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Conserved domains on  [gi|300796048|ref|NP_001178697|]
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arylacetamide deacetylase-like 3 [Rattus norvegicus]

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.
116-379 8.79e-52

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: 172.40  E-value: 8.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  116 IIFFHGGGTILGSLRTHHSICLRLSKDCDAVVISVGYRKSPMYKYPVMKDDCVAATTHFLRSLDVYGVDPDRLVVCGDSV 195
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  196 GGTAAAVTSQTvVHRKDLPQIRAQILIYPSLQLvDFGSPSYQQNFN--VPLLTSNLALYCfcchldvklswqsviksgrh 273
Cdd:pfam07859  81 GGNLAAAVALR-ARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWF-------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  274 lppeiWEKYRKWLGVENiperfkkqgykpiPRgpvnnevyqeiktalnntCSPLLAEDslVSQLPETCIVSCEYDLFRDH 353
Cdd:pfam07859 139 -----WRLYLPGADRDD-------------PL------------------ASPLFASD--LSGLPPALVVVAEFDPLRDE 180
                         250       260
                  ....*....|....*....|....*.
gi 300796048  354 SLLYKKRLEALGVPVTWHHMEDGFHG 379
Cdd:pfam07859 181 GEAYAERLRAAGVPVELIEYPGMPHG 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.
116-379 8.79e-52

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: 172.40  E-value: 8.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  116 IIFFHGGGTILGSLRTHHSICLRLSKDCDAVVISVGYRKSPMYKYPVMKDDCVAATTHFLRSLDVYGVDPDRLVVCGDSV 195
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  196 GGTAAAVTSQTvVHRKDLPQIRAQILIYPSLQLvDFGSPSYQQNFN--VPLLTSNLALYCfcchldvklswqsviksgrh 273
Cdd:pfam07859  81 GGNLAAAVALR-ARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWF-------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  274 lppeiWEKYRKWLGVENiperfkkqgykpiPRgpvnnevyqeiktalnntCSPLLAEDslVSQLPETCIVSCEYDLFRDH 353
Cdd:pfam07859 139 -----WRLYLPGADRDD-------------PL------------------ASPLFASD--LSGLPPALVVVAEFDPLRDE 180
                         250       260
                  ....*....|....*....|....*.
gi 300796048  354 SLLYKKRLEALGVPVTWHHMEDGFHG 379
Cdd:pfam07859 181 GEAYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
102-408 1.72e-45

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 155.80  E-value: 1.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048 102 LYKPKKPSSvPRIGIIFFHGGGTILGSLRTHHSICLRLSKDCDAVVISVGYRKSPMYKYPVMKDDCVAATTHFLRSLDVY 181
Cdd:COG0657    3 VYRPAGAKG-PLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048 182 GVDPDRLVVCGDSVGGTAAAVTSQTvVHRKDLPQIRAQILIYPslqLVDFgspsyqqnfnvplltsnlalycfcchldvk 261
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALR-ARDRGGPRPAAQVLIYP---VLDL------------------------------ 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048 262 lswqsviksgrhlppeiwekyrkwlgveniperfkkqgykpiprgpvnnevyqeiktalnnTCSPLLAEdslVSQLPETC 341
Cdd:COG0657  128 -------------------------------------------------------------TASPLRAD---LAGLPPTL 143
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300796048 342 IVSCEYDLFRDHSLLYKKRLEALGVPVTWHHMEDGFHGvlntfeFGLLS-IPCSLRIMDLIIRFIKKF 408
Cdd:COG0657  144 IVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHG------FGLLAgLPEARAALAEIAAFLRRA 205
PRK10162 PRK10162
acetyl esterase;
98-235 3.16e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 87.47  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  98 IPVKLYKPKKPSsvpRIGIIFFHGGGTILGSLRTHHSICLRLSKDCDAVVISVGYRKSPMYKYPVMKDDCVAATTHFLRS 177
Cdd:PRK10162  69 VETRLYYPQPDS---QATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQH 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300796048 178 LDVYGVDPDRLVVCGDSVGGTAAAVTSQTVVHRK-DLPQIRAQILIYPSLQLVDfgSPS 235
Cdd:PRK10162 146 AEDYGINMSRIGFAGDSAGAMLALASALWLRDKQiDCGKVAGVLLWYGLYGLRD--SVS 202
 
