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Conserved domains on  [gi|27370248|ref|NP_766420|]
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prenylcysteine oxidase-like isoform 1 precursor [Mus musculus]

Protein Classification

prenylcysteine oxidase family protein( domain architecture ID 10602892)

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 ...
120-484 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: 597.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   120 LEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGVEELLYSLGEATFVNMTQRSVAESLLQVG 199
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   200 VTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKA 278
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   279 LYQVAYESDKGNSSDFYDIVVIATPLHLDNSsnnNITFEGFTPPIEDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFA 358
Cdd:pfam07156 161 LYEVTYKTESGTHSDLYDIVVIATPLHRKMS---NITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   359 NILTTDFPS-FFCTLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPR 437
Cdd:pfam07156 238 TILTTDNPSlFINSISSVSPVNISDNPRRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPP 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 27370248   438 FALHDQLFYLNALEWAASSVEVTAVAAKNVALLAYNRWYQDLDKIDQ 484
Cdd:pfam07156 318 FILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
31-96 2.69e-09

NAD(P)-binding Rossmann-like domain;


:

Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.30  E-value: 2.69e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370248    31 VIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLS-LHMQDFVK 96
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKR---GFRVLVLEKRDrLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLD 65
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
120-484 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: 597.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   120 LEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGVEELLYSLGEATFVNMTQRSVAESLLQVG 199
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   200 VTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKA 278
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   279 LYQVAYESDKGNSSDFYDIVVIATPLHLDNSsnnNITFEGFTPPIEDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFA 358
Cdd:pfam07156 161 LYEVTYKTESGTHSDLYDIVVIATPLHRKMS---NITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   359 NILTTDFPS-FFCTLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPR 437
Cdd:pfam07156 238 TILTTDNPSlFINSISSVSPVNISDNPRRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPP 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 27370248   438 FALHDQLFYLNALEWAASSVEVTAVAAKNVALLAYNRWYQDLDKIDQ 484
Cdd:pfam07156 318 FILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
28-305 1.55e-09

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: 59.85  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHfgpRVQIVVYEKG-TVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREV 106
Cdd:COG1232   3 RVAVIGGGIAGLTAAYRLAKA---GHEVTVLEASdRVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGLGDELVW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 107 V--GRSAIF-GGEHFVLEETDWYLL--NLFRLW--WYYGISFLRLQMWVEEVMEkfmriykyqahgyafsgVEELLYS-L 178
Cdd:COG1232  80 PntRKSYIYyGGKLHPLPQGPLALLrsPLLSLAgkLRALLELLAPRRPPGEDES-----------------LAEFVRRrF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 179 GEatfvnmtqrsvaesllqvGVTQRFIDDVVSAVlrasYGQSAS-------MPAFAGAM----SL----------AGAQG 237
Cdd:COG1232 143 GR------------------EVYERLVEPLLEGV----YAGDPDelsadwaFPRLKRLElehgSLikgalalrkgAKAGE 200
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 238 NLWSVEGGNKLVCSGLLKLAKATVIH--ATVTSVTLHSTEgkalYQVAYESDKgnsSDFYDIVVIATPLH 305
Cdd:COG1232 201 VFGYLRGGLGTLVEALAEALEAGEIRlgTRVTAIEREGGG----WRVTTSDGE---TIEADAVVSATPAP 263
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
31-96 2.69e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.30  E-value: 2.69e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370248    31 VIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLS-LHMQDFVK 96
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKR---GFRVLVLEKRDrLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLD 65
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
28-124 1.29e-08

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 56.42  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLglrQRREV 106
Cdd:COG3380   5 DIAIIGAGIAGLAAARALQDA---GHEVTVFEKSRgVGGRMATRRLDGGRFDHGAQYFTARDPRFQALVEEW---LAAGL 78
                        90       100
                ....*....|....*....|..
gi 27370248 107 V----GRSAIFGGEHFVLEETD 124
Cdd:COG3380  79 VapwtFDFVVLDADGLVSPRDD 100
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
28-113 1.09e-06

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 51.00  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   28 KIAVIGAGIGGSAVAHFLQQHFgPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL--RQRR 104
Cdd:PRK11883   2 KVAIIGGGITGLSAAYRLHKKG-PDADITLLEASDrLGGKIQTVRKDGFPIELGPESFLARKPSAPALVKELGLedELVA 80

