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Conserved domains on  [gi|515637308|ref|WP_017069908|]
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MULTISPECIES: arylesterase [Vibrio]

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 ...
 29-203 1.93e-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: 270.15  E-value: 1.93e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGANDGLRGF 108
Cdd:cd01822    2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGIDVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 109 PPKLMSANLEQIIEQIKAAGAKPIMMQIKIPPNYGKRYNQQFEYVFAALADQQNVPLLPFFLEHIILKPEWMMNDGLHPK 188
Cdd:cd01822   82 PPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHPN 161

                        170
                 ....*....|....*
gi 515637308 189 PEAQPWIAEFVAEEL 203
Cdd:cd01822  162 AEGQPIIAENVWPAL 176
 
Name Accession Description Interval E-value
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 29-203 1.93e-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: 270.15  E-value: 1.93e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGANDGLRGF 108
Cdd:cd01822    2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGIDVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 109 PPKLMSANLEQIIEQIKAAGAKPIMMQIKIPPNYGKRYNQQFEYVFAALADQQNVPLLPFFLEHIILKPEWMMNDGLHPK 188
Cdd:cd01822   82 PPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHPN 161

                        170
                 ....*....|....*
gi 515637308 189 PEAQPWIAEFVAEEL 203
Cdd:cd01822  162 AEGQPIIAENVWPAL 176
PRK10528 PRK10528
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
 23-207 2.47e-84

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


Pssm-ID: 182521  Cd Length: 191  Bit Score: 247.75  E-value: 2.47e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  23 ASAQDSkLLVLGDSLSAGYNMDIKQSWPSLLPDalaKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGAN 102
Cdd:PRK10528   7 AAAADT-LLILGDSLSAGYRMPASAAWPALLND---KWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 103 DGLRGFPPKLMSANLEQIIEQIKAAGAKPIMMQIKIPPNYGKRYNQQFEYVFAALADQQNVPLLPFFLEHIILKPEWMMN 182
Cdd:PRK10528  83 DGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFFMEEVYLKPQWMQD 162

                        170       180
                 ....*....|....*....|....*
gi 515637308 183 DGLHPKPEAQPWIAEFVAEELYQYL 207
Cdd:PRK10528 163 DGIHPNRDAQPFIADWMAKQLQPLV 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 22-203 2.47e-52

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: 166.74  E-value: 2.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  22 SASAQDSKLLVLGDSLSAGYNMDIKQSWPSLLPDALAKHDkaVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGA 101
Cdd:COG2755    3 AAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAAD--VRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 102 NDGLRGF--PPKLMSANLEQIIEQIKAAG--AKPIMMQIK--IPPNYGKRYNQQFEYVFAALADQQNVPLLPFF--LEHI 173
Cdd:COG2755   81 NDLLRGLgvSPEEFRANLEALIDRLRAAGpgARVVLVTPPprLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYaaLRDA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515637308 174 ILKPEWMMNDGLHPKPEAQPWIAEFVAEEL 203
Cdd:COG2755  161 GDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 32-190 6.38e-33

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: 116.49  E-value: 6.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308   32 VLGDSLSAGYN-MDIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGANDGLRGFPP 110
Cdd:pfam13472   1 ALGDSITAGYGaTGGDRSYPGWLARLLARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  111 KLMSANLEQIIEQIKAAGAKPIMMQIKIPP---------NYGKRYNQQFEYVFAALADQQNVPLLPF---FLEHIILKPE 178
Cdd:pfam13472  81 ARAAANLEALIDALRAAGPDARVLLIGPLPvgppppldeRRLNARIAEYNAAIREVAAERGVPYVDLwdaLRDDGGWLPD 160

                         170
                  ....*....|..
gi 515637308  179 WMMNDGLHPKPE 190
Cdd:pfam13472 161 LLADDGLHPNAA 172
 
Name Accession Description Interval E-value
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 29-203 1.93e-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: 270.15  E-value: 1.93e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGANDGLRGF 108
Cdd:cd01822    2 TILALGDSLTAGYGLPPEEGWPALLQKRLDARGIDVTVINAGVSGDTTAGGLARLPALLAQHKPDLVILELGGNDGLRGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 109 PPKLMSANLEQIIEQIKAAGAKPIMMQIKIPPNYGKRYNQQFEYVFAALADQQNVPLLPFFLEHIILKPEWMMNDGLHPK 188
Cdd:cd01822   82 PPDQTRANLRQMIETAQARGAPVLLVGMQAPPNYGPRYTRRFAAIYPELAEEYGVPLVPFFLEGVAGDPELMQSDGIHPN 161

