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Conserved domains on  [gi|1213911153|gb|ASH48650|]
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lipase [Listeria monocytogenes serotype 1/2c str. 10-5026]

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.
127-347 3.67e-55

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: 180.10  E-value: 3.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 127 FIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNELGIDASKIGVSGDSA 206
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 207 GGTLAAAVSYMDYEAETNYVGFQALLYPAltlVDEDNDKYQWDISKFGaseDTLPLVASGIigmnssgELLRKAYVRDEN 286
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPG---TDLRTESPSYLAREFA---DGPLLTRAAM-------DWFWRLYLPGAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1213911153 287 PAAPIYSPLSAVDKSIYPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFI 347
Cdd:pfam07859 148 RDDPLASPLFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 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.
127-347 3.67e-55

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: 180.10  E-value: 3.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 127 FIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNELGIDASKIGVSGDSA 206
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 207 GGTLAAAVSYMDYEAETNYVGFQALLYPAltlVDEDNDKYQWDISKFGaseDTLPLVASGIigmnssgELLRKAYVRDEN 286
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPG---TDLRTESPSYLAREFA---DGPLLTRAAM-------DWFWRLYLPGAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1213911153 287 PAAPIYSPLSAVDKSIYPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFI 347
Cdd:pfam07859 148 RDDPLASPLFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
113-371 2.18e-50

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 167.74  E-value: 2.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 113 RIYRHEEATKPVPAFIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNEL 192
Cdd:COG0657     2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 193 GIDASKIGVSGDSAGGTLAAAVSYMDYEAETNYVGFQALLYPALTLVdedndkyqwdiskfgasedtlplvasgiigmns 272
Cdd:COG0657    82 GIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT--------------------------------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 273 sgellrkayvrdenpAAPIYSPLSAVdksiyPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFIDkYGI 352
Cdd:COG0657   129 ---------------ASPLRADLAGL-----PPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGL-LAG 187
                         250
                  ....*....|....*....
gi 1213911153 353 FPQAEDVADEIVQMMKEIF 371
Cdd:COG0657   188 LPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
96-347 1.46e-24

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 102.10  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153  96 VTTEYRVVEGDYGDIPVRIYRheeATKPVPAFIFY-HGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAA 174
Cdd:PRK10162   55 MATRAYMVPTPYGQVETRLYY---PQPDSQATLFYlHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 175 PKDCYRVLEWVVEQSNELGIDASKIGVSGDSAGGTLA-AAVSYM-DYEAETNYVGFQALLYPALTLVDEDNdkyqwdISK 252
Cdd:PRK10162  132 IEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLAlASALWLrDKQIDCGKVAGVLLWYGLYGLRDSVS------RRL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 253 FGASEDtlplvasgiiGMNSSG-ELLRKAYVRDENPAAPIYSPLSAVD--KSIyPPTLIASAEFDALRAFADVFAKELRA 329
Cdd:PRK10162  206 LGGVWD----------GLTQQDlQMYEEAYLSNDADRESPYYCLFNNDltRDV-PPCFIAGAEFDPLLDDSRLLYQTLAA 274
                         250
                  ....*....|....*...
gi 1213911153 330 SGVQTKAIVYQGMCHAFI 347
Cdd:PRK10162  275 HQQPCEFKLYPGTLHAFL 292
 
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.
127-347 3.67e-55

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: 180.10  E-value: 3.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 127 FIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNELGIDASKIGVSGDSA 206
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 207 GGTLAAAVSYMDYEAETNYVGFQALLYPAltlVDEDNDKYQWDISKFGaseDTLPLVASGIigmnssgELLRKAYVRDEN 286
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPG---TDLRTESPSYLAREFA---DGPLLTRAAM-------DWFWRLYLPGAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1213911153 287 PAAPIYSPLSAVDKSIYPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFI 347
Cdd:pfam07859 148 RDDPLASPLFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
113-371 2.18e-50

