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Conserved domains on  [gi|532691798|ref|NP_001269172|]
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cytochrome P450 19A1-like [Chrysemys picta bellii]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
71-484 0e+00

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


:

Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 846.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  71 NACNYYNKMYGEFMRVWISGEETLIISKSSSIFHVMKHGQYICRFGSKLGLQCIGMHENGIIFNNNPALWKEIRPFFTKA 150
Cdd:cd20616    1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 151 LSGPGLVRMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPLDENAIVLKIQNYFDAWQALLLKP 230
Cdd:cd20616   81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 DIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTL 310
Cdd:cd20616  161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 311 SVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRG 390
Cdd:cd20616  241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 391 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNI 470
Cdd:cd20616  321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                        410
                 ....*....|....
gi 532691798 471 QKSNDLSMHPNERQ 484
Cdd:cd20616  401 QKTNDLSLHPDETQ 414
 
Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
71-484 0e+00

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 846.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  71 NACNYYNKMYGEFMRVWISGEETLIISKSSSIFHVMKHGQYICRFGSKLGLQCIGMHENGIIFNNNPALWKEIRPFFTKA 150
Cdd:cd20616    1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 151 LSGPGLVRMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPLDENAIVLKIQNYFDAWQALLLKP 230
Cdd:cd20616   81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 DIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTL 310
Cdd:cd20616  161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 311 SVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRG 390
Cdd:cd20616  241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 391 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNI 470
Cdd:cd20616  321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                        410
                 ....*....|....
gi 532691798 471 QKSNDLSMHPNERQ 484
Cdd:cd20616  401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-480 8.76e-113

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 341.57  E-value: 8.76e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798   47 PGPGFCMGIGPLISHgrflWMGMGNACNYYNKMYGEFMRVWISGEETLIISKSSSIFHVMKH-GQYICRFGSKLGL-QCI 124
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKkGEEFSGRPDEPWFaTSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  125 GMHENGIIFNNNPALWKEIRPFFTKALSGPGLVRMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLG 204
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  205 IPLD------ENAIVLKIQNYFD-----AWQALLLKPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKleE 273
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  274 HMDFASQLIFAQ---SRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD-RDVQSNDM 349
Cdd:pfam00067 238 PRDFLDALLLAKeeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  350 SNLKVVENFINESMRYQPVVD-LVMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPS 423
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 532691798  424 RYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNIQKSNDLSMHP 480
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPP 454
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
80-458 6.71e-40

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 148.89  E-value: 6.71e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  80 YGEFMRVWISGEETLIISKSSSIFHVMKHGQyicRFGSKLGLQCIGMHEN---GIIFNNNPALWKEIRPFFTKALSGPGL 156
Cdd:COG2124   31 YGPVFRVRLPGGGAWLVTRYEDVREVLRDPR---TFSSDGGLPEVLRPLPllgDSLLTLDGPEHTRLRRLVQPAFTPRRV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 157 VRMIAICVESTKDHLDRLEDVtaglGNINVLNFMRQITLDTSNTLFLGIPLDENAivlKIQNYFDAWQALLLKPDIffki 236
Cdd:COG2124  108 AALRPRIREIADELLDRLAAR----GPVDLVEEFARPLPVIVICELLGVPEEDRD---RLRRWSDALLDALGPLPP---- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 237 sWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTvekleehmDFASQLIFAQSRGD-LTGENV-NQCVLeMMIAAPDTLSVTL 314
Cdd:COG2124  177 -ERRRRARRARAELDAYLRELIAERRAEPGD--------DLLSALLAARDDGErLSDEELrDELLL-LLLAGHETTANAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 315 FFMLVLIAEHPKVEEDMMKEiqavigdrdvqsndmsnLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNII 394
Cdd:COG2124  247 AWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVL 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532691798 395 LNIGRMHKLE-FFPKPNEFSLENfeknVPSRYFqPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:COG2124  310 LSLAAANRDPrVFPDPDRFDPDR----PPNAHL-PFGGGPHRCLGAALARLEARIALATLLRRFP 369
PLN02738 PLN02738
carotene beta-ring hydroxylase
232-464 6.05e-24

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 105.38  E-value: 6.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 232 IFFKISWLYKKYEKSVKDLKEAIEVLIEQKRqRLSTVEKLEEHMDFA-----SQLIFAQSRGD-LTGENVNQCVLEMMIA 305
Cdd:PLN02738 324 IWKDISPRQRKVAEALKLINDTLDDLIAICK-RMVEEEELQFHEEYMnerdpSILHFLLASGDdVSSKQLRDDLMTMLIA 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 306 APDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGY 385
Cdd:PLN02738 403 GHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGY 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 386 PVKRGTNIILNIGRMHK-------LEFF---------PKPNEfSLENFeknvpsRYFqPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:PLN02738 483 PIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNF------SYL-PFGGGPRKCVGDMFASFENVVA 554
                        250
                 ....*....|....*
gi 532691798 450 LVTLLRRYRVQTPKG 464
Cdd:PLN02738 555 TAMLVRRFDFQLAPG 569
 
Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
71-484 0e+00

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 846.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  71 NACNYYNKMYGEFMRVWISGEETLIISKSSSIFHVMKHGQYICRFGSKLGLQCIGMHENGIIFNNNPALWKEIRPFFTKA 150
Cdd:cd20616    1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 151 LSGPGLVRMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPLDENAIVLKIQNYFDAWQALLLKP 230
Cdd:cd20616   81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 DIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTL 310
Cdd:cd20616  161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 311 SVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRG 390
Cdd:cd20616  241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 391 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNI 470
Cdd:cd20616  321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                        410
                 ....*....|....
gi 532691798 471 QKSNDLSMHPNERQ 484
Cdd:cd20616  401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-480 8.76e-113