                 ....*....
gi 27370248  105 EVVGRSAIF 113
Cdd:PRK11883  81 NTTGQSYIY 89
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
28-100 6.50e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 48.68  E-value: 6.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370248    28 KIAVIGAGIGGSAVAHFL-QQHFGPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL 100
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLeKEIPELPVELTLVEASDrVGGKIQTVKEDGYLIERGPDSFLERKKSAPDLVKDLGL 78
 
Name Accession Description Interval E-value
Prenylcys_lyase pfam07156
Prenylcysteine lyase; This family contains prenylcysteine lyases (EC:1.8.3.5) that are ...
120-484 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: 597.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   120 LEETDWYLLNLFRLWWYYGISFLRLQMWVEEVMEKFMRIYKYQAHGYAFSGVEELLYSLGEATFVNMTQRSVAESLLQVG 199
Cdd:pfam07156   1 FEESSWSWINLAKLLWRYGFSPLRMQMWVEDILDKFMRIYEYQAHGYAFSSVEELLHALGGDGFLNLTNQTLEEALLKAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   200 VTQRFIDDVVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIHATVTSVTL-HSTEGKA 278
Cdd:pfam07156  81 FSQLFINEIVQAVTRVNYGQSVNINGFVGAVSLAGAQSGLWAVEGGNKLVCSGLLKASKANLINGTVTSIELkQSGGSTS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   279 LYQVAYESDKGNSSDFYDIVVIATPLHLDNSsnnNITFEGFTPPIEDIQGSFQPTVVSLVHGYLNSSYFGFPDPKLFPFA 358
Cdd:pfam07156 161 LYEVTYKTESGTHSDLYDIVVIATPLHRKMS---NITFDNFSPPIPEFPGPYQHTVATLVHGRLNPSYFGLPDPSLFPLA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   359 NILTTDFPS-FFCTLDNICPVNISASFRRKQPQEAAVWRVQSPKPLFRTELKTLFRSYYSVQTAEWQAHPLYGSRRTLPR 437
Cdd:pfam07156 238 TILTTDNPSlFINSISSVSPVNISDNPRRKPPKEAAVWKIFSPEPLSKEQLKSLFSSYDSVQEKDWLAYPHYSPPETFPP 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 27370248   438 FALHDQLFYLNALEWAASSVEVTAVAAKNVALLAYNRWYQDLDKIDQ 484
Cdd:pfam07156 318 FILHDGLYYLNGIEWAASAMEMSAIAAKNVALLAYHRWYGNTDKIDQ 364
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
28-305 1.55e-09

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: 59.85  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHfgpRVQIVVYEKG-TVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREV 106
Cdd:COG1232   3 RVAVIGGGIAGLTAAYRLAKA---GHEVTVLEASdRVGGLIRTVEVDGFRIDRGPHSFLTRDPEVLELLRELGLGDELVW 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 107 V--GRSAIF-GGEHFVLEETDWYLL--NLFRLW--WYYGISFLRLQMWVEEVMEkfmriykyqahgyafsgVEELLYS-L 178
Cdd:COG1232  80 PntRKSYIYyGGKLHPLPQGPLALLrsPLLSLAgkLRALLELLAPRRPPGEDES-----------------LAEFVRRrF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 179 GEatfvnmtqrsvaesllqvGVTQRFIDDVVSAVlrasYGQSAS-------MPAFAGAM----SL----------AGAQG 237
Cdd:COG1232 143 GR------------------EVYERLVEPLLEGV----YAGDPDelsadwaFPRLKRLElehgSLikgalalrkgAKAGE 200
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 238 NLWSVEGGNKLVCSGLLKLAKATVIH--ATVTSVTLHSTEgkalYQVAYESDKgnsSDFYDIVVIATPLH 305
Cdd:COG1232 201 VFGYLRGGLGTLVEALAEALEAGEIRlgTRVTAIEREGGG----WRVTTSDGE---TIEADAVVSATPAP 263
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
31-96 2.69e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.30  E-value: 2.69e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27370248    31 VIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLS-LHMQDFVK 96
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKR---GFRVLVLEKRDrLGGNAYSYRVPGYVFDYGAHIFHGSDePNVRDLLD 65
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
28-124 1.29e-08

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 56.42  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHfgpRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLglrQRREV 106
Cdd:COG3380   5 DIAIIGAGIAGLAAARALQDA---GHEVTVFEKSRgVGGRMATRRLDGGRFDHGAQYFTARDPRFQALVEEW---LAAGL 78
                        90       100
                ....*....|....*....|..
gi 27370248 107 V----GRSAIFGGEHFVLEETD 124
Cdd:COG3380  79 VapwtFDFVVLDADGLVSPRDD 100
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
28-113 1.09e-06

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 51.00  E-value: 1.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   28 KIAVIGAGIGGSAVAHFLQQHFgPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL--RQRR 104
Cdd:PRK11883   2 KVAIIGGGITGLSAAYRLHKKG-PDADITLLEASDrLGGKIQTVRKDGFPIELGPESFLARKPSAPALVKELGLedELVA 80

                 ....*....
gi 27370248  105 EVVGRSAIF 113
Cdd:PRK11883  81 NTTGQSYIY 89
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
24-306 1.62e-06

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 50.30  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248  24 APPGKIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEKGT-VGGRLATISVNKQNY--ESGAASFHSLSLHMQDFVKLLGL 100
Cdd:COG1231   5 ARGKDVVIVGAGLAGLAAARELRKA-GLDV--TVLEARDrVGGRVWTLRFGDDGLyaELGAMRIPPSHTNLLALARELGL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 101 --RQRREVVGRSAI-FGGEHFVLEETDWYLLNLFRLWWyygisflrlqmWVEEVMEKFMRIYKYQAHGYafsgveellys 177
Cdd:COG1231  82 plEPFPNENGNALLyLGGKRVRAGEIAADLRGVAELLA-----------KLLRALAAALDPWAHPAAEL----------- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 178 lgeatfvnmTQRSVAESLLQVGVTQRFIdDVVSAVLRASYGQSA---SMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLL 254
Cdd:COG1231 140 ---------DRESLAEWLRRNGASPSAR-RLLGLLGAGEYGADPdelSLLDLLRYAASAGGGAQQFRIVGGMDQLPRALA 209
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 255 KLAKATVIHAT-VTS-------VTLHSTEGKALYqvayesdkgnssdfYDIVVIATPLHL 306
Cdd:COG1231 210 AELGDRIRLGApVTRirqdgdgVTVTTDDGGTVR--------------ADAVIVTVPPSV 255
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
28-306 1.93e-06

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 50.23  E-value: 1.93e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEK-GTVGGRLATISVNKQNYESGaASFHSLSLHMQDFVKLLGLRQ---- 102
Cdd:COG1233   5 DVVVIGAGIGGLAAAALLARA-GYRV--TVLEKnDTPGGRARTFERPGFRFDVG-PSVLTMPGVLERLFRELGLEDylel 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 103 -RREVVGRSAIFGGEHFVLEETDWYLLNLFRlwwyyGIS------FLRLQMWVEEVMEKFMRIYKYQahgyAFSGVEELL 175
Cdd:COG1233  81 vPLDPAYRVPFPDGRALDLPRDLERTAAELE-----RLFpgdaeaYRRFLAELRRLYDALLEDLLYR----PLLSLRDLL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248 176 YSLGEATFVNMTQRSVAESLlqvgvTQRFIDDVVSAVLRAS---YGQSA-SMPAFAGAMSLAGAQGNLWSVEGGNKLVCS 251
Cdd:COG1233 152 RPLALARLLRLLLRSLRDLL-----RRYFKDPRLRALLAGQalyLGLSPdRTPALYALIAYLEYAGGVWYPKGGMGALAD 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27370248 252 GLLKLAKAT--VIH--ATVTSVTlhsTEGKALYQVAYEsdkgNSSDFY-DIVVI-ATPLHL 306
Cdd:COG1233 227 ALARLAEELggEIRtgAEVERIL---VEGGRATGVRLA----DGEEIRaDAVVSnADPAHT 280
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
28-100 6.50e-06

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 48.68  E-value: 6.50e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27370248    28 KIAVIGAGIGGSAVAHFL-QQHFGPRVQIVVYEKGT-VGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGL 100
Cdd:TIGR00562   4 HVVIIGGGISGLCAAYYLeKEIPELPVELTLVEASDrVGGKIQTVKEDGYLIERGPDSFLERKKSAPDLVKDLGL 78
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
28-72 1.07e-05

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 47.80  E-value: 1.07e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHFgprvQIVVYEKGT-VGGRLATISV 72
Cdd:COG2907   5 RIAVIGSGISGLTAAWLLSRRH----DVTLFEANDrLGGHTHTVDV 46
PLN02576 PLN02576
protoporphyrinogen oxidase
19-84 4.91e-05

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 45.77  E-value: 4.91e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27370248   19 AAGGDAPPGKIAVIGAGIGGSAVAHFLQQHFGPRVqiVVYE-KGTVGGRLATISVNKQNYESGAASF 84
Cdd:PLN02576   5 EGSAAASSKDVAVVGAGVSGLAAAYALASKHGVNV--LVTEaRDRVGGNITSVSEDGFIWEEGPNSF 69
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
36-379 5.44e-05

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: 45.56  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248    36 IGGSAVAHFLQQHfGPRVqiVVYE-KGTVGGRLATISVNKQNYESGAASFHSLSLHMQDFVKLLGLRQRREV----VGRS 110
Cdd:pfam01593   1 LAGLAAARELLRA-GHDV--TVLEaRDRVGGRIRTVRDDGFLIELGAMWFHGAQPPLLALLKELGLEDRLVLpdpaPFYT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   111 AIFGGEHFVLEEtdwyLLNLFRLWWYYgISFLRLQMWVEEVmeKFMRIykyqAHGYAFSGVEELLyslgEATFVNMTQRS 190
Cdd:pfam01593  78 VLFAGGRRYPGD----FRRVPAGWEGL-LEFGRLLSIPEKL--RLGLA----ALASDALDEFDLD----DFSLAESLLFL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   191 VAESLLQVGVTQRFIDD-------VVSAVLRASYGQSASMPAFAGAMSLAGAQGNLWSVEGGNKLVCSGLLKLAKATVIH 263
Cdd:pfam01593 143 GRRGPGDVEVWDRLIDPelfaalpFASGAFAGDPSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAQLLGGDVR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248   264 --ATVTSVTLHSTEgkalYQVAYESDKGNSSDFydiVVIATPLhldnssnNNITFEGFTPPIED-----IQGSFQPTVVS 336
Cdd:pfam01593 223 lnTRVRSIDREGDG----VTVTLTDGEVIEADA---VIVTVPL-------GVLKRILFTPPLPPekaraIRNLGYGPVNK 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 27370248   337 LVHGYlnSSYFgFPDPKLFPFANILTTDFPS-FFCTLDNICPVN 379
Cdd:pfam01593 289 VHLEF--DRKF-WPDLGLLGLLSELLTGLGTaFSWLTFPNRAPP 329
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
28-65 1.93e-03

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 40.27  E-value: 1.93e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHfGprVQIVVYEKGTVGG 65
Cdd:COG0665   4 DVVVIGGGIAGLSTAYHLARR-G--LDVTVLERGRPGS 38
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
29-65 2.22e-03

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 40.23  E-value: 2.22e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 27370248  29 IAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEKGT-VGG 65
Cdd:COG2072   9 VVVIGAGQAGLAAAYHLRRA-GIDF--VVLEKADdVGG 43
PRK07233 PRK07233
hypothetical protein; Provisional
28-69 3.49e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 39.87  E-value: 3.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 27370248   28 KIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEK-GTVGGRLAT 69
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKR-GHEV--TVFEAdDQLGGLAAS 40
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
28-128 5.58e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 38.92  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27370248    28 KIAVIGAGIGGSAVAHFLQQHfGPRVqiVVYEKGTVGGRlATISVNkqnyeSGAASFHSLSLHMQDFVKL--LGLRQRRE 105
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARR-GLSV--TLLERGDDPGS-GASGRN-----AGLIHPGLRYLEPSELARLalEALDLWEE 71
                          90       100
                  ....*....|....*....|...
gi 27370248   106 VVGRSAIfggeHFVLEETDWYLL 128
Cdd:pfam01266  72 LEEELGI----DCGFRRCGVLVL 90
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
28-60 7.92e-03

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 38.38  E-value: 7.92e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 27370248  28 KIAVIGAGIGGSAVAHFLQQHFgprVQIVVYEK 60
Cdd:COG0654   5 DVLIVGGGPAGLALALALARAG---IRVTVVER 34
 
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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