETTTSSIIPNNVSNSS--NSSSQKLP--PGLISISKKKLLKNIDIING-GGQRINAWVDSMRASSPTHLKS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330  81 -LSSFSSEEEHNSWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVT 159
Cdd:PLN03017   76 lPSSISSQQQLNSWIMQHPSALEMFEQIMEASRGKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKCFPTAIVT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 160 GRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFC 239
Cdd:PLN03017  156 GRCIDKVYNFVKLAELYYAGSHGMDIKGPAKGFSRHKRVKQSLLYQPANDYLPMIDEVYRQLLEKTKSTPGAKVENHKFC 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 240 LSVHFRCVDEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDE 319
Cdd:PLN03017  236 ASVHFRCVDEKKWSELVLQVRSVLKNFPTLKLTQGRKVFEIRPMIEWDKGKALEFLLESLGFGNTNNVFPVYIGDDRTDE 315

                  ....*
gi 1063743330 320 DAFKV 324
Cdd:PLN03017  316 DAFKM 320
PLN02151 PLN02151
trehalose-phosphatase
8-324 7.25e-175

trehalose-phosphatase


Pssm-ID: 177812  Cd Length: 354  Bit Score: 488.80  E-value: 7.25e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330   8 VSDAKTGIITVSTVSNSSVFTPTAQKPPTAPgyisvsKKKLLKNLEINGAdqSQRLNSWVDSMRASSPTHLKSLSSFSSe 87
Cdd:PLN02151    5 IEENTTKMLETKTISNSEVLYVGRDDGDTSP------KTKALHDFQINNG--GGLIRSWVDSMRACSPTRPKSFNKQSC- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330  88 eehnsWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVTGRCIDKVY 167
Cdd:PLN02151   76 -----WIKEHPSALNMFEEILHKSEGKQIVMFLDYDGTLSPIVDDPDRAFMSKKMRNTVRKLAKCFPTAIVSGRCREKVS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 168 SFVKLAELYYAGSHGMDIKGPTKGfSRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCV 247
Cdd:PLN02151  151 SFVKLTELYYAGSHGMDIKGPEQG-SKYKKENQSLLCQPATEFLPVINEVYKKLVEKTKSIPGAKVENNKFCASVHFRCV 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063743330 248 DEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDEDAFKV 324
Cdd:PLN02151  230 EENKWSDLANQVRSVLKNYPKLMLTQGRKVLEIRPIIKWDKGKALEFLLESLGYANCTDVFPIYIGDDRTDEDAFKI 306
PLN02580 PLN02580
trehalose-phosphatase
19-324 2.59e-134

trehalose-phosphatase


Pssm-ID: 215317 [Multi-domain]  Cd Length: 384  Bit Score: 387.24  E-value: 2.59e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330  19 STVSNSSVFTPTAQKPPTAPGYISVSKKKLLKNLEINGADQSQRLNSWVDSMRASSPTHLKSLSSFSSEEEHN------- 91
Cdd:PLN02580   16 APINKSRLGIRSNLLPYSSAGASFSSNLFLTIPRKKTGKLDDVRSNGWLDAMKSSSPPRKKLNKDFNVELASPdtdfayr 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330  92 SWIKRHPSALNMFERIIEEARGKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTSIVTGRCIDKVYSFVK 171
Cdd:PLN02580   96 TWMLKYPSALTSFEQIANFAKGKKIALFLDYDGTLSPIVDDPDRALMSDAMRSAVKNVAKYFPTAIISGRSRDKVYELVG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 172 LAELYYAGSHGMDIKGPTKGF----------SRYNKDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLS 241
Cdd:PLN02580  176 LTELYYAGSHGMDIMGPVRESvsndhpncikSTDQQGKEVNLFQPASEFLPMIDEVFRSLVESTKDIKGAKVENHKFCVS 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 242 VHFRCVDEKKWSELASKVRSVVKNYPTLKLSQGRKVFEIRPIIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDEDA 321
Cdd:PLN02580  256 VHYRNVDEKNWPLVAQCVHDVLKKYPRLRLTHGRKVLEVRPVIDWNKGKAVEFLLESLGLSNCDDVLPIYIGDDRTDEDA 335

