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Conserved domains on  [gi|1034582327|ref|XP_016875705|]
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PC-esterase domain-containing protein 1B isoform X1 [Homo sapiens]

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 ...
17-249 9.60e-82

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: 249.34  E-value: 9.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  17 FVVILGDSVHRAVYKDLVLLLQKDRLLTPGQLRARGELNFEQDELVDGGQRghmhnglnyrevrefrsdhhlvrfyfltr 96
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  97 vysdylqtilkelqsgehapDLVIMNSCLWDISRYGPNSWRSYLENLENLFQCLGQVLPESCLLVWNTAMPVGEEVTGGF 176
Cdd:cd01842    52 --------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGF 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034582327 177 LPPKLRRQKATfLKNEVVKANFHSATEARKHNFDVLDLHFHFRHARENLHWDGVHWNGRVHRCLSQLLLAHVA 249
Cdd:cd01842   112 LLPELHDLSKS-LRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 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 ...
17-249 9.60e-82

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: 249.34  E-value: 9.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  17 FVVILGDSVHRAVYKDLVLLLQKDRLLTPGQLRARGELNFEQDELVDGGQRghmhnglnyrevrefrsdhhlvrfyfltr 96
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  97 vysdylqtilkelqsgehapDLVIMNSCLWDISRYGPNSWRSYLENLENLFQCLGQVLPESCLLVWNTAMPVGEEVTGGF 176
Cdd:cd01842    52 --------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGF 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034582327 177 LPPKLRRQKATfLKNEVVKANFHSATEARKHNFDVLDLHFHFRHARENLHWDGVHWNGRVHRCLSQLLLAHVA 249
Cdd:cd01842   112 LLPELHDLSKS-LRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
99-249 1.08e-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: 45.79  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  99 SDYLQTILKELQsgEHAPDLVI----MNsclwDISRYGPNSWRSYLENLENLFQCLGQVLPESCLLVWnTAMPVGEevtg 174
Cdd:COG2755    56 ADLLARLDRDLL--ALKPDLVVielgTN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVLV-TPPPRLR---- 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034582327 175 gflPPKLRRQKATFlkNEVVKAnfhsatEARKHNFDVLDLHFHFR---HARENLHWDGVHWNGRVHRCLSQLLLAHVA 249
Cdd:COG2755   125 ---PNYLNERIEAY--NAAIRE------LAAEYGVPLVDLYAALRdagDLPDLLTADGLHPNAAGYRLIAEAVLPALK 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 ...
17-249 9.60e-82

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: 249.34  E-value: 9.60e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  17 FVVILGDSVHRAVYKDLVLLLQKDRLLTPGQLRARGELNFEQDELVDGGQRghmhnglnyrevrefrsdhhlvrfyfltr 96
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  97 vysdylqtilkelqsgehapDLVIMNSCLWDISRYGPNSWRSYLENLENLFQCLGQVLPESCLLVWNTAMPVGEEVTGGF 176
Cdd:cd01842    52 --------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGF 111
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034582327 177 LPPKLRRQKATfLKNEVVKANFHSATEARKHNFDVLDLHFHFRHARENLHWDGVHWNGRVHRCLSQLLLAHVA 249
Cdd:cd01842   112 LLPELHDLSKS-LRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
98-247 2.05e-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: 59.73  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  98 YSDYLQTILKELQSGEHAPDLVIMNSCLWDISRYGPNSWRSYLENLENLFQCLGQVLPESCLLVWNTAMPVGEEVTGGFL 177
Cdd:cd00229    48 TADALRRLGLRLALLKDKPDLVIIELGTNDLGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRA 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034582327 178 PPKLRRQKAtflknEVVKANfhsateARKHNFDVLDLHFHFRHAR-ENLHWDGVHWNGRVHRCLSQLLLAH 247
Cdd:cd00229   128 LPRYNEAIK-----AVAAEN------PAPSGVDLVDLAALLGDEDkSLYSPDGIHPNPAGHKLIAEALASA 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
99-249 1.08e-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: 45.79  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034582327  99 SDYLQTILKELQsgEHAPDLVI----MNsclwDISRYGPNSWRSYLENLENLFQCLGQVLPESCLLVWnTAMPVGEevtg 174
Cdd:COG2755    56 ADLLARLDRDLL--ALKPDLVVielgTN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVLV-TPPPRLR---- 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034582327 175 gflPPKLRRQKATFlkNEVVKAnfhsatEARKHNFDVLDLHFHFR---HARENLHWDGVHWNGRVHRCLSQLLLAHVA 249
Cdd:COG2755   125 ---PNYLNERIEAY--NAAIRE------LAAEYGVPLVDLYAALRdagDLPDLLTADGLHPNAAGYRLIAEAVLPALK 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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