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Conserved domains on  [gi|7305307|ref|NP_038893|]
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protein NDRG3 isoform 2 [Mus musculus]

Protein Classification

NDRG family protein( domain architecture ID 11140417)

N-myc downstream-regulated gene (NDRG) family protein may be involved in cellular differentiation events; similar to Homo sapiens protein NDRG1, which is a stress-responsive protein involved in hormone responses, cell growth, and differentiation; belongs to the alpha/beta hydrolase superfamily

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
32-317 1.93e-170

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: 476.46  E-value: 1.93e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307     32 EHDIETPHGMVHVTIRGLPKGNRPVILTYHDIGLNHKSCFNTFFNFEDMQEITQHFAVCHVDAPGQQEAAPSFPTGYQYP 111
Cdd:pfam03096   1 EHIIETPCGSVHVTVYGDPEGKKPPILTYHDLGLNHKSCFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYPYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    112 TMDELAEMLPPVLTHLSMKSIIGIGVGAGAYILSRFALNHPELVEGLVLINIDPCAKGWIDWAASKLS-------GFTTN 184
Cdd:pfam03096  81 SMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSskllyyyGMTDS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    185 IVDIILAHHFGQEELQANLDLIQTYRLHIAQDINQENLQLFLGSYNGRRDLEIERPILGQndnrlktlKCSTLLVVGDNS 264
Cdd:pfam03096 161 AKDYLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET--------KCPVLLVVGDNS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7305307    265 PAVEAVVECNSRLDPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIP 317
Cdd:pfam03096 233 PHVDAVVECNTKLDPTKTTLLKVADCGGLVQQEQPGKLTESFKLFLQGMGYYP 285
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
32-317 1.93e-170

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: 476.46  E-value: 1.93e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307     32 EHDIETPHGMVHVTIRGLPKGNRPVILTYHDIGLNHKSCFNTFFNFEDMQEITQHFAVCHVDAPGQQEAAPSFPTGYQYP 111
Cdd:pfam03096   1 EHIIETPCGSVHVTVYGDPEGKKPPILTYHDLGLNHKSCFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYPYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    112 TMDELAEMLPPVLTHLSMKSIIGIGVGAGAYILSRFALNHPELVEGLVLINIDPCAKGWIDWAASKLS-------GFTTN 184
Cdd:pfam03096  81 SMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSskllyyyGMTDS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    185 IVDIILAHHFGQEELQANLDLIQTYRLHIAQDINQENLQLFLGSYNGRRDLEIERPILGQndnrlktlKCSTLLVVGDNS 264
Cdd:pfam03096 161 AKDYLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET--------KCPVLLVVGDNS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7305307    265 PAVEAVVECNSRLDPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIP 317
Cdd:pfam03096 233 PHVDAVVECNTKLDPTKTTLLKVADCGGLVQQEQPGKLTESFKLFLQGMGYYP 285
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
39-312 1.55e-13

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 70.04  E-value: 1.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307   39 HGMVHVTIRGLPKGNRPVILTyHDIGLNHkscFNTFFNFEDMQEITQHFAVCHVDAPGqqeAAPSFPTGYqypTMDELAE 118
Cdd:COG0596   7 ADGVRLAYREAGGGGPPLVLL-HGFPGSS---SVWRPVFKVLPALAARYRVIAPDLRG---HGRSDPAGY---SLSAYAD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307  119 MLPPVLTHLSMKSIIGIGVGAGAYILSRFALNHPELVEGLVLINIDPCAKGWIDWA-------------ASKLSGFTTNI 185
Cdd:COG0596  77 DLAALLDALGLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALrqpagaaplaalaDLLLGLDAAAF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307  186 VDIILAHHFGQEELQANLD-LIQTYRLHIAQDINQENLQLFLGSYNGRRDLEIERPIlgqnDNRLKTLKCSTLLVVGDNS 264
Cdd:COG0596 157 AALLAALGLLAALAAAARAgLAEALRAPLLGAAAAAFARAARADLAAALLALLDRDL----RAALARITVPTLIIHGEDD 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 7305307  265 PAV-EAVVECNSRLDPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQG 312
Cdd:COG0596 233 PVVpAELARRLAAALPNDARLVVIPGAGHFPHLEAPEAFAAALLAFLER 281
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
81-187 4.44e-06

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 47.70  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    81 QEITQHFAVCHVDAPGQQEAapsfpTGYQYPTMDELAEMlppVLTHLSMKSIiGIGVGAGAYILSRFALNHPELVEGLVL 160
Cdd:PRK10349  34 EELSSHFTLHLVDLPGFGRS-----RGFGALSLADMAEA---VLQQAPDKAI-WLGWSLGGLVASQIALTHPERVQALVT 104
                         90       100       110
                 ....*....|....*....|....*....|
gi 7305307   161 INIDPCAKGWIDWAASK---LSGFTTNIVD 187
Cdd:PRK10349 105 VASSPCFSARDEWPGIKpdvLAGFQQQLSD 134
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
32-317 1.93e-170

