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Conserved domains on  [gi|1132326283|gb|APU99639|]
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hypothetical protein BV902_06635 [Sphingobacterium sp. B29]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 17879)

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; also contains C-terminal sialic acid-specific acetylesterase

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 ...
 36-222 2.32e-76

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 cd01827:

Pssm-ID: 470049  Cd Length: 188  Bit Score: 243.12  E-value: 2.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGYGLGNskEDSYPGQLQALLGQRFEVRNFGHSGATLLRKGHRPYYKTEEYRKALDYKPDVAIIHLGLND 115
Cdd:cd01827     2 KVACVGNSITEGAGLRA--YDSYPSPLAQMLGDGYEVGNFGKSARTVLNKGDHPYMNEERYKNALAFNPNIVIIKLGTND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 116 TDPRNWpNYKNSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPRFlSGTRDWYDQIQALIPQIAKNNQVGLIDLNSP 195
Cdd:cd01827    80 AKPQNW-KYKDDFKKDYETMIDSFQALPSKPKIYICYPIPAYYGDGGF-INDNIIKKEIQPMIDKIAKKLNLKLIDLHTP 157

                         170       180
                  ....*....|....*....|....*..
gi 1132326283 196 LRYRIDLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd01827   158 LKGKPELVPDWVHPNEKGAYILAKVVY 184
SASA super family cl04187
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
 313-545 1.12e-11

Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.


The actual alignment was detected with superfamily member pfam03629:

Pssm-ID: 427409  Cd Length: 227  Bit Score: 64.92  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 313 GDVYLASGQSNMAFqlRG---STKGEELIKDAPHLkNVRLFkcrslveTNAVAWDTATlrkvNDLSFFSGAWRQAtgaea 389
Cdd:pfam03629   2 KDIFLLAGQSNMAG--RGgveNWDGVVPPECQPPP-RILRL-------NADLEWEEAR----EPLHADIDAKKTC----- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 390 aqfsAV--AYSFAQQIASEQHI-PIGIIDLSVGGSnteswidrkslenddllasYIHNWQKSDFLQDFCRERASqnLAVS 466
Cdd:pfam03629  63 ----GVgpGMAFANALLRAPPGgVIGLVPCAVGGT-------------------SIEEWARGGLLYQEMVRRAK--AALK 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 467 KVKnqrhpyqpaynfeagvskwlstgLKGILWYQGESNA---HNIELHERLFKTLISSWRKSFHQ-DLPFFFVQLTSIDR 542
Cdd:pfam03629 118 GGE-----------------------IKGILWYQGESDTsdeEDAAAYKEKLEKLITDLRDDLGLpDLPIIQVQLASGEG 174


                  ...
gi 1132326283 543 PSW 545
Cdd:pfam03629 175 PYE 177
 
Name Accession Description Interval E-value
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 36-222 2.32e-76

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: 243.12  E-value: 2.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGYGLGNskEDSYPGQLQALLGQRFEVRNFGHSGATLLRKGHRPYYKTEEYRKALDYKPDVAIIHLGLND 115
Cdd:cd01827     2 KVACVGNSITEGAGLRA--YDSYPSPLAQMLGDGYEVGNFGKSARTVLNKGDHPYMNEERYKNALAFNPNIVIIKLGTND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 116 TDPRNWpNYKNSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPRFlSGTRDWYDQIQALIPQIAKNNQVGLIDLNSP 195
Cdd:cd01827    80 AKPQNW-KYKDDFKKDYETMIDSFQALPSKPKIYICYPIPAYYGDGGF-INDNIIKKEIQPMIDKIAKKLNLKLIDLHTP 157

                         170       180
                  ....*....|....*....|....*..
gi 1132326283 196 LRYRIDLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd01827   158 LKGKPELVPDWVHPNEKGAYILAKVVY 184
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 29-225 3.52e-37

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: 137.47  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  29 AVGQPRTKVACIGNSVTFGYGLgnSKEDSYPGQLQALLGQR-FEVRNFGHSGATLLRKGHRPYykteeyRKALDYKPDVA 107
Cdd:COG2755     3 AAAGKPLRIVALGDSITAGYGA--SRERGWPALLARRLAAAdVRVVNAGISGATTADLLARLD------RDLLALKPDLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 108 IIHLGLNDTDpRNWPNYKNSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPrflsgTRDWYDQIQALIPQIAKNNQV 187
Cdd:COG2755    75 VIELGTNDLL-RGLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNY-----LNERIEAYNAAIRELAAEYGV 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1132326283 188 GLIDLNSPLRYRID----LFDDYLHPNKQGAALIAEQVAHVL 225
Cdd:COG2755   149 PLVDLYAALRDAGDlpdlLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 39-216 3.13e-30

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


Pssm-ID: 463889  Cd Length: 176  Bit Score: 117.26  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  39 CIGNSVTFGYGLGNSkEDSYPGQLQALLGQRF---EVRNFGHSGATLLRKGHRpyykteEYRKALDYKPDVAIIHLGLND 115
Cdd:pfam13472   1 ALGDSITAGYGATGG-DRSYPGWLARLLARRLgadVVNNLGISGATTRLDLLE------RLDDVLRLKPDLVVILLGTND 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 116 TDPRNWPNyknSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPRFLSGTRDWYDQIQALIPQIAKNNQVGLIDLNSP 195
Cdd:pfam13472  74 LGRGVSAA---RAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDA 150

                         170       180
                  ....*....|....*....|....*.
gi 1132326283 196 L-----RYRIDLFDDYLHPNKQGAAL 216
Cdd:pfam13472 151 LrddggWLPDLLADDGLHPNAAGYRL 176
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
 313-545 1.12e-11

Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.


Pssm-ID: 427409  Cd Length: 227  Bit Score: 64.92  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 313 GDVYLASGQSNMAFqlRG---STKGEELIKDAPHLkNVRLFkcrslveTNAVAWDTATlrkvNDLSFFSGAWRQAtgaea 389
Cdd:pfam03629   2 KDIFLLAGQSNMAG--RGgveNWDGVVPPECQPPP-RILRL-------NADLEWEEAR----EPLHADIDAKKTC----- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 390 aqfsAV--AYSFAQQIASEQHI-PIGIIDLSVGGSnteswidrkslenddllasYIHNWQKSDFLQDFCRERASqnLAVS 466
Cdd:pfam03629  63 ----GVgpGMAFANALLRAPPGgVIGLVPCAVGGT-------------------SIEEWARGGLLYQEMVRRAK--AALK 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 467 KVKnqrhpyqpaynfeagvskwlstgLKGILWYQGESNA---HNIELHERLFKTLISSWRKSFHQ-DLPFFFVQLTSIDR 542
Cdd:pfam03629 118 GGE-----------------------IKGILWYQGESDTsdeEDAAAYKEKLEKLITDLRDDLGLpDLPIIQVQLASGEG 174


                  ...
gi 1132326283 543 PSW 545
Cdd:pfam03629 175 PYE 177
 
Name Accession Description Interval E-value
sialate_O-acetylesterase_like1 cd01827
sialate O-acetylesterase_like family of the SGNH hydrolases, a diverse family of lipases and ...
 36-222 2.32e-76

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: 243.12  E-value: 2.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGYGLGNskEDSYPGQLQALLGQRFEVRNFGHSGATLLRKGHRPYYKTEEYRKALDYKPDVAIIHLGLND 115
Cdd:cd01827     2 KVACVGNSITEGAGLRA--YDSYPSPLAQMLGDGYEVGNFGKSARTVLNKGDHPYMNEERYKNALAFNPNIVIIKLGTND 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 116 TDPRNWpNYKNSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPRFlSGTRDWYDQIQALIPQIAKNNQVGLIDLNSP 195
Cdd:cd01827    80 AKPQNW-KYKDDFKKDYETMIDSFQALPSKPKIYICYPIPAYYGDGGF-INDNIIKKEIQPMIDKIAKKLNLKLIDLHTP 157

                         170       180
                  ....*....|....*....|....*..
gi 1132326283 196 LRYRIDLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd01827   158 LKGKPELVPDWVHPNEKGAYILAKVVY 184
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
 29-225 3.52e-37

