NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|768017713|ref|XP_011527230|]
View 

protein NDRG3 isoform X8 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Abhydrolase super family cl21494
alpha/beta hydrolases; A functionally diverse superfamily containing proteases, lipases, ...
 6-225 3.81e-114

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: 330.47  E-value: 3.81e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713    6 QETSRTLTVRYQYPTMDELAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASK 85
Cdd:pfam03096  67 EDGAASFPGGYPYPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713   86 LS-------GLTTNVVDIILAHHFGQEELQANLDLIQTYRMHIAQDINQDNLQLFLNSYNGRRDLEIERPILGQndnksk 158
Cdd:pfam03096 147 LSskllyyyGMTDSAKDYLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET------ 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768017713  159 tlKCSTLLVVGDNSPAVEAVVECNSRLNPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIP 225
Cdd:pfam03096 221 --KCPVLLVVGDNSPHVDAVVECNTKLDPTKTTLLKVADCGGLVQQEQPGKLTESFKLFLQGMGYYP 285
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 6-225 3.81e-114

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: 330.47  E-value: 3.81e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713    6 QETSRTLTVRYQYPTMDELAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASK 85
Cdd:pfam03096  67 EDGAASFPGGYPYPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713   86 LS-------GLTTNVVDIILAHHFGQEELQANLDLIQTYRMHIAQDINQDNLQLFLNSYNGRRDLEIERPILGQndnksk 158
Cdd:pfam03096 147 LSskllyyyGMTDSAKDYLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET------ 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768017713  159 tlKCSTLLVVGDNSPAVEAVVECNSRLNPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIP 225
Cdd:pfam03096 221 --KCPVLLVVGDNSPHVDAVVECNTKLDPTKTTLLKVADCGGLVQQEQPGKLTESFKLFLQGMGYYP 285
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-220 1.19e-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: 51.54  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713  20 TMDELAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINvdpcakgwidwaasklsglttnvvdiila 99
Cdd:COG0596   71 TLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------------- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713 100 hhfgqeelqanlDLIQTYRMHIAQDinQDNLQLFLNSYNGRRDLEIERPIlgqndnksKTLKCSTLLVVGDNSPAV---- 175
Cdd:COG0596  122 ------------EVLAALAEPLRRP--GLAPEALAALLRALARTDLRERL--------ARITVPTLVIWGEKDPIVppal 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768017713 176 -EAVVecnsRLNPiNTTLLKMADCGGLPQVVQPGKLTEAFKYFLQG 220
Cdd:COG0596  180 aRRLA----ELLP-NAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
24-95 2.89e-03

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 38.46  E-value: 2.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768017713  24 LAEMLPPVLTHLSLKSIiGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASK---LSGLTTNVVD 95
Cdd:PRK10349  61 LADMAEAVLQQAPDKAI-WLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKpdvLAGFQQQLSD 134
 
Name Accession Description Interval E-value
Ndr pfam03096
Ndr family; This family consists of proteins from different gene families: Ndr1/RTP/Drg1, Ndr2, ...
 6-225 3.81e-114

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: 330.47  E-value: 3.81e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713    6 QETSRTLTVRYQYPTMDELAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASK 85
Cdd:pfam03096  67 EDGAASFPGGYPYPSMDDLADMLPVVLDHFRLKSVIGMGVGAGAYILARFALKHPERVEGLVLINPTPKAAGWIEWFYNK 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713   86 LS-------GLTTNVVDIILAHHFGQEELQANLDLIQTYRMHIAQDINQDNLQLFLNSYNGRRDLEIERPILGQndnksk 158
Cdd:pfam03096 147 LSskllyyyGMTDSAKDYLLAHYFGKEELSNNSDIVQEYRKFLKERLNPKNLQLYLEAYNSRRDLTIERPGLET------ 220

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768017713  159 tlKCSTLLVVGDNSPAVEAVVECNSRLNPINTTLLKMADCGGLPQVVQPGKLTEAFKYFLQGMGYIP 225
Cdd:pfam03096 221 --KCPVLLVVGDNSPHVDAVVECNTKLDPTKTTLLKVADCGGLVQQEQPGKLTESFKLFLQGMGYYP 285
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 20-220 1.19e-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: 51.54  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713  20 TMDELAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINvdpcakgwidwaasklsglttnvvdiila 99
Cdd:COG0596   71 TLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLVD----------------------------- 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713 100 hhfgqeelqanlDLIQTYRMHIAQDinQDNLQLFLNSYNGRRDLEIERPIlgqndnksKTLKCSTLLVVGDNSPAV---- 175
Cdd:COG0596  122 ------------EVLAALAEPLRRP--GLAPEALAALLRALARTDLRERL--------ARITVPTLVIWGEKDPIVppal 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768017713 176 -EAVVecnsRLNPiNTTLLKMADCGGLPQVVQPGKLTEAFKYFLQG 220
Cdd:COG0596  180 aRRLA----ELLP-NAELVVLPGAGHFPPLEQPEAFAAALRDFLAR 220
Abhydrolase_1 pfam00561
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
 9-199 7.79e-05

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: 43.26  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713    9 SRTLTVRYQYPTMDeLAEMLPPVLTHLSLKSIIGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWID----WAAS 84
Cdd:pfam00561  41 SSRPKAQDDYRTDD-LAEDLEYILEALGLEKVNLVGHSMGGLIALAYAAKYPDRVKALVLLGALDPPHELDEadrfILAL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768017713   85 KLSGLTTNVVDIILAHHfgqeelqanLDLIQTYRMHIAQDINQDNL--QLFLNSYNGRRDLEI--------ERPILGQND 154
Cdd:pfam00561 120 FPGFFDGFVADFAPNPL---------GRLVAKLLALLLLRLRLLKAlpLLNKRFPSGDYALAKslvtgallFIETWSTEL 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 768017713  155 NKSKTLKCS--TLLVVGDNSPAV-EAVVECNSRLNPiNTTLLKMADCG 199
Cdd:pfam00561 191 RAKFLGRLDepTLIIWGDQDPLVpPQALEKLAQLFP-NARLVVIPDAG 237
PRK10349 PRK10349
pimeloyl-ACP methyl ester esterase BioH;
24-95 2.89e-03

pimeloyl-ACP methyl ester esterase BioH;


Pssm-ID: 137836 [Multi-domain]  Cd Length: 256  Bit Score: 38.46  E-value: 2.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768017713  24 LAEMLPPVLTHLSLKSIiGIGVGAGAYILSRFALNHPELVEGLVLINVDPCAKGWIDWAASK---LSGLTTNVVD 95
Cdd:PRK10349  61 LADMAEAVLQQAPDKAI-WLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKpdvLAGFQQQLSD 134
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH