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Conserved domains on  [gi|515524685|ref|WP_016957939|]
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GDSL-type esterase/lipase family protein [Catenovulum agarivorans]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 85)

SGNH/GDSL hydrolase family protein is a hydrolytic enzyme such as an esterase or lipase; may have multifunctional properties including broad substrate specificity and regiospecificity; similar to plant GDSL esterase/lipase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SGNH_hydrolase super family cl01053
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 192-403 9.14e-17

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.


The actual alignment was detected with superfamily member cd04501:

Pssm-ID: 470049  Cd Length: 183  Bit Score: 78.52  E-value: 9.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 192 VVGIGDSIMQG--RTALNSRLMQngvknynpsqqsqsgqisyeVQQAFNVPFLNQGIGGQRTDEIWARWSRDVLAEvyda 269
Cdd:cd04501    3 VVCLGDSITYGypVGPEASWVNL--------------------LAEFLGKEVINRGINGDTTSQMLVRFYEDVIAL---- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 270 gdglgsetlqfnrqKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSCRANNIVCIVNNIGPATDHDATKQAKSRQ---- 345
Cdd:cd04501   59 --------------KPAVVIIMGGTNDIIVNTSLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWLRPAnklk 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515524685 346 -VNNWLNNYLKKKypEIYVIDF---MYWASNGTNNPItlkpnMFADELHPNRDGYRDFSKYV 403
Cdd:cd04501  125 sLNRWLKDYAREN--GLLFLDFyspLLDERNVGLKPG-----LLTDGLHPSREGYRVMAPLA 179
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 192-403 9.14e-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: 78.52  E-value: 9.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 192 VVGIGDSIMQG--RTALNSRLMQngvknynpsqqsqsgqisyeVQQAFNVPFLNQGIGGQRTDEIWARWSRDVLAEvyda 269
Cdd:cd04501    3 VVCLGDSITYGypVGPEASWVNL--------------------LAEFLGKEVINRGINGDTTSQMLVRFYEDVIAL---- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 270 gdglgsetlqfnrqKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSCRANNIVCIVNNIGPATDHDATKQAKSRQ---- 345
Cdd:cd04501   59 --------------KPAVVIIMGGTNDIIVNTSLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWLRPAnklk 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515524685 346 -VNNWLNNYLKKKypEIYVIDF---MYWASNGTNNPItlkpnMFADELHPNRDGYRDFSKYV 403
Cdd:cd04501  125 sLNRWLKDYAREN--GLLFLDFyspLLDERNVGLKPG-----LLTDGLHPSREGYRVMAPLA 179
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 192-405 1.14e-15

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: 75.45  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 192 VVGIGDSIMQGRTALNSR----LMQNGVknynpsqqsqsgqisyevqQAFNVPFLNQGIGGQRTDEIWARWSRDVLAEVY 267
Cdd:COG2755   11 IVALGDSITAGYGASRERgwpaLLARRL-------------------AAADVRVVNAGISGATTADLLARLDRDLLALKP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 268 DagdglgsetlqfnrqkpfAVWIHAGVNDIRQGYDVS--HIATNLENMAQSCRANNIVCIVNNIGPATDHDATK-QAKSR 344
Cdd:COG2755   72 D------------------LVVIELGTNDLLRGLGVSpeEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYlNERIE 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515524685 345 QVNNWLNNYLKKKypEIYVIDFMYWasngTNNPITLKPNMFADELHPNRDGYRDFSKYVFE 405
Cdd:COG2755  134 AYNAAIRELAAEY--GVPLVDLYAA----LRDAGDLPDLLTADGLHPNAAGYRLIAEAVLP 188
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 195-397 5.40e-15

