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Conserved domains on  [gi|1581212577|gb|TAR44738|]
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SGNH/GDSL hydrolase family protein [Lactiplantibacillus plantarum]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
130-322 1.99e-22

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: 92.48  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 130 IGVIGDSVAATAGGFPDI-----------LAHQYNIYVENLSVGGAKMSDYDNNAIVNQASRLKQCDVVIIQGTDDDwvh 198
Cdd:cd00229     1 ILVIGDSITAGYGASSGStfyslllylllLAGGPGVEVINLGVSGATTADALRRLGLRLALLKDKPDLVIIELGTND--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 199 disLGYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCTRQCVGINREYRTEKSKNALgltlidYMEAQKKYLNQQNV 278
Cdd:cd00229    78 ---LGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEA------IKAVAAENPAPSGV 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1581212577 279 PYVDLmkptsiFEPDNPAFKKTMMHDGLHPTPEAHQYIVQEIAK 322
Cdd:cd00229   149 DLVDL------AALLGDEDKSLYSPDGIHPNPAGHKLIAEALAS 186
Periplasmic_Binding_Protein_type1 super family cl10011
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
28-158 4.79e-03

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


The actual alignment was detected with superfamily member cd06322:

Pssm-ID: 471960 [Multi-domain]  Cd Length: 270  Bit Score: 38.03  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577  28 REKQYGIDVREAMAQTAEAiAGVQSTAKKFNQDTKNQVNQLDEKYTREIRAIVLGDTTSVAV-PTIQEPNsEAGNPLPNL 106
Cdd:cd06322     9 LQHPFFVDIKDAMKKEAAE-LGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIvPAIEAAN-EAGIPVFTV 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1581212577 107 Y---------------ETARGQVLYDFVKQSSLTKANKIGVIGD----SVAATAGGFPDILAHQYNIYVEN 158
Cdd:cd06322    87 DvkadgakvvthvgtdNYAGGKLAGEYALKALLGGGGKIAIIDYpeveSVVLRVNGFKEAIKKYPNIEIVA 157
 
Name Accession Description Interval E-value
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
130-322 1.99e-22

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: 92.48  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 130 IGVIGDSVAATAGGFPDI-----------LAHQYNIYVENLSVGGAKMSDYDNNAIVNQASRLKQCDVVIIQGTDDDwvh 198
Cdd:cd00229     1 ILVIGDSITAGYGASSGStfyslllylllLAGGPGVEVINLGVSGATTADALRRLGLRLALLKDKPDLVIIELGTND--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 199 disLGYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCTRQCVGINREYRTEKSKNALgltlidYMEAQKKYLNQQNV 278
Cdd:cd00229    78 ---LGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEA------IKAVAAENPAPSGV 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1581212577 279 PYVDLmkptsiFEPDNPAFKKTMMHDGLHPTPEAHQYIVQEIAK 322
Cdd:cd00229   149 DLVDL------AALLGDEDKSLYSPDGIHPNPAGHKLIAEALAS 186
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
126-322 2.01e-20

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: 87.01  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 126 KANKIGVIGDSVAA-----TAGGFPDILA---HQYNIYVENLSVGGAKMSDYdnnaivnqASRLKQC------DVVIIQ- 190
Cdd:COG2755     7 KPLRIVALGDSITAgygasRERGWPALLArrlAAADVRVVNAGISGATTADL--------LARLDRDllalkpDLVVIEl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 191 GTDDdwvhdisLGYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCT-RQCVGINREYRTEksknalgltlidYMEAQ 269
Cdd:COG2755    79 GTND-------LLRGLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPpRLRPNYLNERIEA------------YNAAI 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1581212577 270 KKYLNQQNVPYVDLMKPTSifepDNPAFKKTMMHDGLHPTPEAHQYIVQEIAK 322
Cdd:COG2755   140 RELAAEYGVPLVDLYAALR----DAGDLPDLLTADGLHPNAAGYRLIAEAVLP 188
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
132-314 8.32e-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: 71.42  E-value: 8.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 132 VIGDSVAA------TAGGFPDILAHQY-----NIYVENLSVGGAKmSDYDNNAIVNQASRLKQcDVVIIQ-GTDDdwvhd 199
Cdd:pfam13472   1 ALGDSITAgygatgGDRSYPGWLARLLarrlgADVVNNLGISGAT-TRLDLLERLDDVLRLKP-DLVVILlGTND----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 200 islgYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCTRQCVGINREYRTEKSKNAlgltliDYMEAQKKYLNQQNVP 279
Cdd:pfam13472  74 ----LGRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLDERRLNARIA------EYNAAIREVAAERGVP 143
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1581212577 280 YVDLmkpTSIFEPDNPAFKKTMMHDGLHPTPEAHQ 314
Cdd:pfam13472 144 YVDL---WDALRDDGGWLPDLLADDGLHPNAAGYR 175
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
28-158 4.79e-03