                        170
                 ....*....|....*
gi 515637308 189 PEAQPWIAEFVAEEL 203
Cdd:cd01822  162 AEGQPIIAENVWPAL 176
PRK10528 PRK10528
multifunctional acyl-CoA thioesterase I and protease I and lysophospholipase L1; Provisional
 23-207 2.47e-84

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


Pssm-ID: 182521  Cd Length: 191  Bit Score: 247.75  E-value: 2.47e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  23 ASAQDSkLLVLGDSLSAGYNMDIKQSWPSLLPDalaKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGAN 102
Cdd:PRK10528   7 AAAADT-LLILGDSLSAGYRMPASAAWPALLND---KWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 103 DGLRGFPPKLMSANLEQIIEQIKAAGAKPIMMQIKIPPNYGKRYNQQFEYVFAALADQQNVPLLPFFLEHIILKPEWMMN 182
Cdd:PRK10528  83 DGLRGFPPQQTEQTLRQIIQDVKAANAQPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDIPLLPFFMEEVYLKPQWMQD 162

                        170       180
                 ....*....|....*....|....*
gi 515637308 183 DGLHPKPEAQPWIAEFVAEELYQYL 207
Cdd:PRK10528 163 DGIHPNRDAQPFIADWMAKQLQPLV 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 22-203 2.47e-52

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: 166.74  E-value: 2.47e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  22 SASAQDSKLLVLGDSLSAGYNMDIKQSWPSLLPDALAKHDkaVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGA 101
Cdd:COG2755    3 AAAGKPLRIVALGDSITAGYGASRERGWPALLARRLAAAD--VRVVNAGISGATTADLLARLDRDLLALKPDLVVIELGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 102 NDGLRGF--PPKLMSANLEQIIEQIKAAG--AKPIMMQIK--IPPNYGKRYNQQFEYVFAALADQQNVPLLPFF--LEHI 173
Cdd:COG2755   81 NDLLRGLgvSPEEFRANLEALIDRLRAAGpgARVVLVTPPprLRPNYLNERIEAYNAAIRELAAEYGVPLVDLYaaLRDA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 515637308 174 ILKPEWMMNDGLHPKPEAQPWIAEFVAEEL 203
Cdd:COG2755  161 GDLPDLLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 32-190 6.38e-33

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: 116.49  E-value: 6.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308   32 VLGDSLSAGYN-MDIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGANDGLRGFPP 110
Cdd:pfam13472   1 ALGDSITAGYGaTGGDRSYPGWLARLLARRLGADVVNNLGISGATTRLDLLERLDDVLRLKPDLVVILLGTNDLGRGVSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  111 KLMSANLEQIIEQIKAAGAKPIMMQIKIPP---------NYGKRYNQQFEYVFAALADQQNVPLLPF---FLEHIILKPE 178
Cdd:pfam13472  81 ARAAANLEALIDALRAAGPDARVLLIGPLPvgppppldeRRLNARIAEYNAAIREVAAERGVPYVDLwdaLRDDGGWLPD 160

                         170
                  ....*....|..
gi 515637308  179 WMMNDGLHPKPE 190
Cdd:pfam13472 161 LLADDGLHPNAA 172
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 30-201 1.62e-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: 100.18  E-value: 1.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  30 LLVLGDSLSAGYNM-DIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLARL--PQLLEEHAPDTVLIELGANDGLR 106
Cdd:cd00229    1 ILVIGDSITAGYGAsSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADALRRLglRLALLKDKPDLVIIELGTNDLGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 107 GF--PPKLMSANLEQIIEQIK--AAGAKPIMM-------QIKIPPNYGKRYNQQFEYVFAALADQQNVPLLPFFLEHIIL 175
Cdd:cd00229   81 GGdtSIDEFKANLEELLDALRerAPGAKVILItppppppREGLLGRALPRYNEAIKAVAAENPAPSGVDLVDLAALLGDE 160

                        170       180
                 ....*....|....*....|....*.
gi 515637308 176 KPEWMMNDGLHPKPEAQPWIAEFVAE 201
Cdd:cd00229  161 DKSLYSPDGIHPNPAGHKLIAEALAS 186
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
30-199 2.14e-25