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: 137.47  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  29 AVGQPRTKVACIGNSVTFGYGLgnSKEDSYPGQLQALLGQR-FEVRNFGHSGATLLRKGHRPYykteeyRKALDYKPDVA 107
Cdd:COG2755     3 AAAGKPLRIVALGDSITAGYGA--SRERGWPALLARRLAAAdVRVVNAGISGATTADLLARLD------RDLLALKPDLV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 108 IIHLGLNDTDpRNWPNYKNSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPrflsgTRDWYDQIQALIPQIAKNNQV 187
Cdd:COG2755    75 VIELGTNDLL-RGLGVSPEEFRANLEALIDRLRAAGPGARVVLVTPPPRLRPNY-----LNERIEAYNAAIRELAAEYGV 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1132326283 188 GLIDLNSPLRYRID----LFDDYLHPNKQGAALIAEQVAHVL 225
Cdd:COG2755   149 PLVDLYAALRDAGDlpdlLTADGLHPNAAGYRLIAEAVLPAL 190
Lipase_GDSL_2 pfam13472
GDSL-like Lipase/Acylhydrolase family; This family of presumed lipases and related enzymes are ...
 39-216 3.13e-30

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


Pssm-ID: 463889  Cd Length: 176  Bit Score: 117.26  E-value: 3.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  39 CIGNSVTFGYGLGNSkEDSYPGQLQALLGQRF---EVRNFGHSGATLLRKGHRpyykteEYRKALDYKPDVAIIHLGLND 115
Cdd:pfam13472   1 ALGDSITAGYGATGG-DRSYPGWLARLLARRLgadVVNNLGISGATTRLDLLE------RLDDVLRLKPDLVVILLGTND 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 116 TDPRNWPNyknSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPRFLSGTRDWYDQIQALIPQIAKNNQVGLIDLNSP 195
Cdd:pfam13472  74 LGRGVSAA---RAAANLEALIDALRAAGPDARVLLIGPLPVGPPPPLDERRLNARIAEYNAAIREVAAERGVPYVDLWDA 150

                         170       180
                  ....*....|....*....|....*.
gi 1132326283 196 L-----RYRIDLFDDYLHPNKQGAAL 216
Cdd:pfam13472 151 LrddggWLPDLLADDGLHPNAAGYRL 176
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
 37-222 1.61e-24

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: 101.33  E-value: 1.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  37 VACIGNSVTFGYG--LGNSKEDSYPGQLQALLGQRFEVRNFGHSGATLLRkghrPYYKTEEYRKALDYKPDVAIIHLGLN 114
Cdd:cd00229     1 ILVIGDSITAGYGasSGSTFYSLLLYLLLLAGGPGVEVINLGVSGATTAD----ALRRLGLRLALLKDKPDLVIIELGTN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 115 DTDpRNWPNYKNSFASDYATLIDSIRSVNPKAQIYICRLTPIF---SGHPRFLSGTRDWYDQIQALIPQIAKNNqvgLID 191
Cdd:cd00229    77 DLG-RGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPpreGLLGRALPRYNEAIKAVAAENPAPSGVD---LVD 152

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1132326283 192 LNSPLR--YRIDLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd00229   153 LAALLGdeDKSLYSPDGIHPNPAGHKLIAEALA 185
SGNH_hydrolase_like_2 cd01834
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
 36-222 4.07e-19

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: 85.81  E-value: 4.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGYGLgnskEDSYPGQLQALL-GQRFEVRNFGHSGAT---LLRKGHRpyykteeyrKALDYKPDVAIIHL 111
Cdd:cd01834     3 RIVFIGNSITDRGGY----VGYVETYLAARYpELKLTFRNLGWSGDTvsdLAARRDR---------DVLPAKPDVVSIMF 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 112 GLNDTD-PRNWPNYKNSFASDYATLIDSIRSVNPKAQIYIcrLTPI-FSGHPRFLSGTRDWYDQIQALIP---QIAKNNQ 186
Cdd:cd01834    70 GINDSFrGFDDPVGLEKFKTNLRRLIDRLKNKESAPRIVL--VSPIaYEANEDPLPDGAEYNANLAAYADavrELAAENG 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1132326283 187 VGLIDLNSPLR------YRIDLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd01834   148 VAFVDLFTPMKeafqkaGEAVLTVDGVHPNEAGHRALARLWL 189
Lipase_GDSL pfam00657
GDSL-like Lipase/Acylhydrolase;
37-221 2.18e-12

