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Conserved domains on  [gi|1475409084|ref|NP_001139748|]
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neutral cholesterol ester hydrolase 1 isoform a [Homo sapiens]

Protein Classification

alpha/beta hydrolase( domain architecture ID 11171394)

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

CATH:  3.40.50.1820
EC:  3.-.-.-
Gene Ontology:  GO:0016787

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
109-389 1.92e-45

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


:

Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 156.22  E-value: 1.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 109 VVYIHGGGWAlasasaswspSDEIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFLKPEvlQKYMV 188
Cdd:pfam07859   1 LVYFHGGGFV----------LGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQA--AELGA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 189 DPGRICISGDSAGGNLAAALGQQFtQDASLkNKLKLQALIYPVLQaLDFNTPSY--QQNVNTPILPRYVMVKYWvdyfkg 266
Cdd:pfam07859  69 DPSRIAVAGDSAGGNLAAAVALRA-RDEGL-PKPAGQVLIYPGTD-LRTESPSYlaREFADGPLLTRAAMDWFW------ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 267 nydfvqamivnnhtsldveeaaavrarlnwtsllpasftKNYKPVVQTTgnarivqelpqllDARSAPLIAdqAVLQLLP 346
Cdd:pfam07859 140 ---------------------------------------RLYLPGADRD-------------DPLASPLFA--SDLSGLP 165
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1475409084 347 KTYILTCEHDVLRDDGIMYAKRLESAGVEVTLDHFEDGFHGCM 389
Cdd:pfam07859 166 PALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
109-389 1.92e-45

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


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 156.22  E-value: 1.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 109 VVYIHGGGWAlasasaswspSDEIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFLKPEvlQKYMV 188
Cdd:pfam07859   1 LVYFHGGGFV----------LGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQA--AELGA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 189 DPGRICISGDSAGGNLAAALGQQFtQDASLkNKLKLQALIYPVLQaLDFNTPSY--QQNVNTPILPRYVMVKYWvdyfkg 266
Cdd:pfam07859  69 DPSRIAVAGDSAGGNLAAAVALRA-RDEGL-PKPAGQVLIYPGTD-LRTESPSYlaREFADGPLLTRAAMDWFW------ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 267 nydfvqamivnnhtsldveeaaavrarlnwtsllpasftKNYKPVVQTTgnarivqelpqllDARSAPLIAdqAVLQLLP 346
Cdd:pfam07859 140 ---------------------------------------RLYLPGADRD-------------DPLASPLFA--SDLSGLP 165
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1475409084 347 KTYILTCEHDVLRDDGIMYAKRLESAGVEVTLDHFEDGFHGCM 389
Cdd:pfam07859 166 PALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
99-416 1.31e-38

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 138.08  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084  99 PKPEEPLKRSVVYIHGGGWAlasasaswspSDEIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFL 178
Cdd:COG0657     6 PAGAKGPLPVVVYFHGGGWV----------SGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 179 kpEVLQKYMVDPGRICISGDSAGGNLAAALGQQFTQDASlkNKLKLQALIYPVlqaldfntpsyqqnvntpilpryvmvk 258
Cdd:COG0657    76 --ANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGG--PRPAAQVLIYPV--------------------------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 259 ywvdyfkgnydfvqamivnnhtsldveeaaavrarlnwtsllpasftknykpvvqttgnarivqelpqlLDARSAPLIAD 338
Cdd:COG0657   125 ---------------------------------------------------------------------LDLTASPLRAD 135
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1475409084 339 qavLQLLPKTYILTCEHDVLRDDGIMYAKRLESAGVEVTLDHFEDGFHGCMIFTSWPtnfsVGIRTRNSYIKWLDQNL 416
Cdd:COG0657   136 ---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLP----EARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
84-207 1.01e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 62.43  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084  84 DTDFDGVEVRVFegppKPEEPLKRSVVYIHGGGWALasasaswspsDEIRYYDELCTAMAEELNAVIVSIEYRLVPKVYF 163
Cdd:PRK10162   63 PTPYGQVETRLY----YPQPDSQATLFYLHGGGFIL----------GNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARF 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1475409084 164 PEQIHDVVRATKYFlkPEVLQKYMVDPGRICISGDSAGGNLAAA 207
Cdd:PRK10162  129 PQAIEEIVAVCCYF--HQHAEDYGINMSRIGFAGDSAGAMLALA 170
 
Name Accession Description Interval E-value
Abhydrolase_3 pfam07859
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
109-389 1.92e-45

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


Pssm-ID: 400284 [Multi-domain]  Cd Length: 208  Bit Score: 156.22  E-value: 1.92e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 109 VVYIHGGGWAlasasaswspSDEIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFLKPEvlQKYMV 188
Cdd:pfam07859   1 LVYFHGGGFV----------LGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQA--AELGA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 189 DPGRICISGDSAGGNLAAALGQQFtQDASLkNKLKLQALIYPVLQaLDFNTPSY--QQNVNTPILPRYVMVKYWvdyfkg 266
Cdd:pfam07859  69 DPSRIAVAGDSAGGNLAAAVALRA-RDEGL-PKPAGQVLIYPGTD-LRTESPSYlaREFADGPLLTRAAMDWFW------ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 267 nydfvqamivnnhtsldveeaaavrarlnwtsllpasftKNYKPVVQTTgnarivqelpqllDARSAPLIAdqAVLQLLP 346
Cdd:pfam07859 140 ---------------------------------------RLYLPGADRD-------------DPLASPLFA--SDLSGLP 165
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1475409084 347 KTYILTCEHDVLRDDGIMYAKRLESAGVEVTLDHFEDGFHGCM 389
Cdd:pfam07859 166 PALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
99-416 1.31e-38

