NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|284061759|gb|ADB72698|]
View 

hypothetical protein LM5923_2857 [Listeria monocytogenes 08-5923]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 6.28e-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: 179.33  E-value: 6.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  127 FIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNELGIDASKIGVSGDSA 206
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  207 GGTLAAAVSYMDYEAETNYVGFQALLYPAltlVDEDNEKYQWDISKFGaseDTLPLVAPGIigmnssgELLRTAYVRDEN 286
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPG---TDLRTESPSYLAREFA---DGPLLTRAAM-------DWFWRLYLPGAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284061759  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 6.28e-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: 179.33  E-value: 6.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  127 FIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNELGIDASKIGVSGDSA 206
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  207 GGTLAAAVSYMDYEAETNYVGFQALLYPAltlVDEDNEKYQWDISKFGaseDTLPLVAPGIigmnssgELLRTAYVRDEN 286
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPG---TDLRTESPSYLAREFA---DGPLLTRAAM-------DWFWRLYLPGAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284061759  287 PAAPIYSPLSAVDKSIYPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFI 347
Cdd:pfam07859 148 RDDPLASPLFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
113-371 2.79e-50

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 167.36  E-value: 2.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 113 RIYRHEEATKPVPAFIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNEL 192
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 193 GIDASKIGVSGDSAGGTLAAAVSYMDYEAETNYVGFQALLYPALTLVdednekyqwdiskfgasedtlplvapgiigmns 272
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT--------------------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 273 sgellrtayvrdenpAAPIYSPLSAVdksiyPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFIDkYGI 352
Cdd:COG0657  129 ---------------ASPLRADLAGL-----PPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGL-LAG 187
                        250
                 ....*....|....*....
gi 284061759 353 FPQAEDVADEIVQMMKEIF 371
Cdd:COG0657  188 LPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
96-347 4.24e-24

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 100.95  E-value: 4.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  96 VTTEYRVVEGDYGDIPVRIYRheeATKPVPAFIFY-HGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAA 174
Cdd:PRK10162  55 MATRAYMVPTPYGQVETRLYY---PQPDSQATLFYlHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 175 PKDCYRVLEWVVEQSNELGIDASKIGVSGDSAGGTLA-AAVSYM-DYEAETNYVGFQALLYPALTLVDEDNekyqwdISK 252
Cdd:PRK10162 132 IEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLAlASALWLrDKQIDCGKVAGVLLWYGLYGLRDSVS------RRL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 253 FGASEDtlplvapgiiGMNSSG-ELLRTAYVRDENPAAPIYSPLSAVD--KSIyPPTLIASAEFDALRAFADVFAKELRA 329
Cdd:PRK10162 206 LGGVWD----------GLTQQDlQMYEEAYLSNDADRESPYYCLFNNDltRDV-PPCFIAGAEFDPLLDDSRLLYQTLAA 274
                        250
                 ....*....|....*...
gi 284061759 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 6.28e-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: 179.33  E-value: 6.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  127 FIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNELGIDASKIGVSGDSA 206
Cdd:pfam07859   1 LVYFHGGGFVLGSADTHDRLCRRLAAEAGAVVVSVDYRLAPEHPFPAAYDDAYAALRWLAEQAAELGADPSRIAVAGDSA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  207 GGTLAAAVSYMDYEAETNYVGFQALLYPAltlVDEDNEKYQWDISKFGaseDTLPLVAPGIigmnssgELLRTAYVRDEN 286
Cdd:pfam07859  81 GGNLAAAVALRARDEGLPKPAGQVLIYPG---TDLRTESPSYLAREFA---DGPLLTRAAM-------DWFWRLYLPGAD 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 284061759  287 PAAPIYSPLSAVDKSIYPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFI 347
Cdd:pfam07859 148 RDDPLASPLFASDLSGLPPALVVVAEFDPLRDEGEAYAERLRAAGVPVELIEYPGMPHGFH 208
Aes COG0657
Acetyl esterase/lipase [Lipid transport and metabolism];
113-371 2.79e-50

Acetyl esterase/lipase [Lipid transport and metabolism];