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 167.74  E-value: 2.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 113 RIYRHEEATKPVPAFIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNEL 192
Cdd:COG0657     2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 193 GIDASKIGVSGDSAGGTLAAAVSYMDYEAETNYVGFQALLYPALTLVdedndkyqwdiskfgasedtlplvasgiigmns 272
Cdd:COG0657    82 GIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT--------------------------------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 273 sgellrkayvrdenpAAPIYSPLSAVdksiyPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFIDkYGI 352
Cdd:COG0657   129 ---------------ASPLRADLAGL-----PPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGL-LAG 187
                         250
                  ....*....|....*....
gi 1213911153 353 FPQAEDVADEIVQMMKEIF 371
Cdd:COG0657   188 LPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
96-347 1.46e-24

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 102.10  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153  96 VTTEYRVVEGDYGDIPVRIYRheeATKPVPAFIFY-HGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAA 174
Cdd:PRK10162   55 MATRAYMVPTPYGQVETRLYY---PQPDSQATLFYlHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 175 PKDCYRVLEWVVEQSNELGIDASKIGVSGDSAGGTLA-AAVSYM-DYEAETNYVGFQALLYPALTLVDEDNdkyqwdISK 252
Cdd:PRK10162  132 IEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLAlASALWLrDKQIDCGKVAGVLLWYGLYGLRDSVS------RRL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 253 FGASEDtlplvasgiiGMNSSG-ELLRKAYVRDENPAAPIYSPLSAVD--KSIyPPTLIASAEFDALRAFADVFAKELRA 329
Cdd:PRK10162  206 LGGVWD----------GLTQQDlQMYEEAYLSNDADRESPYYCLFNNDltRDV-PPCFIAGAEFDPLLDDSRLLYQTLAA 274
                         250
                  ....*....|....*...
gi 1213911153 330 SGVQTKAIVYQGMCHAFI 347
Cdd:PRK10162  275 HQQPCEFKLYPGTLHAFL 292
BD-FAE pfam20434
BD-FAE; This family represents a novel bifunctional feruloyl and acetyl xylan esterase (BD-FAE, ...
114-316 1.65e-19

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: 85.69  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 114 IYRHEEATKPVPAFIFYHGGGFVGGTPAVVENFCKGIAEKLPA---VVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSN 190
Cdd:pfam20434   3 IYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALLKagyAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 191 ELGIDASKIGVSGDSAGGTLA--AAVSYMDYEAETNYVGFQALLYPAltlvdedNDKYQWDISKFGASEDTLPLVASGII 268
Cdd:pfam20434  83 KYGIDTNKIALMGFSAGGHLAllAGLSNNNKEFEGNVGDYTPESSKE-------SFKVNAVVDFYGPTDLLDMDSCGTHN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1213911153 269 GMNSSGELLRKAYVRDENPAAPIYSPLSAVDKSiYPPTLIASAEFDAL 316
Cdd:pfam20434 156 DAKSPETLLLGAPPLENPDLAKSASPITYVDKN-DPPFLIIHGDKDPL 202
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
106-350 8.10e-07

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 49.63  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 106 DYGDIPVRIYRHEEAtKPVPAFIFYHGGgfvggtPAVVENFCKGIAEKLPA---VVINVDYH---LAPEFPAPAAPKDCY 179
Cdd:COG1506     6 DGTTLPGWLYLPADG-KKYPVVVYVHGG------PGSRDDSFLPLAQALASrgyAVLAPDYRgygESAGDWGGDEVDDVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 180 RVLEWVVEQSnelGIDASKIGVSGDSAGG--TLAAAVSYMDYeaetnyvgFQA--LLYPALTLVDEDNDKYQWDISKFGA 255
Cdd:COG1506    79 AAIDYLAARP---YVDPDRIGIYGHSYGGymALLAAARHPDR--------FKAavALAGVSDLRSYYGTTREYTERLMGG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1213911153 256 SEDtlplvasgiigmnsSGELLRKayvrdenpaapiYSPLSAVDKsIYPPTLIASAEFDALRAFADV--FAKELRASGVQ 333
Cdd:COG1506   148 PWE--------------DPEAYAA------------RSPLAYADK-LKTPLLLIHGEADDRVPPEQAerLYEALKKAGKP 200
                         250
                  ....*....|....*..
gi 1213911153 334 TKAIVYQGMCHAFIDKY 350
Cdd:COG1506   201 VELLVYPGEGHGFSGAG 217
 
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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