GDSL-like Lipase/Acylhydrolase;


Pssm-ID: 459892 [Multi-domain]  Cd Length: 210  Bit Score: 66.83  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  37 VACIGNSVTFGYGLGNSKEDSYPGQLQALLGQRFEVR--------NFGHSGATLLRKGHRP-YYKTEEYRKALDYKPDVA 107
Cdd:pfam00657   1 IVAFGDSLTDGGGDGPGGRFSWGDLLADFLARKLGVPgsgynhgaNFAIGGATIEDLPIQLeQLLRLISDVKDQAKPDLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 108 IIHLGLNDTDPRNWP--NYKNSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHP-------------RFLSGTRDWYD 172
Cdd:pfam00657  81 TIFIGANDLCNFLSSpaRSKKRVPDLLDELRANLPQLGLGARKFWVHGLGPLGCTPpkgcyelynalaeEYNERLNELVN 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1132326283 173 QIQalipQIAKNNQVGLIDLNSPL-----RYRIDLFDDYLHPNKQGAALIAEQV 221
Cdd:pfam00657 161 SLA----AAAEDANVVYVDIYGFEdptdpCCGIGLEPDGLHPSEKGYKAVAEAI 210
SASA pfam03629
Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this ...
 313-545 1.12e-11

Carbohydrate esterase, sialic acid-specific acetylesterase; The catalytic triad of this esterase enzyme comprises residues Ser127, His403 and Asp391 in UniProtKB:P70665.


Pssm-ID: 427409  Cd Length: 227  Bit Score: 64.92  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 313 GDVYLASGQSNMAFqlRG---STKGEELIKDAPHLkNVRLFkcrslveTNAVAWDTATlrkvNDLSFFSGAWRQAtgaea 389
Cdd:pfam03629   2 KDIFLLAGQSNMAG--RGgveNWDGVVPPECQPPP-RILRL-------NADLEWEEAR----EPLHADIDAKKTC----- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 390 aqfsAV--AYSFAQQIASEQHI-PIGIIDLSVGGSnteswidrkslenddllasYIHNWQKSDFLQDFCRERASqnLAVS 466
Cdd:pfam03629  63 ----GVgpGMAFANALLRAPPGgVIGLVPCAVGGT-------------------SIEEWARGGLLYQEMVRRAK--AALK 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 467 KVKnqrhpyqpaynfeagvskwlstgLKGILWYQGESNA---HNIELHERLFKTLISSWRKSFHQ-DLPFFFVQLTSIDR 542
Cdd:pfam03629 118 GGE-----------------------IKGILWYQGESDTsdeEDAAAYKEKLEKLITDLRDDLGLpDLPIIQVQLASGEG 174


                  ...
gi 1132326283 543 PSW 545
Cdd:pfam03629 175 PYE 177
sialate_O-acetylesterase_like2 cd01828
sialate_O-acetylesterase_like subfamily of the SGNH-hydrolases, a diverse family of lipases ...
 40-230 2.46e-11

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: 62.68  E-value: 2.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  40 IGNSVTfgygLGNSKEDSYPGqlqallgqrFEVRNFGHSGATllrkghrpyykTEEYRKALD----YKPDVAIIHLGLND 115
Cdd:cd01828     5 LGDSLT----EGGPWALLFPD---------VKVANRGISGDT-----------TRGLLARLDedvaLQPKAIFIMIGIND 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 116 ----TDPRnwpnyknSFASDYATLIDSIRSVNPKAQIYICRLTPIFSGHPRFLSgtrdwydQIQAL---IPQIAKNNQVG 188
Cdd:cd01828    61 laqgTSDE-------DIVANYRTILEKLRKHFPNIKIVVQSILPVGELKSIPNE-------QIEELnrqLAQLAQQEGVT 126

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1132326283 189 LIDLNSPLR-----YRIDLFDDYLHPNKQGAAliaeQVAHVLIPVLQ 230
Cdd:cd01828   127 FLDLWAVFTnadgdLKNEFTTDGLHLNAKGYA----VWAAALQPYLA 169
Endoglucanase_E_like cd01831
Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the ...
 36-220 3.38e-11

Endoglucanase E-like members of the SGNH hydrolase family; Endoglucanase E catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.


