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Conserved domains on  [gi|45552777|ref|NP_995913|]
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misexpression suppressor of KSR 2, isoform F [Drosophila melanogaster]

Protein Classification

alpha/beta hydrolase family protein( domain architecture ID 229394)

alpha/beta hydrolase family protein may catalyze the hydrolysis of substrates with different chemical composition or physicochemical properties using a nucleophile-His-acid catalytic triad

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
133-419 1.93e-123

alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, peroxidases, esterases, epoxide hydrolases and dehalogenases. The catalytic apparatus typically involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine, and often the mechanism involves a nucleophilic attack on a carbonyl carbon atom.


The actual alignment was detected with superfamily member pfam03096:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 285  Bit Score: 360.13  E-value: 1.93e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   133 VPTDKGDVHVAIQGD--TAKPAIITYHDLGLNYATSFAGFFNFPVMRGLLENFCVYHVTAPGQEEGAPTLPEDYVYPTMD 210
Cdd:pfam03096   4 IETPCGSVHVTVYGDpeGKKPPILTYHDLGLNHKSCFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYPYPSMD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   211 DLAAQLLFVLSHFGLKSVIGFGVGAGANILARFAHAHPDKVGALCLINCVSTQSGWIEWGYQSFNARFLRTKGMTQGVID 290
Cdd:pfam03096  84 DLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLLYYYGMTDSAKD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   291 YLMWHHFGRNPEERNHDLVQMYKQHFERGVNPTNLAMLINAYIHRNDLHLARTPPGTpgsetaattlKMPVINITGSLSP 370
Cdd:pfam03096 164 YLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET----------KCPVLLVVGDNSP 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 45552777   371 HVDDTVTFNGRLDPTNSSWMKISDC-ALVLEEQPAKLAEAFRLFLQGEGY 419
Cdd:pfam03096 234 HVDAVVECNTKLDPTKTTLLKVADCgGLVQQEQPGKLTESFKLFLQGMGY 283
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
133-419 1.93e-123

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 360.13  E-value: 1.93e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   133 VPTDKGDVHVAIQGD--TAKPAIITYHDLGLNYATSFAGFFNFPVMRGLLENFCVYHVTAPGQEEGAPTLPEDYVYPTMD 210
Cdd:pfam03096   4 IETPCGSVHVTVYGDpeGKKPPILTYHDLGLNHKSCFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYPYPSMD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   211 DLAAQLLFVLSHFGLKSVIGFGVGAGANILARFAHAHPDKVGALCLINCVSTQSGWIEWGYQSFNARFLRTKGMTQGVID 290
Cdd:pfam03096  84 DLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLLYYYGMTDSAKD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   291 YLMWHHFGRNPEERNHDLVQMYKQHFERGVNPTNLAMLINAYIHRNDLHLARTPPGTpgsetaattlKMPVINITGSLSP 370
Cdd:pfam03096 164 YLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET----------KCPVLLVVGDNSP 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 45552777   371 HVDDTVTFNGRLDPTNSSWMKISDC-ALVLEEQPAKLAEAFRLFLQGEGY 419
Cdd:pfam03096 234 HVDAVVECNTKLDPTKTTLLKVADCgGLVQQEQPGKLTESFKLFLQGMGY 283
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
129-258 1.01e-09

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 58.47  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777 129 EQRRVPTDKGDVHVAIQGDTAKPAIITyHDLGLNyATSFAgffnfPVMRGLLENFCVYHVTAPGQeeGAPTLPEDYVypT 208
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGPDGPPVVLL-HGLPGS-SYEWR-----PLIPALAAGYRVIAPDLRGH--GRSDKPAGGY--T 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45552777 209 MDDLAAQLLFVLSHFGLKSVIGFGVGAGANILARFAHAHPDKVGALCLIN 258
Cdd:COG0596  72 LDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD 121
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
133-419 1.93e-123

Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, and Ndr3. Their similarity was previously noted. The precise molecular and cellular function of members of this family is still unknown. Yet, they are known to be involved in cellular differentiation events. The Ndr1 group was the first to be discovered. Their expression is repressed by the proto-oncogenes N-myc and c-myc, and in line with this observation, Ndr1 protein expression is down-regulated in neoplastic cells, and is reactivated when differentiation is induced by chemicals such as retinoic acid. Ndr2 and Ndr3 expression is not under the control of N-myc or c-myc. Ndr1 expression is also activated by several chemicals: tunicamycin and homocysteine induce Ndr1 in human umbilical endothelial cells; nickel induces Ndr1 in several cell types. Members of this family are found in wide variety of multicellular eukaryotes, including an Ndr1 type protein in Helianthus annuus (sunflower), known as Sf21. Interestingly, the highest scoring matches in the noise are all alpha/beta hydrolases pfam00561, suggesting that this family may have an enzymatic function (Bateman A pers. obs.).


Pssm-ID: 397285 [Multi-domain]  Cd Length: 285  Bit Score: 360.13  E-value: 1.93e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   133 VPTDKGDVHVAIQGD--TAKPAIITYHDLGLNYATSFAGFFNFPVMRGLLENFCVYHVTAPGQEEGAPTLPEDYVYPTMD 210
Cdd:pfam03096   4 IETPCGSVHVTVYGDpeGKKPPILTYHDLGLNHKSCFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYPYPSMD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   211 DLAAQLLFVLSHFGLKSVIGFGVGAGANILARFAHAHPDKVGALCLINCVSTQSGWIEWGYQSFNARFLRTKGMTQGVID 290
Cdd:pfam03096  84 DLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLLYYYGMTDSAKD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   291 YLMWHHFGRNPEERNHDLVQMYKQHFERGVNPTNLAMLINAYIHRNDLHLARTPPGTpgsetaattlKMPVINITGSLSP 370
Cdd:pfam03096 164 YLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET----------KCPVLLVVGDNSP 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 45552777   371 HVDDTVTFNGRLDPTNSSWMKISDC-ALVLEEQPAKLAEAFRLFLQGEGY 419
Cdd:pfam03096 234 HVDAVVECNTKLDPTKTTLLKVADCgGLVQQEQPGKLTESFKLFLQGMGY 283
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
129-258 1.01e-09

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 58.47  E-value: 1.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777 129 EQRRVPTDKGDVHVAIQGDTAKPAIITyHDLGLNyATSFAgffnfPVMRGLLENFCVYHVTAPGQeeGAPTLPEDYVypT 208
Cdd:COG0596   3 TPRFVTVDGVRLHYREAGPDGPPVVLL-HGLPGS-SYEWR-----PLIPALAAGYRVIAPDLRGH--GRSDKPAGGY--T 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 45552777 209 MDDLAAQLLFVLSHFGLKSVIGFGVGAGANILARFAHAHPDKVGALCLIN 258
Cdd:COG0596  72 LDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD 121
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
173-316 4.85e-04

alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.


Pssm-ID: 395444 [Multi-domain]  Cd Length: 245  Bit Score: 41.72  E-value: 4.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45552777   173 FPVMRGLLENfcVYHVTAP-----GQEEGAPTlPEDYvypTMDDLAAQLLFVLSHFGLKSVIGFGVGAGANILARFAHAH 247
Cdd:pfam00561  17 RKLAPALARD--GFRVIALdlrgfGKSSRPKA-QDDY---RTDDLAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKY 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45552777   248 PDKVGALCLINCVSTQSGWIEW------GYQSFNARFLR---TKGMTQGVIDYLMWHHFGRNPEERNHDLVQMYKQHF 316
Cdd:pfam00561  91 PDRVKALVLLGALDPPHELDEAdrfilaLFPGFFDGFVAdfaPNPLGRLVAKLLALLLLRLRLLKALPLLNKRFPSGD 168
 
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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