NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1953337371|ref|XP_038289230|]
View 

PC-esterase domain-containing protein 1A isoform X1 [Canis lupus familiaris]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 1.02e-111

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: 326.76  E-value: 1.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371  34 FVVILGDSIQRAVYKDLVLLLQRDSLLTAAQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371 114 trvyseylegvleeltygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERVTGG 193
Cdd:cd01842    52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953337371 194 FLLPELQPLAGSLRRDVVEGNFYSATLARDHCFDVLDLHFHFRHAVQHRHRDGVHWDQHAHRHLSHLLLTHVA 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 1.02e-111

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: 326.76  E-value: 1.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371  34 FVVILGDSIQRAVYKDLVLLLQRDSLLTAAQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371 114 trvyseylegvleeltygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERVTGG 193
Cdd:cd01842    52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953337371 194 FLLPELQPLAGSLRRDVVEGNFYSATLARDHCFDVLDLHFHFRHAVQHRHRDGVHWDQHAHRHLSHLLLTHVA 266
Cdd:cd01842   111 FLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
119-266 2.54e-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: 38.86  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371 119 EYLEGVLEELtygpAPDLVII----NsclwDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVwnMAMPLgeRVTGGF 194
Cdd:COG2755    60 ARLDRDLLAL----KPDLVVIelgtN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVL--VTPPP--RLRPNY 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953337371 195 LLPELQPLAGSLRRdvvegnfysatLARDHCFDVLDLHFHFRHAVQHRHR---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 1.02e-111

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: 326.76  E-value: 1.02e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371  34 FVVILGDSIQRAVYKDLVLLLQRDSLLTAAQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371 114 trvyseylegvleeltygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERVTGG 193
Cdd:cd01842    52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953337371 194 FLLPELQPLAGSLRRDVVEGNFYSATLARDHCFDVLDLHFHFRHAVQHRHRDGVHWDQHAHRHLSHLLLTHVA 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 3.52e-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: 50.49  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371  35 VVILGDSIQRAVYkdlvlllqrdslltaAQLKAKGELSFEQDQLVAGGQLGELHNgtqyrevrqfCSGSGHHLVRFYFLT 114
Cdd:cd00229     1 ILVIGDSITAGYG---------------ASSGSTFYSLLLYLLLLAGGPGVEVIN----------LGVSGATTADALRRL 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371 115 RVYSEYLegvleeltyGPAPDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNMAMPLGERVTGGF 194
Cdd:cd00229    56 GLRLALL---------KDKPDLVIIELGTNDLGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGR 126
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953337371 195 LLPELQPLAGSLRrdvvegnfysATLARDHCFDVLDLHFHFRHAVQHRHR-DGVHWDQHAHRHLSHLLLTH 264
Cdd:cd00229   127 ALPRYNEAIKAVA----------AENPAPSGVDLVDLAALLGDEDKSLYSpDGIHPNPAGHKLIAEALASA 187
TesA COG2755
Lysophospholipase L1 or related esterase. Includes spore coat protein LipC/YcsK [Cell cycle ...
119-266 2.54e-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: 38.86  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953337371 119 EYLEGVLEELtygpAPDLVII----NsclwDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVwnMAMPLgeRVTGGF 194
Cdd:COG2755    60 ARLDRDLLAL----KPDLVVIelgtN----DLLRGLGVSPEEFRANLEALIDRLRAAGPGARVVL--VTPPP--RLRPNY 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953337371 195 LLPELQPLAGSLRRdvvegnfysatLARDHCFDVLDLHFHFRHAVQHRHR---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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH