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Conserved domains on  [gi|6322140|ref|NP_012215|]
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putative polyprenol reductase [Saccharomyces cerevisiae S288C]

Protein Classification

phosphatidylethanolamine N-methyltransferase family domain-containing protein( domain architecture ID 229533)

phosphatidylethanolamine N-methyltransferase (PEMT) family domain-containing protein similar to Homo sapiens PEMT, which catalyzes the three sequential steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME), PMME to phosphatidyldimethylethanolamine (PDME), and PDME to phosphatidylcholine (PC)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ICMT super family cl21511
Isoprenylcysteine carboxyl methyltransferase (ICMT) family; The isoprenylcysteine ...
60-252 1.66e-25

Isoprenylcysteine carboxyl methyltransferase (ICMT) family; The isoprenylcysteine o-methyltransferase (EC:2.1.1.100) family carry out carboxyl methylation of cleaved eukaryotic proteins that terminate in a CaaX motif. In Saccharomyces cerevisiae this methylation is carried out by Ste14p, an integral endoplasmic reticulum membrane protein. Ste14p is the founding member of the isoprenylcysteine carboxyl methyltransferase (ICMT) family, whose members share significant sequence homology.


The actual alignment was detected with superfamily member PLN03164:

Pssm-ID: 473892 [Multi-domain]  Cd Length: 323  Bit Score: 102.20  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    60 KKFTVPKAYFSHFYYLA----TFLSLVT-LYFYPKFPI------------------------------------VWIIF- 97
Cdd:PLN03164  37 QKFTVPQRFFSHFYVVGvvwtTLLLAATwLYAYKMAPLsseefqysdiasqlaggshifsfhksrstpvehryrVWRSVf 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    98 ------GHSLRRLYETLYVLHYTSNSRMNWSHYLVGIWFYSVLLLILNISLYKNSIPNTLN------------MNAF--- 156
Cdd:PLN03164 117 llllmeIHVLRRLYESLYVFKYSPSARMHILGYLTGLFFYVAAPLSLCCNCAPEVAKFVGNqvaefivkgksaMSAIefd 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140   157 -------------------IIFCIASWDQYKNHVILANLVK-------YSLPTGRLFRLVCCPHYLDEIIIYSTLL---- 206
Cdd:PLN03164 197 wwdfvsplmklgwfqwigaAIFLWGWIHQYRCHAILGSLREhkkqadeYVIPYGDWFEMVSCPHYLAEIVIYAGLLiasg 276
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 6322140   207 PYEQEFYLTLVWVITSLTISALETKNYYRHKFKDNHVAPYAIIPFI 252
Cdd:PLN03164 277 GTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFV 322
 
Name Accession Description Interval E-value
PLN03164 PLN03164
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional
60-252 1.66e-25

3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional


Pssm-ID: 215610 [Multi-domain]  Cd Length: 323  Bit Score: 102.20  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    60 KKFTVPKAYFSHFYYLA----TFLSLVT-LYFYPKFPI------------------------------------VWIIF- 97
Cdd:PLN03164  37 QKFTVPQRFFSHFYVVGvvwtTLLLAATwLYAYKMAPLsseefqysdiasqlaggshifsfhksrstpvehryrVWRSVf 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    98 ------GHSLRRLYETLYVLHYTSNSRMNWSHYLVGIWFYSVLLLILNISLYKNSIPNTLN------------MNAF--- 156
Cdd:PLN03164 117 llllmeIHVLRRLYESLYVFKYSPSARMHILGYLTGLFFYVAAPLSLCCNCAPEVAKFVGNqvaefivkgksaMSAIefd 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140   157 -------------------IIFCIASWDQYKNHVILANLVK-------YSLPTGRLFRLVCCPHYLDEIIIYSTLL---- 206
Cdd:PLN03164 197 wwdfvsplmklgwfqwigaAIFLWGWIHQYRCHAILGSLREhkkqadeYVIPYGDWFEMVSCPHYLAEIVIYAGLLiasg 276
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 6322140   207 PYEQEFYLTLVWVITSLTISALETKNYYRHKFKDNHVAPYAIIPFI 252
Cdd:PLN03164 277 GTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFV 322
Steroid_dh pfam02544
3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid ...
156-252 5.70e-07

3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid 4-dehydrogenases, EC:1.3.99.5 Also known as Steroid 5-alpha-reductase, the reaction catalyzed by this enzyme is: 3-oxo-5-alpha-steroid + acceptor <=> 3-oxo-delta(4)-steroid + reduced acceptor. The Steroid 5-alpha-reductase enzyme is responsible for the formation of dihydrotestosterone, this hormone promotes the differentiation of male external genitalia and the prostate during fetal development. In humans mutations in this enzyme can cause a form of male pseudohermaphorditism in which the external genitalia and prostate fail to develop normally. A related enzyme is also found in plants is DET2, a steroid reductase from Arabidopsis. Mutations in this enzyme cause defects in light-regulated development.


