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Conserved domains on  [gi|1783384186|ref|NP_001181592|]
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PC-esterase domain-containing protein 1A [Macaca mulatta]

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 ...
34-215 6.95e-110

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: 320.22  E-value: 6.95e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186  34 FVVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAK----YLEDVLEEltyGPAPDLVIINSCLWDLSRYGRCSMESYRKN 109
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKgelsFENDVLLE---GGRLDLVIMNSCLWDLSRYQRNSMKTYREN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186 110 LERVFVRMDQVLPDSCLLVWNMAMPLGERITGGFLLPELQPLAGSLRRDVVEGNFYSATLAGDHCFDVLDLHFHFRHAVQ 189
Cdd:cd01842    78 LERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGFLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQ 157
                         170       180
                  ....*....|....*....|....*.
gi 1783384186 190 HRHRDGVHWDQHAHRHLSHLLLTHVA 215
Cdd:cd01842   158 HRVRDGVHWNYVAHRRLSNLLLAHVA 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 ...
34-215 6.95e-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: 320.22  E-value: 6.95e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186  34 FVVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAK----YLEDVLEEltyGPAPDLVIINSCLWDLSRYGRCSMESYRKN 109
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKgelsFENDVLLE---GGRLDLVIMNSCLWDLSRYQRNSMKTYREN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186 110 LERVFVRMDQVLPDSCLLVWNMAMPLGERITGGFLLPELQPLAGSLRRDVVEGNFYSATLAGDHCFDVLDLHFHFRHAVQ 189
Cdd:cd01842    78 LERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGFLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQ 157
                         170       180
                  ....*....|....*....|....*.
gi 1783384186 190 HRHRDGVHWDQHAHRHLSHLLLTHVA 215
Cdd:cd01842   158 HRVRDGVHWNYVAHRRLSNLLLAHVA 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 ...
34-215 6.95e-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: 320.22  E-value: 6.95e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186  34 FVVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAK----YLEDVLEEltyGPAPDLVIINSCLWDLSRYGRCSMESYRKN 109
Cdd:cd01842     1 FVVILGDSIQRAVYKDLVLLLQKDSLLSSSQLKAKgelsFENDVLLE---GGRLDLVIMNSCLWDLSRYQRNSMKTYREN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186 110 LERVFVRMDQVLPDSCLLVWNMAMPLGERITGGFLLPELQPLAGSLRRDVVEGNFYSATLAGDHCFDVLDLHFHFRHAVQ 189
Cdd:cd01842    78 LERLFSKLDSVLPIECLIVWNTAMPVAEEIKGGFLLPELHDLSKSLRYDVLEGNFYSATLAKCYGFDVLDLHYHFRHAMQ 157
                         170       180
                  ....*....|....*....|....*.
gi 1783384186 190 HRHRDGVHWDQHAHRHLSHLLLTHVA 215
Cdd:cd01842   158 HRVRDGVHWNYVAHRRLSNLLLAHVA 183
SGNH_hydrolase cd00229
SGNH_hydrolase, or GDSL_hydrolase, is a diverse family of lipases and esterases. The tertiary ...
35-213 6.81e-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: 52.41  E-value: 6.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186  35 VVILGDSIQRAVYKDLVLLLQKDSLLTAAQLKAKYLE------------DVLEELTY-----GPAPDLVIINSCLWDLSR 97
Cdd:cd00229     1 ILVIGDSITAGYGASSGSTFYSLLLYLLLLAGGPGVEvinlgvsgattaDALRRLGLrlallKDKPDLVIIELGTNDLGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1783384186  98 YGRCSMESYRKNLERVFVRMDQVLPDSCLLVWNMAMPLGERITGGFLLPELQplagSLRRDVVEGNFYSATLagdhcfDV 177
Cdd:cd00229    81 GGDTSIDEFKANLEELLDALRERAPGAKVILITPPPPPPREGLLGRALPRYN----EAIKAVAAENPAPSGV------DL 150
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1783384186 178 LDLHFHFRHAVQHRHR-DGVHWDQHAHRHLSHLLLTH 213
Cdd:cd00229   151 VDLAALLGDEDKSLYSpDGIHPNPAGHKLIAEALASA 187
 
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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