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Conserved domains on  [gi|301767994|ref|XP_002919412|]
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PREDICTED: polyprenol reductase [Ailuropoda melanoleuca]

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 ...
38-318 2.53e-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: 151.51  E-value: 2.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994  38 GLLPGCAlfqdliRYGKTKREGQSRpavcrvFDVPKRYFSHFYIISALWNGFLLwhLTQSVFLGVPFPNWLHGLLRILGA 117
Cdd:PLN03164  20 GLVLGFA------RRGKILHSSSQK------FTVPQRFFSHFYVVGVVWTTLLL--AATWLYAYKMAPLSSEEFQYSDIA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 118 SQFQGG-----------------ELALSAFLVLVFLWLHSLRRLFECFYVSVFSNTV-IHIVQYCFGLVYYVLTGLTVLS 179
Cdd:PLN03164  86 SQLAGGshifsfhksrstpvehrYRVWRSVFLLLLMEIHVLRRLYESLYVFKYSPSArMHILGYLTGLFFYVAAPLSLCC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 180 QVPMD------GRNAYVIGK----------------NLLMQARWFHILGMLMFIWSSVHQYKCHVILGNLRKNKAGVVih 237
Cdd:PLN03164 166 NCAPEvakfvgNQVAEFIVKgksamsaiefdwwdfvSPLMKLGWFQWIGAAIFLWGWIHQYRCHAILGSLREHKKQAD-- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 238 cNHRIPFGDWFEYVSSPNYLAELMIYISMAVTFGFHNLTWWLVVTYVFFSQALSAFLSHKFYKSKFVSYPKHRKAFLPFL 317
Cdd:PLN03164 244 -EYVIPYGDWFEMVSCPHYLAEIVIYAGLLIASGGTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFV 322

                 .
gi 301767994 318 F 318
Cdd:PLN03164 323 Y 323
 
Name Accession Description Interval E-value
PLN03164 PLN03164
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional
38-318 2.53e-43

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


Pssm-ID: 215610 [Multi-domain]  Cd Length: 323  Bit Score: 151.51  E-value: 2.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994  38 GLLPGCAlfqdliRYGKTKREGQSRpavcrvFDVPKRYFSHFYIISALWNGFLLwhLTQSVFLGVPFPNWLHGLLRILGA 117
Cdd:PLN03164  20 GLVLGFA------RRGKILHSSSQK------FTVPQRFFSHFYVVGVVWTTLLL--AATWLYAYKMAPLSSEEFQYSDIA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 118 SQFQGG-----------------ELALSAFLVLVFLWLHSLRRLFECFYVSVFSNTV-IHIVQYCFGLVYYVLTGLTVLS 179
Cdd:PLN03164  86 SQLAGGshifsfhksrstpvehrYRVWRSVFLLLLMEIHVLRRLYESLYVFKYSPSArMHILGYLTGLFFYVAAPLSLCC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 180 QVPMD------GRNAYVIGK----------------NLLMQARWFHILGMLMFIWSSVHQYKCHVILGNLRKNKAGVVih 237
Cdd:PLN03164 166 NCAPEvakfvgNQVAEFIVKgksamsaiefdwwdfvSPLMKLGWFQWIGAAIFLWGWIHQYRCHAILGSLREHKKQAD-- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 238 cNHRIPFGDWFEYVSSPNYLAELMIYISMAVTFGFHNLTWWLVVTYVFFSQALSAFLSHKFYKSKFVSYPKHRKAFLPFL 317
Cdd:PLN03164 244 -EYVIPYGDWFEMVSCPHYLAEIVIYAGLLIASGGTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFV 322

                 .
gi 301767994 318 F 318
Cdd:PLN03164 323 Y 323
Steroid_dh pfam02544
3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid ...
201-318 2.00e-18

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: 80.53  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994  201 WFHILGMLMFIWSSVHQYKCHVILGNLRKNKAGvvihcNHRIPFGDWFEYVSSPNYLAELMIYISMAVtfgfhnLTW-WL 279
Cdd:pfam02544  40 PRFLIGIGLFVTGMLINIKSDIILRTLRKPGNT-----GYKIPRGGLFELVSCPNYFGEIMEWIGYAL------ATWsLP 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 301767994  280 VVTYVFFS---QALSAFLSHKFYKSKFVSYPKHRKAFLPFLF 318
Cdd:pfam02544 109 ALAFAFFTvcnLTPRAKAHHKWYLKKFEKYPKSRKALIPFVF 150
 
Name Accession Description Interval E-value
PLN03164 PLN03164
3-oxo-5-alpha-steroid 4-dehydrogenase, C-terminal domain containing protein; Provisional
38-318 2.53e-43

