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Conserved domains on  [gi|1952961072|ref|XP_038407474|]
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prenylcysteine oxidase 1 isoform X1 [Canis lupus familiaris]

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: 641.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 128 FEESSWFIMNMIKLIWHYGFQSLRMHMWVEDILDKFMRIYRYQSHDYAFSSVERLLHSLGGDEFLGMLNRTLLETLQKAG 207
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 208 FSEKFLDEIVAPVMRVNYGQSMNINGFVGAVSMSCADSGLWAVQGGNKLVCSGLLRASRSNLIAGSVLYIEEktrtKHTG 287
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIEL----KQSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 288 NPAKMYEVIYQSGPETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLIKGQLNSTLFSSRALDKFDL 367
Cdd:pfam07156 157 GSTSLYEVTYKTESGTHSDLYDIVVIATPLHRKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 368 STILTTDNSDLFINSIGIVSSVTENDSPQP-LGDRGYVWKIFSQEILTKEQILKLFLSYDYAVKQPWLAYPHYRPPEKCP 446
Cdd:pfam07156 237 ATILTTDNPSLFINSISSVSPVNISDNPRRkPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFP 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1952961072 447 SIILHDRLYYLNGIECAASAMEMSAIAAHNAALLAYHRWNGHTDMIDQ 494
Cdd:pfam07156 317 PFILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
HemY super family cl34197
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
48-108 1.59e-06

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


The actual alignment was detected with superfamily member COG1232:

Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 50.60  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952961072  48 SAAYYLRQkfgKDVKIDVFERGE-VGGRLATVTVRGQEYEAGGSVIHPLNLHMKRFVKDLGL 108
Cdd:COG1232    15 TAAYRLAK---AGHEVTVLEASDrVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGL 73
 
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: 641.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 128 FEESSWFIMNMIKLIWHYGFQSLRMHMWVEDILDKFMRIYRYQSHDYAFSSVERLLHSLGGDEFLGMLNRTLLETLQKAG 207
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 208 FSEKFLDEIVAPVMRVNYGQSMNINGFVGAVSMSCADSGLWAVQGGNKLVCSGLLRASRSNLIAGSVLYIEEktrtKHTG 287
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIEL----KQSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 288 NPAKMYEVIYQSGPETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLIKGQLNSTLFSSRALDKFDL 367
Cdd:pfam07156 157 GSTSLYEVTYKTESGTHSDLYDIVVIATPLHRKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 368 STILTTDNSDLFINSIGIVSSVTENDSPQP-LGDRGYVWKIFSQEILTKEQILKLFLSYDYAVKQPWLAYPHYRPPEKCP 446
Cdd:pfam07156 237 ATILTTDNPSLFINSISSVSPVNISDNPRRkPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFP 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1952961072 447 SIILHDRLYYLNGIECAASAMEMSAIAAHNAALLAYHRWNGHTDMIDQ 494
Cdd:pfam07156 317 PFILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
48-108 1.59e-06

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: 50.60  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952961072  48 SAAYYLRQkfgKDVKIDVFERGE-VGGRLATVTVRGQEYEAGGSVIHPLNLHMKRFVKDLGL 108
Cdd:COG1232    15 TAAYRLAK---AGHEVTVLEASDrVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGL 73
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
48-204 5.99e-06

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 48.76  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072  48 SAAYYLRQKfGKDVKidVFE-RGEVGGRLATVTV--RGQEYEAGGSVIHPLNLHMKRFVKDLGLSTV---QSSGGLLGVY 121
Cdd:COG1231    21 AAARELRKA-GLDVT--VLEaRDRVGGRVWTLRFgdDGLYAELGAMRIPPSHTNLLALARELGLPLEpfpNENGNALLYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 122 NGETLVFEESSWFIMNMIKLIWHYG---FQSLRMHMWVEDILDKfMRIYRYQSHDYAFSSVERLLHSLGGDEFLGMLNR- 197
Cdd:COG1231    98 GGKRVRAGEIAADLRGVAELLAKLLralAAALDPWAHPAAELDR-ESLAEWLRRNGASPSARRLLGLLGAGEYGADPDEl 176

