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Conserved domains on  [gi|1447699315|ref|NP_308585|]
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acyl-CoA thioesterase I [Escherichia coli O157:H7 str. Sakai]

Protein Classification

arylesterase( domain architecture ID 10793407)

lysophospholipase A is an arylesterase.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10528 PRK10528
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
 7-197 2.66e-139

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


:

Pssm-ID: 182521  Cd Length: 191  Bit Score: 386.43  E-value: 2.66e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315   7 VLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELG 86
Cdd:PRK10528    1 VLLTFRAAAADTLLILGDSLSAGYRMPASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  87 GNDGLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFLMEEVYLKPQWM 166
Cdd:PRK10528   81 GNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFFMEEVYLKPQWM 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699315 167 QDDGIHPNRDAQPFIADWMAKQLQPLVNHDS 197
Cdd:PRK10528  161 QDDGIHPNRDAQPFIADWMAKQLQPLVNHDS 191
 
Name Accession Description Interval E-value
PRK10528 PRK10528
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
 7-197 2.66e-139

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


Pssm-ID: 182521  Cd Length: 191  Bit Score: 386.43  E-value: 2.66e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315   7 VLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELG 86
Cdd:PRK10528    1 VLLTFRAAAADTLLILGDSLSAGYRMPASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  87 GNDGLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFLMEEVYLKPQWM 166
Cdd:PRK10528   81 GNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFFMEEVYLKPQWM 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699315 167 QDDGIHPNRDAQPFIADWMAKQLQPLVNHDS 197
Cdd:PRK10528  161 QDDGIHPNRDAQPFIADWMAKQLQPLVNHDS 191
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 17-190 1.25e-93

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: 270.54  E-value: 1.25e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  17 DTLLILGDSLSAGYRMSASAAWPALLNDKWQSK---TSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRG 93
Cdd:cd01822     1 VTILALGDSLTAGYGLPPEEGWPALLQKRLDARgidVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  94 FQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFLMEEVYLKPQWMQDDGIHP 173
Cdd:cd01822    81 IPPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHP 160

                         170
                  ....*....|....*..
gi 1447699315 174 NRDAQPFIADWMAKQLQ 190
Cdd:cd01822   161 NAEGQPIIAENVWPALE 177
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 10-189 2.34e-51

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: 163.66  E-value: 2.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  10 TFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKT-SVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGN 88
Cdd:COG2755     2 KAAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAADvRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  89 DGLRGFQ--PQQTEQTLRQILQDVKAAN--AEPLLMQI--RLPANYGRRYNEAFSAIYPKLAKEFDVPLLPF--LMEEVY 160
Cdd:COG2755    82 DLLRGLGvsPEEFRANLEALIDRLRAAGpgARVVLVTPppRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLyaALRDAG 161

                         170       180
                  ....*....|....*....|....*....
gi 1447699315 161 LKPQWMQDDGIHPNRDAQPFIADWMAKQL 189
Cdd:COG2755   162 DLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 21-174 5.73e-30

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: 108.40  E-value: 5.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  21 ILGDSLSAGYR-MSASAAWPALLNDKWQSKTS---VVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQP 96
Cdd:pfam13472   1 ALGDSITAGYGaTGGDRSYPGWLARLLARRLGadvVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  97 QQTEQTLRQILQDVKAANAEPLLMQI---------RLPANYGRRYNEAFSAIYPKLAKEFDVPLLPF---LMEEVYLKPQ 164
Cdd:pfam13472  81 ARAAANLEALIDALRAAGPDARVLLIgplpvgpppPLDERRLNARIAEYNAAIREVAAERGVPYVDLwdaLRDDGGWLPD 160

                         170
                  ....*....|
gi 1447699315 165 WMQDDGIHPN 174
Cdd:pfam13472 161 LLADDGLHPN 170
 
Name Accession Description Interval E-value
PRK10528 PRK10528
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
 7-197 2.66e-139

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


Pssm-ID: 182521  Cd Length: 191  Bit Score: 386.43  E-value: 2.66e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315   7 VLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELG 86
Cdd:PRK10528    1 VLLTFRAAAADTLLILGDSLSAGYRMPASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  87 GNDGLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFLMEEVYLKPQWM 166
Cdd:PRK10528   81 GNDGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFFMEEVYLKPQWM 160

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699315 167 QDDGIHPNRDAQPFIADWMAKQLQPLVNHDS 197
Cdd:PRK10528  161 QDDGIHPNRDAQPFIADWMAKQLQPLVNHDS 191
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 17-190 1.25e-93

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: 270.54  E-value: 1.25e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  17 DTLLILGDSLSAGYRMSASAAWPALLNDKWQSK---TSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRG 93
Cdd:cd01822     1 VTILALGDSLTAGYGLPPEEGWPALLQKRLDARgidVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  94 FQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFLMEEVYLKPQWMQDDGIHP 173
Cdd:cd01822    81 IPPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHP 160

                         170
                  ....*....|....*..
gi 1447699315 174 NRDAQPFIADWMAKQLQ 190
Cdd:cd01822   161 NAEGQPIIAENVWPALE 177
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 10-189 2.34e-51

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: 163.66  E-value: 2.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  10 TFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKT-SVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGN 88
Cdd:COG2755     2 KAAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAADvRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGTN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  89 DGLRGFQ--PQQTEQTLRQILQDVKAAN--AEPLLMQI--RLPANYGRRYNEAFSAIYPKLAKEFDVPLLPF--LMEEVY 160
Cdd:COG2755    82 DLLRGLGvsPEEFRANLEALIDRLRAAGpgARVVLVTPppRLRPNYLNERIEAYNAAIRELAAEYGVPLVDLyaALRDAG 161

                         170       180
                  ....*....|....*....|....*....
gi 1447699315 161 LKPQWMQDDGIHPNRDAQPFIADWMAKQL 189
Cdd:COG2755   162 DLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 21-174 5.73e-30

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: 108.40  E-value: 5.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  21 ILGDSLSAGYR-MSASAAWPALLNDKWQSKTS---VVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQP 96
Cdd:pfam13472   1 ALGDSITAGYGaTGGDRSYPGWLARLLARRLGadvVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  97 QQTEQTLRQILQDVKAANAEPLLMQI---------RLPANYGRRYNEAFSAIYPKLAKEFDVPLLPF---LMEEVYLKPQ 164
Cdd:pfam13472  81 ARAAANLEALIDALRAAGPDARVLLIgplpvgpppPLDERRLNARIAEYNAAIREVAAERGVPYVDLwdaLRDDGGWLPD 160

                         170
                  ....*....|
gi 1447699315 165 WMQDDGIHPN 174
Cdd:pfam13472 161 LLADDGLHPN 170
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 19-188 5.67e-26

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: 98.64  E-value: 5.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  19 LLILGDSLSAGYRMSASAAWPALLNDKWQSKT----SVVNASISGDTSQQGLARL--PALLKQHQPRWVLVELGGNDGLR 92
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLLYLLLLAGgpgvEVINLGVSGATTADALRRLglRLALLKDKPDLVIIELGTNDLGR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  93 GFQ--PQQTEQTLRQILQDVK--AANAEPLLM-------QIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFLMEEVYL 161
Cdd:cd00229    81 GGDtsIDEFKANLEELLDALRerAPGAKVILItppppppREGLLGRALPRYNEAIKAVAAENPAPSGVDLVDLAALLGDE 160

                         170       180
                  ....*....|....*....|....*..
gi 1447699315 162 KPQWMQDDGIHPNRDAQPFIADWMAKQ 188
Cdd:cd00229   161 DKSLYSPDGIHPNPAGHKLIAEALASA 187
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
19-185 7.32e-23

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 91.10  E-value: 7.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  19 LLILGDSLSAGYRMSASA--AWPALLNDKWQSK--------TSVVNASISGDTSQ---QGLARLPAL----LKQHQPRWV 81
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGGrfSWGDLLADFLARKlgvpgsgyNHGANFAIGGATIEdlpIQLEQLLRLisdvKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  82 LVELGGNDGLRGF-QPQQTEQTLRQILQDVKAA--------------NAEPLLMQIRLPANY-----GRRYNEAFSAIYP 141
Cdd:pfam00657  81 TIFIGANDLCNFLsSPARSKKRVPDLLDELRANlpqlglgarkfwvhGLGPLGCTPPKGCYElynalAEEYNERLNELVN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1447699315 142 KLAKE---FDVPLLPF--LMEEVYLKPQWMQD-DGIHPNRDAQPFIADWM 185
Cdd:pfam00657 161 SLAAAaedANVVYVDIygFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 22-189 5.76e-17