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: 73.35  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685  195 IGDSIMQGRTALNSrlmQNGVKNYNPSQqsqsgqisyeVQQAFNVPF-LNQGIGGQRTDEIWARWSRDVLaevydagdgl 273
Cdd:pfam13472   2 LGDSITAGYGATGG---DRSYPGWLARL----------LARRLGADVvNNLGISGATTRLDLLERLDDVL---------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685  274 gsetlqfnRQKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSCRANNIVCIVNNIG--PATDHDATKQAKSRQVNNWLN 351
Cdd:pfam13472  59 --------RLKPDLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLIGplPVGPPPPLDERRLNARIAEYN 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 515524685  352 NYLKK--KYPEIYVIDFMYWASNGTNNpitLKPNMFADELHPNRDGYR 397
Cdd:pfam13472 131 AAIREvaAERGVPYVDLWDALRDDGGW---LPDLLADDGLHPNAAGYR 175
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 192-403 9.14e-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: 78.52  E-value: 9.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 192 VVGIGDSIMQG--RTALNSRLMQngvknynpsqqsqsgqisyeVQQAFNVPFLNQGIGGQRTDEIWARWSRDVLAEvyda 269
Cdd:cd04501    3 VVCLGDSITYGypVGPEASWVNL--------------------LAEFLGKEVINRGINGDTTSQMLVRFYEDVIAL---- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 270 gdglgsetlqfnrqKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSCRANNIVCIVNNIGPATDHDATKQAKSRQ---- 345
Cdd:cd04501   59 --------------KPAVVIIMGGTNDIIVNTSLEMIKDNIRSMVELAEANGIKVILASPLPVDDYPWKPQWLRPAnklk 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515524685 346 -VNNWLNNYLKKKypEIYVIDF---MYWASNGTNNPItlkpnMFADELHPNRDGYRDFSKYV 403
Cdd:cd04501  125 sLNRWLKDYAREN--GLLFLDFyspLLDERNVGLKPG-----LLTDGLHPSREGYRVMAPLA 179
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 192-405 1.14e-15

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: 75.45  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 192 VVGIGDSIMQGRTALNSR----LMQNGVknynpsqqsqsgqisyevqQAFNVPFLNQGIGGQRTDEIWARWSRDVLAEVY 267
Cdd:COG2755   11 IVALGDSITAGYGASRERgwpaLLARRL-------------------AAADVRVVNAGISGATTADLLARLDRDLLALKP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 268 DagdglgsetlqfnrqkpfAVWIHAGVNDIRQGYDVS--HIATNLENMAQSCRANNIVCIVNNIGPATDHDATK-QAKSR 344
Cdd:COG2755   72 D------------------LVVIELGTNDLLRGLGVSpeEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNYlNERIE 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515524685 345 QVNNWLNNYLKKKypEIYVIDFMYWasngTNNPITLKPNMFADELHPNRDGYRDFSKYVFE 405
Cdd:COG2755  134 AYNAAIRELAAEY--GVPLVDLYAA----LRDAGDLPDLLTADGLHPNAAGYRLIAEAVLP 188
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 195-397 5.40e-15

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: 73.35  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685  195 IGDSIMQGRTALNSrlmQNGVKNYNPSQqsqsgqisyeVQQAFNVPF-LNQGIGGQRTDEIWARWSRDVLaevydagdgl 273
Cdd:pfam13472   2 LGDSITAGYGATGG---DRSYPGWLARL----------LARRLGADVvNNLGISGATTRLDLLERLDDVL---------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685  274 gsetlqfnRQKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSCRANNIVCIVNNIG--PATDHDATKQAKSRQVNNWLN 351
Cdd:pfam13472  59 --------RLKPDLVVILLGTNDLGRGVSAARAAANLEALIDALRAAGPDARVLLIGplPVGPPPPLDERRLNARIAEYN 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 515524685  352 NYLKK--KYPEIYVIDFMYWASNGTNNpitLKPNMFADELHPNRDGYR 397
Cdd:pfam13472 131 AAIREvaAERGVPYVDLWDALRDDGGW---LPDLLADDGLHPNAAGYR 175
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 192-405 1.78e-10