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 98.03  E-value: 2.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308   30 LLVLGDSLSAGYNMD--IKQSWPSLLPDALAKH-----DKAVTVVNGSISGDTTGNGLARLPQLLE-------EHAPDTV 95
Cdd:pfam00657   1 IVAFGDSLTDGGGDGpgGRFSWGDLLADFLARKlgvpgSGYNHGANFAIGGATIEDLPIQLEQLLRlisdvkdQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308   96 LIELGANDGLRGF------------PPKLMSANLEQI---IEQIKAAGAKPIMMQIKIPPNY-----GKRYNQQFEYVFA 155
Cdd:pfam00657  81 TIFIGANDLCNFLssparskkrvpdLLDELRANLPQLglgARKFWVHGLGPLGCTPPKGCYElynalAEEYNERLNELVN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 515637308  156 ALADQQ---NVPLLPF--FLEHIILKPEWMMN-DGLHPKPEAQPWIAEFV 199
Cdd:pfam00657 161 SLAAAAedaNVVYVDIygFEDPTDPCCGIGLEpDGLHPSEKGYKAVAEAI 210
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 30-197 1.41e-19

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: 81.56  E-value: 1.41e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  30 LLVLGDSLSAGYnmdikqSWPSLLPDalakhdkaVTVVNGSISGDTTGNGLARLPQLLEEHaPDTVLIELGANDGLRGFP 109
Cdd:cd01828    2 LVFLGDSLTEGG------PWALLFPD--------VKVANRGISGDTTRGLLARLDEDVALQ-PKAIFIMIGINDLAQGTS 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 110 PKLMSANLEQIIEQIKAAGAK-PIMMQiKIPPNYGK--RYNQQFEYV---FAALADQQNVPLL----PFFLEHIILKPEW 179
Cdd:cd01828   67 DEDIVANYRTILEKLRKHFPNiKIVVQ-SILPVGELksIPNEQIEELnrqLAQLAQQEGVTFLdlwaVFTNADGDLKNEF 145

                        170
                 ....*....|....*....
gi 515637308 180 mMNDGLHPKPEA-QPWIAE 197
Cdd:cd01828  146 -TTDGLHLNAKGyAVWAAA 163
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
 29-203 8.77e-18

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: 77.69  E-value: 8.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYN------MDIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTG---------NGLARLPQLLEEHAP- 92
Cdd:cd01839    1 TILCFGDSNTWGIIpdtggrYPFEDRWPGVLEKALGANGENVRVIEDGLPGRTTVlddpffpgrNGLTYLPQALESHSPl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  93 DTVLIELGANDGLRGF--PPKLMSANLEQIIEQIKAAGAKPIMMQIKI----PP-------------NYGKRYNQQFEYV 153
Cdd:cd01839   81 DLVIIMLGTNDLKSYFnlSAAEIAQGLGALVDIIRTAPIEPGMPAPKIlivaPPpirtpkgslagkfAGAEEKSKGLADA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515637308 154 FAALADQQNVpllPFFLEHIILKPEWMmnDGLHPKPEAQPWIAEFVAEEL 203
Cdd:cd01839  161 YRALAEELGC---HFFDAGSVGSTSPV--DGVHLDADQHAALGQALASVI 205
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 29-203 7.14e-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: 7.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQSWPSLLpdalaKHDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGANDGLRGF 108
Cdd:cd04501    2 RVVCLGDSITYGYPVGPEASWVNLL-----AEFLGKEVINRGINGDTTSQMLVRFYEDVIALKPAVVIIMGGTNDIIVNT 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 109 PPKLMSANLEQIIEQIKAAGAKPIM------------MQIKIPPNYGKRYNQQFEyvfaALADQQNVPLLPFFLEHIILK 176
Cdd:cd04501   77 SLEMIKDNIRSMVELAEANGIKVILasplpvddypwkPQWLRPANKLKSLNRWLK----DYARENGLLFLDFYSPLLDER 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 515637308 177 PEWM----MNDGLHPKPEAQPWIAEFVAEEL 203
Cdd:cd04501  153 NVGLkpglLTDGLHPSREGYRVMAPLAEKAL 183
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 31-200 1.30e-16