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: 74.67  E-value: 5.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  22 LGDSLSAGYRMSASAAWPALLNDKwqSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQ 101
Cdd:cd04501     6 LGDSITYGYPVGPEASWVNLLAEF--LGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNTSLEMIKD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315 102 TLRQILQDVKAANAEPLLMqIRLPAN------YGRRYNEA---FSAIYPKLAKEFDVPLLPF---LMEE--VYLKPQwMQ 167
Cdd:cd04501    84 NIRSMVELAEANGIKVILA-SPLPVDdypwkpQWLRPANKlksLNRWLKDYARENGLLFLDFyspLLDErnVGLKPG-LL 161

                         170       180
                  ....*....|....*....|..
gi 1447699315 168 DDGIHPNRDAQPFIADWMAKQL 189
Cdd:cd04501   162 TDGLHPSREGYRVMAPLAEKAL 183
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 19-182 1.11e-14

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: 68.46  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  19 LLILGDSLSAGyrmsasAAWPALLNDKwqsktSVVNASISGDTSQQGLARLPALLKQhQPRWVLVELGGNDGLRGFQPQQ 98
Cdd:cd01828     2 LVFLGDSLTEG------GPWALLFPDV-----KVANRGISGDTTRGLLARLDEDVAL-QPKAIFIMIGINDLAQGTSDED 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  99 TEQTLRQILQDVKAANAE-PLLMQIRLP-ANYGRRYNEAFSAI---YPKLAKEFDVPLL---PFLMEEVYLKPQWMQDDG 170
Cdd:cd01828    70 IVANYRTILEKLRKHFPNiKIVVQSILPvGELKSIPNEQIEELnrqLAQLAQQEGVTFLdlwAVFTNADGDLKNEFTTDG 149

                         170       180
                  ....*....|....*....|
gi 1447699315 171 IHPNRDA--------QPFIA 182
Cdd:cd01828   150 LHLNAKGyavwaaalQPYLA 169
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 17-188 1.32e-12

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: 63.47  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  17 DTLLILGDSL--SAGYRMSASAAWPALLNDKwqsKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGF 94
Cdd:cd01834     2 DRIVFIGNSItdRGGYVGYVETYLAARYPEL---KLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDSFRGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  95 ----QPQQTEQTLRQILQDV--KAANAEPLLM------QIRLPANYGRRYN---EAFSAIYPKLAKEFDVPLLPF--LME 157
Cdd:cd01834    79 ddpvGLEKFKTNLRRLIDRLknKESAPRIVLVspiayeANEDPLPDGAEYNanlAAYADAVRELAAENGVAFVDLftPMK 158

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1447699315 158 EVYLKPQWMQ--DDGIHPNRDAQPFIADWMAKQ 188
Cdd:cd01834   159 EAFQKAGEAVltVDGVHPNEAGHRALARLWLEA 191
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 19-172 1.96e-10

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: 57.65  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  19 LLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQH---QPRWVLVELGGNDGLRGFQ 95
Cdd:cd01838     2 IVLFGDSITQFSFDQGEFGFGAALADVYSRKLDVINRGFSGYNTRWALKVLPKIFLEEklaQPDLVTIFFGANDAALPGQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  96 PQ-----QTEQTLRQILQDVKAANAEPLL---------------MQIRLPANYGRR------YNEAFSaiypKLAKEFDV 149
Cdd:cd01838    82 PQhvpldEYKENLRKIVSHLKSLSPKTKVilitpppvdeeawekSLEDGGSQPGRTnellkqYAEACV----EVAEELGV 157

                         170       180
                  ....*....|....*....|....*
gi 1447699315 150 PLLPF--LMEEVYLKPQWMQDDGIH 172
Cdd:cd01838   158 PVIDLwtAMQEEAGWLESLLTDGLH 182
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
 18-117 3.63e-07

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: 48.42  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  18 TLLILGDSLSAGY------RMSASAAWPALLND-------KWQ-------SKTSVVNASISGDTSqqGLARLPALLKQHQ 77
Cdd:cd01839     1 TILCFGDSNTWGIipdtggRYPFEDRWPGVLEKalgangeNVRviedglpGRTTVLDDPFFPGRN--GLTYLPQALESHS 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1447699315  78 PR-WVLVELGGNDGLRGFQ--PQQTEQTLRQILQDVKAANAEP 117
Cdd:cd01839    79 PLdLVIIMLGTNDLKSYFNlsAAEIAQGLGALVDIIRTAPIEP 121
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 18-183 3.76e-07