Pssm-ID: 238869  Cd Length: 169  Bit Score: 62.36  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGYG-LGNSKED----------SYPGQLQALLGQRFEVrnFGHSGatllrKGhrpyykteeyrkaldykP 104
Cdd:cd01831     1 KIEFIGDSITCGYGvTGKSRCDfsaatedpslSYAALLARALNAEYSI--IAYSG-----IG-----------------P 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 105 DVAIIHLGLNDTDPRNWPNyKNSFASDYATLIDSIRSVNPKAQIYICrLTPIFSGHPRFLSGTRDWYDQIqalipQIAKN 184
Cdd:cd01831    57 DLVVINLGTNDFSTGNNPP-GEDFTNAYVEFIEELRKRYPDAPIVLM-LGPMLFGPYGTEEEIKRVAEAF-----KDQKS 129

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1132326283 185 NQVGLIDlnSPLRYRIDLFDDYLHPNKQGAALIAEQ 220
Cdd:cd01831   130 KKVHYFD--TPGILQHNDIGCDWHPTVAGHQKIAKH 163
SGNH_hydrolase_YpmR_like cd04506
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 36-222 1.51e-10

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: 61.11  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTfgYGLGNSKEDSYPGQLQALL-----GQRFEVRNFGHSGAT---LLRKghrpyYKTEEYRKALDyKPDVA 107
Cdd:cd04506     1 KIVALGDSLT--EGVGDETGKGGYVGRLDKLietktVKKVTVQNFGVSGDRsdqLLKR-----LKTKKVQKELK-KADVI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 108 IIHLGLNDTDPRNWPNYKNSFASDYA-----------TLIDSIRSVNPKAQIYICRL-TPI---FSGHPRFLSGTRDWYD 172
Cdd:cd04506    73 TITIGGNDLMQVLEKNFLSLDVEDFKkaeetyqnnlkKIFKEIRKLNPDAPIFLVGLyNPFyvyFPNITEINDIVNDWNE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1132326283 173 QIQALIpqiAKNNQVGLIDLNSPLRYRI---DLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd04506   153 ASQKLA---SQYKNAYFVPIFDLFSDGQnkyLLTSDHFHPNDKGYQLIADRVF 202
XynB_like cd01833
SGNH_hydrolase subfamily, similar to Ruminococcus flavefaciens XynB. Most likely a secreted ...
 74-219 5.34e-10

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: 58.40  E-value: 5.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  74 NFGHSG--ATLLRKGHRPYYKTeeyrkaldYKPDVAIIHLGLNDTdprNWPNYKNSFASDYATLIDSIRSVNPKAQIYIC 151
Cdd:cd01833    17 HEGHSGylIDQIAAAAADWVLA--------AKPDVVLLHLGTNDL---VLNRDPDTAPDRLRALIDQMRAANPDVKIIVA 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1132326283 152 RLTPIfsghpRFLSGTRDWyDQIQALIPQIA-----KNNQVGLIDLNSPLRYRIDLFDDyLHPNKQGAALIAE 219
Cdd:cd01833    86 TLIPT-----TDASGNARI-AEYNAAIPGVVadlrtAGSPVVLVDMSTGYTTADDLYDG-LHPNDQGYKKMAD 151
Lysophospholipase_L1_like cd01822
Lysophospholipase L1-like subgroup of SGNH-hydrolases. The best characterized member in this ...
 36-225 6.32e-10

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: 58.68  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGYGLgnSKEDSYPGQLQALL---GQRFEVRNFGHSGAT----LLRkghrpyykteeYRKALD-YKPDVA 107
Cdd:cd01822     2 TILALGDSLTAGYGL--PPEEGWPALLQKRLdarGIDVTVINAGVSGDTtaggLAR-----------LPALLAqHKPDLV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 108 IIHLGLND----TDPrnwpnykNSFASDYATLIDSIRSVNpkaqiyicrLTPIFSGHPRFLSGTRDWYDQIQALIPQIAK 183
Cdd:cd01822    69 ILELGGNDglrgIPP-------DQTRANLRQMIETAQARG---------APVLLVGMQAPPNYGPRYTRRFAAIYPELAE 132

