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Conserved domains on  [gi|166795301|ref|NP_057381|]
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prenylcysteine oxidase 1 precursor [Homo sapiens]

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 ...
 128-494 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: 649.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  128 FEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVEKLLHALGGDDFLGMLNRTLLETLQKAG 207
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  208 FSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSLSCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEktktKYTG 287
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIEL----KQSG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  288 NPTKMYEVVYQIGTETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSRPIDKFGL 367
Cdd:pfam07156 157 GSTSLYEVTYKTESGTHSDLYDIVVIATPLHRKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  368 NTVLTTDNSDLFINSIGIVPSVREKEDPEPS-TDGTYVWKIFSQETLTKAQILKLFLSYDYAVKKPWLAYPHYKPPEKCP 446
Cdd:pfam07156 237 ATILTTDNPSLFINSISSVSPVNISDNPRRKpPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFP 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 166795301  447 SIILHDRLYYLNGIECAASAMEMSAIAAHNAALLAYHRWNGHTDMIDQ 494
Cdd:pfam07156 317 PFILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
Amino_oxidase super family cl38049
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 48-112 5.62e-09

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


The actual alignment was detected with superfamily member pfam01593:

Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 58.27  E-value: 5.62e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166795301   48 SAAYYLrQKFGKDVKIdlFE-REEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQ 112
Cdd:pfam01593   5 AAAREL-LRAGHDVTV--LEaRDRVGGRIRTVRDDGFLIELGAMWFHGAQPPLLALLKELGLEDRL 67
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
 128-494 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: 649.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  128 FEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVEKLLHALGGDDFLGMLNRTLLETLQKAG 207
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  208 FSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSLSCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEktktKYTG 287
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIEL----KQSG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  288 NPTKMYEVVYQIGTETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSRPIDKFGL 367
Cdd:pfam07156 157 GSTSLYEVTYKTESGTHSDLYDIVVIATPLHRKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  368 NTVLTTDNSDLFINSIGIVPSVREKEDPEPS-TDGTYVWKIFSQETLTKAQILKLFLSYDYAVKKPWLAYPHYKPPEKCP 446
Cdd:pfam07156 237 ATILTTDNPSLFINSISSVSPVNISDNPRRKpPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFP 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 166795301  447 SIILHDRLYYLNGIECAASAMEMSAIAAHNAALLAYHRWNGHTDMIDQ 494
Cdd:pfam07156 317 PFILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 48-112 5.62e-09

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 58.27  E-value: 5.62e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166795301   48 SAAYYLrQKFGKDVKIdlFE-REEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQ 112
Cdd:pfam01593   5 AAAREL-LRAGHDVTV--LEaRDRVGGRIRTVRDDGFLIELGAMWFHGAQPPLLALLKELGLEDRL 67
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 48-108 2.19e-05

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 46.75  E-value: 2.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166795301  48 SAAYYLRQkfgKDVKIDLFEREE-VGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGL 108
Cdd:COG1232   15 TAAYRLAK---AGHEVTVLEASDrVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGL 73
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
48-204 2.72e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 40.29  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  48 SAAYYLRQKfGKDVKIdlFE-REEVGGRLAT--MMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLS---AVQASGGLLGIY 121
Cdd:COG1231   21 AAARELRKA-GLDVTV--LEaRDRVGGRVWTlrFGDDGLYAELGAMRIPPSHTNLLALARELGLPlepFPNENGNALLYL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301 122 NGETLVFEESNWFIINVIKLVWRYG---FQSLRMHMWVEDVLDKfMRIYRYQSHDYAFSSVEKLLHALGGDDFLGMLNR- 197
Cdd:COG1231   98 GGKRVRAGEIAADLRGVAELLAKLLralAAALDPWAHPAAELDR-ESLAEWLRRNGASPSARRLLGLLGAGEYGADPDEl 176


                 ....*..
gi 166795301 198 TLLETLQ 204
Cdd:COG1231  177 SLLDLLR 183
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
 128-494 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: 649.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  128 FEESNWFIINVIKLVWRYGFQSLRMHMWVEDVLDKFMRIYRYQSHDYAFSSVEKLLHALGGDDFLGMLNRTLLETLQKAG 207
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  208 FSEKFLNEMIAPVMRVNYGQSTDINAFVGAVSLSCSDSGLWAVEGGNKLVCSGLLQASKSNLISGSVMYIEEktktKYTG 287
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIEL----KQSG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  288 NPTKMYEVVYQIGTETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLVKGELNTSIFSSRPIDKFGL 367
Cdd:pfam07156 157 GSTSLYEVTYKTESGTHSDLYDIVVIATPLHRKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  368 NTVLTTDNSDLFINSIGIVPSVREKEDPEPS-TDGTYVWKIFSQETLTKAQILKLFLSYDYAVKKPWLAYPHYKPPEKCP 446
Cdd:pfam07156 237 ATILTTDNPSLFINSISSVSPVNISDNPRRKpPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFP 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 166795301  447 SIILHDRLYYLNGIECAASAMEMSAIAAHNAALLAYHRWNGHTDMIDQ 494
Cdd:pfam07156 317 PFILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 48-112 5.62e-09

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 58.27  E-value: 5.62e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 166795301   48 SAAYYLrQKFGKDVKIdlFE-REEVGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLSAVQ 112
Cdd:pfam01593   5 AAAREL-LRAGHDVTV--LEaRDRVGGRIRTVRDDGFLIELGAMWFHGAQPPLLALLKELGLEDRL 67
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 48-108 2.19e-05

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 46.75  E-value: 2.19e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 166795301  48 SAAYYLRQkfgKDVKIDLFEREE-VGGRLATMMVQGQEYEAGGSVIHPLNLHMKRFVKDLGL 108
Cdd:COG1232   15 TAAYRLAK---AGHEVTVLEASDrVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGL 73
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
48-204 2.72e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 40.29  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301  48 SAAYYLRQKfGKDVKIdlFE-REEVGGRLAT--MMVQGQEYEAGGSVIHPLNLHMKRFVKDLGLS---AVQASGGLLGIY 121
Cdd:COG1231   21 AAARELRKA-GLDVTV--LEaRDRVGGRVWTlrFGDDGLYAELGAMRIPPSHTNLLALARELGLPlepFPNENGNALLYL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 166795301 122 NGETLVFEESNWFIINVIKLVWRYG---FQSLRMHMWVEDVLDKfMRIYRYQSHDYAFSSVEKLLHALGGDDFLGMLNR- 197
Cdd:COG1231   98 GGKRVRAGEIAADLRGVAELLAKLLralAAALDPWAHPAAELDR-ESLAEWLRRNGASPSARRLLGLLGAGEYGADPDEl 176


                 ....*..
gi 166795301 198 TLLETLQ 204
Cdd:COG1231  177 SLLDLLR 183
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
45-106 9.64e-03

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 34.81  E-value: 9.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 166795301   45 GGTSAAYYLRQkfgKDVKIDLFE-REEVGGRLATMMVQGQEYEAGGSVIHPLN-LHMKRFVKDL 106
Cdd:pfam13450   7 AGLVAAALLAK---RGFRVLVLEkRDRLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLDEL 67
 
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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