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 341.57  E-value: 8.76e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798   47 PGPGFCMGIGPLISHgrflWMGMGNACNYYNKMYGEFMRVWISGEETLIISKSSSIFHVMKH-GQYICRFGSKLGL-QCI 124
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKkGEEFSGRPDEPWFaTSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  125 GMHENGIIFNNNPALWKEIRPFFTKALSGPGLVRMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLG 204
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  205 IPLD------ENAIVLKIQNYFD-----AWQALLLKPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKleE 273
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  274 HMDFASQLIFAQ---SRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD-RDVQSNDM 349
Cdd:pfam00067 238 PRDFLDALLLAKeeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  350 SNLKVVENFINESMRYQPVVD-LVMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPS 423
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 532691798  424 RYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNIQKSNDLSMHP 480
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPP 454
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
81-460 1.95e-64

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 213.92  E-value: 1.95e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  81 GEFMRVWISGEETLIISKSSSIFHVMKHGQYICRFGSkLGLQCIGMHENGIIFNNNPALWKEIRPFFTKALSGPGLVRMI 160
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAG-PGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 161 AICVESTKDHLDRLEDvtAGLGNINVLNFMRQITLDTSNTLFLGIplDENAIVLKIQNYFDAWQALLLKPDIFFKISWLY 240
Cdd:cd00302   80 PVIREIARELLDRLAA--GGEVGDDVADLAQPLALDVIARLLGGP--DLGEDLEELAELLEALLKLLGPRLLRPLPSPRL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 241 KKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQlifaqsrGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVL 320
Cdd:cd00302  156 RRLRRARARLRDYLEELIARRRAEPADDLDLLLLADADDG-------GGLSDEEIVAELLTLLLAGHETTASLLAWALYL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 321 IAEHPKVEEDMMKEIQAVIGDRDVQsnDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRM 400
Cdd:cd00302  229 LARHPEVQERLRAEIDAVLGDGTPE--DLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYAA 306
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532691798 401 HKLE-FFPKPNEFSLENF--EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQ 460
Cdd:cd00302  307 HRDPeVFPDPDEFDPERFlpEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFE 369
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
129-464 1.74e-47

cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of Mycobacterium tuberculosis cytochrome P450 132 (CYP132) and similar proteins. The function of CYP132 is as yet unknown. CYP132 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410713 [Multi-domain]  Cd Length: 406  Bit Score: 169.30  E-value: 1.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 129 NGIIfNNNPALWKEIR----PFFT-KALSGpglvrMIAICVESTKDHLDRLEDvTAGLGNINVLNFMRQITLDT-SNTLF 202
Cdd:cd20620   48 NGLL-TSEGDLWRRQRrlaqPAFHrRRIAA-----YADAMVEATAALLDRWEA-GARRGPVDVHAEMMRLTLRIvAKTLF 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 203 ----------LGIPLDE--NAIVLKIQNYFDAWQALLLKPDiffkiswlyKKYEKSVKDLKEAIEVLIEQKRQRLstvek 270
Cdd:cd20620  121 gtdvegeadeIGDALDValEYAARRMLSPFLLPLWLPTPAN---------RRFRRARRRLDEVIYRLIAERRAAP----- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 271 lEEHMDFASQLIFAQSRGDLTGENVNQC---VLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSN 347
Cdd:cd20620  187 -ADGGDLLSMLLAARDEETGEPMSDQQLrdeVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTAE 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 348 DMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLENFEKNVPSR-- 424
Cdd:cd20620  266 DLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPrFWPDPEAFDPERFTPEREAArp 345
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 532691798 425 ---YFqPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKG 464
Cdd:cd20620  346 ryaYF-PFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPG 387
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
81-482 1.99e-46

cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome P450 families 1 (CYP1) and 2 (CYP2), CYP17A1, and CYP21 in vertebrates, as well as insect and crustacean CYPs similar to CYP15A1 and CYP306A1. CYP1 and CYP2 enzymes are involved in the metabolism of endogenous and exogenous compounds such as hormones, xenobiotics, and drugs. CYP17A1 catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products, while CYP21 catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. Members of this group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 167.00  E-value: 1.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  81 GEFMRVWISGEETLIISKSSSI--FHVMKHGQYICRFGSKLGLqcIGMHENGIIFNNNPaLWKEIRPFFTKALSGPGLVR 158
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIkeAFVKNGDNFSDRPLLPSFE--IISGGKGILFSNGD-YWKELRRFALSSLTKTKLKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 159 -MIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLG--IPLDENAIVLKIQNYFDAWQALLLKPDIFFK 235
Cdd:cd20617   78 kMEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGkrFPDEDDGEFLKLVKPIEEIFKELGSGNPSDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 236 ISWL-------YKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPD 308
Cdd:cd20617  158 IPILlpfyflyLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLFLAGTD 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 309 TLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYP 386
Cdd:cd20617  238 TTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGnDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLgLPRVTTEDTEIGGYF 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 387 VKRGTNIILNIGRMHKLE-FFPKPNEFSLENF---EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTP 462
Cdd:cd20617  318 IPKGTQIIINIYSLHRDEkYFEDPEEFNPERFlenDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFKSS 397
                        410       420
                 ....*....|....*....|.
gi 532691798 463 KgrGLKNIQKSND-LSMHPNE 482
Cdd:cd20617  398 D--GLPIDEKEVFgLTLKPKP 416
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
81-459 3.73e-45

cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the omega-hydroxylation of the terminal carbon of fatty acids, including essential signaling molecules such as eicosanoids, prostaglandins and leukotrienes, and they are important for chemical defense. There are seven vertebrate family 4 subfamilies: CYP4A, CYP4B, CYP4F, CYP4T, CYP4V, CYP4X, and CYP4Z; three (CYP4X, CYP4A, CYP4Z) are specific to mammals. CYP4 enzymes metabolize fatty acids off various length, level of saturation, and branching. Specific subfamilies show preferences for the length of fatty acids; CYP4B, CYP4A and CYP4V, and CYP4F preferentially metabolize short (C7-C10), medium (C10-C16), and long to very long (C18-C26) fatty acid chains, respectively. CYP4 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410721 [Multi-domain]  Cd Length: 426  Bit Score: 163.46  E-value: 3.73e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  81 GEFMRVWISGEETLIISKSSSIFHVMKHGQYICRFGSKLGLQC-IGmheNGIIFNNNPAlWKEIRPFFTKALSGPGLVRM 159
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPwLG---DGLLTSTGEK-WRKRRKLLTPAFHFKILESF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 160 IAICVESTKDHLDRLEDVtAGLGNINVLNFMRQITLDT-SNTLfLGIPLDENAIvlKIQNYFDAWQAL-----------L 227
Cdd:cd20628   77 VEVFNENSKILVEKLKKK-AGGGEFDIFPYISLCTLDIiCETA-MGVKLNAQSN--EDSEYVKAVKRIleiilkrifspW 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 228 LKPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEE---------HMDFASQLIFAQSRGD-LTGENVNQ 297
Cdd:cd20628  153 LRFDFIFRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEeddefgkkkRKAFLDLLLEAHEDGGpLTDEDIRE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 298 CVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD--RDVQSNDMSNLKVVENFINESMRYQPVVDLVMRK 375
Cdd:cd20628  233 EVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 376 ALQDDVIDGYPVKRGTNIILNIGRMHKL-EFFPKPNEFSLENFEK-NVPSRY---FQPFGFGPRGCVG-KFiAMVMMKAI 449
Cdd:cd20628  313 LTEDIKLDGYTIPKGTTVVISIYALHRNpEYFPDPEKFDPDRFLPeNSAKRHpyaYIPFSAGPRNCIGqKF-AMLEMKTL 391
                        410
                 ....*....|
gi 532691798 450 LVTLLRRYRV 459
Cdd:cd20628  392 LAKILRNFRV 401
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
78-464 2.63e-40

cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410677 [Multi-domain]  Cd Length: 426  Bit Score: 150.37  E-value: 2.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  78 KMYGEFMRVWISGEETLIISKSSSIFHVMKH-GQYICRFGSKLgLQCIGMHEN---GIIFNNNPAlWKEIRPFFTKALSG 153
Cdd:cd11054    2 KKYGPIVREKLGGRDIVHLFDPDDIEKVFRNeGKYPIRPSLEP-LEKYRKKRGkplGLLNSNGEE-WHRLRSAVQKPLLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 154 PGLV-RMIAICVESTKDHLDRLEDvTAGLGNINVLNFMRQI---TLDTSNTLFLG---------IPLDENAIVLKIQNYF 220
Cdd:cd11054   80 PKSVaSYLPAINEVADDFVERIRR-LRDEDGEEVPDLEDELykwSLESIGTVLFGkrlgclddnPDSDAQKLIEAVKDIF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 221 DAWQALLLKPDIFFKISW-LYKKYEKSVKDLKEAIEVLIEQKRQRL-STVEKLEEHMDFASQLIfaqSRGDLTGENVNQC 298
Cdd:cd11054  159 ESSAKLMFGPPLWKYFPTpAWKKFVKAWDTIFDIASKYVDEALEELkKKDEEDEEEDSLLEYLL---SKPGLSKKEIVTM 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 299 VLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRD-VQSNDMSNLKVVENFINESMRYQPVVDLVMRKaL 377
Cdd:cd11054  236 ALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEpITAEDLKKMPYLKACIKESLRLYPVAPGNGRI-L 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 378 QDD-VIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLE-----NFEKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:cd11054  315 PKDiVLSGYHIPKGTLVVLSNYVMGRDEeYFPDPEEFIPErwlrdDSENKNIHPFaSLPFGFGPRMCIGRRFAELEMYLL 394
                        410
                 ....*....|....*
gi 532691798 450 LVTLLRRYRVQTPKG 464
Cdd:cd11054  395 LAKLLQNFKVEYHHE 409
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
80-458 6.71e-40

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 148.89  E-value: 6.71e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  80 YGEFMRVWISGEETLIISKSSSIFHVMKHGQyicRFGSKLGLQCIGMHEN---GIIFNNNPALWKEIRPFFTKALSGPGL 156
Cdd:COG2124   31 YGPVFRVRLPGGGAWLVTRYEDVREVLRDPR---TFSSDGGLPEVLRPLPllgDSLLTLDGPEHTRLRRLVQPAFTPRRV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 157 VRMIAICVESTKDHLDRLEDVtaglGNINVLNFMRQITLDTSNTLFLGIPLDENAivlKIQNYFDAWQALLLKPDIffki 236
Cdd:COG2124  108 AALRPRIREIADELLDRLAAR----GPVDLVEEFARPLPVIVICELLGVPEEDRD---RLRRWSDALLDALGPLPP---- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 237 sWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTvekleehmDFASQLIFAQSRGD-LTGENV-NQCVLeMMIAAPDTLSVTL 314
Cdd:COG2124  177 -ERRRRARRARAELDAYLRELIAERRAEPGD--------DLLSALLAARDDGErLSDEELrDELLL-LLLAGHETTANAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 315 FFMLVLIAEHPKVEEDMMKEiqavigdrdvqsndmsnLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNII 394
Cdd:COG2124  247 AWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVL 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532691798 395 LNIGRMHKLE-FFPKPNEFSLENfeknVPSRYFqPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:COG2124  310 LSLAAANRDPrVFPDPDRFDPDR----PPNAHL-PFGGGPHRCLGAALARLEARIALATLLRRFP 369
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
132-480 1.45e-38

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 145.82  E-value: 1.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 132 IFNNNPALWKEIR-----PFFTKALSGpglvrMIAICVESTKDHLDRLEDVtAGLGNINVLNFMRQITLDTSNTLFLGip 206
Cdd:cd11057   47 LFSAPYPIWKLQRkalnpSFNPKILLS-----FLPIFNEEAQKLVQRLDTY-VGGGEFDILPDLSRCTLEMICQTTLG-- 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 207 LDENAIVLKIQNYFDAWQALL-----------LKPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRL---STVEKLE 272
Cdd:cd11057  119 SDVNDESDGNEEYLESYERLFeliakrvlnpwLHPEFIYRLTGDYKEEQKARKILRAFSEKIIEKKLQEVeleSNLDSEE 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 273 EHMDFASQLIF-------AQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRD-- 343
Cdd:cd11057  199 DEENGRKPQIFidqllelARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGqf 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 344 VQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVID-GYPVKRGTNIILNIGRMHKLEFF--PKPNEFSLENFE-K 419
Cdd:cd11057  279 ITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIwgPDADQFDPDNFLpE 358
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532691798 420 NVPSRY---FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPkgRGLKNIQKSNDLSMHP 480
Cdd:cd11057  359 RSAQRHpyaFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTS--LRLEDLRFKFNITLKL 420
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
140-461 2.56e-36

cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 139.26  E-value: 2.56e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 140 WKEIRPFFTKALSGPGLVRMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPLD-----ENAIVL 214
Cdd:cd11055   60 WKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDsqnnpDDPFLK 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 215 KIQNYFDAWQ-----ALLLKPDIFFKISWLYK-KYEKSVKDLKEAIEVLIEQKRQrlstvEKLEEHMDFASQLIFAQSRG 288
Cdd:cd11055  140 AAKKIFRNSIirlflLLLLFPLRLFLFLLFPFvFGFKSFSFLEDVVKKIIEQRRK-----NKSSRRKDLLQLMLDAQDSD 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 289 DLTGEN-------VNQCVLeMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQS-NDMSNLKVVENFIN 360
Cdd:cd11055  215 EDVSKKkltddeiVAQSFI-FLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTyDTVSKLKYLDMVIN 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 361 ESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENF---EKNVPSRY-FQPFGFGPRG 435
Cdd:cd11055  294 ETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHdPEFWPDPEKFDPERFspeNKAKRHPYaYLPFGAGPRN 373
                        330       340
                 ....*....|....*....|....*.
gi 532691798 436 CVGKFIAMVMMKAILVTLLRRYRVQT 461
Cdd:cd11055  374 CIGMRFALLEVKLALVKILQKFRFVP 399
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
80-460 5.01e-35

Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; Fusarium verticillioides cytochrome P450 monooxygenase FUM15, is also called fumonisin biosynthesis cluster protein 15. The FUM15 gene is part of the gene cluster that mediates the biosynthesis of fumonisins B1, B2, B3, and B4, which are carcinogenic mycotoxins. This FUM15-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410692 [Multi-domain]  Cd Length: 437  Bit Score: 135.86  E-value: 5.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  80 YGEFMRVW-ISGEETLIISKSSSIFHVMKHGQY-------ICRFGSKLGlqcigmhENGIIF-----------NNNPAL- 139
Cdd:cd11069    1 YGGLIRYRgLFGSERLLVTDPKALKHILVTNSYdfekppaFRRLLRRIL-------GDGLLAaegeehkrqrkILNPAFs 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 140 ---WKEIRP-FFTKALSgpgLVRMIAICVESTKDhldrledvtaGLGNINVLNFMRQITLDTSNTLFLGIplDENAIVLK 215
Cdd:cd11069   74 yrhVKELYPiFWSKAEE---LVDKLEEEIEESGD----------ESISIDVLEWLSRATLDIIGLAGFGY--DFDSLENP 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 216 IQNYFDAWQALL----LKPDIFFKISWLYKKYE-----KSVKDLKEAIEVL-------IEQKRQRLSTVEKLEEhMDFAS 279
Cdd:cd11069  139 DNELAEAYRRLFeptlLGSLLFILLLFLPRWLVrilpwKANREIRRAKDVLrrlareiIREKKAALLEGKDDSG-KDILS 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 280 QLI---FAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVI---GDRDVQSNDMSNLK 353
Cdd:cd11069  218 ILLranDFADDERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdpPDGDLSYDDLDRLP 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 354 VVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKLEFF--PKPNEF-------SLENFEKNVPSR 424
Cdd:cd11069  298 YLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIwgPDAEEFnperwlePDGAASPGGAGS 377
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 532691798 425 Y--FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQ 460
Cdd:cd11069  378 NyaLLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFE 415
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
80-480 2.61e-33

cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). Members of the CYP97 clan include Arabidopsis thaliana cytochrome P450s 97A3 (CYP97A3), CYP97B3, and CYP97C1. CYP97A3 is also called protein LUTEIN DEFICIENT 5 (LUT5) and CYP97C1 is also called carotene epsilon-monooxygenase or protein LUTEIN DEFICIENT 1 (LUT1). These cytochromes function as beta- and epsilon-ring carotenoid hydroxylases and are involved in the biosynthesis of xanthophylls. CYP97 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 131.33  E-value: 2.61e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  80 YGEFMRVWISGEETLIISKSSSIFHVMK---HGQYICRFGSKLgLQCI-GmheNGIIfNNNPALWKEIRpfftKALSgPG 155
Cdd:cd11046   10 YGPIYKLAFGPKSFLVISDPAIAKHVLRsnaFSYDKKGLLAEI-LEPImG---KGLI-PADGEIWKKRR----RALV-PA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 156 L--------VRMIAICVESTkdhLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFL----GIPLDENAIVLKIQN-YFDA 222
Cdd:cd11046   80 LhkdylemmVRVFGRCSERL---MEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFnydfGSVTEESPVIKAVYLpLVEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 223 -----WQALLLKPDIFFKISWLYKKYEKSVKDLKEAIEVLIeQKRQRLSTVEKLE-EHMDF-----ASQLIF-AQSRG-D 289
Cdd:cd11046  157 ehrsvWEPPYWDIPAALFIVPRQRKFLRDLKLLNDTLDDLI-RKRKEMRQEEDIElQQEDYlneddPSLLRFlVDMRDeD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 290 LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSN-DMSNLKVVENFINESMRYQPV 368
Cdd:cd11046  236 VDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYeDLKKLKYTRRVLNESLRLYPQ 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 369 VDLVMRKALQDDVIDG--YPVKRGTNIILNIGRMHKL-EFFPKPNEFSLENFE---KNVPSRY-----FQPFGFGPRGCV 437
Cdd:cd11046  316 PPVLIRRAVEDDKLPGggVKVPAGTDIFISVYNLHRSpELWEDPEEFDPERFLdpfINPPNEViddfaFLPFGGGPRKCL 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 532691798 438 GKFIAMVMMKAILVTLLRRYRVQTPKGRGlkniqksnDLSMHP 480
Cdd:cd11046  396 GDQFALLEATVALAMLLRRFDFELDVGPR--------HVGMTT 430
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
80-460 8.40e-32

cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, and similar cytochrome P450s; CYP46A1 is also called cholesterol 24-hydroxylase (EC 1.14.14.25), CH24H, cholesterol 24-monooxygenase, or cholesterol 24S-hydroxylase. It catalyzes the conversion of cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. CYP46A1 is associated with high-order brain functions; increased expression improves cognition while a reduction leads to a poor cognitive performance. It also plays a role in the pathogenesis or progression of neurodegenerative disorders. CYP46A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410706 [Multi-domain]  Cd Length: 429  Bit Score: 126.87  E-value: 8.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  80 YGEFMRVWISGEETLIISKSSSIFHVM------KHGQYICRFGSKLGLQCIGmheNGIIFNNNPALWKEIRPFFTKALSG 153
Cdd:cd20613   11 YGPVFVFWILHRPIVVVSDPEAVKEVLitlnlpKPPRVYSRLAFLFGERFLG---NGLVTEVDHEKWKKRRAILNPAFHR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 154 PGLVRMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPLD-----ENAIVLKIQNYFDAWQALLL 228
Cdd:cd20613   88 KYLKNLMDEFNESADLLVEKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNsiedpDSPFPKAISLVLEGIQESFR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 229 KPDIFFKIS-WLY-KKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEhmDFASQLI-FAQSRGDLTGENVNQCVLEMMIA 305
Cdd:cd20613  168 NPLLKYNPSkRKYrREVREAIKFLRETGRECIEERLEALKRGEEVPN--DILTHILkASEEEPDFDMEELLDDFVTFFIA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 306 APDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDR-DVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDG 384
Cdd:cd20613  246 GQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKqYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGG 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 385 YPVKRGTNIILNIGRMHKLE-FFPKPNEFSLENFEKNVPSR-----YFqPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:cd20613  326 YKIPAGTTVLVSTYVMGRMEeYFEDPLKFDPERFSPEAPEKipsyaYF-PFSLGPRSCIGQQFAQIEAKVILAKLLQNFK 404

                 ..
gi 532691798 459 VQ 460
Cdd:cd20613  405 FE 406
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
110-473 7.79e-31

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 123.90  E-value: 7.79e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 110 QYICRFGSKLGLQCIGM-HENGIIFNNNPAlWKEIRPFFTKALSGPGLVRMIAICVESTKDHLDRLEDVtaglgNINVLN 188
Cdd:cd20621   29 QNHHYYKKKFGPLGIDRlFGKGLLFSEGEE-WKKQRKLLSNSFHFEKLKSRLPMINEITKEKIKKLDNQ-----NVNIIQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 189 FMRQITLDTSNTLFLGIPLDE---------NAIVLKIQNYFDAW---------QALLLKPDIFFKISWLYKKYEKSVKDL 250
Cdd:cd20621  103 FLQKITGEVVIRSFFGEEAKDlkingkeiqVELVEILIESFLYRfsspyfqlkRLIFGRKSWKLFPTKKEKKLQKRVKEL 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 251 KEAIEVLIEQKRQRL---STVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKV 327
Cdd:cd20621  183 RQFIEKIIQNRIKQIkknKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEI 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 328 EEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVD-LVMRKALQDDVIDGYPVKRGTNI-ILNIGRMHKLE 404
Cdd:cd20621  263 QEKLRQEIKSVVGnDDDITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQIGDLKIKKGWIVnVGYIYNHFNPK 342
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532691798 405 FFPKPNEFS----LENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNIQKS 473
Cdd:cd20621  343 YFENPDEFNperwLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIPNPKLKLIFKL 415
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
151-458 1.25e-30