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1132326283 184 NNQV--------GLIDLNSPLRyridlfDDYLHPNKQGAALIAEQVAHVL 225
Cdd:cd01822   133 EYGVplvpffleGVAGDPELMQ------SDGIHPNAEGQPIIAENVWPAL 176
SGNH_hydrolase_like_4 cd04501
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 35-225 6.08e-09

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: 56.18  E-value: 6.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  35 TKVACIGNSVTFGYGLGnsKEDSYPGQLQALLGqrFEVRNFGHSGATllrkghrpyykTEE-----YRKALDYKPDVAII 109
Cdd:cd04501     1 MRVVCLGDSITYGYPVG--PEASWVNLLAEFLG--KEVINRGINGDT-----------TSQmlvrfYEDVIALKPAVVII 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 110 HLGLNDTdprnWPNYKNSfasdyaTLIDSIRSVNPKAQ-------------IYICRLTPIFSGHPRFLSGTRDWYDqiqa 176
Cdd:cd04501    66 MGGTNDI----IVNTSLE------MIKDNIRSMVELAEangikvilasplpVDDYPWKPQWLRPANKLKSLNRWLK---- 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1132326283 177 lipQIAKNNQVGLIDLNSPL-----RYRID-LFDDYLHPNKQGAALIAEQVAHVL 225
Cdd:cd04501   132 ---DYARENGLLFLDFYSPLldernVGLKPgLLTDGLHPSREGYRVMAPLAEKAL 183
NnaC_like cd01841
NnaC (CMP-NeuNAc synthetase) _like subfamily of SGNH_hydrolases, a diverse family of lipases ...
 50-219 8.80e-09

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: 55.41  E-value: 8.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  50 LGNSKEDSYPgqLQALLGQRFEVRNFGHSGATllrkghrpyykTEEYRKALD-----YKPDVAIIHLGLNDTDprnWPNY 124
Cdd:cd01841     6 IGDSLFEGWP--LYEAEGKGKTVNNLGIAGIS-----------SRQYLEHIEpqliqKNPSKVFLFLGTNDIG---KEVS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 125 KNSFASDYATLIDSIRSVNPKAQIYICRLTPIfSGHPRFLSGTRDWYDQIQALIPQIAKNNQVGLIDLNSPLR-YRIDLF 203
Cdd:cd01841    70 SNQFIKWYRDIIEQIREEFPNTKIYLLSVLPV-LEEDEIKTRSNTRIQRLNDAIKELAPELGVTFIDLNDVLVdEFGNLK 148

                         170       180
                  ....*....|....*....|
gi 1132326283 204 DDY----LHPNKQGAALIAE 219
Cdd:cd01841   149 KEYttdgLHFNPKGYQKLLE 168
Rhamnogalacturan_acetylesterase_like cd01821
Rhamnogalacturan_acetylesterase_like subgroup of SGNH-hydrolases. Rhamnogalacturan ...
 60-222 9.08e-08

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: 52.99  E-value: 9.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  60 GQ-LQALLGQRFEVRNFGHSGATLlrkghRPYYKTEEYRKALDY--KPDVAIIHLGLNDTdPRNWPNYKNSFASDYATLI 136
Cdd:cd01821    24 GQaLPQYLDTGITVVNHAKGGRSS-----RSFRDEGRWDAILKLikPGDYVLIQFGHNDQ-KPKDPEYTEPYTTYKEYLR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 137 DSIRSVNPKAQIYICrLTPI----FSGHPRFLSGTRDWydqIQALIpQIAKNNQVGLIDLNS-------------PLRYR 199
Cdd:cd01821    98 RYIAEARAKGATPIL-VTPVtrrtFDEGGKVEDTLGDY---PAAMR-ELAAEEGVPLIDLNAasralyeaigpekSKKYF 172

                         170       180
                  ....*....|....*....|...
gi 1132326283 200 IDLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd01821   173 PEGPGDNTHFSEKGADVVARLVA 195
SEST_like cd01823
SEST_like. A family of secreted SGNH-hydrolases similar to Streptomyces scabies esterase (SEST) ...
 56-221 9.56e-08