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: 74.23  E-value: 1.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  31 LVLGDSLSAGYNMDIK----QSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLAR-LPQLLEeHAPDTVLIELGANDGL 105
Cdd:cd01832    3 VALGDSITEGVGDPVPdggyRGWADRLAAALAAADPGIEYANLAVRGRRTAQILAEqLPAALA-LRPDLVTLLAGGNDIL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 106 R-GFPPKLMSANLEQIIEQIKAAGAKPIMMQIkipPNYG-------------KRYNQqfeyVFAALADQQNVPLLPFFLE 171
Cdd:cd01832   82 RpGTDPDTYRADLEEAVRRLRAAGARVVVFTI---PDPAvlepfrrrvrarlAAYNA----VIRAVAARYGAVHVDLWEH 154

                        170       180
                 ....*....|....*....|....*....
gi 515637308 172 HIILKPEWMMNDGLHPKPEAQPWIAEFVA 200
Cdd:cd01832  155 PEFADPRLWASDRLHPSAAGHARLAALVL 183
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 27-201 5.63e-16

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: 72.71  E-value: 5.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  27 DSKLLVLGDSLSAGynmdikQSWPSLLPDALAK--HDKAVTVVNGSISGDTTGNGLARLPQLLEEHAPDTVLIELGANDG 104
Cdd:cd01834    1 GDRIVFIGNSITDR------GGYVGYVETYLAAryPELKLTFRNLGWSGDTVSDLAARRDRDVLPAKPDVVSIMFGINDS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 105 LRGFP----PKLMSANLEQIIEQI--KAAGAKPIMM------QIKIPPNYGKRYN---QQFEYVFAALADQQNVPLLPFF 169
Cdd:cd01834   75 FRGFDdpvgLEKFKTNLRRLIDRLknKESAPRIVLVspiayeANEDPLPDGAEYNanlAAYADAVRELAAENGVAFVDLF 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515637308 170 ---LEH-IILKPEWMMNDGLHPKPEAQPWIAEFVAE 201
Cdd:cd01834  155 tpmKEAfQKAGEAVLTVDGVHPNEAGHRALARLWLE 190
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 29-203 1.09e-11

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: 61.13  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMD-IKQSWPSLLPDALAK-HDKAVTVVNGSISGDTTGNGLARLPQLLEEHaPDTVLIELGANDGLR 106
Cdd:cd01836    4 RLLVLGDSTAAGVGVEtQDQALAGQLARGLAAiTGRGVRWRLFAKTGATSADLLRQLAPLPETR-FDVAVISIGVNDVTH 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 107 GFPPKLMSANLEQIIEQIKAA-GAKPIMmQIKIPP----------------NYGKRYNQQFEyvfAALADQQNVPLLPFf 169
Cdd:cd01836   83 LTSIARWRKQLAELVDALRAKfPGARVV-VTAVPPlgrfpalpqplrwllgRRARLLNRALE---RLASEAPRVTLLPA- 157

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515637308 170 leHIILKPEWMMNDGLHPKPEAQPWIAEFVAEEL 203
Cdd:cd01836  158 --TGPLFPALFASDGFHPSAAGYAVWAEALAPAI 189
SGNH_hydrolase_like_3 cd01835
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 27-199 6.34e-11

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: 58.89  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  27 DSKLLVLGDSLSAGYNMDIKQSWPS-LLPDALAKHDkAVTVVNGSISGDTTGNGLARLPQL----LEEHAPDTVLIELGA 101
Cdd:cd01835    1 PKRLIVVGDSLVYGWGDPEGGGWVGrLRARWMNLGD-DPVLYNLGVRGDGSEDVAARWRAEwsrrGELNVPNRLVLSVGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 102 NDGLRGFPPKLMSAN------LEQIIEQIKAAgaKPIMMqIKIPPNY----------GKRYNQQFEYVFAaladQQNVPL 165
Cdd:cd01835   80 NDTARGGRKRPQLSAraflfgLNQLLEEAKRL--VPVLV-VGPTPVDeakmpysnrrIARLETAFAEVCL----RRDVPF 152

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 515637308 166 LPFF---LEHIILKPEWMMNDGLHPKPEAQPWIAEFV 199
Cdd:cd01835  153 LDTFtplLNHPQWRRELAATDGIHPNAAGYGWLAWLV 189
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 29-203 8.63e-11