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


Pssm-ID: 215610 [Multi-domain]  Cd Length: 323  Bit Score: 151.51  E-value: 2.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994  38 GLLPGCAlfqdliRYGKTKREGQSRpavcrvFDVPKRYFSHFYIISALWNGFLLwhLTQSVFLGVPFPNWLHGLLRILGA 117
Cdd:PLN03164  20 GLVLGFA------RRGKILHSSSQK------FTVPQRFFSHFYVVGVVWTTLLL--AATWLYAYKMAPLSSEEFQYSDIA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 118 SQFQGG-----------------ELALSAFLVLVFLWLHSLRRLFECFYVSVFSNTV-IHIVQYCFGLVYYVLTGLTVLS 179
Cdd:PLN03164  86 SQLAGGshifsfhksrstpvehrYRVWRSVFLLLLMEIHVLRRLYESLYVFKYSPSArMHILGYLTGLFFYVAAPLSLCC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 180 QVPMD------GRNAYVIGK----------------NLLMQARWFHILGMLMFIWSSVHQYKCHVILGNLRKNKAGVVih 237
Cdd:PLN03164 166 NCAPEvakfvgNQVAEFIVKgksamsaiefdwwdfvSPLMKLGWFQWIGAAIFLWGWIHQYRCHAILGSLREHKKQAD-- 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 238 cNHRIPFGDWFEYVSSPNYLAELMIYISMAVTFGFHNLTWWLVVTYVFFSQALSAFLSHKFYKSKFVSYPKHRKAFLPFL 317
Cdd:PLN03164 244 -EYVIPYGDWFEMVSCPHYLAEIVIYAGLLIASGGTDLTIWLLFGFVVANLTFAAAETHRWYLQKFENYPRNRYAIIPFV 322

                 .
gi 301767994 318 F 318
Cdd:PLN03164 323 Y 323
Steroid_dh pfam02544
3-oxo-5-alpha-steroid 4-dehydrogenase; This family consists of 3-oxo-5-alpha-steroid ...
201-318 2.00e-18

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: 80.53  E-value: 2.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994  201 WFHILGMLMFIWSSVHQYKCHVILGNLRKNKAGvvihcNHRIPFGDWFEYVSSPNYLAELMIYISMAVtfgfhnLTW-WL 279
Cdd:pfam02544  40 PRFLIGIGLFVTGMLINIKSDIILRTLRKPGNT-----GYKIPRGGLFELVSCPNYFGEIMEWIGYAL------ATWsLP 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 301767994  280 VVTYVFFS---QALSAFLSHKFYKSKFVSYPKHRKAFLPFLF 318
Cdd:pfam02544 109 ALAFAFFTvcnLTPRAKAHHKWYLKKFEKYPKSRKALIPFVF 150
PLN02392 PLN02392
probable steroid reductase DET2
201-318 1.27e-08

probable steroid reductase DET2


Pssm-ID: 178015  Cd Length: 260  Bit Score: 54.82  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 201 WFHILGMLMFIWSSVHQYKCHVILGNLRKNKAGvvihcnHRIPFGDWFEYVSSPNYLAELMIYISMAVtfgfhnLTW-WL 279
Cdd:PLN02392 150 WRFFGGLVVFLWGMRINVWSDRVLVGLKREGGG------YKVPRGGWFELVSCPNYFGEIVEWLGWAV------MTWsWA 217
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 301767994 280 VVTYVFFSQA---LSAFLSHKFYKSKF-VSYPKHRKAFLPFLF 318
Cdd:PLN02392 218 GFGFFLYTCSnlvPRACANHKWYLEKFgEDYPKGRKAVIPFLY 260
PLN02560 PLN02560
enoyl-CoA reductase
131-317 2.59e-03

enoyl-CoA reductase


Pssm-ID: 178174 [Multi-domain]  Cd Length: 308  Bit Score: 38.94  E-value: 2.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 131 LVLVFLWLHSLRRLFECFYVSVFSNTVIHIVQYCFGLVYYVLTGLTVLSQV------PMDGRNAYV-IGKNLLMQARWFH 203
Cdd:PLN02560 131 YAMYYWCFHYAKRILETFFVHRFSHATSPLFNVFRNCAYYWTFGAYIAYFVnhplytPVSETQMKVgFGFGLVCQLANFY 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 301767994 204 ilgmlmfiwssvhqykCHVILGNLRKNKAgvviHCNHRIPFGDWFEYVSSPNYLAELMIYIsmavtfGFhNLTWWLVVTY 283
Cdd:PLN02560 211 ----------------CHIILRNLRKPDG----KGGYQIPRGFLFNYVTCANYTTEIYQWL------GF-NIATQTVAGY 263
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 301767994 284 VFFSQALS-----AFLSHKFYKSKF------VSYPKHRKAFLPFL 317
Cdd:PLN02560 264 LFLAVAAAimtnwALAKHRRLKKLFdgkdgrPKYPRRWVILPPFL 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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