Pssm-ID: 460585 [Multi-domain]  Cd Length: 150  Bit Score: 47.78  E-value: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    156 FIIFCIASWDQYKNHVILANLVK-----YSLPTGRLFRLVCCPHYLDEIIIY--STLLPYEQEFYLTLVWVITSLTISAL 228
Cdd:pfam02544  46 IGLFVTGMLINIKSDIILRTLRKpgntgYKIPRGGLFELVSCPNYFGEIMEWigYALATWSLPALAFAFFTVCNLTPRAK 125
                          90       100
                  ....*....|....*....|....
gi 6322140    229 ETKNYYRHKFKDNHVAPYAIIPFI 252
Cdd:pfam02544 126 AHHKWYLKKFEKYPKSRKALIPFV 149
 
Name Accession Description Interval E-value
PLN03164 PLN03164
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional
60-252 1.66e-25

3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional


Pssm-ID: 215610 [Multi-domain]  Cd Length: 323  Bit Score: 102.20  E-value: 1.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    60 KKFTVPKAYFSHFYYLA----TFLSLVT-LYFYPKFPI------------------------------------VWIIF- 97
Cdd:PLN03164  37 QKFTVPQRFFSHFYVVGvvwtTLLLAATwLYAYKMAPLsseefqysdiasqlaggshifsfhksrstpvehryrVWRSVf 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    98 ------GHSLRRLYETLYVLHYTSNSRMNWSHYLVGIWFYSVLLLILNISLYKNSIPNTLN------------MNAF--- 156
Cdd:PLN03164 117 llllmeIHVLRRLYESLYVFKYSPSARMHILGYLTGLFFYVAAPLSLCCNCAPEVAKFVGNqvaefivkgksaMSAIefd 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140   157 -------------------IIFCIASWDQYKNHVILANLVK-------YSLPTGRLFRLVCCPHYLDEIIIYSTLL---- 206
Cdd:PLN03164 197 wwdfvsplmklgwfqwigaAIFLWGWIHQYRCHAILGSLREhkkqadeYVIPYGDWFEMVSCPHYLAEIVIYAGLLiasg 276
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 6322140   207 PYEQEFYLTLVWVITSLTISALETKNYYRHKFKDNHVAPYAIIPFI 252
Cdd:PLN03164 277 GTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFV 322
Steroid_dh pfam02544
3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid ...
156-252 5.70e-07

3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid 4-dehydrogenases, EC:1.3.99.5 Also known as Steroid 5-alpha-reductase, the reaction catalyzed by this enzyme is: 3-oxo-5-alpha-steroid + acceptor <=> 3-oxo-delta(4)-steroid + reduced acceptor. The Steroid 5-alpha-reductase enzyme is responsible for the formation of dihydrotestosterone, this hormone promotes the differentiation of male external genitalia and the prostate during fetal development. In humans mutations in this enzyme can cause a form of male pseudohermaphorditism in which the external genitalia and prostate fail to develop normally. A related enzyme is also found in plants is DET2, a steroid reductase from Arabidopsis. Mutations in this enzyme cause defects in light-regulated development.


Pssm-ID: 460585 [Multi-domain]  Cd Length: 150  Bit Score: 47.78  E-value: 5.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    156 FIIFCIASWDQYKNHVILANLVK-----YSLPTGRLFRLVCCPHYLDEIIIY--STLLPYEQEFYLTLVWVITSLTISAL 228
Cdd:pfam02544  46 IGLFVTGMLINIKSDIILRTLRKpgntgYKIPRGGLFELVSCPNYFGEIMEWigYALATWSLPALAFAFFTVCNLTPRAK 125
                          90       100
                  ....*....|....*....|....
gi 6322140    229 ETKNYYRHKFKDNHVAPYAIIPFI 252
Cdd:pfam02544 126 AHHKWYLKKFEKYPKSRKALIPFV 149
PLN02560 PLN02560
enoyl-CoA reductase
72-199 6.68e-03

enoyl-CoA reductase


Pssm-ID: 178174 [Multi-domain]  Cd Length: 308  Bit Score: 37.01  E-value: 6.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140    72 FYYLATFLSLVTLYFYPKfpiVWIIFG--------------------HSLRRLYETLYVLHYT------SNSRMNWSHYl 125
Cdd:PLN02560  95 FEYLGPLLIYPLFYFFPQ---VYKYFGyparrvihpvqtyamyywcfHYAKRILETFFVHRFShatsplFNVFRNCAYY- 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322140   126 vgiW-FYSVLLLILNISLYkNSIPNTLNMNAFIIFCIASWDQYKNHVILANLVK------YSLPTGRLFRLVCCPHYLDE 198
Cdd:PLN02560 171 ---WtFGAYIAYFVNHPLY-TPVSETQMKVGFGFGLVCQLANFYCHIILRNLRKpdgkggYQIPRGFLFNYVTCANYTTE 246

                 .
gi 6322140   199 I 199
Cdd:PLN02560 247 I 247
 
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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