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: 58.76  E-value: 8.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQS-WPSLLPDALakhDKAVTVVNGSISGDTT----GNGlaRLPQLLEEHAP-DTVLIELGAN 102
Cdd:cd01821    2 TIFLAGDSTVADYDPGAPQAgWGQALPQYL---DTGITVVNHAKGGRSSrsfrDEG--RWDAILKLIKPgDYVLIQFGHN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 103 DGLRGFPPKLMS-----ANLEQIIEQIKAAGAKPIMMQikiP------PNYGKRYNQQFEYVFAA--LADQQNVPLLPff 169
Cdd:cd01821   77 DQKPKDPEYTEPyttykEYLRRYIAEARAKGATPILVT---PvtrrtfDEGGKVEDTLGDYPAAMreLAAEEGVPLID-- 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 515637308 170 LEHIILK------PE-------WMMNDGLHPKPEAQPWIAEFVAEEL 203
Cdd:cd01821  152 LNAASRAlyeaigPEkskkyfpEGPGDNTHFSEKGADVVARLVAEEL 198
Isoamyl_acetate_hydrolase_like cd01838
Isoamyl-acetate hydrolyzing esterase-like proteins. SGNH_hydrolase subfamily similar to the ...
 29-203 9.32e-11

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: 58.80  E-value: 9.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQSWPSLLPDALAKhdkAVTVVNGSISGDTTGNGLARLPQLLEEHA---PDTVLIELGANDGL 105
Cdd:cd01838    1 KIVLFGDSITQFSFDQGEFGFGAALADVYSR---KLDVINRGFSGYNTRWALKVLPKIFLEEKlaqPDLVTIFFGANDAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 106 -----RGFPPKLMSANLEQIIEQIKAA--GAKPIMM------QIKIPPNYGKRYNQQF-------EYVFAA--LADQQNV 163
Cdd:cd01838   78 lpgqpQHVPLDEYKENLRKIVSHLKSLspKTKVILItpppvdEEAWEKSLEDGGSQPGrtnellkQYAEACveVAEELGV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 515637308 164 PLLPF---FLEHIILKPEwMMNDGLHPKPEAQpwiaEFVAEEL 203
Cdd:cd01838  158 PVIDLwtaMQEEAGWLES-LLTDGLHFSSKGY----ELLFEEI 195
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 30-136 1.06e-06

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: 47.24  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  30 LLVLGDSL--SAGYNMDIKQSWPSLLPDALAKH--DKAVTVVNGSISG-----DTTG-NGLARLPQ-LLEEHAPDTVLIE 98
Cdd:cd01830    2 VVALGDSItdGRGSTPDANNRWPDLLAARLAARagTRGIAVLNAGIGGnrllaDGLGpSALARFDRdVLSQPGVRTVIIL 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515637308  99 LGAND---GLRGFPPKLMSAN-----LEQIIEQIKAAGAKPIMMQI 136
Cdd:cd01830   82 EGVNDigaSGTDFAAAPVTAEeliagYRQLIRRAHARGIKVIGATI 127
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 65-203 1.52e-06