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: 54.00  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  56 DSYPGQLQALLGQR-FEVRNFGHSGATLLRKGHRPYYKTEEYRKALDYKPDVAIIHLGLNDT----------DPRNWPNY 124
Cdd:cd01823    32 NSYPTLLARALGDEtLSFTDVACSGATTTDGIEPQQGGIAPQAGALDPDTDLVTITIGGNDLgfadvvkaciLTGGGSSL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 125 K--------------NSFASDYATLIDSIRSVNPKAQIYicrltpiFSGHPRFLSGTRDWYDQIQALIPQIAKNNQVGLI 190
Cdd:cd01823   112 AqekgaadgardaalDEVGARLKAVLDRIRERAPNARVV-------VVGYPRLFPPDGGDCDKSCSPGTPLTPADRPELN 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1132326283 191 D----LNSPLRYRIDLFDDY-------------------------------------LHPNKQGAALIAEQV 221
Cdd:cd01823   185 QlvdkLNALIRRAAADAGDYkvrfvdtdapfaghracspdpwsrsvldllptrqgkpFHPNAAGHRAIADLI 256
FeeA_FeeB_like cd01836
SGNH_hydrolase subfamily, FeeA, FeeB and similar esterases/lipases. FeeA and FeeB are part of ...
 40-222 3.76e-07

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: 51.11  E-value: 3.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  40 IGNSVTFGYGLGNSKEdSYPGQ----LQALLGQRFEVRNFGHSGATllrkghrpyykTEEYRKALD----YKPDVAIIHL 111
Cdd:cd01836     8 LGDSTAAGVGVETQDQ-ALAGQlargLAAITGRGVRWRLFAKTGAT-----------SADLLRQLAplpeTRFDVAVISI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 112 GLND----TDPRNWpnyknsfASDYATLIDSIRSVNPKAQIYICRLTPI--FSGHPRFLSGTRDWYDQI--QALIPQIAK 183
Cdd:cd01836    76 GVNDvthlTSIARW-------RKQLAELVDALRAKFPGARVVVTAVPPLgrFPALPQPLRWLLGRRARLlnRALERLASE 148

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1132326283 184 NNQVGLIDLNSPLRYRIdLFDDYLHPNKQGAALIAEQVA 222
Cdd:cd01836   149 APRVTLLPATGPLFPAL-FASDGFHPSAAGYAVWAEALA 186
SGNH_hydrolase_like_1 cd01832
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 37-223 1.87e-06

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


Pssm-ID: 238870  Cd Length: 185  Bit Score: 48.80  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  37 VACIGNSVTFGYG--LGNSKEDSYPGQLQALLGQR---FEVRNFGHSGATLlrkghrPYYKTEEYRKALDYKPDVAIIHL 111
Cdd:cd01832     2 YVALGDSITEGVGdpVPDGGYRGWADRLAAALAAAdpgIEYANLAVRGRRT------AQILAEQLPAALALRPDLVTLLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 112 GLND-----TDPrnwpnykNSFASDYATLIDSIRSvnPKAQIYICRLtPIFSGHPRFLSGTRDWYDQIQALIPQIAKNNQ 186
Cdd:cd01832    76 GGNDilrpgTDP-------DTYRADLEEAVRRLRA--AGARVVVFTI-PDPAVLEPFRRRVRARLAAYNAVIRAVAARYG 145

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1132326283 187 VGLIDLNS-PLRYRIDLFD-DYLHPNKQGAALIAEQVAH 223
Cdd:cd01832   146 AVHVDLWEhPEFADPRLWAsDRLHPSAAGHARLAALVLA 184
SGNH_hydrolase_like_7 cd04502
Members of the SGNH-hydrolase superfamily, a diverse family of lipases and esterases. The ...
 72-219 3.45e-06

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


Pssm-ID: 239946  Cd Length: 171  Bit Score: 47.67  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  72 VRNFGHSGATLLRKGHrpYYKteeyRKALDYKPDVAIIHLGLNDTDPRNWPNyknSFASDYATLIDSIRSVNPKAQIYIC 151
Cdd:cd04502    25 VVNRGFGGSTLADCLH--YFD----RLVLPYQPRRVVLYAGDNDLASGRTPE---EVLRDFRELVNRIRAKLPDTPIAII 95