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 138.08  E-value: 1.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084  99 PKPEEPLKRSVVYIHGGGWAlasasaswspSDEIRYYDELCTAMAEELNAVIVSIEYRLVPKVYFPEQIHDVVRATKYFL 178
Cdd:COG0657     6 PAGAKGPLPVVVYFHGGGWV----------SGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 179 kpEVLQKYMVDPGRICISGDSAGGNLAAALGQQFTQDASlkNKLKLQALIYPVlqaldfntpsyqqnvntpilpryvmvk 258
Cdd:COG0657    76 --ANAAELGIDPDRIAVAGDSAGGHLAAALALRARDRGG--PRPAAQVLIYPV--------------------------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084 259 ywvdyfkgnydfvqamivnnhtsldveeaaavrarlnwtsllpasftknykpvvqttgnarivqelpqlLDARSAPLIAD 338
Cdd:COG0657   125 ---------------------------------------------------------------------LDLTASPLRAD 135
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1475409084 339 qavLQLLPKTYILTCEHDVLRDDGIMYAKRLESAGVEVTLDHFEDGFHGCMIFTSWPtnfsVGIRTRNSYIKWLDQNL 416
Cdd:COG0657   136 ---LAGLPPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLLAGLP----EARAALAEIAAFLRRAL 206
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
98-209 2.97e-14

BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, previously known as bifunctional carbohydrate esterase (CE)), which is active on complex natural xylans and was identified as the basis of a monophyletic clade gathering all homologs identified in PULs (polysaccharide utilization loci) predicted to act on xylan. It adopts an alpha-beta-hydrolase fold with the catalytic triad Ser-Asp-His. This new family of proteins is a new candidate for biomass processing due to its capacity to remove ferulic acid and acetic acid from natural corn and birchwood xylan substrates.


Pssm-ID: 466583 [Multi-domain]  Cd Length: 215  Bit Score: 71.44  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084  98 PPKPEEPLKrSVVYIHGGGWALASAsaswspSDEIRYYDELCTAMAEELNAViVSIEYRLVPKVYFPEQIHDVVRATKYF 177
Cdd:pfam20434   6 PKNAKGPYP-VVIWIHGGGWNSGDK------EADMGFMTNTVKALLKAGYAV-ASINYRLSTDAKFPAQIQDVKAAIRFL 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1475409084 178 LKPEvlQKYMVDPGRICISGDSAGGNLAAALG 209
Cdd:pfam20434  78 RANA--AKYGIDTNKIALMGFSAGGHLALLAG 107
PRK10162 PRK10162
acetyl esterase;
84-207 1.01e-10

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 62.43  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084  84 DTDFDGVEVRVFegppKPEEPLKRSVVYIHGGGWALasasaswspsDEIRYYDELCTAMAEELNAVIVSIEYRLVPKVYF 163
Cdd:PRK10162   63 PTPYGQVETRLY----YPQPDSQATLFYLHGGGFIL----------GNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARF 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1475409084 164 PEQIHDVVRATKYFlkPEVLQKYMVDPGRICISGDSAGGNLAAA 207
Cdd:PRK10162  129 PQAIEEIVAVCCYF--HQHAEDYGINMSRIGFAGDSAGAMLALA 170
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
87-208 4.98e-06

Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 47.32  E-value: 4.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1475409084  87 FDGVEVRVFEGPPKPEEPLKrSVVYIHGGgwalasasaswsPSDEIRYYDELCTAMAEeLNAVIVSIEYRLVPK---VYF 163
Cdd:COG1506     5 ADGTTLPGWLYLPADGKKYP-VVVYVHGG------------PGSRDDSFLPLAQALAS-RGYAVLAPDYRGYGEsagDWG 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1475409084 164 PEQIHDVVRATKYflkpeVLQKYMVDPGRICISGDSAGGNLAAAL 208
Cdd:COG1506    71 GDEVDDVLAAIDY-----LAARPYVDPDRIGIYGHSYGGYMALLA 110
Peptidase_S9 pfam00326
Prolyl oligopeptidase family;
167-211 7.26e-03

Prolyl oligopeptidase family;


Pssm-ID: 459761 [Multi-domain]  Cd Length: 213  Bit Score: 37.59  E-value: 7.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1475409084 167 IHDVVRATKYFLKpevlQKYmVDPGRICISGDSAGGNL-AAALGQQ 211
Cdd:pfam00326  45 FDDFIAAAEYLIE----QGY-TDPDRLAIWGGSYGGYLtGAALNQR 85
 
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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