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Conserved domains on  [gi|281360129|ref|NP_001163519|]
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uncharacterized protein Dmel_CG2082, isoform M [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, ...
 31-210 5.02e-89

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: 263.44  E-value: 5.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129   31 YNISTEKCGDLTVIVQGDlsQQEKRAVFITVHDLGCNHNS-FQEFVSSPCMTEIKERSCFIHVDVPGHADNAEALADGFP 109
Cdd:pfam03096   1 EHIIETPCGSVHVTVYGD--PEGKKPPILTYHDLGLNHKScFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129  110 FPSLQSLGEDLVTVLDYLHVKYVIGLGEGAGANVLARFGLAHPSRVLGLILINATGSAASVVQSFKNKFISWK--SDEVA 187
Cdd:pfam03096  79 YPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLlyYYGMT 158

                         170       180
                  ....*....|....*....|...
gi 281360129  188 QSAESFLMYHKFGHVMEVNRSNV 210
Cdd:pfam03096 159 DSAKDYLLAHYFGKEELSNNSDI 181
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 31-210 5.02e-89

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: 263.44  E-value: 5.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129   31 YNISTEKCGDLTVIVQGDlsQQEKRAVFITVHDLGCNHNS-FQEFVSSPCMTEIKERSCFIHVDVPGHADNAEALADGFP 109
Cdd:pfam03096   1 EHIIETPCGSVHVTVYGD--PEGKKPPILTYHDLGLNHKScFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129  110 FPSLQSLGEDLVTVLDYLHVKYVIGLGEGAGANVLARFGLAHPSRVLGLILINATGSAASVVQSFKNKFISWK--SDEVA 187
Cdd:pfam03096  79 YPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLlyYYGMT 158

                         170       180
                  ....*....|....*....|...
gi 281360129  188 QSAESFLMYHKFGHVMEVNRSNV 210
Cdd:pfam03096 159 DSAKDYLLAHYFGKEELSNNSDI 181
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 61-164 1.23e-07

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: 50.38  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129  61 VHDLGCNHNSFQEFvsspcMTEIKERSCFIHVDVPGHADNAEALADgfpfPSLQSLGEDLVTVLDYLHVKYVIGLGEGAG 140
Cdd:COG0596   29 LHGLPGSSYEWRPL-----IPALAAGYRVIAPDLRGHGRSDKPAGG----YTLDDLADDLAALLDALGLERVVLVGHSMG 99

                         90       100
                 ....*....|....*....|....
gi 281360129 141 ANVLARFGLAHPSRVLGLILINAT 164
Cdd:COG0596  100 GMVALELAARHPERVAGLVLVDEV 123
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 92-161 1.30e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.85  E-value: 1.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129  92 VDVPGHADNAEALADGfpfpSLQSLGEDLVTVLDYLHVKYVIGLGEGAGANVLARFGLAHPSRVLGLILI 161
Cdd:PRK14875 163 LDLPGHGASSKAVGAG----SLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI 228
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 31-210 5.02e-89

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: 263.44  E-value: 5.02e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129   31 YNISTEKCGDLTVIVQGDlsQQEKRAVFITVHDLGCNHNS-FQEFVSSPCMTEIKERSCFIHVDVPGHADNAEALADGFP 109
Cdd:pfam03096   1 EHIIETPCGSVHVTVYGD--PEGKKPPILTYHDLGLNHKScFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129  110 FPSLQSLGEDLVTVLDYLHVKYVIGLGEGAGANVLARFGLAHPSRVLGLILINATGSAASVVQSFKNKFISWK--SDEVA 187
Cdd:pfam03096  79 YPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSSKLlyYYGMT 158

                         170       180
                  ....*....|....*....|...
gi 281360129  188 QSAESFLMYHKFGHVMEVNRSNV 210
Cdd:pfam03096 159 DSAKDYLLAHYFGKEELSNNSDI 181
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 61-164 1.23e-07

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: 50.38  E-value: 1.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129  61 VHDLGCNHNSFQEFvsspcMTEIKERSCFIHVDVPGHADNAEALADgfpfPSLQSLGEDLVTVLDYLHVKYVIGLGEGAG 140
Cdd:COG0596   29 LHGLPGSSYEWRPL-----IPALAAGYRVIAPDLRGHGRSDKPAGG----YTLDDLADDLAALLDALGLERVVLVGHSMG 99

                         90       100
                 ....*....|....*....|....
gi 281360129 141 ANVLARFGLAHPSRVLGLILINAT 164
Cdd:COG0596  100 GMVALELAARHPERVAGLVLVDEV 123
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
 92-161 1.30e-04

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 41.85  E-value: 1.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129  92 VDVPGHADNAEALADGfpfpSLQSLGEDLVTVLDYLHVKYVIGLGEGAGANVLARFGLAHPSRVLGLILI 161
Cdd:PRK14875 163 LDLPGHGASSKAVGAG----SLDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI 228
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 57-169 8.85e-03

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: 36.33  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 281360129   57 VFITVHDLGCNHNSFQEFVSSpcmteIKERSCFIHV-DVPGHADNAEALA-DGFPFPSLQslgEDLVTVLDYLHVKYVIG 134
Cdd:pfam00561   2 PVLLLHGLPGSSDLWRKLAPA-----LARDGFRVIAlDLRGFGKSSRPKAqDDYRTDDLA---EDLEYILEALGLEKVNL 73

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 281360129  135 LGEGAGANVLARFGLAHPSRVLGLILINATGSAAS 169
Cdd:pfam00561  74 VGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHE 108
 
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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