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 38.03  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577  28 REKQYGIDVREAMAQTAEAiAGVQSTAKKFNQDTKNQVNQLDEKYTREIRAIVLGDTTSVAV-PTIQEPNsEAGNPLPNL 106
Cdd:cd06322     9 LQHPFFVDIKDAMKKEAAE-LGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIvPAIEAAN-EAGIPVFTV 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1581212577 107 Y---------------ETARGQVLYDFVKQSSLTKANKIGVIGD----SVAATAGGFPDILAHQYNIYVEN 158
Cdd:cd06322    87 DvkadgakvvthvgtdNYAGGKLAGEYALKALLGGGGKIAIIDYpeveSVVLRVNGFKEAIKKYPNIEIVA 157
 
Name Accession Description Interval E-value
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
130-322 1.99e-22

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: 92.48  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 130 IGVIGDSVAATAGGFPDI-----------LAHQYNIYVENLSVGGAKMSDYDNNAIVNQASRLKQCDVVIIQGTDDDwvh 198
Cdd:cd00229     1 ILVIGDSITAGYGASSGStfyslllylllLAGGPGVEVINLGVSGATTADALRRLGLRLALLKDKPDLVIIELGTND--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 199 disLGYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCTRQCVGINREYRTEKSKNALgltlidYMEAQKKYLNQQNV 278
Cdd:cd00229    78 ---LGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYNEA------IKAVAAENPAPSGV 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1581212577 279 PYVDLmkptsiFEPDNPAFKKTMMHDGLHPTPEAHQYIVQEIAK 322
Cdd:cd00229   149 DLVDL------AALLGDEDKSLYSPDGIHPNPAGHKLIAEALAS 186
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
126-322 2.01e-20

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: 87.01  E-value: 2.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 126 KANKIGVIGDSVAA-----TAGGFPDILA---HQYNIYVENLSVGGAKMSDYdnnaivnqASRLKQC------DVVIIQ- 190
Cdd:COG2755     7 KPLRIVALGDSITAgygasRERGWPALLArrlAAADVRVVNAGISGATTADL--------LARLDRDllalkpDLVVIEl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 191 GTDDdwvhdisLGYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCT-RQCVGINREYRTEksknalgltlidYMEAQ 269
Cdd:COG2755    79 GTND-------LLRGLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPpRLRPNYLNERIEA------------YNAAI 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1581212577 270 KKYLNQQNVPYVDLMKPTSifepDNPAFKKTMMHDGLHPTPEAHQYIVQEIAK 322
Cdd:COG2755   140 RELAAEYGVPLVDLYAALR----DAGDLPDLLTADGLHPNAAGYRLIAEAVLP 188
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
132-314 8.32e-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: 71.42  E-value: 8.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 132 VIGDSVAA------TAGGFPDILAHQY-----NIYVENLSVGGAKmSDYDNNAIVNQASRLKQcDVVIIQ-GTDDdwvhd 199
Cdd:pfam13472   1 ALGDSITAgygatgGDRSYPGWLARLLarrlgADVVNNLGISGAT-TRLDLLERLDDVLRLKP-DLVVILlGTND----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 200 islgYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCTRQCVGINREYRTEKSKNAlgltliDYMEAQKKYLNQQNVP 279
Cdd:pfam13472  74 ----LGRGVSAARAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLDERRLNARIA------EYNAAIREVAAERGVP 143
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1581212577 280 YVDLmkpTSIFEPDNPAFKKTMMHDGLHPTPEAHQ 314
Cdd:pfam13472 144 YVDL---WDALRDDGGWLPDLLADDGLHPNAAGYR 175
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
129-283 2.58e-11

SGNH_peri1; 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: 238863  Cd Length: 189  Bit Score: 61.91  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 129 KIGVIGDSVAAtAGGFPDILAHQYNIYVENLSVGGAKMSDY---DNNAIVNQASRLKQcDVVIIQ-GTDDdwvhdislGY 204
Cdd:cd01825     1 RIAQLGDSHIA-GDFFTDVLRGLLGVIYDNLGVNGASASLLlkwDAEFLQAQLAALPP-DLVILSyGTNE--------AF 70
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1581212577 205 AGDTDIKTYLGGLQETIKRVKNNNPNAKLIVVNCTrqcvgiNREYRTEKSKNALGLTLIDYMEAQKKYLNQQNVPYVDL 283
Cdd:cd01825    71 NKQLNASEYRQQLREFIKRLRQILPNASILLVGPP------DSLQKTGAGRWRTPPGLDAVIAAQRRVAKEEGIAFWDL 143
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
130-320 2.94e-11

