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Conserved domains on  [gi|488003447|ref|WP_002075186|]
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MULTISPECIES: arylesterase [Acinetobacter]

Protein Classification

arylesterase( domain architecture ID 10110701)

lysophospholipase A is an arylesterase.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 28-204 1.00e-96

Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.


:

Pssm-ID: 238860 [Multi-domain]  Cd Length: 177  Bit Score: 278.63  E-value: 1.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGYGIDPKQGWVQLLQKRLDQQYPkQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRG 107
Cdd:cd01822    2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGI-DVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 108 QPPQMIQKNLSQLIQLSQKQKAKVILFGMKIPPNYGTAYSKAFENSYKTVSQKYQVKLLPFFLDGVAGQKQLMQNDLIHP 187
Cdd:cd01822   81 IPPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHP 160

                        170
                 ....*....|....*..
gi 488003447 188 NTQAQSKLLNLAYPYIK 204
Cdd:cd01822  161 NAEGQPIIAENVWPALE 177
 
Name Accession Description Interval E-value
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 28-204 1.00e-96

Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.


Pssm-ID: 238860 [Multi-domain]  Cd Length: 177  Bit Score: 278.63  E-value: 1.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGYGIDPKQGWVQLLQKRLDQQYPkQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRG 107
Cdd:cd01822    2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGI-DVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 108 QPPQMIQKNLSQLIQLSQKQKAKVILFGMKIPPNYGTAYSKAFENSYKTVSQKYQVKLLPFFLDGVAGQKQLMQNDLIHP 187
Cdd:cd01822   81 IPPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHP 160

                        170
                 ....*....|....*..
gi 488003447 188 NTQAQSKLLNLAYPYIK 204
Cdd:cd01822  161 NAEGQPIIAENVWPALE 177
PRK10528 PRK10528
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
 24-192 2.28e-56

multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional


Pssm-ID: 182521  Cd Length: 191  Bit Score: 176.88  E-value: 2.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  24 VSAKTILILGDSISAGYGIDPKQGWVQLLQKrldqQYPKQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGND 103
Cdd:PRK10528   8 AAADTLLILGDSLSAGYRMPASAAWPALLND----KWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGND 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 104 GLRGQPPQMIQKNLSQLIQLSQKQKAKVILFGMKIPPNYGTAYSKAFENSYKTVSQKYQVKLLPFFLDGVAGQKQLMQND 183
Cdd:PRK10528  84 GLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFFMEEVYLKPQWMQDD 163


                 ....*....
gi 488003447 184 LIHPNTQAQ 192
Cdd:PRK10528 164 GIHPNRDAQ 172
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 25-204 1.85e-50

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 161.74  E-value: 1.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  25 SAKTILILGDSISAGYGIDPKQGWVQLLQKRLDQQypkQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDG 104
Cdd:COG2755    7 KPLRIVALGDSITAGYGASRERGWPALLARRLAAA---DVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 105 LRGQ--PPQMIQKNLSQLIQLSQKQ--KAKVILFGMK--IPPNYGTAYSKAFENSYKTVSQKYQVKLLPFF--LDGVAGQ 176
Cdd:COG2755   84 LRGLgvSPEEFRANLEALIDRLRAAgpGARVVLVTPPprLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYaaLRDAGDL 163

                        170       180
                 ....*....|....*....|....*...
gi 488003447 177 KQLMQNDLIHPNTQAQSKLLNLAYPYIK 204
Cdd:COG2755  164 PDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 31-188 2.18e-28

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 104.93  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447   31 ILGDSISAGYGI-DPKQGWVQLLQKRLDQQYPKQHkVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRGQP 109
Cdd:pfam13472   1 ALGDSITAGYGAtGGDRSYPGWLARLLARRLGADV-VNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  110 PQMIQKNLSQLIQLSQKQKAKVILFGMKIPP---------NYGTAYSKAFENSYKTVSQKYQVKLLPF---FLDGVAGQK 177
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPvgppppldeRRLNARIAEYNAAIREVAAERGVPYVDLwdaLRDDGGWLP 159

                         170
                  ....*....|.
gi 488003447  178 QLMQNDLIHPN 188
Cdd:pfam13472 160 DLLADDGLHPN 170
 
Name Accession Description Interval E-value
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 28-204 1.00e-96

Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this family is TesA, an E. coli periplasmic protein with thioesterase, esterase, arylesterase, protease and lysophospholipase activity.


