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Conserved domains on  [gi|147905893|ref|NP_001078973|]
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uncharacterized protein LOC230890 [Mus musculus]

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, ...
115-378 1.11e-40

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 pfam07859:

Pssm-ID: 473884 [Multi-domain]  Cd Length: 208  Bit Score: 143.51  E-value: 1.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  115 IIFYHGGAAAFGSLDIYHNLCSFLVRETDSVLLSVGYRKLPKHHHPAALNDCLSATILFLKALETYGVDPSRVVLCGDSF 194
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  195 GGWVVASISQTLVSTpSLPQIRAQVLIYPILQvINFLLPSLQQNKNipllskdlliifvcnylaidlsWGDSMLTGAVIp 274
Cdd:pfam07859  81 GGNLAAAVALRARDE-GLPKPAGQVLIYPGTD-LRTESPSYLAREF----------------------ADGPLLTRAAM- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  275 ldkwkkyrkwlssdnipRRLWSQdtqpeflghfneaaYLETKHIFNPEISPIIADDktIAQLPEAFLVSCEYDIVRDDTL 354
Cdd:pfam07859 136 -----------------DWFWRL--------------YLPGADRDDPLASPLFASD--LSGLPPALVVVAEFDPLRDEGE 182
                         250       260
                  ....*....|....*....|....
gi 147905893  355 LYKKRLEDQGVPVTWHHVMDGFHG 378
Cdd:pfam07859 183 AYAERLRAAGVPVELIEYPGMPHG 206
 
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.
115-378 1.11e-40

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: 143.51  E-value: 1.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  115 IIFYHGGAAAFGSLDIYHNLCSFLVRETDSVLLSVGYRKLPKHHHPAALNDCLSATILFLKALETYGVDPSRVVLCGDSF 194
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  195 GGWVVASISQTLVSTpSLPQIRAQVLIYPILQvINFLLPSLQQNKNipllskdlliifvcnylaidlsWGDSMLTGAVIp 274
Cdd:pfam07859  81 GGNLAAAVALRARDE-GLPKPAGQVLIYPGTD-LRTESPSYLAREF----------------------ADGPLLTRAAM- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  275 ldkwkkyrkwlssdnipRRLWSQdtqpeflghfneaaYLETKHIFNPEISPIIADDktIAQLPEAFLVSCEYDIVRDDTL 354
Cdd:pfam07859 136 -----------------DWFWRL--------------YLPGADRDDPLASPLFASD--LSGLPPALVVVAEFDPLRDEGE 182
                         250       260
                  ....*....|....*....|....
gi 147905893  355 LYKKRLEDQGVPVTWHHVMDGFHG 378
Cdd:pfam07859 183 AYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
100-382 1.95e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 134.62  E-value: 1.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893 100 RLFQPKAVSSKlRRGIIFYHGGAAAFGSLDIYHNLCSFLVRETDSVLLSVGYRKLPKHHHPAALNDCLSATILFLKALET 179
Cdd:COG0657    2 DVYRPAGAKGP-LPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893 180 YGVDPSRVVLCGDSFGGWVVASISQTLvSTPSLPQIRAQVLIYPILqvinfllpslqqnknipllskdlliifvcnylai 259
Cdd:COG0657   81 LGIDPDRIAVAGDSAGGHLAAALALRA-RDRGGPRPAAQVLIYPVL---------------------------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893 260 DLSwgdsmltgavipldkwkkyrkwlssdniprrlwsqdtqpeflghfneaayletkhifnpeISPIIADdktIAQLPEA 339
Cdd:COG0657  126 DLT------------------------------------------------------------ASPLRAD---LAGLPPT 142
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 147905893 340 FLVSCEYDIVRDDTLLYKKRLEDQGVPVTWHHVMDGFHGCVLL 382
Cdd:COG0657  143 LIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLL 185
PRK10162 PRK10162
acetyl esterase;
95-195 3.69e-11

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 63.58  E-value: 3.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  95 GTIPVRLFQPKAVSsklrRGIIFY-HGGAAAFGSLDIYHNLCSFLVRETDSVLLSVGYRKLPKHHHPAALNDCLSATILF 173
Cdd:PRK10162  67 GQVETRLYYPQPDS----QATLFYlHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYF 142
                         90       100
                 ....*....|....*....|..
gi 147905893 174 LKALETYGVDPSRVVLCGDSFG 195
Cdd:PRK10162 143 HQHAEDYGINMSRIGFAGDSAG 164
 
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.
115-378 1.11e-40

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: 143.51  E-value: 1.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  115 IIFYHGGAAAFGSLDIYHNLCSFLVRETDSVLLSVGYRKLPKHHHPAALNDCLSATILFLKALETYGVDPSRVVLCGDSF 194
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  195 GGWVVASISQTLVSTpSLPQIRAQVLIYPILQvINFLLPSLQQNKNipllskdlliifvcnylaidlsWGDSMLTGAVIp 274
Cdd:pfam07859  81 GGNLAAAVALRARDE-GLPKPAGQVLIYPGTD-LRTESPSYLAREF----------------------ADGPLLTRAAM- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  275 ldkwkkyrkwlssdnipRRLWSQdtqpeflghfneaaYLETKHIFNPEISPIIADDktIAQLPEAFLVSCEYDIVRDDTL 354
Cdd:pfam07859 136 -----------------DWFWRL--------------YLPGADRDDPLASPLFASD--LSGLPPALVVVAEFDPLRDEGE 182
                         250       260
                  ....*....|....*....|....
gi 147905893  355 LYKKRLEDQGVPVTWHHVMDGFHG 378
Cdd:pfam07859 183 AYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
100-382 1.95e-37

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 134.62  E-value: 1.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893 100 RLFQPKAVSSKlRRGIIFYHGGAAAFGSLDIYHNLCSFLVRETDSVLLSVGYRKLPKHHHPAALNDCLSATILFLKALET 179
Cdd:COG0657    2 DVYRPAGAKGP-LPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893 180 YGVDPSRVVLCGDSFGGWVVASISQTLvSTPSLPQIRAQVLIYPILqvinfllpslqqnknipllskdlliifvcnylai 259
Cdd:COG0657   81 LGIDPDRIAVAGDSAGGHLAAALALRA-RDRGGPRPAAQVLIYPVL---------------------------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893 260 DLSwgdsmltgavipldkwkkyrkwlssdniprrlwsqdtqpeflghfneaayletkhifnpeISPIIADdktIAQLPEA 339
Cdd:COG0657  126 DLT------------------------------------------------------------ASPLRAD---LAGLPPT 142
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 147905893 340 FLVSCEYDIVRDDTLLYKKRLEDQGVPVTWHHVMDGFHGCVLL 382
Cdd:COG0657  143 LIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGLL 185
PRK10162 PRK10162
acetyl esterase;
95-195 3.69e-11

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 63.58  E-value: 3.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  95 GTIPVRLFQPKAVSsklrRGIIFY-HGGAAAFGSLDIYHNLCSFLVRETDSVLLSVGYRKLPKHHHPAALNDCLSATILF 173
Cdd:PRK10162  67 GQVETRLYYPQPDS----QATLFYlHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYF 142
                         90       100
                 ....*....|....*....|..
gi 147905893 174 LKALETYGVDPSRVVLCGDSFG 195
Cdd:PRK10162 143 HQHAEDYGINMSRIGFAGDSAG 164
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
115-196 1.90e-06

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: 48.33  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  115 IIFYHGGAAAFGS----LDIYHNLCSFLVrETDSVLLSVGYRKLPKHHHPAALNDCLSAtILFLKA-LETYGVDPSRVVL 189
Cdd:pfam20434  16 VIWIHGGGWNSGDkeadMGFMTNTVKALL-KAGYAVASINYRLSTDAKFPAQIQDVKAA-IRFLRAnAAKYGIDTNKIAL 93

                  ....*..
gi 147905893  190 CGDSFGG 196
Cdd:pfam20434  94 MGFSAGG 100
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
96-224 3.90e-04

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 41.54  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  96 TIPVRLFQPKAvsSKLRRGIIFYHGGAAAfgSLDIYHNLCSFLVREtDSVLLSVGYR---KLPKHHHPAALNDCLSAtil 172
Cdd:COG1506    9 TLPGWLYLPAD--GKKYPVVVYVHGGPGS--RDDSFLPLAQALASR-GYAVLAPDYRgygESAGDWGGDEVDDVLAA--- 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 147905893 173 fLKAL-ETYGVDPSRVVLCGDSFGGWVVAsisQTLVSTPSLpqIRAQVLIYPI 224
Cdd:COG1506   81 -IDYLaARPYVDPDRIGIYGHSYGGYMAL---LAAARHPDR--FKAAVALAGV 127
DLH COG0412
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
95-223 1.30e-03

Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440181 [Multi-domain]  Cd Length: 226  Bit Score: 39.95  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 147905893  95 GTIPVRLFQPKAVSSklRRGIIFYHGgaaAFGSLDIYHNLCSFLVREtdsvllsvGY--------------------RKL 154
Cdd:COG0412   14 VTLPGYLARPAGGGP--RPGVVVLHE---IFGLNPHIRDVARRLAAA--------GYvvlapdlygrggpgddpdeaRAL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 147905893 155 PKHHHPAALNDCLSATILFLKALEtyGVDPSRVVLCGDSFGGWVVasisqtLVSTPSLPQIRAQVLIYP 223
Cdd:COG0412   81 MGALDPELLAADLRAALDWLKAQP--EVDAGRVGVVGFCFGGGLA------LLAAARGPDLAAAVSFYG 141
 
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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