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: 48.49  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  18 TLLILGDSLSAGYRMSASAAWPALLNDKWQSKTS---VVNASISGDTSQQGLARLPAL----LKQHQPRWVLVELGGNDG 90
Cdd:cd01835     3 RLIVVGDSLVYGWGDPEGGGWVGRLRARWMNLGDdpvLYNLGVRGDGSEDVAARWRAEwsrrGELNVPNRLVLSVGLNDT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  91 LRGFQ--PQQTEQTLRQILQ--DVKAANAEPLLMqIRLPANY--GRRYNEAFSAIYPKL----AKEFDVPLLPfLMEEVY 160
Cdd:cd01835    83 ARGGRkrPQLSARAFLFGLNqlLEEAKRLVPVLV-VGPTPVDeaKMPYSNRRIARLETAfaevCLRRDVPFLD-TFTPLL 160

                         170       180
                  ....*....|....*....|....*..
gi 1447699315 161 LKPQWMQD----DGIHPNRDAQPFIAD 183
Cdd:cd01835   161 NHPQWRRElaatDGIHPNAAGYGWLAW 187
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 20-183 1.38e-06

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: 46.49  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  20 LILGDSLSAGYRMSASAA----WPALLNDKWQSKTSVV---NASISGDTSQQGLAR-LPALLKqHQPRWVLVELGGNDGL 91
Cdd:cd01832     3 VALGDSITEGVGDPVPDGgyrgWADRLAAALAAADPGIeyaNLAVRGRRTAQILAEqLPAALA-LRPDLVTLLAGGNDIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  92 R-GFQPQQTEQTLRQILQDVKAANAEPLLMQI-------RLPANYGRRYnEAFSAIYPKLAKEFDVPLLPFLMEEVYLKP 163
Cdd:cd01832    82 RpGTDPDTYRADLEEAVRRLRAAGARVVVFTIpdpavlePFRRRVRARL-AAYNAVIRAVAARYGAVHVDLWEHPEFADP 160

                         170       180
                  ....*....|....*....|
gi 1447699315 164 QWMQDDGIHPNRDAQPFIAD 183
Cdd:cd01832   161 RLWASDRLHPSAAGHARLAA 180
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 18-152 1.40e-05

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: 43.74  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  18 TLLILGDSLSA-GYRMSASAAW----PALLNDKWQsktsVVNASISGDTSQ--QGLARLPALLKQHQPR-WVLVELGGND 89
Cdd:cd01821     2 TIFLAGDSTVAdYDPGAPQAGWgqalPQYLDTGIT----VVNHAKGGRSSRsfRDEGRWDAILKLIKPGdYVLIQFGHND 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699315  90 ----GLRGFQPQQTEQT-LRQILQDVKAANAEPLLM--QIRLPANYGRRYNEAFSAiYPK----LAKEFDVPLL 152
Cdd:cd01821    78 qkpkDPEYTEPYTTYKEyLRRYIAEARAKGATPILVtpVTRRTFDEGGKVEDTLGD-YPAamreLAAEEGVPLI 150
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 18-114 2.21e-05

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: 43.38  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  18 TLLILGDSLSAGYRMSASA--AWPALLNDKWQ-----SKTSVVNASISGDTSQQ------GLARLPA-LLKQHQPRWVLV 83
Cdd:cd01830     1 SVVALGDSITDGRGSTPDAnnRWPDLLAARLAaragtRGIAVLNAGIGGNRLLAdglgpsALARFDRdVLSQPGVRTVII 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1447699315  84 ELGGND----GLRGFQPQQTEQTL----RQILQDVKAAN 114
Cdd:cd01830    81 LEGVNDigasGTDFAAAPVTAEELiagyRQLIRRAHARG 119
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 54-183 3.00e-05

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: 42.61  E-value: 3.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  54 NASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAAN--AEPLLMQI--RLPANYG 129
Cdd:cd01833    17 HEGHSGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNRDPDTAPDRLRALIDQMRAANpdVKIIVATLipTTDASGN 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699315 130 RRYNEaFSAIYPKLAKEFDVPLLPFL---MEEVYLKPQwMQDDGIHPNRDAQPFIAD 183
Cdd:cd01833    97 ARIAE-YNAAIPGVVADLRTAGSPVVlvdMSTGYTTAD-DLYDGLHPNDQGYKKMAD 151
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 18-116 1.59e-04