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.
116-379 8.79e-52

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: 172.40  E-value: 8.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  116 IIFFHGGGTILGSLRTHHSICLRLSKDCDAVVISVGYRKSPMYKYPVMKDDCVAATTHFLRSLDVYGVDPDRLVVCGDSV 195
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  196 GGTAAAVTSQTvVHRKDLPQIRAQILIYPSLQLvDFGSPSYQQNFN--VPLLTSNLALYCfcchldvklswqsviksgrh 273
Cdd:pfam07859  81 GGNLAAAVALR-ARDEGLPKPAGQVLIYPGTDL-RTESPSYLAREFadGPLLTRAAMDWF-------------------- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  274 lppeiWEKYRKWLGVENiperfkkqgykpiPRgpvnnevyqeiktalnntCSPLLAEDslVSQLPETCIVSCEYDLFRDH 353
Cdd:pfam07859 139 -----WRLYLPGADRDD-------------PL------------------ASPLFASD--LSGLPPALVVVAEFDPLRDE 180
                         250       260
                  ....*....|....*....|....*.
gi 300796048  354 SLLYKKRLEALGVPVTWHHMEDGFHG 379
Cdd:pfam07859 181 GEAYAERLRAAGVPVELIEYPGMPHG 206
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
102-408 1.72e-45

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 155.80  E-value: 1.72e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048 102 LYKPKKPSSvPRIGIIFFHGGGTILGSLRTHHSICLRLSKDCDAVVISVGYRKSPMYKYPVMKDDCVAATTHFLRSLDVY 181
Cdd:COG0657    3 VYRPAGAKG-PLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048 182 GVDPDRLVVCGDSVGGTAAAVTSQTvVHRKDLPQIRAQILIYPslqLVDFgspsyqqnfnvplltsnlalycfcchldvk 261
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALR-ARDRGGPRPAAQVLIYP---VLDL------------------------------ 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048 262 lswqsviksgrhlppeiwekyrkwlgveniperfkkqgykpiprgpvnnevyqeiktalnnTCSPLLAEdslVSQLPETC 341
Cdd:COG0657  128 -------------------------------------------------------------TASPLRAD---LAGLPPTL 143
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300796048 342 IVSCEYDLFRDHSLLYKKRLEALGVPVTWHHMEDGFHGvlntfeFGLLS-IPCSLRIMDLIIRFIKKF 408
Cdd:COG0657  144 IVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHG------FGLLAgLPEARAALAEIAAFLRRA 205
PRK10162 PRK10162
acetyl esterase;
98-235 3.16e-19

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 87.47  E-value: 3.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  98 IPVKLYKPKKPSsvpRIGIIFFHGGGTILGSLRTHHSICLRLSKDCDAVVISVGYRKSPMYKYPVMKDDCVAATTHFLRS 177
Cdd:PRK10162  69 VETRLYYPQPDS---QATLFYLHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQAIEEIVAVCCYFHQH 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300796048 178 LDVYGVDPDRLVVCGDSVGGTAAAVTSQTVVHRK-DLPQIRAQILIYPSLQLVDfgSPS 235
Cdd:PRK10162 146 AEDYGINMSRIGFAGDSAGAMLALASALWLRDKQiDCGKVAGVLLWYGLYGLRD--SVS 202
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
96-224 4.14e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 47.70  E-value: 4.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  96 ETIPVKLYKPKKPSSVPriGIIFFHGGGTilGSLRTHHSICLRLSKDcDAVVISVGYR---KSPMYKYPVMKDDCVAATt 172
Cdd:COG1506    8 TTLPGWLYLPADGKKYP--VVVYVHGGPG--SRDDSFLPLAQALASR-GYAVLAPDYRgygESAGDWGGDEVDDVLAAI- 81
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 300796048 173 HFLRSLDvyGVDPDRLVVCGDSVGGTAAAvtsQTVVHRKDLpqIRAQILIYP 224
Cdd:COG1506   82 DYLAARP--YVDPDRIGIYGHSYGGYMAL---LAAARHPDR--FKAAVALAG 126
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
102-197 6.05e-05

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: 43.71  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300796048  102 LYKPKKpSSVPRIGIIFFHGGGTILGS----LRTHHSICLRLSKDCDAVViSVGYRKSPMYKYPVMKDDCVAATThFLRS 177
Cdd:pfam20434   3 IYLPKN-AKGPYPVVIWIHGGGWNSGDkeadMGFMTNTVKALLKAGYAVA-SINYRLSTDAKFPAQIQDVKAAIR-FLRA 79
                          90       100
                  ....*....|....*....|.
gi 300796048  178 -LDVYGVDPDRLVVCGDSVGG 197
Cdd:pfam20434  80 nAAKYGIDTNKIALMGFSAGG 100
 
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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