Pssm-ID: 440422 [Multi-domain]  Cd Length: 207  Bit Score: 167.36  E-value: 2.79e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 113 RIYRHEEATKPVPAFIFYHGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSNEL 192
Cdd:COG0657    2 DVYRPAGAKGPLPVVVYFHGGGWVSGSKDTHDPLARRLAARAGAAVVSVDYRLAPEHPFPAALEDAYAALRWLRANAAEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 193 GIDASKIGVSGDSAGGTLAAAVSYMDYEAETNYVGFQALLYPALTLVdednekyqwdiskfgasedtlplvapgiigmns 272
Cdd:COG0657   82 GIDPDRIAVAGDSAGGHLAAALALRARDRGGPRPAAQVLIYPVLDLT--------------------------------- 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 273 sgellrtayvrdenpAAPIYSPLSAVdksiyPPTLIASAEFDALRAFADVFAKELRASGVQTKAIVYQGMCHAFIDkYGI 352
Cdd:COG0657  129 ---------------ASPLRADLAGL-----PPTLIVTGEADPLVDESEALAAALRAAGVPVELHVYPGGGHGFGL-LAG 187
                        250
                 ....*....|....*....
gi 284061759 353 FPQAEDVADEIVQMMKEIF 371
Cdd:COG0657  188 LPEARAALAEIAAFLRRAL 206
PRK10162 PRK10162
acetyl esterase;
96-347 4.24e-24

acetyl esterase;


Pssm-ID: 236660 [Multi-domain]  Cd Length: 318  Bit Score: 100.95  E-value: 4.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  96 VTTEYRVVEGDYGDIPVRIYRheeATKPVPAFIFY-HGGGFVGGTPAVVENFCKGIAEKLPAVVINVDYHLAPEFPAPAA 174
Cdd:PRK10162  55 MATRAYMVPTPYGQVETRLYY---PQPDSQATLFYlHGGGFILGNLDTHDRIMRLLASYSGCTVIGIDYTLSPEARFPQA 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 175 PKDCYRVLEWVVEQSNELGIDASKIGVSGDSAGGTLA-AAVSYM-DYEAETNYVGFQALLYPALTLVDEDNekyqwdISK 252
Cdd:PRK10162 132 IEEIVAVCCYFHQHAEDYGINMSRIGFAGDSAGAMLAlASALWLrDKQIDCGKVAGVLLWYGLYGLRDSVS------RRL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 253 FGASEDtlplvapgiiGMNSSG-ELLRTAYVRDENPAAPIYSPLSAVD--KSIyPPTLIASAEFDALRAFADVFAKELRA 329
Cdd:PRK10162 206 LGGVWD----------GLTQQDlQMYEEAYLSNDADRESPYYCLFNNDltRDV-PPCFIAGAEFDPLLDDSRLLYQTLAA 274
                        250
                 ....*....|....*...
gi 284061759 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 2.80e-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: 85.31  E-value: 2.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  114 IYRHEEATKPVPAFIFYHGGGFVGGTPAVVENFCKGIAEKLPA---VVINVDYHLAPEFPAPAAPKDCYRVLEWVVEQSN 190
Cdd:pfam20434   3 IYLPKNAKGPYPVVIWIHGGGWNSGDKEADMGFMTNTVKALLKagyAVASINYRLSTDAKFPAQIQDVKAAIRFLRANAA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759  191 ELGIDASKIGVSGDSAGGTLA--AAVSYMDYEAETNYVGFQALLYPAltlvdedNEKYQWDISKFGASEDTLPLVAPGII 268
Cdd:pfam20434  83 KYGIDTNKIALMGFSAGGHLAllAGLSNNNKEFEGNVGDYTPESSKE-------SFKVNAVVDFYGPTDLLDMDSCGTHN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 284061759  269 GMNSSGELLRTAYVRDENPAAPIYSPLSAVDKSiYPPTLIASAEFDAL 316
Cdd:pfam20434 156 DAKSPETLLLGAPPLENPDLAKSASPITYVDKN-DPPFLIIHGDKDPL 202
DAP2 COG1506
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
106-350 1.30e-06

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


Pssm-ID: 441115 [Multi-domain]  Cd Length: 234  Bit Score: 48.86  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 106 DYGDIPVRIYRHEEAtKPVPAFIFYHGGgfvggtPAVVENFCKGIAEKLPA---VVINVDYH---LAPEFPAPAAPKDCY 179
Cdd:COG1506    6 DGTTLPGWLYLPADG-KKYPVVVYVHGG------PGSRDDSFLPLAQALASrgyAVLAPDYRgygESAGDWGGDEVDDVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 180 RVLEWVVEQSnelGIDASKIGVSGDSAGG--TLAAAVSYMDYeaetnyvgFQA--LLYPALTLVDEDNEKYQWDISKFGA 255
Cdd:COG1506   79 AAIDYLAARP---YVDPDRIGIYGHSYGGymALLAAARHPDR--------FKAavALAGVSDLRSYYGTTREYTERLMGG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 284061759 256 SEDTlplvapgiigmnssgellRTAYVRdenpaapiYSPLSAVDKsIYPPTLIASAEFDALRAFADV--FAKELRASGVQ 333
Cdd:COG1506  148 PWED------------------PEAYAA--------RSPLAYADK-LKTPLLLIHGEADDRVPPEQAerLYEALKKAGKP 200
                        250
                 ....*....|....*..
gi 284061759 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH