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Conserved domains on  [gi|27881427|ref|NP_065636|]
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polyprenol reductase [Mus musculus]

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 ...
51-330 2.12e-43

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: 151.89  E-value: 2.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427   51 RYGKTKQSGSRRpavcraFDVPKRYFSHFYVISVVWNGSLLWLLSQSLFLGAPF---PNWLSALLRTLGATQFQALEMES 127
Cdd:PLN03164  27 RRGKILHSSSQK------FTVPQRFFSHFYVVGVVWTTLLLAATWLYAYKMAPLsseEFQYSDIASQLAGGSHIFSFHKS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  128 KASRMPAAELALSAFLVLVFLWVHSLRRLFECFYVSVFSNAA-IHVVQYCFGLVYYVLVGLTVLSQ-VPMDDKNV----- 200
Cdd:PLN03164 101 RSTPVEHRYRVWRSVFLLLLMEIHVLRRLYESLYVFKYSPSArMHILGYLTGLFFYVAAPLSLCCNcAPEVAKFVgnqva 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  201 --YVLGKNL--------------LIQARWFHILGMVMFFWSSAHQYKCHVILSNLRRNKKGVVihcQHRIPFGDWFEYVS 264
Cdd:PLN03164 181 efIVKGKSAmsaiefdwwdfvspLMKLGWFQWIGAAIFLWGWIHQYRCHAILGSLREHKKQAD---EYVIPYGDWFEMVS 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881427  265 SANYLAELMIYISMAVTFGLHNLTWWLVVTYVFSSQALSAFFNHKFYRSTFVSYPKHRKAFLPFLF 330
Cdd:PLN03164 258 CPHYLAEIVIYAGLLIASGGTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFVY 323
 
Name Accession Description Interval E-value
PLN03164 PLN03164
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional
51-330 2.12e-43

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


Pssm-ID: 215610 [Multi-domain]  Cd Length: 323  Bit Score: 151.89  E-value: 2.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427   51 RYGKTKQSGSRRpavcraFDVPKRYFSHFYVISVVWNGSLLWLLSQSLFLGAPF---PNWLSALLRTLGATQFQALEMES 127
Cdd:PLN03164  27 RRGKILHSSSQK------FTVPQRFFSHFYVVGVVWTTLLLAATWLYAYKMAPLsseEFQYSDIASQLAGGSHIFSFHKS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  128 KASRMPAAELALSAFLVLVFLWVHSLRRLFECFYVSVFSNAA-IHVVQYCFGLVYYVLVGLTVLSQ-VPMDDKNV----- 200
Cdd:PLN03164 101 RSTPVEHRYRVWRSVFLLLLMEIHVLRRLYESLYVFKYSPSArMHILGYLTGLFFYVAAPLSLCCNcAPEVAKFVgnqva 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  201 --YVLGKNL--------------LIQARWFHILGMVMFFWSSAHQYKCHVILSNLRRNKKGVVihcQHRIPFGDWFEYVS 264
Cdd:PLN03164 181 efIVKGKSAmsaiefdwwdfvspLMKLGWFQWIGAAIFLWGWIHQYRCHAILGSLREHKKQAD---EYVIPYGDWFEMVS 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881427  265 SANYLAELMIYISMAVTFGLHNLTWWLVVTYVFSSQALSAFFNHKFYRSTFVSYPKHRKAFLPFLF 330
Cdd:PLN03164 258 CPHYLAEIVIYAGLLIASGGTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFVY 323
Steroid_dh pfam02544
3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid ...
213-330 1.29e-17

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: 78.22  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427   213 WFHILGMVMFFWSSAHQYKCHVILSNLRRNKKGvvihcQHRIPFGDWFEYVSSANYLAELMIYISMAVTFglHNLTWWLV 292
Cdd:pfam02544  40 PRFLIGIGLFVTGMLINIKSDIILRTLRKPGNT-----GYKIPRGGLFELVSCPNYFGEIMEWIGYALAT--WSLPALAF 112
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27881427   293 VTYVFSSQALSAFFNHKFYRSTFVSYPKHRKAFLPFLF 330
Cdd:pfam02544 113 AFFTVCNLTPRAKAHHKWYLKKFEKYPKSRKALIPFVF 150
 
Name Accession Description Interval E-value
PLN03164 PLN03164
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional
51-330 2.12e-43

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


Pssm-ID: 215610 [Multi-domain]  Cd Length: 323  Bit Score: 151.89  E-value: 2.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427   51 RYGKTKQSGSRRpavcraFDVPKRYFSHFYVISVVWNGSLLWLLSQSLFLGAPF---PNWLSALLRTLGATQFQALEMES 127
Cdd:PLN03164  27 RRGKILHSSSQK------FTVPQRFFSHFYVVGVVWTTLLLAATWLYAYKMAPLsseEFQYSDIASQLAGGSHIFSFHKS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  128 KASRMPAAELALSAFLVLVFLWVHSLRRLFECFYVSVFSNAA-IHVVQYCFGLVYYVLVGLTVLSQ-VPMDDKNV----- 200
Cdd:PLN03164 101 RSTPVEHRYRVWRSVFLLLLMEIHVLRRLYESLYVFKYSPSArMHILGYLTGLFFYVAAPLSLCCNcAPEVAKFVgnqva 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  201 --YVLGKNL--------------LIQARWFHILGMVMFFWSSAHQYKCHVILSNLRRNKKGVVihcQHRIPFGDWFEYVS 264
Cdd:PLN03164 181 efIVKGKSAmsaiefdwwdfvspLMKLGWFQWIGAAIFLWGWIHQYRCHAILGSLREHKKQAD---EYVIPYGDWFEMVS 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27881427  265 SANYLAELMIYISMAVTFGLHNLTWWLVVTYVFSSQALSAFFNHKFYRSTFVSYPKHRKAFLPFLF 330
Cdd:PLN03164 258 CPHYLAEIVIYAGLLIASGGTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFVY 323
Steroid_dh pfam02544
3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid ...
213-330 1.29e-17

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: 78.22  E-value: 1.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427   213 WFHILGMVMFFWSSAHQYKCHVILSNLRRNKKGvvihcQHRIPFGDWFEYVSSANYLAELMIYISMAVTFglHNLTWWLV 292
Cdd:pfam02544  40 PRFLIGIGLFVTGMLINIKSDIILRTLRKPGNT-----GYKIPRGGLFELVSCPNYFGEIMEWIGYALAT--WSLPALAF 112
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 27881427   293 VTYVFSSQALSAFFNHKFYRSTFVSYPKHRKAFLPFLF 330
Cdd:pfam02544 113 AFFTVCNLTPRAKAHHKWYLKKFEKYPKSRKALIPFVF 150
PLN02392 PLN02392
probable steroid reductase DET2
213-330 5.57e-08

probable steroid reductase DET2


Pssm-ID: 178015  Cd Length: 260  Bit Score: 52.89  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  213 WFHILGMVMFFWSSAHQYKCHVILSNLRRNKKGvvihcqHRIPFGDWFEYVSSANYLAELMIYISMAVtfglhnLTW-WL 291
Cdd:PLN02392 150 WRFFGGLVVFLWGMRINVWSDRVLVGLKREGGG------YKVPRGGWFELVSCPNYFGEIVEWLGWAV------MTWsWA 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 27881427  292 ---VVTYVFSSQALSAFFNHKFYRSTF-VSYPKHRKAFLPFLF 330
Cdd:PLN02392 218 gfgFFLYTCSNLVPRACANHKWYLEKFgEDYPKGRKAVIPFLY 260
PLN02560 PLN02560
enoyl-CoA reductase
143-329 4.29e-06

enoyl-CoA reductase


Pssm-ID: 178174 [Multi-domain]  Cd Length: 308  Bit Score: 47.80  E-value: 4.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  143 LVLVFLWVHSLRRLFECFYVSVFSNAAIHVVQYCFGLVYYVLVGLTVLSQV------PMDDKNVYV-LGKNLLIQARWFH 215
Cdd:PLN02560 131 YAMYYWCFHYAKRILETFFVHRFSHATSPLFNVFRNCAYYWTFGAYIAYFVnhplytPVSETQMKVgFGFGLVCQLANFY 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27881427  216 ilgmvmffwssahqykCHVILSNLRR--NKKGvvihcqHRIPFGDWFEYVSSANYLAELMIYIsmavtfgLHNLTWWLVV 293
Cdd:PLN02560 211 ----------------CHIILRNLRKpdGKGG------YQIPRGFLFNYVTCANYTTEIYQWL-------GFNIATQTVA 261
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 27881427  294 TYVFSSQALS-----AFFNHKFYRSTF------VSYPKHRKAFLPFL 329
Cdd:PLN02560 262 GYLFLAVAAAimtnwALAKHRRLKKLFdgkdgrPKYPRRWVILPPFL 308
 
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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