Pssm-ID: 238860 [Multi-domain]  Cd Length: 177  Bit Score: 278.63  E-value: 1.00e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGYGIDPKQGWVQLLQKRLDQQYPkQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRG 107
Cdd:cd01822    2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGI-DVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 108 QPPQMIQKNLSQLIQLSQKQKAKVILFGMKIPPNYGTAYSKAFENSYKTVSQKYQVKLLPFFLDGVAGQKQLMQNDLIHP 187
Cdd:cd01822   81 IPPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHP 160

                        170
                 ....*....|....*..
gi 488003447 188 NTQAQSKLLNLAYPYIK 204
Cdd:cd01822  161 NAEGQPIIAENVWPALE 177
PRK10528 PRK10528
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
 24-192 2.28e-56

multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional


Pssm-ID: 182521  Cd Length: 191  Bit Score: 176.88  E-value: 2.28e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  24 VSAKTILILGDSISAGYGIDPKQGWVQLLQKrldqQYPKQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGND 103
Cdd:PRK10528   8 AAADTLLILGDSLSAGYRMPASAAWPALLND----KWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGND 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 104 GLRGQPPQMIQKNLSQLIQLSQKQKAKVILFGMKIPPNYGTAYSKAFENSYKTVSQKYQVKLLPFFLDGVAGQKQLMQND 183
Cdd:PRK10528  84 GLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFFMEEVYLKPQWMQDD 163


                 ....*....
gi 488003447 184 LIHPNTQAQ 192
Cdd:PRK10528 164 GIHPNRDAQ 172
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 25-204 1.85e-50

Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle control, cell division, chromosome partitioning, Lipid transport and metabolism];


Pssm-ID: 442045 [Multi-domain]  Cd Length: 191  Bit Score: 161.74  E-value: 1.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  25 SAKTILILGDSISAGYGIDPKQGWVQLLQKRLDQQypkQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDG 104
Cdd:COG2755    7 KPLRIVALGDSITAGYGASRERGWPALLARRLAAA---DVRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTNDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 105 LRGQ--PPQMIQKNLSQLIQLSQKQ--KAKVILFGMK--IPPNYGTAYSKAFENSYKTVSQKYQVKLLPFF--LDGVAGQ 176
Cdd:COG2755   84 LRGLgvSPEEFRANLEALIDRLRAAgpGARVVLVTPPprLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYaaLRDAGDL 163

                        170       180
                 ....*....|....*....|....*...
gi 488003447 177 KQLMQNDLIHPNTQAQSKLLNLAYPYIK 204
Cdd:COG2755  164 PDLLTADGLHPNAAGYRLIAEAVLPALK 191
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 31-188 2.18e-28

GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are similar to pfam00657.


Pssm-ID: 463889  Cd Length: 176  Bit Score: 104.93  E-value: 2.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447   31 ILGDSISAGYGI-DPKQGWVQLLQKRLDQQYPKQHkVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRGQP 109
Cdd:pfam13472   1 ALGDSITAGYGAtGGDRSYPGWLARLLARRLGADV-VNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  110 PQMIQKNLSQLIQLSQKQKAKVILFGMKIPP---------NYGTAYSKAFENSYKTVSQKYQVKLLPF---FLDGVAGQK 177
Cdd:pfam13472  80 AARAAANLEALIDALRAAGPDARVLLIGPLPvgppppldeRRLNARIAEYNAAIREVAAERGVPYVDLwdaLRDDGGWLP 159

                         170
                  ....*....|.
gi 488003447  178 QLMQNDLIHPN 188
Cdd:pfam13472 160 DLLADDGLHPN 170
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 29-195 2.51e-25

SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 238141 [Multi-domain]  Cd Length: 187  Bit Score: 97.10  E-value: 2.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  29 ILILGDSISAGYGIDPKQGWVQLLQKRLDQQYPKQHKVVNASVSGETTSGALARL--PKLLQTYKPEVVVIELGGNDGLR 106
Cdd:cd00229    1 ILVIGDSITAGYGASSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADALRRLglRLALLKDKPDLVIIELGTNDLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 107 GQ--PPQMIQKNLSQLIQ--LSQKQKAKVILFGMKIPPNYGTAYSKA---FENSYKTVSQKYQ----VKLLPFFLDGVAG 175
Cdd:cd00229   81 GGdtSIDEFKANLEELLDalRERAPGAKVILITPPPPPPREGLLGRAlprYNEAIKAVAAENPapsgVDLVDLAALLGDE 160

                        170       180
                 ....*....|....*....|
gi 488003447 176 QKQLMQNDLIHPNTQAQSKL 195
Cdd:cd00229  161 DKSLYSPDGIHPNPAGHKLI 180
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 29-188 1.33e-19

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid.