                  ...
gi 1063743330 322 FKV 324
Cdd:PLN02580  336 FKV 338
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
119-324 5.99e-78

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 238.00  E-value: 5.99e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 119 FLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTS--IVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGfSRYN 196
Cdd:pfam02358   1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPNTvaIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGG-DWYN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 197 kdkpsvlyQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEK----KWSELASKVRSVVKNYPTLKLS 272
Cdd:pfam02358  80 --------QAEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDfgsfQAKELAEHLESVLQDNPPLRVT 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063743330 273 QGRKVFEIRPIIKWnKGKALEFLLESLGFENCNDVFPIYIGDDKTDEDAFKV 324
Cdd:pfam02358 152 QGKKVVEVRPVGVS-KGKAVEFILEELGSAGSLPDFPLCIGDDRTDEDMFSV 202
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
117-324 7.31e-58

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 186.34  E-value: 7.31e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 117 VMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAK--CFPTSIVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPTKGFSR 194
Cdd:cd01627     1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAAdpKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 195 YNKDKPSvlyqpagdfLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVD---EKKWSELASKVRSVVKNYPTLKl 271
Cdd:cd01627    81 TLAPKAD---------LEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADpegARAALELALHLASDLLKALEVV- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063743330 272 sQGRKVFEIRPiIKWNKGKALEFLLESLGFEncnDVFPIYIGDDKTDEDAFKV 324
Cdd:cd01627   151 -PGKKVVEVRP-VGVNKGEAVERILGELPFA---GDFVLCAGDDVTDEDAFRA 198
OtsB COG1877
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
113-324 1.90e-52

Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 441481 [Multi-domain]  Cd Length: 242  Bit Score: 173.07  E-value: 1.90e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 113 GKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTS--IVTGRCIDKVYSFVKLAELYYAGSHGMDIKGPtk 190
Cdd:COG1877     1 APRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPGGAvaIVSGRDLADLDRLLGPLGLPLAGSHGAERRLP-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 191 gfsrynkDKPSVLYQPAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEKKWSELASKVRSVVKNY-PTL 269
Cdd:COG1877    79 -------GGEWEVLPLAAEAPEWLDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLgPGL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063743330 270 KLSQGRKVFEIRPiIKWNKGKALEFLLESLGFencnDVFPIYIGDDKTDEDAFKV 324
Cdd:COG1877   152 EVLPGKKVVELRP-AGVDKGRAVRALLAELPF----GRAPVFIGDDVTDEDAFAA 201
T6PP TIGR00685
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ...
113-330 2.70e-33

trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273219 [Multi-domain]  Cd Length: 244  Bit Score: 123.02  E-value: 2.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 113 GKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFP--TSIVTGRCIDKVYSFVKLAELYYAGSHG--MDIKGP 188
Cdd:TIGR00685   1 ARKRAFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHnaIWIISGRKFLEKWLGVKLPGLGLAGEHGceMKDNGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 189 TKGFSRynkdkpsvlyqpAGDFLPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFR-CVD----EKKWSELASKVRSvv 263
Cdd:TIGR00685  81 CQDWVN------------LTEKIPSWKVRANELREEITTRPGVFIERKGVALAWHYRqAPVpelaRFRAKELKEKILS-- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063743330 264 knYPTLKLSQGRKVFEIRPiIKWNKGKALEFLLESLGFENCNdvfPIYIGDDKTDEDAFKVYITNEN 330
Cdd:TIGR00685 147 --FTDLEVMDGKAVVELKP-RFVNKGEIVKRLLWHQPGSGIS---PVYLGDDITDEDAFRVVNNQWG 207
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
98-323 7.85e-30