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 62.21  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 130 IGVIGDSVAATAG-------GFPDILA-----------HQYNIYVeNLSVGGAKMSDYDN-----NAIVNQASRLKQCDV 186
Cdd:pfam00657   1 IVAFGDSLTDGGGdgpggrfSWGDLLAdflarklgvpgSGYNHGA-NFAIGGATIEDLPIqleqlLRLISDVKDQAKPDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 187 VIIQ-GTDDdwvhdISLGYAGDTDIKTYLGG-LQETIKRVKNNNPNAKLIVVNCTRQcVGINREYRTEKSKNALGLTLID 264
Cdd:pfam00657  80 VTIFiGAND-----LCNFLSSPARSKKRVPDlLDELRANLPQLGLGARKFWVHGLGP-LGCTPPKGCYELYNALAEEYNE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 265 YMEAQKKYLNQQ----NVPYVDLMKPtsiFEPDNPAFKKTMMHDGLHPTPEAHQYIVQEI 320
Cdd:pfam00657 154 RLNELVNSLAAAaedaNVVYVDIYGF---EDPTDPCCGIGLEPDGLHPSEKGYKAVAEAI 210
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
128-322 1.69e-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: 238872  Cd Length: 191  Bit Score: 50.75  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 128 NKIGVIGDSVAAtAGG----FPDILAHQY---NIYVENLSVGGAKMSDydnnaivnQASRL------KQCDVVIIQ-GTD 193
Cdd:cd01834     2 DRIVFIGNSITD-RGGyvgyVETYLAARYpelKLTFRNLGWSGDTVSD--------LAARRdrdvlpAKPDVVSIMfGIN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 194 DDWVhdislGYAGDTDIKTYLGGLQETIKRVKNNNPNAKLIVV--NCTRQcvgINREYRTEKSKNAlglTLIDYMEAQKK 271
Cdd:cd01834    73 DSFR-----GFDDPVGLEKFKTNLRRLIDRLKNKESAPRIVLVspIAYEA---NEDPLPDGAEYNA---NLAAYADAVRE 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1581212577 272 YLNQQNVPYVDLmkptsiFEPDNPAFKK----TMMHDGLHPTPEAHQYIVQEIAK 322
Cdd:cd01834   142 LAAENGVAFVDL------FTPMKEAFQKageaVLTVDGVHPNEAGHRALARLWLE 190
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
129-285 8.14e-04

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: 39.89  E-value: 8.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 129 KIGVIGDSVAAT------AGGFPDILAHQYN--IYVENLSVGGAKMSDYDN----NAIvnqASRLKQCDVVIIQ------ 190
Cdd:cd01821     2 TIFLAGDSTVADydpgapQAGWGQALPQYLDtgITVVNHAKGGRSSRSFRDegrwDAI---LKLIKPGDYVLIQfghndq 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 191 GTDDDWVHDIslgyagDTDIKTYLgglQETIKRVKNnnpnAKLIVVNCTRQcvginrEYRTEKSKNALGLTLIDYMEAQK 270
Cdd:cd01821    79 KPKDPEYTEP------YTTYKEYL---RRYIAEARA----KGATPILVTPV------TRRTFDEGGKVEDTLGDYPAAMR 139
                         170
                  ....*....|....*
gi 1581212577 271 KYLNQQNVPYVDLMK 285
Cdd:cd01821   140 ELAAEEGVPLIDLNA 154
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
133-323 1.98e-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: 38.46  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 133 IGDSVAataGGFPDILAHQYNIYVENLSVGGAKMSDYDNNaIVNQASRLKQCDVVIIQGTDDdwvhdISLGYagdtDIKT 212
Cdd:cd01841     6 IGDSLF---EGWPLYEAEGKGKTVNNLGIAGISSRQYLEH-IEPQLIQKNPSKVFLFLGTND-----IGKEV----SSNQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577 213 YLGGLQETIKRVKNNNPNAKLIVVNCTRQCVGINREYRTEKSKNALGLTLidymeaqkKYLNQQ-NVPYVDLmkpTSIFE 291
Cdd:cd01841    73 FIKWYRDIIEQIREEFPNTKIYLLSVLPVLEEDEIKTRSNTRIQRLNDAI--------KELAPElGVTFIDL---NDVLV 141
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1581212577 292 PDNPAFKKTMMHDGLHPTPEAHQYIVQEIAKD 323
Cdd:cd01841   142 DEFGNLKKEYTTDGLHFNPKGYQKLLEILEEY 173
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
28-158 4.79e-03

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 38.03  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1581212577  28 REKQYGIDVREAMAQTAEAiAGVQSTAKKFNQDTKNQVNQLDEKYTREIRAIVLGDTTSVAV-PTIQEPNsEAGNPLPNL 106
Cdd:cd06322     9 LQHPFFVDIKDAMKKEAAE-LGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIvPAIEAAN-EAGIPVFTV 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1581212577 107 Y---------------ETARGQVLYDFVKQSSLTKANKIGVIGD----SVAATAGGFPDILAHQYNIYVEN 158
Cdd:cd06322    87 DvkadgakvvthvgtdNYAGGKLAGEYALKALLGGGGKIAIIDYpeveSVVLRVNGFKEAIKKYPNIEIVA 157
 
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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