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: 60.50  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 192 VVGIGDSIMQGRTAlnsrlmqngvknYNPSQQSQSGQISYEVQQAFNVPFLNQGIGGQRTDEIWARWSRDVLAEVYDAGd 271
Cdd:cd00229    1 ILVIGDSITAGYGA------------SSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTADALRRLGLRLALLKDKPD- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 272 glgsetlqfnrqkpfAVWIHAGVNDIRQGYDVS--HIATNLENMAQSCR--ANNIVCIVNNIGPATDHDATKQAKSRQVN 347
Cdd:cd00229   68 ---------------LVIIELGTNDLGRGGDTSidEFKANLEELLDALRerAPGAKVILITPPPPPPREGLLGRALPRYN 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 515524685 348 NWLNNyLKKKYPEIYVIDFMYWASNGTNNPitlKPNMFADELHPNRDGYRDFSKYVFE 405
Cdd:cd00229  133 EAIKA-VAAENPAPSGVDLVDLAALLGDED---KSLYSPDGIHPNPAGHKLIAEALAS 186
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 238-397 3.63e-10

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: 59.22  E-value: 3.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 238 NVPFLNQGIGGQRTDEIWARWSRDVLAevydagdglgsetlqfnrqKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSC 317
Cdd:cd01828   21 DVKVANRGISGDTTRGLLARLDEDVAL-------------------QPKAIFIMIGINDLAQGTSDEDIVANYRTILEKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 318 RA--NNIVCIVNNIGPATDHDATKQAKSRQVNNWLNNYLKKKypEIYVIDFMYWASNGTNNpitLKPNMFADELHPNRDG 395
Cdd:cd01828   82 RKhfPNIKIVVQSILPVGELKSIPNEQIEELNRQLAQLAQQE--GVTFLDLWAVFTNADGD---LKNEFTTDGLHLNAKG 156


                 ..
gi 515524685 396 YR 397
Cdd:cd01828  157 YA 158
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 243-405 7.14e-07

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: 49.16  E-value: 7.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 243 NQGIGGQRTDEIwARWSRDVLAEvydagdglgsetlqfnrQKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSCRANN- 321
Cdd:cd01833   17 HEGHSGYLIDQI-AAAAADWVLA-----------------AKPDVVLLHLGTNDLVLNRDPDTAPDRLRALIDQMRAANp 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 322 -IVCIVNNIGPATdhDATKQAKSRQVNNWLNNYLKKKY---PEIYVIDFMywasngtnnPITLKPNMFADELHPNRDGYR 397
Cdd:cd01833   79 dVKIIVATLIPTT--DASGNARIAEYNAAIPGVVADLRtagSPVVLVDMS---------TGYTTADDLYDGLHPNDQGYK 147


                 ....*...
gi 515524685 398 DFSKYVFE 405
Cdd:cd01833  148 KMADAWYE 155
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 192-397 1.15e-04

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: 43.77  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 192 VVGIGDSIMQGRTA-----------LNSRLMQNGVKNynpsqqsqsgqisyevqqafNVPFLNQGIGGQR--TDEI---- 254
Cdd:cd01830    2 VVALGDSITDGRGStpdannrwpdlLAARLAARAGTR--------------------GIAVLNAGIGGNRllADGLgpsa 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 255 WARWSRDVLAevydagdglgsetlqfnRQKPFAVWIHAGVNDIRQG----YDVSHIATNLEN----MAQSCRANNIVCIV 326
Cdd:cd01830   62 LARFDRDVLS-----------------QPGVRTVIILEGVNDIGASgtdfAAAPVTAEELIAgyrqLIRRAHARGIKVIG 124

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515524685 327 NNIGP---ATDHDATKQAKSRQVNNWLNNylkkkyPEIY--VIDFMYwASNGTNNPITLKPNM-FADELHPNRDGYR 397
Cdd:cd01830  125 ATITPfegSGYYTPAREATRQAVNEWIRT------SGAFdaVVDFDA-ALRDPADPSRLRPAYdSGDHLHPNDAGYQ 194
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 238-402 2.28e-04

