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Conserved domains on  [gi|1238278477|dbj|GAX67596|]
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hypothetical protein SCKG_0697 [Saccharomyces cerevisiae]

Protein Classification

phosphatidylinositol-specific phospholipase C/glycerophosphodiester phosphodiesterase family protein( domain architecture ID 10171156)

phosphatidylinositol-specific phospholipase C/glycerophosphodiester phosphodiesterase family protein may hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PI-PLCc_GDPD_SF_unchar3 cd08577
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
115-382 2.31e-78

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


:

Pssm-ID: 176519 [Multi-domain]  Cd Length: 228  Bit Score: 241.00  E-value: 2.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 115 MPVHSHNDYWRKLPLFEGLAYGASSTEADVWNIDEKiLAVGHNEAYLDPvELTLDKLYTGPLLEILDEVNCQdsdsdrkn 194
Cdd:cd08577     1 INAHSHNDYWRKRPLYDALSAGFGSIEADVWLVNGD-LLVAHDEVDLSP-ARTLESLYLDPLLEILDQNNGQ-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 195 gvFFNSPETSLFFYIDFKSDDNeLTYKLLmEQYFKSLIDSGYLTYYdmkkDEIIWRPVTVILTGNYPTSLDildngndng 274
Cdd:cd08577    71 --AYNDPEQPLQLLIDIKTDGE-STYPAL-EEVLKPYIDIGYLSYY----DKLVPGPVTVVITGNRPKEEV--------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 275 yFESNQRFAFLDAPLLSLEPKySKLSVAATvSFSQLMKHCGsdHWKVslRGRMDSNEISCAKSIIDGAHALKLKTRIWGA 354
Cdd:cd08577   134 -KSQYPRYIFFDGRLDEDLPD-EQLARLSP-MISASFAKFS--KWNG--KGDTPEDEKEKLKSIIDKAHARGKKVRFWGT 206
                         250       260
                  ....*....|....*....|....*...
gi 1238278477 355 PTwpanlVETISRQIIhDLGSDLLNLDN 382
Cdd:cd08577   207 PD-----RPNVWKTLM-ELGVDLLNTDD 228
 
Name Accession Description Interval E-value
PI-PLCc_GDPD_SF_unchar3 cd08577
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
115-382 2.31e-78

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176519 [Multi-domain]  Cd Length: 228  Bit Score: 241.00  E-value: 2.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 115 MPVHSHNDYWRKLPLFEGLAYGASSTEADVWNIDEKiLAVGHNEAYLDPvELTLDKLYTGPLLEILDEVNCQdsdsdrkn 194
Cdd:cd08577     1 INAHSHNDYWRKRPLYDALSAGFGSIEADVWLVNGD-LLVAHDEVDLSP-ARTLESLYLDPLLEILDQNNGQ-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 195 gvFFNSPETSLFFYIDFKSDDNeLTYKLLmEQYFKSLIDSGYLTYYdmkkDEIIWRPVTVILTGNYPTSLDildngndng 274
Cdd:cd08577    71 --AYNDPEQPLQLLIDIKTDGE-STYPAL-EEVLKPYIDIGYLSYY----DKLVPGPVTVVITGNRPKEEV--------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 275 yFESNQRFAFLDAPLLSLEPKySKLSVAATvSFSQLMKHCGsdHWKVslRGRMDSNEISCAKSIIDGAHALKLKTRIWGA 354
Cdd:cd08577   134 -KSQYPRYIFFDGRLDEDLPD-EQLARLSP-MISASFAKFS--KWNG--KGDTPEDEKEKLKSIIDKAHARGKKVRFWGT 206
                         250       260
                  ....*....|....*....|....*...
gi 1238278477 355 PTwpanlVETISRQIIhDLGSDLLNLDN 382
Cdd:cd08577   207 PD-----RPNVWKTLM-ELGVDLLNTDD 228
 
Name Accession Description Interval E-value
PI-PLCc_GDPD_SF_unchar3 cd08577
Uncharacterized hypothetical proteins similar to the catalytic domains of ...
115-382 2.31e-78

Uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipaseand Glycerophosphodiester phosphodiesterases; This subfamily corresponds to a group of uncharacterized hypothetical proteins similar to the catalytic domains of Phosphoinositide-specific phospholipase C (PI-PLC), and glycerophosphodiester phosphodiesterases (GP-GDE), and also sphingomyelinases D (SMases D) and similar proteins. They hydrolyze the 3'-5' phosphodiester bonds in different substrates, utilizing a similar mechanism of general base and acid catalysis involving two conserved histidine residues.


Pssm-ID: 176519 [Multi-domain]  Cd Length: 228  Bit Score: 241.00  E-value: 2.31e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 115 MPVHSHNDYWRKLPLFEGLAYGASSTEADVWNIDEKiLAVGHNEAYLDPvELTLDKLYTGPLLEILDEVNCQdsdsdrkn 194
Cdd:cd08577     1 INAHSHNDYWRKRPLYDALSAGFGSIEADVWLVNGD-LLVAHDEVDLSP-ARTLESLYLDPLLEILDQNNGQ-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 195 gvFFNSPETSLFFYIDFKSDDNeLTYKLLmEQYFKSLIDSGYLTYYdmkkDEIIWRPVTVILTGNYPTSLDildngndng 274
Cdd:cd08577    71 --AYNDPEQPLQLLIDIKTDGE-STYPAL-EEVLKPYIDIGYLSYY----DKLVPGPVTVVITGNRPKEEV--------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238278477 275 yFESNQRFAFLDAPLLSLEPKySKLSVAATvSFSQLMKHCGsdHWKVslRGRMDSNEISCAKSIIDGAHALKLKTRIWGA 354
Cdd:cd08577   134 -KSQYPRYIFFDGRLDEDLPD-EQLARLSP-MISASFAKFS--KWNG--KGDTPEDEKEKLKSIIDKAHARGKKVRFWGT 206
                         250       260
                  ....*....|....*....|....*...
gi 1238278477 355 PTwpanlVETISRQIIhDLGSDLLNLDN 382
Cdd:cd08577   207 PD-----RPNVWKTLM-ELGVDLLNTDD 228
 
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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