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: 46.55  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  65 TVVNGSISGDTTGNGLARL-PQLLEEhAPDTVLIELGANDGLRGFPPKLMSANLEQIIEQIKaagAKPIMMQIKIPPNYG 143
Cdd:cd01841   25 TVNNLGIAGISSRQYLEHIePQLIQK-NPSKVFLFLGTNDIGKEVSSNQFIKWYRDIIEQIR---EEFPNTKIYLLSVLP 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515637308 144 ---------------KRYNQQFEYvfaaLADQQNV---PLLPFFLEHIILKPEWMMNDGLHPKPEAQPWIAEFVAEEL 203
Cdd:cd01841  101 vleedeiktrsntriQRLNDAIKE----LAPELGVtfiDLNDVLVDEFGNLKKEYTTDGLHFNPKGYQKLLEILEEYL 174
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 72-201 4.90e-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: 41.84  E-value: 4.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  72 SGDTTGNGLARLPQLLEEHAPDTVLIELGANDGLRGFPPKLMSANLEQIIEQIKAA--GAKPIMMQIkIP------PNYG 143
Cdd:cd01833   21 SGYLIDQIAAAAADWVLAAKPDVVLLHLGTNDLVLNRDPDTAPDRLRALIDQMRAAnpDVKIIVATL-IPttdasgNARI 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515637308 144 KRYNQQFEYVFAALADQQ-NVPLLPFfleHIILKPEWMMNDGLHPKPEAQPWIAEFVAE 201
Cdd:cd01833  100 AEYNAAIPGVVADLRTAGsPVVLVDM---STGYTTADDLYDGLHPNDQGYKKMADAWYE 155
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 29-124 2.05e-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: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQSWPSLLPDAL--AKHDKAVTVVNGSISGDTTGNGLARL---PQLLEEHAPDTVLIELGAND 103
Cdd:cd04506    1 KIVALGDSLTEGVGDETGKGGYVGRLDKLieTKTVKKVTVQNFGVSGDRSDQLLKRLktkKVQKELKKADVITITIGGND 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515637308 104 ---GLRGFPPKLMSA-----------NLEQIIEQI 124
Cdd:cd04506   81 lmqVLEKNFLSLDVEdfkkaeetyqnNLKKIFKEI 115
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 29-142 3.27e-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: 40.12  E-value: 3.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYNMDIKQSWPSLLPDALAKhdkAVTVVNGSISGDTTGNGLARlPQLLEE-------HAPDTVLIELGA 101
Cdd:cd01827    2 KVACVGNSITEGAGLRAYDSYPSPLAQMLGD---GYEVGNFGKSARTVLNKGDH-PYMNEEryknalaFNPNIVIIKLGT 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515637308 102 NDGlRGFPPKLMS---ANLEQIIEQIKAAGAKPIMMQIKIPPNY 142
Cdd:cd01827   78 NDA-KPQNWKYKDdfkKDYETMIDSFQALPSKPKIYICYPIPAY 120
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 32-153 3.42e-04

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: 40.51  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  32 VLGDSLSAGYN----MDI--------KQSWPSLLPDALAkhDKAVTVVNGSISGDTTGNGL----ARLPQLLEEHAPDT- 94
Cdd:cd01823    5 ALGDSYAAGPGagplDDGpddgcrrsSNSYPTLLARALG--DETLSFTDVACSGATTTDGIepqqGGIAPQAGALDPDTd 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  95 -VLIELGANDglRGFPPKLMSANLEQIIEQIKAAGAKPIMMQIKIPPNYGKRYNQQFEYV 153
Cdd:cd01823   83 lVTITIGGND--LGFADVVKACILTGGGSSLAQEKGAADGARDAALDEVGARLKAVLDRI 140
SGNH_hydrolase_peri2 cd01829
SGNH_peri2; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 29-104 3.77e-04

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: 39.95  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  29 KLLVLGDSLSAGYnmdikqsWPSLLpDALAKHDkAVTVVNGSIsGDTtgnGLAR---------LPQLLEEHAPDTVLIEL 99
Cdd:cd01829    1 RVLVIGDSLAQGL-------APGLL-RALADNP-GIRVINRSK-GSS---GLVRpdffdwpekLKELIAEEKPDVVVVFL 67


                 ....*
gi 515637308 100 GANDG 104
Cdd:cd01829   68 GANDR 72
PAF_acetylesterase_like cd01820
PAF_acetylhydrolase (PAF-AH)_like subfamily of SGNH-hydrolases. Platelet-activating factor ...
 23-207 8.23e-03

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: 36.11  E-value: 8.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308  23 ASAQDSKLLVLGDSlsagynmdIKQSWPSLLPDALAKHDKAVTVVNGSISGDTTGNGLARLPQ-LLEEHAPDTVLIELGA 101
Cdd:cd01820   28 AKQKEPDVVFIGDS--------ITQNWEFTGLEVWRELYAPLHALNFGIGGDRTQNVLWRLENgELDGVNPKVVVLLIGT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515637308 102 NDGLRGFPPKLMSANLEQIIEQI--KAAGAKPIMMQI----KIPPNYGKRYNQQFEYVFAALADQQNVPLL---PFFLEH 172
Cdd:cd01820  100 NNIGHTTTAEEIAEGILAIVEEIreKLPNAKILLLGLlprgQNPNPLRERNAQVNRLLAVRYDGLPNVTFLdidKGFVQS 179

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515637308 173 ---IILKPewmMNDGLHPKPEAQPWIAEFVAEELYQYL 207
Cdd:cd01820  180 dgtISHHD---MPDYLHLTAAGYRKWADALHPTLARLL 214
 
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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