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 123.06  E-value: 1.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 151 LSGPGL-VRMIAICVESTKDHLDRLEDvtagLGNINVLNFMRQITLDTSNTLFLGIplDENAIVLKIQNYFDAWQALLLK 229
Cdd:cd11043   74 LGPEALkDRLLGDIDELVRQHLDSWWR----GKSVVVLELAKKMTFELICKLLLGI--DPEEVVEELRKEFQAFLEGLLS 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 230 pdifFKISWLYKKYEKSVK---DLKEAIEVLIEQKRQRLstvEKLEEHMDFASQLIFAQSRGD--LTGENVNQCVLEMMI 304
Cdd:cd11043  148 ----FPLNLPGTTFHRALKarkRIRKELKKIIEERRAEL---EKASPKGDLLDVLLEEKDEDGdsLTDEEILDNILTLLF 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 305 AAPDTLSVTLFFMLVLIAEHPKVEEDMMKEiQAVI-----GDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQD 379
Cdd:cd11043  221 AGHETTSTTLTLAVKFLAENPKVLQELLEE-HEEIakrkeEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQD 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 380 DVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENFEKN--VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11043  300 VEYKGYTIPKGWKVLWSARATHLdPEYFPDPLKFNPWRWEGKgkGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTR 379

                 ..
gi 532691798 457 YR 458
Cdd:cd11043  380 FR 381
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
141-458 2.84e-30

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 122.39  E-value: 2.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 141 KEIRPFFTKALSGPGLVRMIAICVESTKDHLDRLEDVtaglGNINVLNFMRQITLDTSNTLFLGipLDENAIVLKIQNYF 220
Cdd:cd11044   80 RRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLKA----GEVALYPELRRLTFDVAARLLLG--LDPEVEAEALSQDF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 221 DAW-QALL-LKPDIFFKiswLYKKYEKSVKDLKEAIEVLIEQKRQrlstvEKLEEHMDFASQLIFAQ-SRG-DLTGENVN 296
Cdd:cd11044  154 ETWtDGLFsLPVPLPFT---PFGRAIRARNKLLARLEQAIRERQE-----EENAEAKDALGLLLEAKdEDGePLSMDELK 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 297 QCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKA 376
Cdd:cd11044  226 DQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKV 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 377 LQDDVIDGYPVKRGTNIILNIGRMHKL-EFFPKPNEFSLENF------EKNVPSRYFqPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:cd11044  306 LEDFELGGYQIPKGWLVYYSIRDTHRDpELYPDPERFDPERFsparseDKKKPFSLI-PFGGGPRECLGKEFAQLEMKIL 384

                 ....*....
gi 532691798 450 LVTLLRRYR 458
Cdd:cd11044  385 ASELLRNYD 393
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
82-460 3.33e-30

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 122.31  E-value: 3.33e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  82 EFMRVWISGEETLIISKSSSIFHVMKH--------GQYICRFGSKLGlqcigmheNGIiFNNNPALWKEIRPFFTKALSG 153
Cdd:cd11064    2 TFRGPWPGGPDGIVTADPANVEHILKTnfdnypkgPEFRDLFFDLLG--------DGI-FNVDGELWKFQRKTASHEFSS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 154 PGLVRMIAICV-ESTKDHLDRLEDVTAGLGNinVLN----FMRqITLDTSNTLFLGIPLDENAIVLKIQNY---FDAWQA 225
Cdd:cd11064   73 RALREFMESVVrEKVEKLLVPLLDHAAESGK--VVDlqdvLQR-FTFDVICKIAFGVDPGSLSPSLPEVPFakaFDDASE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 226 LLLKPDIFFKISWLYKK-----YEKSvkdLKEAIEVL-------IEQKRQRL-STVEKLEEHMDFASqlIFAQSRGDLTG 292
Cdd:cd11064  150 AVAKRFIVPPWLWKLKRwlnigSEKK---LREAIRVIddfvyevISRRREELnSREEENNVREDLLS--RFLASEEEEGE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQ----CVLEMMIAAPDTLSVTL--FFmlVLIAEHPKVEEDMMKEIQAVIGDRDVQSN------DMSNLKVVENFIN 360
Cdd:cd11064  225 PVSDKflrdIVLNFILAGRDTTAAALtwFF--WLLSKNPRVEEKIREELKSKLPKLTTDESrvptyeELKKLVYLHAALS 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 361 ESMRYQPVVDLVMRKALQDDVI-DGYPVKRGTNIILNI---GRMHK------LEFfpKPNEF-SLENFEKNVPSRYFQPF 429
Cdd:cd11064  303 ESLRLYPPVPFDSKEAVNDDVLpDGTFVKKGTRIVYSIyamGRMESiwgedaLEF--KPERWlDEDGGLRPESPYKFPAF 380
                        410       420       430
                 ....*....|....*....|....*....|.
gi 532691798 430 GFGPRGCVGKFIAMVMMKAILVTLLRRYRVQ 460
Cdd:cd11064  381 NAGPRICLGKDLAYLQMKIVAAAILRRFDFK 411
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
132-457 4.55e-29

cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 118.81  E-value: 4.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 132 IFNNNPALWKE----IRPFFTKalsgpglvrmiaicveSTKDHLDRLEDvtaglgniNVLNFMRQI-------------- 193
Cdd:cd11063   52 IFTSDGEEWKHsralLRPQFSR----------------DQISDLELFER--------HVQNLIKLLprdgstvdlqdlff 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 194 --TLDTS---------NTLFLGIPLDENAIVLKIQNYFDAWQALLLKpdiFFKISWLY--KKYEKSVKDLKEAIEVLIEQ 260
Cdd:cd11063  108 rlTLDSAteflfgesvDSLKPGGDSPPAARFAEAFDYAQKYLAKRLR---LGKLLWLLrdKKFREACKVVHRFVDPYVDK 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 261 --KRQRLSTVEKLEEHMDFASQLI-FAQSRGDLTGEnvnqcVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQA 337
Cdd:cd11063  185 alARKEESKDEESSDRYVFLDELAkETRDPKELRDQ-----LLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLS 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 338 VIGD-RDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVI------DGYP---VKRGTNIILNIGRMHKLE--F 405
Cdd:cd11063  260 LFGPePTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLprgggpDGKSpifVPKGTRVLYSVYAMHRRKdiW 339
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 532691798 406 FPKPNEFSLENFEKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd11063  340 GPDAEEFRPERWEDLKRPGWeYLPFNGGPRICLGQQFALTEASYVLVRLLQTF 392
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
190-465 5.08e-29

cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 118.51  E-value: 5.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 190 MRQITLDTSNTLFLGIPLDENAIV-----LKIQNYFDAWQALLLKpdiffkisWLYK-------KYEKSVKDLKEAIEVL 257
Cdd:cd11049  116 MHRLTLRVVARTLFSTDLGPEAAAelrqaLPVVLAGMLRRAVPPK--------FLERlptpgnrRFDRALARLRELVDEI 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 258 IEQKRQRLstveklEEHMDFASQLIFA--QSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEI 335
Cdd:cd11049  188 IAEYRASG------TDRDDLLSLLLAArdEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAEL 261
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 336 QAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKL-EFFPKPNEFS- 413
Cdd:cd11049  262 DAVLGGRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDpEVYPDPERFDp 341
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 532691798 414 ---LENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGR 465
Cdd:cd11049  342 drwLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGR 396
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
227-461 1.05e-28

cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of vertebrate cytochrome P450 family 4, subfamily V (CYP4V) enzymes and similar proteins, including invertebrate subfamily C (CYP4C). Insect CYP4C enzymes may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. CYP4V2, the most characterized member of the CYP4V subfamily, is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 117.75  E-value: 1.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 227 LLKPDIFFKISWLYKKYEKSVKDLKE-AIEVLIEQKRQRLSTVEKLEEHMDFASQ-----------LIFA-QSRGDLTGE 293
Cdd:cd20660  152 WLWPDFIYSLTPDGREHKKCLKILHGfTNKVIQERKAELQKSLEEEEEDDEDADIgkrkrlafldlLLEAsEEGTKLSDE 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 294 NVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD--RDVQSNDMSNLKVVENFINESMRYQPVVDL 371
Cdd:cd20660  232 DIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDsdRPATMDDLKEMKYLECVIKEALRLFPSVPM 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 372 VMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENF-EKNVPSRY---FQPFGFGPRGCVGKFIAMVMM 446
Cdd:cd20660  312 FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRdPRQFPDPEKFDPDRFlPENSAGRHpyaYIPFSAGPRNCIGQKFALMEE 391
                        250
                 ....*....|....*
gi 532691798 447 KAILVTLLRRYRVQT 461
Cdd:cd20660  392 KVVLSSILRNFRIES 406
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
184-481 1.30e-28

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 117.78  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 184 INVLNFMRQITLDTSNTLFLGIPLDENAIVLKI-QNY----FDAWQALLLKPDIFFKI-SWLYKKYEKSVKDLKEAIEVL 257
Cdd:cd11041  108 VNLYDTVLRIVARVSARVFVGPPLCRNEEWLDLtINYtidvFAAAAALRLFPPFLRPLvAPFLPEPRRLRRLLRRARPLI 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 258 IE--QKRQRLSTVEKLEEHMDFASQLI-FAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKE 334
Cdd:cd11041  188 IPeiERRRKLKKGPKEDKPNDLLQWLIeAAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREE 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 335 IQAVIGDRDVQSND-MSNLKVVENFINESMRYQPVVDLVM-RKALQDDVI-DGYPVKRGTNIILNIGRMHKLE-FFPKPN 410
Cdd:cd11041  268 IRSVLAEHGGWTKAaLNKLKKLDSFMKESQRLNPLSLVSLrRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPdIYPDPE 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 411 EF---------SLENFEKN----VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGL-KNIQKSNDL 476
Cdd:cd11041  348 TFdgfrfyrlrEQPGQEKKhqfvSTSPDFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERpKNIWFGEFI 427

                 ....*
gi 532691798 477 SMHPN 481
Cdd:cd11041  428 MPDPN 432
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
74-458 1.59e-28

Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP72 clan is associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. This clan includes: CYP734 enzymes that are involved in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis; CYP714 enzymes that are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels; and CYP72 family enzymes, among others. The CYP72 clan belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 117.44  E-value: 1.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  74 NYYNKMYGEFMRVWISGEETLIISKSSSIFHVMKHGQ-YICRFGSKLGLQciGMHENGIIFNNNPAlWKEIRPFFTKALS 152
Cdd:cd11052    5 YHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEgYFGKSPLQPGLK--KLLGRGLVMSNGEK-WAKHRRIANPAFH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 153 GPGLVRMIAICVESTKDHLDRLEDVTAGLGN-INVLNFMRQITLDT-SNTLFlGIPLDENAIVLKIQnyfDAWQALLLKP 230
Cdd:cd11052   82 GEKLKGMVPAMVESVSDMLERWKKQMGEEGEeVDVFEEFKALTADIiSRTAF-GSSYEEGKEVFKLL---RELQKICAQA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 --DIFFKISWLYK-KYEKSVKDLKEAIEVL---IEQKRQRLSTVEKLEEH-MDFASQLIFA-QSRGDLTGENVNQCVLE- 301
Cdd:cd11052  158 nrDVGIPGSRFLPtKGNKKIKKLDKEIEDSlleIIKKREDSLKMGRGDDYgDDLLGLLLEAnQSDDQNKNMTVQEIVDEc 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 302 --MMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMR-YQPVVDLVmRKALQ 378
Cdd:cd11052  238 ktFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLRlYPPAVFLT-RKAKE 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 379 DDVIDGYPVKRGTNIILNIGRMHKLEFF--PKPNEFSLENFEKNVP-----SRYFQPFGFGPRGCVGKFIAMVMMKAILV 451
Cdd:cd11052  317 DIKLGGLVIPKGTSIWIPVLALHHDEEIwgEDANEFNPERFADGVAkaakhPMAFLPFGLGPRNCIGQNFATMEAKIVLA 396