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: 476.46  E-value: 1.93e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307     32 EHDIETPHGMVHVTIRGLPKGNRPVILTYHDIGLNHKSCFNTFFNFEDMQEITQHFAVCHVDAPGQQEAAPSFPTGYQYP 111
Cdd:pfam03096   1 EHIIETPCGSVHVTVYGDPEGKKPPILTYHDLGLNHKSCFQGLFNSESMQEILENFCIYHVDAPGQEDGAASFPGGYPYP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    112 TMDELAEMLPPVLTHLSMKSIIGIGVGAGAYILSRFALNHPELVEGLVLINIDPCAKGWIDWAASKLS-------GFTTN 184
Cdd:pfam03096  81 SMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNKLSskllyyyGMTDS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    185 IVDIILAHHFGQEELQANLDLIQTYRLHIAQDINQENLQLFLGSYNGRRDLEIERPILGQndnrlktlKCSTLLVVGDNS 264
Cdd:pfam03096 161 AKDYLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET--------KCPVLLVVGDNS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 7305307    265 PAVEAVVECNSRLDPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIP 317
Cdd:pfam03096 233 PHVDAVVECNTKLDPTKTTLLKVADCGGLVQQEQPGKLTESFKLFLQGMGYYP 285
MhpC COG0596
Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General ...
39-312 1.55e-13

Pimeloyl-ACP methyl ester carboxylesterase [Coenzyme transport and metabolism, General function prediction only];


Pssm-ID: 223669 [Multi-domain]  Cd Length: 282  Bit Score: 70.04  E-value: 1.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307   39 HGMVHVTIRGLPKGNRPVILTyHDIGLNHkscFNTFFNFEDMQEITQHFAVCHVDAPGqqeAAPSFPTGYqypTMDELAE 118
Cdd:COG0596   7 ADGVRLAYREAGGGGPPLVLL-HGFPGSS---SVWRPVFKVLPALAARYRVIAPDLRG---HGRSDPAGY---SLSAYAD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307  119 MLPPVLTHLSMKSIIGIGVGAGAYILSRFALNHPELVEGLVLINIDPCAKGWIDWA-------------ASKLSGFTTNI 185
Cdd:COG0596  77 DLAALLDALGLEKVVLVGHSMGGAVALALALRHPDRVRGLVLIGPAPPPGLLEAALrqpagaaplaalaDLLLGLDAAAF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307  186 VDIILAHHFGQEELQANLD-LIQTYRLHIAQDINQENLQLFLGSYNGRRDLEIERPIlgqnDNRLKTLKCSTLLVVGDNS 264
Cdd:COG0596 157 AALLAALGLLAALAAAARAgLAEALRAPLLGAAAAAFARAARADLAAALLALLDRDL----RAALARITVPTLIIHGEDD 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 7305307  265 PAV-EAVVECNSRLDPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQG 312
Cdd:COG0596 233 PVVpAELARRLAAALPNDARLVVIPGAGHFPHLEAPEAFAAALLAFLER 281
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
81-187 4.44e-06

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 47.70  E-value: 4.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    81 QEITQHFAVCHVDAPGQQEAapsfpTGYQYPTMDELAEMlppVLTHLSMKSIiGIGVGAGAYILSRFALNHPELVEGLVL 160
Cdd:PRK10349  34 EELSSHFTLHLVDLPGFGRS-----RGFGALSLADMAEA---VLQQAPDKAI-WLGWSLGGLVASQIALTHPERVQALVT 104
                         90       100       110
                 ....*....|....*....|....*....|
gi 7305307   161 INIDPCAKGWIDWAASK---LSGFTTNIVD 187
Cdd:PRK10349 105 VASSPCFSARDEWPGIKpdvLAGFQQQLSD 134
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
55-174 1.40e-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: 42.88  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307     55 PVILTYHDIGLNHKSCFNTFFNFEDmqeitQHFAVCHVDAPGQQEA-APSFPTGYqypTMDELAEMLPPVLTHLSMKSII 133
Cdd:pfam00561   1 PPVLLLHGLPGSSDLWRKLAPALAR-----DGFRVIALDLRGFGKSsRPKAQDDY---RTDDLAEDLEYILEALGLEKVN 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 7305307    134 GIGVGAGAYILSRFALNHPELVEGLVLINIDPCAKGWIDWA 174
Cdd:pfam00561  73 LVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEAD 113
PRK14875 PRK14875
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
35-161 4.01e-03

acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional


Pssm-ID: 184875 [Multi-domain]  Cd Length: 371  Bit Score: 38.77  E-value: 4.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7305307    35 IETPHGMVHVTIRGlPKGNRPVILTyHDIG--LNhkscfNTFFNFEDMQEitqHFAVCHVDAPGQQEAAPSFPTGyqypT 112
Cdd:PRK14875 114 ARIGGRTVRYLRLG-EGDGTPVVLI-HGFGgdLN-----NWLFNHAALAA---GRPVIALDLPGHGASSKAVGAG----S 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 7305307   113 MDELAEMLPPVLTHLSMKSIIGIGVGAGAYILSRFALNHPELVEGLVLI 161
Cdd:PRK14875 180 LDELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAARAPQRVASLTLI 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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