                  ....*..
gi 1952961072 198 TLLETLQ 204
Cdd:COG1231   177 SLLDLLR 183
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
45-106 3.98e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 38.67  E-value: 3.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952961072  45 GGTSAAYYLRQkfgKDVKIDVFERGE-VGGRLATVTVRGQEYEAGGSVIHPLN-LHMKRFVKDL 106
Cdd:pfam13450   7 AGLVAAALLAK---RGFRVLVLEKRDrLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLDEL 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: 641.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 128 FEESSWFIMNMIKLIWHYGFQSLRMHMWVEDILDKFMRIYRYQSHDYAFSSVERLLHSLGGDEFLGMLNRTLLETLQKAG 207
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 208 FSEKFLDEIVAPVMRVNYGQSMNINGFVGAVSMSCADSGLWAVQGGNKLVCSGLLRASRSNLIAGSVLYIEEktrtKHTG 287
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIEL----KQSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 288 NPAKMYEVIYQSGPETRSDFYDIVLVATPLNRKMSNITFLNFDPPIEEFHQYYQHIVTTLIKGQLNSTLFSSRALDKFDL 367
Cdd:pfam07156 157 GSTSLYEVTYKTESGTHSDLYDIVVIATPLHRKMSNITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 368 STILTTDNSDLFINSIGIVSSVTENDSPQP-LGDRGYVWKIFSQEILTKEQILKLFLSYDYAVKQPWLAYPHYRPPEKCP 446
Cdd:pfam07156 237 ATILTTDNPSLFINSISSVSPVNISDNPRRkPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFP 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1952961072 447 SIILHDRLYYLNGIECAASAMEMSAIAAHNAALLAYHRWNGHTDMIDQ 494
Cdd:pfam07156 317 PFILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
48-338 4.19e-12

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: 67.90  E-value: 4.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072  48 SAAYYLrQKFGKDVKidVFE-RGEVGGRLATVTVRGQEYEAGGSVIHPLNLHMKRFVKDLGLSTVQSSG----------G 116
Cdd:pfam01593   5 AAAREL-LRAGHDVT--VLEaRDRVGGRIRTVRDDGFLIELGAMWFHGAQPPLLALLKELGLEDRLVLPdpapfytvlfA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 117 LLGVYNG---------ETLVFEESSWFIMNMIKLiwhyGFQSLRMHMWVEDILDKFmriyryqSHDYAFSSVERllHSLG 187
Cdd:pfam01593  82 GGRRYPGdfrrvpagwEGLLEFGRLLSIPEKLRL----GLAALASDALDEFDLDDF-------SLAESLLFLGR--RGPG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 188 GDEflgMLNRTLLETLQKAG--FSEKFLDEIVAPVMRVNYGQSMNINGFVGavsmscadsGLWAVQGGNklvcSGLLRAS 265
Cdd:pfam01593 149 DVE---VWDRLIDPELFAALpfASGAFAGDPSELSAGLALPLLWALLGEGG---------SLLLPRGGL----GALPDAL 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952961072 266 RSNLIAGSVLYieektRTKHTG--NPAKMYEVIYQSGPETRSDFydiVLVATPLnRKMSNItflNFDPPIEEFHQ 338
Cdd:pfam01593 213 AAQLLGGDVRL-----NTRVRSidREGDGVTVTLTDGEVIEADA---VIVTVPL-GVLKRI---LFTPPLPPEKA 275
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
48-108 1.59e-06

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: 50.60  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1952961072  48 SAAYYLRQkfgKDVKIDVFERGE-VGGRLATVTVRGQEYEAGGSVIHPLNLHMKRFVKDLGL 108
Cdd:COG1232    15 TAAYRLAK---AGHEVTVLEASDrVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGL 73
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
48-204 5.99e-06

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 48.76  E-value: 5.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072  48 SAAYYLRQKfGKDVKidVFE-RGEVGGRLATVTV--RGQEYEAGGSVIHPLNLHMKRFVKDLGLSTV---QSSGGLLGVY 121
Cdd:COG1231    21 AAARELRKA-GLDVT--VLEaRDRVGGRVWTLRFgdDGLYAELGAMRIPPSHTNLLALARELGLPLEpfpNENGNALLYL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952961072 122 NGETLVFEESSWFIMNMIKLIWHYG---FQSLRMHMWVEDILDKfMRIYRYQSHDYAFSSVERLLHSLGGDEFLGMLNR- 197
Cdd:COG1231    98 GGKRVRAGEIAADLRGVAELLAKLLralAAALDPWAHPAAELDR-ESLAEWLRRNGASPSARRLLGLLGAGEYGADPDEl 176

                  ....*..
gi 1952961072 198 TLLETLQ 204
Cdd:COG1231   177 SLLDLLR 183
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
45-106 3.98e-04

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 38.67  E-value: 3.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1952961072  45 GGTSAAYYLRQkfgKDVKIDVFERGE-VGGRLATVTVRGQEYEAGGSVIHPLN-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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