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Conserved domains on  [gi|190684707|ref|NP_848877|]
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PC-esterase domain-containing protein 1A [Mus musculus]

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 4.08e-110

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: 322.53  E-value: 4.08e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  34 FVVILGDSIQRAVYKDLVLLLQKDTLLTASQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842    1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707 114 trvyseyledileelsygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNLAMPLGERVTGG 193
Cdd:cd01842   52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190684707 194 FLLPELQPLAVSLRQDVVEGNFYSATLAGKHCFDVLDLHFHFRHAVRHRHRDGVHWDQHAHRHLSHLLLAHVA 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 4.08e-110

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: 322.53  E-value: 4.08e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  34 FVVILGDSIQRAVYKDLVLLLQKDTLLTASQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842    1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707 114 trvyseyledileelsygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNLAMPLGERVTGG 193
Cdd:cd01842   52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190684707 194 FLLPELQPLAVSLRQDVVEGNFYSATLAGKHCFDVLDLHFHFRHAVRHRHRDGVHWDQHAHRHLSHLLLAHVA 266
Cdd:cd01842  111 FLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQHRVRDGVHWNYVAHRRLSNLLLAHVA 183
PC-Esterase pfam13839
GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is ...
20-249 4.83e-03

GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is comprised of Cas1p, the Homo sapiens C7orf58, Arabidopsis thaliana PMR5 and a group of plant freezing resistance/cold acclimatization proteins typified by Arabidopsis thaliana ESKIMO1, animal FAM55D proteins, and animal FAM113 proteins. The PC-Esterase family has features that are both similar and different from the canonical GDSL/SGNH superfamily. The members of this family are predicted to have Acyl esterase activity and predicted to modify cell-surface biopolymers such as glycans and glycoproteins. The Cas1p protein has a Cas1_AcylT domain, in addition, with the opposing acyltransferase activity. The C7orf58 family has a ATP-Grasp domain fused to the PC-Esterase and is the first identified secreted tubulin-tyrosine ligase like enzyme in eukaryotes. The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich potential sugar binding domain followed by PC-Esterase domain.


Pssm-ID: 463996  Cd Length: 281  Bit Score: 38.71  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707   20 HFHASEVQQLLHNKFVVILGDSIQRAVYKDLVLLLQKdtlltasqlkakgelSFEQDQLVaggqlgelHNGTQYREVRQF 99
Cdd:pfam13839   3 RFDAAEFLERLRGKRIAFVGDSLARNQWESLLCLLSS---------------AVEDPKSV--------YKITKDRGFRRF 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  100 CSGSGHHLVRFY---FLTRVYSE-----------YLeDILEE--LSYGPAPDLVIINSCLWDLSR---------YGRCS- 153
Cdd:pfam13839  60 RFPDYNFTVEFYwspFLVDSVEDpngpgkgkrvlHL-DSIDErwASQWKGADVLVFNTGHWWLRPkiyyeggdyFGCGGk 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  154 -------MESYRENLERVFVRMDQVLPDSCLLV--------------WNLA------MPL-GERVTGGFLLPELQPLAVs 205
Cdd:pfam13839 139 nytdmdrLDAYRKALRTWARWVDSNLDPSKTRVffrtfspshfeggeWNTGgscnrtRPLsEGEYPLGGLDPEMRRIQE- 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 190684707  206 lrqDVVEGNfysatlaGKHCFDVLDL--------------HFHFRHAVRHRHRDGVHW 249
Cdd:pfam13839 218 ---EVLRSK-------MGTPVRLLDItklselrkdghpsvYGGKKPFAPKGYNDCSHW 265
 
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 4.08e-110

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: 322.53  E-value: 4.08e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  34 FVVILGDSIQRAVYKDLVLLLQKDTLLTASQLKAKGELSFEQDQLVAGGQLgelhngtqyrevrqfcsgsghhlvrfyfl 113
Cdd:cd01842    1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKGELSFENDVLLEGGRL----------------------------- 51
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707 114 trvyseyledileelsygpapDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNLAMPLGERVTGG 193
Cdd:cd01842   52 ---------------------DLVIMNSCLWDLSRYQRNSMKTYRENLERLFSKLDSVLPIECLIVWNTAMPVAEEIKGG 110
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190684707 194 FLLPELQPLAVSLRQDVVEGNFYSATLAGKHCFDVLDLHFHFRHAVRHRHRDGVHWDQHAHRHLSHLLLAHVA 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 5.56e-08

