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Conserved domains on  [gi|2428898134|ref|NP_001403065|]
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PC-esterase domain-containing protein 1B [Mus musculus]

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 ...
17-253 8.20e-79

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 cd01842:

Pssm-ID: 470049  Cd Length: 183  Bit Score: 242.02  E-value: 8.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134  17 FVVVLGDSVHRAVYKDLVLLLQKDCLLTNKQLRTKGELSFEKDQLKMGGELDtlhnrtdyrevrefcsdhhlvrfyfltr 96
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRLD---------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134  97 vyseymesvleelqsgnhapdVIIMNSCLWDVSRYGRNSLSSYKQNLENLFGRMDQVLPKSCLLVWNTAMPLGDKIKAAF 176
Cdd:cd01842    53 ---------------------LVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGF 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2428898134 177 LPQKCKGQYPrisvaTLKRKVTQANLYSHAEATKHYFDVLDLNFHFRQARKHLQGDGVHWNEHAHRKLSYLLLAHMA 253
Cdd:cd01842   112 LLPELHDLSK-----SLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_5 cd01842
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
17-253 8.20e-79

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: 238880  Cd Length: 183  Bit Score: 242.02  E-value: 8.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134  17 FVVVLGDSVHRAVYKDLVLLLQKDCLLTNKQLRTKGELSFEKDQLKMGGELDtlhnrtdyrevrefcsdhhlvrfyfltr 96
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRLD---------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134  97 vyseymesvleelqsgnhapdVIIMNSCLWDVSRYGRNSLSSYKQNLENLFGRMDQVLPKSCLLVWNTAMPLGDKIKAAF 176
Cdd:cd01842    53 ---------------------LVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGF 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2428898134 177 LPQKCKGQYPrisvaTLKRKVTQANLYSHAEATKHYFDVLDLNFHFRQARKHLQGDGVHWNEHAHRKLSYLLLAHMA 253
Cdd:cd01842   112 LLPELHDLSK-----SLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
113-253 3.07e-05

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: 44.63  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134 113 NHAPDVII----MNsclwDVSRYGRNSLSSYKQNLENLFGRMDQVLPKSCLLVwnTAMPlgdkikaaflpqkckgqyPRI 188
Cdd:COG2755    68 ALKPDLVVielgTN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVL--VTPP------------------PRL 123
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2428898134 189 SVATLKRKVTQANLYSHAEATKHYFDVLDLNFHFR---QARKHLQGDGVHWNEHAHRKLSYLLLAHMA 253
Cdd:COG2755   124 RPNYLNERIEAYNAAIRELAAEYGVPLVDLYAALRdagDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
 
Name Accession Description Interval E-value
SGNH_hydrolase_like_5 cd01842
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
17-253 8.20e-79

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: 238880  Cd Length: 183  Bit Score: 242.02  E-value: 8.20e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134  17 FVVVLGDSVHRAVYKDLVLLLQKDCLLTNKQLRTKGELSFEKDQLKMGGELDtlhnrtdyrevrefcsdhhlvrfyfltr 96
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRLD---------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134  97 vyseymesvleelqsgnhapdVIIMNSCLWDVSRYGRNSLSSYKQNLENLFGRMDQVLPKSCLLVWNTAMPLGDKIKAAF 176
Cdd:cd01842    53 ---------------------LVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGF 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2428898134 177 LPQKCKGQYPrisvaTLKRKVTQANLYSHAEATKHYFDVLDLNFHFRQARKHLQGDGVHWNEHAHRKLSYLLLAHMA 253
Cdd:cd01842   112 LLPELHDLSK-----SLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
114-251 1.13e-09

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: 57.42  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134 114 HAPDVIIMNSCLWDVSRYGRNSLSSYKQNLENLFGRMDQVLPKSCLLVWNTAMPLGDkikaaflpqkcKGQYPRISVATL 193
Cdd:cd00229    64 DKPDLVIIELGTNDLGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPR-----------EGLLGRALPRYN 132
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2428898134 194 KRKVTQANLYSHAeatkHYFDVLDLNFHFRQARKHL-QGDGVHWNEHAHRKLSYLLLAH 251
Cdd:cd00229   133 EAIKAVAAENPAP----SGVDLVDLAALLGDEDKSLySPDGIHPNPAGHKLIAEALASA 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
113-253 3.07e-05

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: 44.63  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2428898134 113 NHAPDVII----MNsclwDVSRYGRNSLSSYKQNLENLFGRMDQVLPKSCLLVwnTAMPlgdkikaaflpqkckgqyPRI 188
Cdd:COG2755    68 ALKPDLVVielgTN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVL--VTPP------------------PRL 123
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2428898134 189 SVATLKRKVTQANLYSHAEATKHYFDVLDLNFHFR---QARKHLQGDGVHWNEHAHRKLSYLLLAHMA 253
Cdd:COG2755   124 RPNYLNERIEAYNAAIRELAAEYGVPLVDLYAALRdagDLPDLLTADGLHPNAAGYRLIAEAVLPALK 191
 
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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