Pssm-ID: 239945  Cd Length: 183  Bit Score: 81.99  E-value: 1.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  29 ILILGDSISAGYGIDPKQGWVQLLQKRLDQQYpkqhkvVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRGQ 108
Cdd:cd04501    3 VVCLGDSITYGYPVGPEASWVNLLAEFLGKEV------INRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 109 PPQMIQKNLSQLIQLSQKQKAKVILfGMKIPPN-YGTA-YSKAFENSYKTVSQKY----QVKLLPF------FLDGVAGQ 176
Cdd:cd04501   77 SLEMIKDNIRSMVELAEANGIKVIL-ASPLPVDdYPWKpQWLRPANKLKSLNRWLkdyaRENGLLFldfyspLLDERNVG 155

                        170
                 ....*....|...
gi 488003447 177 -KQLMQNDLIHPN 188
Cdd:cd04501  156 lKPGLLTDGLHPS 168
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 29-204 3.44e-15

sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238866  Cd Length: 169  Bit Score: 70.00  E-value: 3.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  29 ILILGDSISAGYGidpkqgWVQLLQkrldqqypkQHKVVNASVSGETTSGALARLPKLLQTyKPEVVVIELGGNDGLRGQ 108
Cdd:cd01828    2 LVFLGDSLTEGGP------WALLFP---------DVKVANRGISGDTTRGLLARLDEDVAL-QPKAIFIMIGINDLAQGT 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 109 PPQMIQKNLSQLIQLSQKQKAKVILFGMKIPPnygTAYSKAFENS--------YKTVSQKYQVKLL---PFFLDGVAGQK 177
Cdd:cd01828   66 SDEDIVANYRTILEKLRKHFPNIKIVVQSILP---VGELKSIPNEqieelnrqLAQLAQQEGVTFLdlwAVFTNADGDLK 142

                        170       180
                 ....*....|....*....|....*..
gi 488003447 178 QLMQNDLIHPNTQAQSKLLNLAYPYIK 204
Cdd:cd01828  143 NEFTTDGLHLNAKGYAVWAAALQPYLA 169
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
29-195 5.34e-15

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 70.29  E-value: 5.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447   29 ILILGDSISAGYGIDP--KQGWVQLLQKRLDQQ--YPKQH--KVVNASVSGETTSGALARLPKLLQT-------YKPEVV 95
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPggRFSWGDLLADFLARKlgVPGSGynHGANFAIGGATIEDLPIQLEQLLRLisdvkdqAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447   96 VIELGGNDGLRGQ-PPQMIQKNLSQLIQL-------SQKQKAKVILFGMK---IPPNYG---------TAYSKAFENSYK 155
Cdd:pfam00657  81 TIFIGANDLCNFLsSPARSKKRVPDLLDElranlpqLGLGARKFWVHGLGplgCTPPKGcyelynalaEEYNERLNELVN 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 488003447  156 TVSQK---YQVKLLPF--FLDGV-AGQKQLMQNDLIHPNTQAQSKL 195
Cdd:pfam00657 161 SLAAAaedANVVYVDIygFEDPTdPCCGIGLEPDGLHPSEKGYKAV 206
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 29-140 2.81e-14

Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the Saccharomyces cerevisiae IAH1. IAH1 may be the major esterase that hydrolyses isoamyl acetate in sake mash. The SGNH-family of hydrolases is a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases


Pssm-ID: 238876  Cd Length: 199  Bit Score: 68.05  E-value: 2.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  29 ILILGDSISAGYGIDPKQGWVQLLQKRldqqYPKQHKVVNASVSGETTSGALARLPKLL---QTYKPEVVVIELGGNDGL 105
Cdd:cd01838    2 IVLFGDSITQFSFDQGEFGFGAALADV----YSRKLDVINRGFSGYNTRWALKVLPKIFleeKLAQPDLVTIFFGANDAA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488003447 106 RGQPPQMI-----QKNLSQLIQL--SQKQKAKVILFGmkiPP 140
Cdd:cd01838   78 LPGQPQHVpldeyKENLRKIVSHlkSLSPKTKVILIT---PP 116
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 27-198 1.33e-13

SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238873  Cd Length: 193  Bit Score: 66.21  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  27 KTILILGDSISAGYGiDPK-QGWVQllqkRLDQQYPKQHK---VVNASVSGETTSGALARL----PKLLQTYKPEVVVIE 98
Cdd:cd01835    2 KRLIVVGDSLVYGWG-DPEgGGWVG----RLRARWMNLGDdpvLYNLGVRGDGSEDVAARWraewSRRGELNVPNRLVLS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  99 LGGNDGLRGQPP------QMIQKNLSQLIQLSqKQKAKVILFGMkiPP------NYGTAYSKAFENSYKTVSQKYQVKLL 166
Cdd:cd01835   77 VGLNDTARGGRKrpqlsaRAFLFGLNQLLEEA-KRLVPVLVVGP--TPvdeakmPYSNRRIARLETAFAEVCLRRDVPFL 153

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 488003447 167 PFF---LDGVAGQKQLMQNDLIHPNTQAQSKLLNL 198
Cdd:cd01835  154 DTFtplLNHPQWRRELAATDGIHPNAAGYGWLAWL 188
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 28-140 1.30e-12

SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of a biosynthetic gene cluster and may participate in the biosynthesis of long-chain N-acyltyrosines by providing saturated and unsaturated fatty acids, which it turn are loaded onto the acyl carrier protein FeeL. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238874  Cd Length: 191  Bit Score: 63.44  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGYGID-PKQGWVQLLQKRLDQQYPKQHKVVNASVSGETTSGALARLPKLLQTyKPEVVVIELGGNDGLR 106
Cdd:cd01836    4 RLLVLGDSTAAGVGVEtQDQALAGQLARGLAAITGRGVRWRLFAKTGATSADLLRQLAPLPET-RFDVAVISIGVNDVTH 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488003447 107 GQPPQMIQKNLSQLIQ-LSQKQKAKVILFGmKIPP 140
Cdd:cd01836   83 LTSIARWRKQLAELVDaLRAKFPGARVVVT-AVPP 116
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
 28-172 2.24e-10

SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating enzyme) of A. tumefaciens. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238877  Cd Length: 208  Bit Score: 57.66  E-value: 2.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGY------GIDPKQGWVQLLQKRLDQQYpKQHKVVNASVSGETTSGA---------LARLPKLLQTYKP 92
Cdd:cd01839    1 TILCFGDSNTWGIipdtggRYPFEDRWPGVLEKALGANG-ENVRVIEDGLPGRTTVLDdpffpgrngLTYLPQALESHSP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  93 -EVVVIELGGNDGLR--GQPPQMIQKNLSQLIQLSQK-------QKAKVILF---GMKIPP-------NYGTAYSKAFEN 152
Cdd:cd01839   80 lDLVIIMLGTNDLKSyfNLSAAEIAQGLGALVDIIRTapiepgmPAPKILIVappPIRTPKgslagkfAGAEEKSKGLAD 159

                        170       180
                 ....*....|....*....|
gi 488003447 153 SYKTVSQKYQVkllpFFLDG 172
Cdd:cd01839  160 AYRALAEELGC----HFFDA 175
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 29-188 2.63e-10

SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238872  Cd Length: 191  Bit Score: 57.30  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  29 ILILGDSISAGygidpkQGWVQLLQKRLDQQYPKQH-KVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRG 107
Cdd:cd01834    4 IVFIGNSITDR------GGYVGYVETYLAARYPELKlTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDSFRG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 108 QP----PQMIQKNLSQLIQ--LSQKQKAKVILFgmkIPPNY------------GTAYSKAFENSYKTVSQKYQVKLLPFF 169
Cdd:cd01834   78 FDdpvgLEKFKTNLRRLIDrlKNKESAPRIVLV---SPIAYeanedplpdgaeYNANLAAYADAVRELAAENGVAFVDLF 154

                        170       180
                 ....*....|....*....|...
gi 488003447 170 --LDGV--AGQKQLMQNDLIHPN 188
Cdd:cd01834  155 tpMKEAfqKAGEAVLTVDGVHPN 177
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 29-192 2.30e-08

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.


Pssm-ID: 238870  Cd Length: 185  Bit Score: 51.89  E-value: 2.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  29 ILILGDSISAGYGIDPK----QGWVQLLQKRLDQQYPKQHkVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDG 104
Cdd:cd01832    2 YVALGDSITEGVGDPVPdggyRGWADRLAAALAAADPGIE-YANLAVRGRRTAQILAEQLPAALALRPDLVTLLAGGNDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 105 LR-GQPPQMIQKNLSQLIQLSQKQKAKVILFGMkipPNYG---------TAYSKAFENSYKTVSQKYQVKLLPFFLDGVA 174
Cdd:cd01832   81 LRpGTDPDTYRADLEEAVRRLRAAGARVVVFTI---PDPAvlepfrrrvRARLAAYNAVIRAVAARYGAVHVDLWEHPEF 157

                        170
                 ....*....|....*...
gi 488003447 175 GQKQLMQNDLIHPNTQAQ 192
Cdd:cd01832  158 ADPRLWASDRLHPSAAGH 175
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 28-136 2.73e-07

Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxlic acid. This subfamily contains sequences similar to Bacillus YpmR.


Pssm-ID: 239947  Cd Length: 204  Bit Score: 49.17  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGYGiDP--KQGWVQLLQKRLDQQYPKQHKVVNASVSGETTSGALARL---PKLLQTYKPEVVVIELGGN 102
Cdd:cd04506    1 KIVALGDSLTEGVG-DEtgKGGYVGRLDKLIETKTVKKVTVQNFGVSGDRSDQLLKRLktkKVQKELKKADVITITIGGN 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488003447 103 D---GLRG-----------QPPQMIQKNLSQLIQLSQKQ--KAKVILFGM 136
Cdd:cd04506   80 DlmqVLEKnflsldvedfkKAEETYQNNLKKIFKEIRKLnpDAPIFLVGL 129
SGNH_hydrolase_peri2 cd01829
SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 28-205 6.74e-07

SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238867  Cd Length: 200  Bit Score: 47.66  E-value: 6.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGygidpkqgwvqlLQKRLDQQYPKQH--KVVNASVSgetTSGaLAR---------LPKLLQTYKPEVVV 96
Cdd:cd01829    1 RVLVIGDSLAQG------------LAPGLLRALADNPgiRVINRSKG---SSG-LVRpdffdwpekLKELIAEEKPDVVV 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  97 IELGGNDGLRGQPPQMIQKNLSQ------------LIQLSQKQKAKVILFGMkiPPNYGTAYSK--AFENS-YKTVSQKY 161
Cdd:cd01829   65 VFLGANDRQDIRDGDGYLKFGSPeweeeyrqrideLLNVARAKGVPVIWVGL--PAMRSPKLSAdmVYLNSlYREEVAKA 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 488003447 162 QVKLL---PFFLDG----------VAGQK-QLMQNDLIHPNTQAQSKLLNLAYPYIKG 205
Cdd:cd01829  143 GGEFVdvwDGFVDEngrftysgtdVNGKKvRLRTNDGIHFTAAGGRKLAFYVEKLIRR 200
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 28-147 7.60e-07

SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238868  Cd Length: 204  Bit Score: 47.62  E-value: 7.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGYGIDPKQG--WVQLLQKRLDQQYPKQHK-VVNASVSGET--TSG----ALARLPK--LLQtykPEV-- 94
Cdd:cd01830    1 SVVALGDSITDGRGSTPDANnrWPDLLAARLAARAGTRGIaVLNAGIGGNRllADGlgpsALARFDRdvLSQ---PGVrt 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488003447  95 VVIELGGND-GLRGQPPQMIQKNLSQLI----QLSQKQKAK-VILFGMKIPPNYGTAYS 147
Cdd:cd01830   78 VIILEGVNDiGASGTDFAAAPVTAEELIagyrQLIRRAHARgIKVIGATITPFEGSGYY 136
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 29-203 5.93e-06

SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted hydrolase with xylanase activity. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238871  Cd Length: 157  Bit Score: 44.53  E-value: 5.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  29 ILILGDSISAGygidpkqgwvqllqkrlDQQypkqhkvvNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLRGQ 108
Cdd:cd01833    3 IMPLGDSITWG-----------------DKD--------HEGHSGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNR 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 109 PPQMIQKNLSQLIQ--LSQKQKAKVILfgMKIPPN---YGTAYSKAFENSYKTVSQKYQVKLLPFFL----DGVAGQKQL 179
Cdd:cd01833   58 DPDTAPDRLRALIDqmRAANPDVKIIV--ATLIPTtdaSGNARIAEYNAAIPGVVADLRTAGSPVVLvdmsTGYTTADDL 135

                        170       180
                 ....*....|....*....|....
gi 488003447 180 mqNDLIHPNTQAQSKLLNLAYPYI 203
Cdd:cd01833  136 --YDGLHPNDQGYKKMADAWYEAL 157
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 28-134 6.28e-06

Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan acetylesterase removes acetyl esters from rhamnogalacturonan substrates, and renders them susceptible to degradation by rhamnogalacturonases. Rhamnogalacturonans are highly branched regions in pectic polysaccharides, consisting of repeating -(1,2)-L-Rha-(1,4)-D-GalUA disaccharide units, with many rhamnose residues substituted by neutral oligosaccharides such as arabinans, galactans and arabinogalactans. Extracellular enzymes participating in the degradation of plant cell wall polymers, such as Rhamnogalacturonan acetylesterase, would typically be found in saprophytic and plant pathogenic fungi and bacteria.


