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Conserved domains on  [gi|15238431|ref|NP_200758|]
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protein C-terminal S-isoprenylcysteine carboxyl O-methyltransferase [Arabidopsis thaliana]

Protein Classification

methyltransferase family protein( domain architecture ID 10005179)

methyltransferase family protein such as methanethiol S-methyltransferase that catalyzes the methylation of methanethiol (MeSH) to yield dimethylsulphide (DMS)

EC:  2.1.1.-
Gene Ontology:  GO:0008168|GO:0032259

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 286-395 2.35e-17

Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 77.12  E-value: 2.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238431 286 WILIVITMLMHYDSTLYLARYSEKVV---VPTAVVQFGPYRWVRHPIYASTMLLFAAYCTALRAPLSLLfLLAVCLVYYN 362
Cdd:COG2020   3 LVLILLGLLLRLWAVLTLGRSWTTLVpprKAHRLVTTGPYRYVRHPMYLGFLLLLLGLALLLGSLLALL-LALLLLLLYV 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 15238431 363 KKAKMEEELMVESFGQSYSDYADKVRhKFIPFV 395
Cdd:COG2020  82 LRIRREERRLRARFGEEYRAYAARVP-RLIPRL 113
 
Name Accession Description Interval E-value
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 286-395 2.35e-17

Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 77.12  E-value: 2.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238431 286 WILIVITMLMHYDSTLYLARYSEKVV---VPTAVVQFGPYRWVRHPIYASTMLLFAAYCTALRAPLSLLfLLAVCLVYYN 362
Cdd:COG2020   3 LVLILLGLLLRLWAVLTLGRSWTTLVpprKAHRLVTTGPYRYVRHPMYLGFLLLLLGLALLLGSLLALL-LALLLLLLYV 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 15238431 363 KKAKMEEELMVESFGQSYSDYADKVRhKFIPFV 395
Cdd:COG2020  82 LRIRREERRLRARFGEEYRAYAARVP-RLIPRL 113
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 314-379 1.65e-03

Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) has a broad substrate specificity of unsaturated phospholipids.


Pssm-ID: 461218 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15238431   314 TAVVQFGPYRWVRHPIYASTMLLFAAYCTALRAPLSLLFLLAVCLVYYNKKAKMEEELMVESFGQS 379
Cdd:pfam04191  40 DKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLLVYFIALKFVEEPHMAKIYGKR 105
 
Name Accession Description Interval E-value
STE14 COG2020
Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein ...
 286-395 2.35e-17

Protein-S-isoprenylcysteine O-methyltransferase Ste14 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441623 [Multi-domain]  Cd Length: 113  Bit Score: 77.12  E-value: 2.35e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238431 286 WILIVITMLMHYDSTLYLARYSEKVV---VPTAVVQFGPYRWVRHPIYASTMLLFAAYCTALRAPLSLLfLLAVCLVYYN 362
Cdd:COG2020   3 LVLILLGLLLRLWAVLTLGRSWTTLVpprKAHRLVTTGPYRYVRHPMYLGFLLLLLGLALLLGSLLALL-LALLLLLLYV 81

                        90       100       110
                ....*....|....*....|....*....|...
gi 15238431 363 KKAKMEEELMVESFGQSYSDYADKVRhKFIPFV 395
Cdd:COG2020  82 LRIRREERRLRARFGEEYRAYAARVP-RLIPRL 113
YpbQ COG1755
Uncharacterized conserved protein YpbQ, isoprenylcysteine carboxyl methyltransferase (ICMT) ...
 264-356 1.29e-04

Uncharacterized conserved protein YpbQ, isoprenylcysteine carboxyl methyltransferase (ICMT) family [Function unknown];


Pssm-ID: 441361  Cd Length: 171  Bit Score: 42.13  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15238431 264 WLAA--FEGPELHRLPGGWANVGIWILIVITMLMHYDSTLYLARY-SEKV-VVPTA-VVQFGPYRWVRHPIYASTM---- 334
Cdd:COG1755  53 FLASliLEALLRGRPFLPPLSWIGLALFLLAQALRYWVIRSLGRRwTTRIiVLPGApLVTSGPYRYLRHPNYFLVVlela 132

                        90       100
                ....*....|....*....|....*
gi 15238431 335 ---LLFAAYCTALRAPLSLLFLLAV 356
Cdd:COG1755 133 alpLLFGAWITALLFSLLNALLLAV 157
PEMT pfam04191
Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) ...
 314-379 1.65e-03

Phospholipid methyltransferase; The S. cerevisiae phospholipid methyltransferase (EC:2.1.1.16) has a broad substrate specificity of unsaturated phospholipids.


Pssm-ID: 461218 [Multi-domain]  Cd Length: 105  Bit Score: 37.54  E-value: 1.65e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15238431   314 TAVVQFGPYRWVRHPIYASTMLLFAAYCTALRAPLSLLFLLAVCLVYYNKKAKMEEELMVESFGQS 379
Cdd:pfam04191  40 DKLVTGGPYRYLNNPMYVGGTLGFLGLALITGSPAGLLLALLVLLVYFIALKFVEEPHMAKIYGKR 105
 
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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