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: 40.69  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  18 TLLILGDSLSAGY----------RMSAsaawpALLNDKWQSKTSVVNASISGDTSQQGLARlpalLKQHQPRW------- 80
Cdd:cd04506     1 KIVALGDSLTEGVgdetgkggyvGRLD-----KLIETKTVKKVTVQNFGVSGDRSDQLLKR----LKTKKVQKelkkadv 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1447699315  81 VLVELGGND---GLRGF----------QPQQTEQT-LRQILQDVKAANAE 116
Cdd:cd04506    72 ITITIGGNDlmqVLEKNflsldvedfkKAEETYQNnLKKIFKEIRKLNPD 121
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 15-189 1.74e-04

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: 40.71  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  15 AADTLLILGDSLSAGYRMS----ASAAWPA-LLNDKWQSKTSVVNASISGDTSQQGLARLpALLKQHQPRWVLVELGGND 89
Cdd:cd01836     1 PPLRLLVLGDSTAAGVGVEtqdqALAGQLArGLAAITGRGVRWRLFAKTGATSADLLRQL-APLPETRFDVAVISIGVND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  90 GLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLP----------------ANYGRRYNEAFSAIypkLAKEFDVPLLP 153
Cdd:cd01836    80 VTHLTSIARWRKQLAELVDALRAKFPGARVVVTAVPplgrfpalpqplrwllGRRARLLNRALERL---ASEAPRVTLLP 156

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1447699315 154 FLMeevYLKPQWMQDDGIHPNRDAQPFIADWMAKQL 189
Cdd:cd01836   157 ATG---PLFPALFASDGFHPSAAGYAVWAEALAPAI 189
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 17-177 6.29e-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: 38.85  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  17 DTLLIlGDSLSAGYrmsasAAWPALLNDKwqsktSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQP 96
Cdd:cd01841     2 NIVFI-GDSLFEGW-----PLYEAEGKGK-----TVNNLGIAGISSRQYLEHIEPQLIQKNPSKVFLFLGTNDIGKEVSS 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  97 QQTEQTLRQILQDVKAANAeplLMQIRLPANYGR---------------RYNEAFSAIYPKLAKEFdVPLLPFLMEEVYL 161
Cdd:cd01841    71 NQFIKWYRDIIEQIREEFP---NTKIYLLSVLPVleedeiktrsntriqRLNDAIKELAPELGVTF-IDLNDVLVDEFGN 146

                         170
                  ....*....|....*.
gi 1447699315 162 KPQWMQDDGIHPNRDA 177
Cdd:cd01841   147 LKKEYTTDGLHFNPKG 162
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 19-192 8.06e-04

PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor (PAF) and PAF-AH are key players in inflammation and in atherosclerosis. PAF-AH is a calcium independent phospholipase A2 which exhibits strong substrate specificity towards PAF, hydrolyzing an acetyl ester at the sn-2 position. PAF-AH also degrades a family of oxidized PAF-like phospholipids with short sn-2 residues. In addition, PAF and PAF-AH are associated with neural migration and mammalian reproduction.


Pssm-ID: 238858  Cd Length: 214  Bit Score: 38.81  E-value: 8.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  19 LLILGDSLSAGYRMSASAAWpallnDKWQSKTSVVNASISGDTSQQGLARLpallkQH------QPRWVLVELGGNDGLR 92
Cdd:cd01820    35 VVFIGDSITQNWEFTGLEVW-----RELYAPLHALNFGIGGDRTQNVLWRL-----ENgeldgvNPKVVVLLIGTNNIGH 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699315  93 GFQPQQTEQTLRQILQDV--KAANAEPLLMQIrLPA----NYGRRYNEAFSAIYP-KLAKEFDVPLLP----FLMEEVYL 161
Cdd:cd01820   105 TTTAEEIAEGILAIVEEIreKLPNAKILLLGL-LPRgqnpNPLRERNAQVNRLLAvRYDGLPNVTFLDidkgFVQSDGTI 183

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1447699315 162 KPQWMQdDGIHPNRDAQPFIADWMAKQLQPL 192
Cdd:cd01820   184 SHHDMP-DYLHLTAAGYRKWADALHPTLARL 213
 
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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