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Conserved domains on  [gi|530425903|ref|XP_005260861|]
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PC-esterase domain-containing protein 1A isoform X1 [Homo sapiens]

Protein Classification

SGNH/GDSL hydrolase family protein( domain architecture ID 10110893)

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_like_5 cd01842
SGNH_hydrolase subfamily. SGNH hydrolases are a diverse family of lipases and esterases. The ...
34-266 2.33e-113

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: 331.00  E-value: 2.33e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903  34 FVVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842    1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903 114 trvyseyledvleeltygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERITGG 193
Cdd:cd01842   52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530425903 194 FLLPELQPLAGSLRRDVVEGNFYSATLAGDHCFDVLDLHFHFRHAVQHRHRDGVHWDQHAHRHLSHLLLTHVA 266
Cdd:cd01842  111 FLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 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 ...
34-266 2.33e-113

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: 331.00  E-value: 2.33e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903  34 FVVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842    1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903 114 trvyseyledvleeltygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERITGG 193
Cdd:cd01842   52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530425903 194 FLLPELQPLAGSLRRDVVEGNFYSATLAGDHCFDVLDLHFHFRHAVQHRHRDGVHWDQHAHRHLSHLLLTHVA 266
Cdd:cd01842  111 FLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
119-266 5.18e-03

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: 38.09  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903 119 EYLEDVLEELtygpAPDLVII----NsclwDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVwnMAMPLgeRITGGF 194
Cdd:COG2755   60 ARLDRDLLAL----KPDLVVIelgtN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVL--VTPPP--RLRPNY 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425903 195 LLPELQPLAGSLRRdvvegnfysatLAGDHCFDVLDLHFHFRHAVQHRHR---DGVHWDQHAHRHLSHLLLTHVA 266
Cdd:COG2755  128 LNERIEAYNAAIRE-----------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 ...
34-266 2.33e-113

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: 331.00  E-value: 2.33e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903  34 FVVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842    1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903 114 trvyseyledvleeltygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERITGG 193
Cdd:cd01842   52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530425903 194 FLLPELQPLAGSLRRDVVEGNFYSATLAGDHCFDVLDLHFHFRHAVQHRHRDGVHWDQHAHRHLSHLLLTHVA 266
Cdd:cd01842  111 FLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
35-264 2.73e-07

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: 50.87  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903  35 VVILGDSIQRAVYkdlvlllqkdslltaAQLKAKGELSFEQDQLVAGGQLGELHNgtqyrevrqfCSGSGHHLVRFYFLT 114
Cdd:cd00229    1 ILVIGDSITAGYG---------------ASSGSTFYSLLLYLLLLAGGPGVEVIN----------LGVSGATTADALRRL 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903 115 RVYSEYLedvleeltyGPAPDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERITGGF 194
Cdd:cd00229   56 GLRLALL---------KDKPDLVIIELGTNDLGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGR 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530425903 195 LLPELQplagSLRRDVVEGNFYSATLagdhcfDVLDLHFHFRHAVQHRHR-DGVHWDQHAHRHLSHLLLTH 264
Cdd:cd00229  127 ALPRYN----EAIKAVAAENPAPSGV------DLVDLAALLGDEDKSLYSpDGIHPNPAGHKLIAEALASA 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
119-266 5.18e-03

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: 38.09  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530425903 119 EYLEDVLEELtygpAPDLVII----NsclwDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVwnMAMPLgeRITGGF 194
Cdd:COG2755   60 ARLDRDLLAL----KPDLVVIelgtN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVL--VTPPP--RLRPNY 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530425903 195 LLPELQPLAGSLRRdvvegnfysatLAGDHCFDVLDLHFHFRHAVQHRHR---DGVHWDQHAHRHLSHLLLTHVA 266
Cdd:COG2755  128 LNERIEAYNAAIRE-----------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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