Pssm-ID: 238859  Cd Length: 198  Bit Score: 44.90  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  28 TILILGDSISAGYGIDPKQ-GWVQLLQKRLDqqypKQHKVVNASVSGETTSGALA--RLPKLLQTYKPE-VVVIELGGND 103
Cdd:cd01821    2 TIFLAGDSTVADYDPGAPQaGWGQALPQYLD----TGITVVNHAKGGRSSRSFRDegRWDAILKLIKPGdYVLIQFGHND 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488003447 104 ----GLRGQPPQM-IQKNLSQLIQLSQKQKAKVILF 134
Cdd:cd01821   78 qkpkDPEYTEPYTtYKEYLRRYIAEARAKGATPILV 113
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 27-197 1.06e-04

NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases. E. coli NnaC appears to be involved in polysaccharide synthesis.


Pssm-ID: 238879  Cd Length: 174  Bit Score: 41.16  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  27 KTILILGDSISAGYGIdpkQGWVQllqkrldqqypKQHKVVNASVSGETTSGALARLPKLLQTYKPEVVVIELGGNDGLR 106
Cdd:cd01841    1 KNIVFIGDSLFEGWPL---YEAEG-----------KGKTVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGK 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 107 GQPPQMIQKNLSQLIQlSQKQKAKV-------ILFGMKIPPNYGTAYSKAFENS--YKTVSQKYQVK---LLPFFLDGVA 174
Cdd:cd01841   67 EVSSNQFIKWYRDIIE-QIREEFPNtkiyllsVLPVLEEDEIKTRSNTRIQRLNdaIKELAPELGVTfidLNDVLVDEFG 145

                        170       180
                 ....*....|....*....|...
gi 488003447 175 GQKQLMQNDLIHPNTQAQSKLLN 197
Cdd:cd01841  146 NLKKEYTTDGLHFNPKGYQKLLE 168
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 32-188 5.94e-04

sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.


Pssm-ID: 238865  Cd Length: 188  Bit Score: 39.35  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  32 LGDSISAGYGIDPKQGWVQLLQKRLDQQYpkqhKVVNASVSGETTSGALARlP-------KLLQTYKPEVVVIELGGNDG 104
Cdd:cd01827    6 VGNSITEGAGLRAYDSYPSPLAQMLGDGY----EVGNFGKSARTVLNKGDH-PymneeryKNALAFNPNIVIIKLGTNDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447 105 LRGQP--PQMIQKNLSQLIQLSQKQKAKVILFGMKIPPNYGTAY--------SKAFENSYKTVSQKYQVKLLPFF--LDG 172
Cdd:cd01827   81 KPQNWkyKDDFKKDYETMIDSFQALPSKPKIYICYPIPAYYGDGgfindniiKKEIQPMIDKIAKKLNLKLIDLHtpLKG 160

                        170
                 ....*....|....*.
gi 488003447 173 vagqKQLMQNDLIHPN 188
Cdd:cd01827  161 ----KPELVPDWVHPN 172
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 32-103 2.31e-03

SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST), a causal agent of the potato scab disease, which hydrolyzes a specific ester bond in suberin, a plant lipid. The tertiary fold of this enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles two of the three components of typical Ser-His-Asp(Glu) triad from other serine hydrolases, but may lack the carboxylic acid.


Pssm-ID: 238861  Cd Length: 259  Bit Score: 37.82  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488003447  32 LGDSISAGYGIDP------------KQGWVQLLQKRLDQqypKQHKVVNASVSGETTSGALARL--------PKLLQTyk 91
Cdd:cd01823    6 LGDSYAAGPGAGPlddgpddgcrrsSNSYPTLLARALGD---ETLSFTDVACSGATTTDGIEPQqggiapqaGALDPD-- 80

                         90
                 ....*....|..
gi 488003447  92 PEVVVIELGGND 103
Cdd:cd01823   81 TDLVTITIGGND 92
 
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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