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: 42.67  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 238 NVPFLNQGIGGQRTDEIWARWSRDVLAevydagdglgsetlqfnrQKPFAVWIHAGVNDIRQGYDVSHIATNLEN----- 312
Cdd:cd01834   33 KLTFRNLGWSGDTVSDLAARRDRDVLP------------------AKPDVVSIMFGINDSFRGFDDPVGLEKFKTnlrrl 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 313 MAQSCRANNIVCIVNNIGPATDHDATKQAKSRQVNNWLNNY------LKKKYpEIYVIDFmYWASNGTNnpITLKPNMFA 386
Cdd:cd01834   95 IDRLKNKESAPRIVLVSPIAYEANEDPLPDGAEYNANLAAYadavreLAAEN-GVAFVDL-FTPMKEAF--QKAGEAVLT 170

                        170
                 ....*....|....*..
gi 515524685 387 -DELHPNRDGYRDFSKY 402
Cdd:cd01834  171 vDGVHPNEAGHRALARL 187
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 232-406 3.55e-03

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: 39.15  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 232 EVQQAFNVPFLNQGIGGQRTDEIWARwsrdvlaevydagdgLGSETLQFNRQKPFAVWIHAGVNDIRQG-------YDVS 304
Cdd:cd04506   31 ETKTVKKVTVQNFGVSGDRSDQLLKR---------------LKTKKVQKELKKADVITITIGGNDLMQVleknflsLDVE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 305 HIA-------TNLENMAQSCRANN----IVcIVNNIGPATDHDATKQAKSRQVNNWlNNYLKK---KYPEIYVIDFMYWA 370
Cdd:cd04506   96 DFKkaeetyqNNLKKIFKEIRKLNpdapIF-LVGLYNPFYVYFPNITEINDIVNDW-NEASQKlasQYKNAYFVPIFDLF 173

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 515524685 371 SNGTNNPItlkpnMFADELHPNRDGYRDFSKYVFEN 406
Cdd:cd04506  174 SDGQNKYL-----LTSDHFHPNDKGYQLIADRVFKA 204
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
192-403 3.74e-03

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 39.09  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685  192 VVGIGDSIMQGRtalnsrLMQNGVKNYNPSQQSQSGQISYEVQQAFNVPFLNQGIGGQRTDEIWARwSRDVLAEVYDAGD 271
Cdd:pfam00657   1 IVAFGDSLTDGG------GDGPGGRFSWGDLLADFLARKLGVPGSGYNHGANFAIGGATIEDLPIQ-LEQLLRLISDVKD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685  272 GLgsetlqfnrqKPFAVWIHAGVNDIRQGY-----DVSHIATNLENMAQSCRANNIVC---IVNNIGP----------AT 333
Cdd:pfam00657  74 QA----------KPDLVTIFIGANDLCNFLssparSKKRVPDLLDELRANLPQLGLGArkfWVHGLGPlgctppkgcyEL 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515524685  334 DHDATKQAKSRqVNNWLNnYLKKKYPE--IYVIDFmywasNGTNNPITLKPNMF--ADELHPNRDGYRDFSKYV 403
Cdd:pfam00657 144 YNALAEEYNER-LNELVN-SLAAAAEDanVVYVDI-----YGFEDPTDPCCGIGlePDGLHPSEKGYKAVAEAI 210
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 283-403 7.17e-03

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: 37.69  E-value: 7.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515524685 283 QKPFAVWIHAGVNDIRQGYDVSHIATNLENMAQSCRANNIVCIVN--NIGPATDHDATKQAKSRQVNNWlNNYLKKKYPE 360
Cdd:cd01841   50 KNPSKVFLFLGTNDIGKEVSSNQFIKWYRDIIEQIREEFPNTKIYllSVLPVLEEDEIKTRSNTRIQRL-NDAIKELAPE 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 515524685 361 IYVIdFMYWASNGTNNPITLKPNMFADELHPNRDGYRDFSKYV 403
Cdd:cd01841  129 LGVT-FIDLNDVLVDEFGNLKKEYTTDGLHFNPKGYQKLLEIL 170
 
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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