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1132326283 152 RLTPifsghprflSGTR----DWYDQIQALIPQIAKNN-QVGLIDLNSPL-----RYRIDLF-DDYLHPNKQGAALIAE 219
Cdd:cd04502    96 SIKP---------SPARwalrPKIRRFNALLKELAETRpNLTYIDVASPMldadgKPRAELFqEDGLHLNDAGYALWRK 165
SGNH_arylesterase_like cd01839
SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating ...
 36-226 8.61e-06

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: 47.26  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGY----GLGNSKEDSYPGQLQALLGQR---FEVRNFGHSGATLL--------RKGhRPYYKTeeyrkAL 100
Cdd:cd01839     1 TILCFGDSNTWGIipdtGGRYPFEDRWPGVLEKALGANgenVRVIEDGLPGRTTVlddpffpgRNG-LTYLPQ-----AL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 101 -DYKP-DVAIIHLGLNDTDPRNWPNYKNSfASDYATLIDSIRSVN-----PKAQIYICRLTPIFSGHPRFLSGTRDWYDQ 173
Cdd:cd01839    75 eSHSPlDLVIIMLGTNDLKSYFNLSAAEI-AQGLGALVDIIRTAPiepgmPAPKILIVAPPPIRTPKGSLAGKFAGAEEK 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1132326283 174 IQALIPQI---AKNNQVGLIDLN-----SPLryridlfdDYLHPNKQGAALIAEQVAHVLI 226
Cdd:cd01839   154 SKGLADAYralAEELGCHFFDAGsvgstSPV--------DGVHLDADQHAALGQALASVIR 206
XynE_like cd01830
SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen ...
 37-221 1.42e-05

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


Pssm-ID: 238868  Cd Length: 204  Bit Score: 46.47  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  37 VACIGNSVTFGYGLGNSKEDSYPGQLQALLGQR-----FEVRNFGHSGATLLRKGHRPyykteeyrKALD-YKPDV---- 106
Cdd:cd01830     2 VVALGDSITDGRGSTPDANNRWPDLLAARLAARagtrgIAVLNAGIGGNRLLADGLGP--------SALArFDRDVlsqp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 107 ----AIIHLGLNDTdprNWPNYKNSFAS-DYATLIDSIRSVNPKAQ-----IYICRLTPiFSGHPrFLSGTR-------- 168
Cdd:cd01830    74 gvrtVIILEGVNDI---GASGTDFAAAPvTAEELIAGYRQLIRRAHargikVIGATITP-FEGSG-YYTPAReatrqavn 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1132326283 169 DW------YDqiqalipqiaknnqvGLIDLNS-------PLRYRIDlFD--DYLHPNKQGAALIAEQV 221
Cdd:cd01830   149 EWirtsgaFD---------------AVVDFDAalrdpadPSRLRPA-YDsgDHLHPNDAGYQAMADAV 200
SGNH_hydrolase_peri1 cd01825
SGNH_peri1; putative periplasmic member of the SGNH-family of hydrolases, a diverse family of ...
 36-226 2.39e-05

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: 45.73  E-value: 2.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283  36 KVACIGNSVTFGyglgnskeDSYPGQLQALLGQRFEvrNFGHSGATLLRKGHRPYYKTEEYRKALdyKPDVAIIHLGLND 115
Cdd:cd01825     1 RIAQLGDSHIAG--------DFFTDVLRGLLGVIYD--NLGVNGASASLLLKWDAEFLQAQLAAL--PPDLVILSYGTNE 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1132326283 116 TDPRNWpNYkNSFASDYATLIDSIRSVNPKAQIYIcrLTPIfsghPRFLS-GTRDW-----YDQIQALIPQIAKNNQVGL 189
Cdd:cd01825    69 AFNKQL-NA-SEYRQQLREFIKRLRQILPNASILL--VGPP----DSLQKtGAGRWrtppgLDAVIAAQRRVAKEEGIAF 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1132326283 190 IDL---------NSPLRYRIDLFDDYLHPNKQGAALIAEQVAHVLI 226
Cdd:cd01825   141 WDLyaamggeggIWQWAEPGLARKDYVHLTPRGYERLANLLYEALL 186
 
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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