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Conserved domains on  [gi|1958743041|ref|XP_038952753|]
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prenylcysteine oxidase-like isoform X2 [Rattus norvegicus]

Protein Classification

prenylcysteine oxidase family protein( domain architecture ID 10537445)

prenylcysteine oxidase family protein similar to Arabidopsis thaliana farnesylcysteine lyase that cleaves specifically the thioether bond of S-farnesyl-L-cysteine and has no activity with S-geranylgeranyl-L-cysteine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
1-338 0e+00

Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps.


:

Pssm-ID: 462104 [Multi-domain]  Cd Length: 364  Bit Score: 505.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041   1 MWVEEVMEKFMRIYKYQAHGYAFSGTEELLYSLGEATFVNMTQRSVAESLLQVGVTQRFIDDVVSAVLRASYGQSASMPA 80
Cdd:pfam07156  27 MWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAGFSQLFINEIVQAVTRVNYGQSVNING 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041  81 FAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKALYQVGYETDKGNSSDFYDIVVIATPL 159
Cdd:pfam07156 107 FVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTSLYEVTYKTESGTHSDLYDIVVIATPL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041 160 HldNSSSNITFEGFTPPIDDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFANILTTDFPS-FFCSLDNICPVNISASF 238
Cdd:pfam07156 187 H--RKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLATILTTDNPSlFINSISSVSPVNISDNP 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041 239 RRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPKFALHDQLFYLNALEWAASSVEVAAVAA 318
Cdd:pfam07156 265 RRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPPFILHDGLYYLNGIEWAASAMEMSAIAA 344
                         330       340
                  ....*....|....*....|
gi 1958743041 319 KNVALLAYNRWYQDLDKIDQ 338
Cdd:pfam07156 345 KNVALLAYHRWYGNTDKIDQ 364
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
1-338 0e+00

Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps.


Pssm-ID: 462104 [Multi-domain]  Cd Length: 364  Bit Score: 505.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041   1 MWVEEVMEKFMRIYKYQAHGYAFSGTEELLYSLGEATFVNMTQRSVAESLLQVGVTQRFIDDVVSAVLRASYGQSASMPA 80
Cdd:pfam07156  27 MWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAGFSQLFINEIVQAVTRVNYGQSVNING 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041  81 FAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKALYQVGYETDKGNSSDFYDIVVIATPL 159
Cdd:pfam07156 107 FVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTSLYEVTYKTESGTHSDLYDIVVIATPL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041 160 HldNSSSNITFEGFTPPIDDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFANILTTDFPS-FFCSLDNICPVNISASF 238
Cdd:pfam07156 187 H--RKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLATILTTDNPSlFINSISSVSPVNISDNP 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041 239 RRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPKFALHDQLFYLNALEWAASSVEVAAVAA 318
Cdd:pfam07156 265 RRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPPFILHDGLYYLNGIEWAASAMEMSAIAA 344
                         330       340
                  ....*....|....*....|
gi 1958743041 319 KNVALLAYNRWYQDLDKIDQ 338
Cdd:pfam07156 345 KNVALLAYHRWYGNTDKIDQ 364
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
1-338 0e+00

Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are approximately 500 residues long. Prenylcysteine lyase is a FAD-dependent thioether oxidase that degrades a variety of prenylcysteines, producing free cysteine, an isoprenoid aldehyde and hydrogen peroxide as products of the reaction. It has been noted that this enzyme has considerable homology with ClP55, a 55 kDa protein that is associated with chloride ion pumps.


Pssm-ID: 462104 [Multi-domain]  Cd Length: 364  Bit Score: 505.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041   1 MWVEEVMEKFMRIYKYQAHGYAFSGTEELLYSLGEATFVNMTQRSVAESLLQVGVTQRFIDDVVSAVLRASYGQSASMPA 80
Cdd:pfam07156  27 MWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAGFSQLFINEIVQAVTRVNYGQSVNING 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041  81 FAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKALYQVGYETDKGNSSDFYDIVVIATPL 159
Cdd:pfam07156 107 FVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTSLYEVTYKTESGTHSDLYDIVVIATPL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041 160 HldNSSSNITFEGFTPPIDDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFANILTTDFPS-FFCSLDNICPVNISASF 238
Cdd:pfam07156 187 H--RKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLATILTTDNPSlFINSISSVSPVNISDNP 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743041 239 RRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPKFALHDQLFYLNALEWAASSVEVAAVAA 318
Cdd:pfam07156 265 RRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPPFILHDGLYYLNGIEWAASAMEMSAIAA 344
                         330       340
                  ....*....|....*....|
gi 1958743041 319 KNVALLAYNRWYQDLDKIDQ 338
Cdd:pfam07156 345 KNVALLAYHRWYGNTDKIDQ 364
 
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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