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: 52.80  E-value: 5.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  35 VVILGDSIQRAVYkdlvlllqkdtlltaSQLKAKGELSFEQDQLVAGGQLGELHNgtqyrevrqfCSGSGHHLVRFYFLT 114
Cdd:cd00229    1 ILVIGDSITAGYG---------------ASSGSTFYSLLLYLLLLAGGPGVEVIN----------LGVSGATTADALRRL 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707 115 RVYSEYLedileelsyGPAPDLVIINSCLWDLSRYGRCSMESYRENLERVFVRMDQVLPDSCLLVWNLAMPLGERvtggF 194
Cdd:cd00229   56 GLRLALL---------KDKPDLVIIELGTNDLGRGGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPRE----G 122
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 190684707 195 LLPELQPLAVSLRQDVVEGNFYSATLagkhcfDVLDLHFHFRHAVRHRHR-DGVHWDQHAHRHLSHLLLAH 264
Cdd:cd00229  123 LLGRALPRYNEAIKAVAAENPAPSGV------DLVDLAALLGDEDKSLYSpDGIHPNPAGHKLIAEALASA 187
PC-Esterase pfam13839
GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is ...
20-249 4.83e-03

GDSL/SGNH-like Acyl-Esterase family found in Pmr5 and Cas1p; The PC-Esterase family is comprised of Cas1p, the Homo sapiens C7orf58, Arabidopsis thaliana PMR5 and a group of plant freezing resistance/cold acclimatization proteins typified by Arabidopsis thaliana ESKIMO1, animal FAM55D proteins, and animal FAM113 proteins. The PC-Esterase family has features that are both similar and different from the canonical GDSL/SGNH superfamily. The members of this family are predicted to have Acyl esterase activity and predicted to modify cell-surface biopolymers such as glycans and glycoproteins. The Cas1p protein has a Cas1_AcylT domain, in addition, with the opposing acyltransferase activity. The C7orf58 family has a ATP-Grasp domain fused to the PC-Esterase and is the first identified secreted tubulin-tyrosine ligase like enzyme in eukaryotes. The plant family with PMR5, ESK1, TBL3 etc have a N-terminal C rich potential sugar binding domain followed by PC-Esterase domain.


Pssm-ID: 463996  Cd Length: 281  Bit Score: 38.71  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707   20 HFHASEVQQLLHNKFVVILGDSIQRAVYKDLVLLLQKdtlltasqlkakgelSFEQDQLVaggqlgelHNGTQYREVRQF 99
Cdd:pfam13839   3 RFDAAEFLERLRGKRIAFVGDSLARNQWESLLCLLSS---------------AVEDPKSV--------YKITKDRGFRRF 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  100 CSGSGHHLVRFY---FLTRVYSE-----------YLeDILEE--LSYGPAPDLVIINSCLWDLSR---------YGRCS- 153
Cdd:pfam13839  60 RFPDYNFTVEFYwspFLVDSVEDpngpgkgkrvlHL-DSIDErwASQWKGADVLVFNTGHWWLRPkiyyeggdyFGCGGk 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684707  154 -------MESYRENLERVFVRMDQVLPDSCLLV--------------WNLA------MPL-GERVTGGFLLPELQPLAVs 205
Cdd:pfam13839 139 nytdmdrLDAYRKALRTWARWVDSNLDPSKTRVffrtfspshfeggeWNTGgscnrtRPLsEGEYPLGGLDPEMRRIQE- 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 190684707  206 lrqDVVEGNfysatlaGKHCFDVLDL--------------HFHFRHAVRHRHRDGVHW 249
Cdd:pfam13839 218 ---EVLRSK-------MGTPVRLLDItklselrkdghpsvYGGKKPFAPKGYNDCSHW 265
 
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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