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 120.03  E-value: 7.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330  98 PSALNMFERIIEEAR-GKQIVMFLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCFPTS--IVTGRCIDKVYSFVKLAE 174
Cdd:PRK14501  474 PITPAAAEEIIARYRaASRRLLLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADPNTDvaIISGRDRDTLERWFGDLP 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 175 LYYAGSHGMDIKGPTKGFSRynkdkpsvLYQPAGDFlpmIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVD----EK 250
Cdd:PRK14501  554 IHLVAEHGAWSRAPGGEWQL--------LEPVATEW---KDAVRPILEEFVDRTPGSFIEEKEASLAWHYRNADpelgEA 622
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063743330 251 KWSELASKVRSVVKNYPtLKLSQGRKVFEIRPiIKWNKGKALEFLLESLgfencNDVFPIYIGDDKTDEDAFK 323
Cdd:PRK14501  623 RANELILALSSLLSNAP-LEVLRGNKVVEVRP-AGVNKGRAVRRLLEAG-----PYDFVLAIGDDTTDEDMFR 688
HAD-SF-IIB TIGR01484
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ...
117-324 1.57e-16

HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 273651 [Multi-domain]  Cd Length: 207  Bit Score: 77.04  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 117 VMFLDYDGTLSpivdDPDRAFMTSKMRRTVKKMAKC-FPTSIVTGRC---IDKVYSFVKLAeLYYAGSHGMDIKGPTKGF 192
Cdd:TIGR01484   1 LLFFDLDGTLL----DPNAHELSPETIEALERLREAgVKVVIVTGRSlaeIKELLKQLNLP-LPLIAENGALIFYPGEIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 193 SRYNKDKPSVLYqpaGDFLPMIDEVYKQLVEKTkstPGAKVENNKFCLSVHFrcVDEKKWSELASKVRSVVKNYPTLKL- 271
Cdd:TIGR01484  76 YIEPSDVFEEIL---GIKFEEIGAELKSLSEHY---VGTFIEDKAIAVAIHY--VGAELGQELDSKMRERLEKIGRNDLe 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063743330 272 ----SQGRKVFEIRPIiKWNKGKALEFLLESLGFENCNdvfPIYIGDDKTDEDAFKV 324
Cdd:TIGR01484 148 leaiYSGKTDLEVLPA-GVNKGSALQALLQELNGKKDE---ILAFGDSGNDEEMFEV 200
PRK10187 PRK10187
trehalose-6-phosphate phosphatase; Provisional
119-324 5.66e-15

trehalose-6-phosphate phosphatase; Provisional


Pssm-ID: 182291 [Multi-domain]  Cd Length: 266  Bit Score: 73.62  E-value: 5.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 119 FLDYDGTLSPIVDDPDRAFMTSKMRRTVKKMAKCF--PTSIVTGRCIDKVYSFVKLAELYYAGSHGM---DIKGPTKgfs 193
Cdd:PRK10187   18 FFDLDGTLAEIKPHPDQVVVPDNILQGLQLLATANdgALALISGRSMVELDALAKPYRFPLAGVHGAerrDINGKTH--- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 194 rynkdkpsVLYQPAgdflPMIDEVYKQLVEKTKSTPGAKVENNKFCLSVHFRCVDEKKWSELASKVRsVVKNYPTLKLSQ 273
Cdd:PRK10187   95 --------IVHLPD----AIARDISVQLHTALAQLPGAELEAKGMAFALHYRQAPQHEDALLALAQR-ITQIWPQLALQP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063743330 274 GRKVFEIRPIiKWNKGKALEFLLESLGFENcndVFPIYIGDDKTDEDAFKV 324
Cdd:PRK10187  162 GKCVVEIKPR-GTNKGEAIAAFMQEAPFAG---RTPVFVGDDLTDEAGFAV 208
PLN02205 PLN02205
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
101-328 2.81e-08

alpha,alpha-trehalose-phosphate synthase [UDP-forming]


Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 55.41  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 101 LNMfERIIEE-ARGKQIVMFLDYDGTLSP---IVDDPdrafmTSKMRRTVKKMA--KCFPTSIVTGRCIDKVYS-FVKLA 173
Cdd:PLN02205  582 LSM-EHIVSAyKRTTTRAILLDYDGTLMPqasIDKSP-----SSKSIDILNTLCrdKNNMVFIVSARSRKTLADwFSPCE 655
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 174 ELYYAGSHGMdikgptkgFSRYNKDkpsVLYQPAgdfLPMIDEVYKQLVEK-----TKSTPGAKVENNKFCLSVHFRCVD 248
Cdd:PLN02205  656 KLGIAAEHGY--------FLRLKRD---VEWETC---VPVADCSWKQIAEPvmqlyTETTDGSTIEDKETALVWCYEDAD 721
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 249 EKKWS----ELASKVRSVVKNYPtLKLSQGRKVFEIRPiIKWNKGKALEFLLESLGFENCNDVFPIYIGDDKTDEDAFKV 324
Cdd:PLN02205  722 PDFGScqakELLDHLESVLANEP-VTVKSGQNIVEVKP-QGVSKGLVAKRLLSIMQERGMLPDFVLCIGDDRSDEDMFEV 799

                  ....
gi 1063743330 325 YITN 328
Cdd:PLN02205  800 ITSS 803
PRK01158 PRK01158
phosphoglycolate phosphatase; Provisional
114-324 8.80e-04

phosphoglycolate phosphatase; Provisional


Pssm-ID: 234910 [Multi-domain]  Cd Length: 230  Bit Score: 39.96  E-value: 8.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 114 KQIVmfLDYDGTLSpivdDPDRAFMTSKMRRTVKKMAKCFPTSIVTGRCIDKVYSFVKLAelyyaGSHGMDIkGPTKGFS 193
Cdd:PRK01158    4 KAIA--IDIDGTIT----DKDRRLSLKAVEAIRKAEKLGIPVILATGNVLCFARAAAKLI-----GTSGPVI-AENGGVI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 194 RYNKDKPSVlyqpagdFLPMIDEVYKQLVEKTKSTPGAKVENNKFclsvhfrcVDEKKWSELA-------SKVRSVVKny 266
Cdd:PRK01158   72 SVGFDGKRI-------FLGDIEECEKAYSELKKRFPEASTSLTKL--------DPDYRKTEVAlrrtvpvEEVRELLE-- 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063743330 267 ptlklSQGRKV------FEIRPIIKW-NKGKALEFLLESLGFENcNDVfpIYIGDDKTDEDAFKV 324
Cdd:PRK01158  135 -----ELGLDLeivdsgFAIHIKSPGvNKGTGLKKLAELMGIDP-EEV--AAIGDSENDLEMFEV 191
Pglycolate_arch TIGR01487
phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be ...
121-324 6.39e-03

phosphoglycolate phosphatase, TA0175-type; This group of Archaeal sequences, now known to be phosphoglycolate phosphatases, is most closely related to the sucrose-phosphate phosphatases from plants and cyanobacteria (TIGR01485). Together, these two models comprise a subfamily model (TIGR01482). TIGR01482, in turn, is a member of the IIB subfamily (TIGR01484) of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases.


Pssm-ID: 273652 [Multi-domain]  Cd Length: 215  Bit Score: 37.41  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 121 DYDGTLSpivdDPDRAFMTSKMRRTVKKMAKCFPTSIVTGRcidkVYSFVklaelyYAGSHGMDIKGPTKGfsrynKDKP 200
Cdd:TIGR01487   7 DIDGTLT----DPNRMISERAIEAIRKAEKKGIPVSLVTGN----TVPFA------RALAVLIGTSGPVVA-----ENGG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063743330 201 SVLYQPAGDFLPMIDEVYKQLVEKTKSTPGA--KVENNKFCLSVHFRCVDEKKWSELASKVRsvvknyptLKLSQGRKVF 278
Cdd:TIGR01487  68 VIFYNKEDIFLANMEEEWFLDEEKKKRFPRDrlSNEYPRASLVIMREGKDVDEVREIIKERG--------LNLVASGFAI 139
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063743330 279 EIRPiiKW-NKGKALEFLLESLGFeNCNDVfpIYIGDDKTDEDAFKV 324
Cdd:TIGR01487 140 HIMK--KGvDKGVGVEKLKELLGI-KPEEV--AAIGDSENDIDLFRV 181
 
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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