                 ....*..
gi 532691798 452 TLLRRYR 458
Cdd:cd11052  397 MILQRFS 403
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
184-465 1.00e-27

cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410676 [Multi-domain]  Cd Length: 415  Bit Score: 114.99  E-value: 1.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 184 INVLNFMRQITLD-TSNTLFlGipLDENAIVLKIQNYFDAWQALLLKPDIFFK------ISWL-YKKYEKSVKDLKEAIE 255
Cdd:cd11053  111 FDLRELMQEITLEvILRVVF-G--VDDGERLQELRRLLPRLLDLLSSPLASFPalqrdlGPWSpWGRFLRARRRIDALIY 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 256 VLIEQKRQrlstvEKLEEHMDFASQLIFAQ-------SRGDLTGEnvnqcVLEMMIAAPDTLSVTLFFMLVLIAEHPKVE 328
Cdd:cd11053  188 AEIAERRA-----EPDAERDDILSLLLSARdedgqplSDEELRDE-----LMTLLFAGHETTATALAWAFYWLHRHPEVL 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 329 EDMMKEIQAVIGDRDVQsnDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFP 407
Cdd:cd11053  258 ARLLAELDALGGDPDPE--DIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPdLYP 335
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532691798 408 KPNEFSLENFEKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGR 465
Cdd:cd11053  336 DPERFRPERFLGRKPSPYeYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPR 394
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
190-459 1.89e-27

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 113.95  E-value: 1.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 190 MRQITLDTSNTLFLGIPLDENAIvlKIQNYF-DAWQA---LLLKPDIFFKiswlYKKYEKSVKDLKEAIEVLIEQKRQRL 265
Cdd:cd11045  115 IKELTLDLATRVFLGVDLGPEAD--KVNKAFiDTVRAstaIIRTPIPGTR----WWRGLRGRRYLEEYFRRRIPERRAGG 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 266 STvekleehmDFASQLIFAQSR-GD-LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAvIGDRD 343
Cdd:cd11045  189 GD--------DLFSALCRAEDEdGDrFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLA-LGKGT 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 344 VQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKL-EFFPKPNEFSLENF----- 417
Cdd:cd11045  260 LDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMpEYWPNPERFDPERFspera 339
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 532691798 418 EKNVpSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRV 459
Cdd:cd11045  340 EDKV-HRYaWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRW 381
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
226-459 4.30e-27

cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is composed of family 4 cytochrome P450s from vertebrate subfamilies A (CYP4A), B (CYP4B), F (CYP4F), T (CYP4T), X (CYP4X), and Z (CYP4Z). Also included are similar proteins from lancelets, tunicates, hemichordates, echinoderms, mollusks, annelid worms, sponges, and choanoflagellates, among others. The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B and CYP4F are conserved among vertebrates. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4F enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4B_4F-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 113.03  E-value: 4.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 226 LLLKPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTvEKLEE-----HMDFASQLIFAQ-SRGD-LTGENVNQC 298
Cdd:cd20659  153 PLLHFDWIYYLTPEGRRFKKACDYVHKFAEEIIKKRRKELED-NKDEAlskrkYLDFLDILLTARdEDGKgLTDEEIRDE 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 299 VLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDR-DVQSNDMSNLKVVENFINESMRYQPVVDLVMRKAL 377
Cdd:cd20659  232 VDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLT 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 378 QDDVIDGYPVKRGTNIILNIGRMHK--------LEFfpKPNEFSLENFeKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:cd20659  312 KPITIDGVTLPAGTLIAINIYALHHnptvwedpEEF--DPERFLPENI-KKRDPFAFIPFSAGPRNCIGQNFAMNEMKVV 388
                        250
                 ....*....|
gi 532691798 450 LVTLLRRYRV 459
Cdd:cd20659  389 LARILRRFEL 398
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
81-480 1.26e-26

unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 111.64  E-value: 1.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  81 GEFMRVWISGEETLIISKSSSIFHVMKHGQYICRFGSKL--GLQCIGMHEngiIFNNNPALWKEIRPFFTKALSGPGLVR 158
Cdd:cd11083    1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFRRISSLesVFREMGING---VFSAEGDAWRRQRRLVMPAFSPKHLRY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 159 MIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLD-TSNTLF---------LGIPLDEN------AIVLKIQNYFDA 222
Cdd:cd11083   78 FFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDvTTSLAFgydlntlerGGDPLQEHlervfpMLNRRVNAPFPY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 223 WQALLLKPDiffkiswlyKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQS--RGDLTGENVNQCVL 300
Cdd:cd11083  158 WRYLRLPAD---------RALDRALVEVRALVLDIIAAARARLAANPALAEAPETLLAMMLAEDdpDARLTDDEIYANVL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 301 EMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQ--SNDMSNLKVVENFINESMRYQPVVDLVMRKALQ 378
Cdd:cd11083  229 TLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPplLEALDRLPYLEAVARETLRLKPVAPLLFLEPNE 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 379 DDVIDGYPVKRGTNIIL---NIGRmhKLEFFPKPNEFSLENFEKNVPSRY------FQPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:cd11083  309 DTVVGDIALPAGTPVFLltrAAGL--DAEHFPDPEEFDPERWLDGARAAEphdpssLLPFGAGPRLCPGRSLALMEMKLV 386
                        410       420       430
                 ....*....|....*....|....*....|.
gi 532691798 450 LVTLLRRYRVQTPKGRGlkNIQKSNDLSMHP 480
Cdd:cd11083  387 FAMLCRNFDIELPEPAP--AVGEEFAFTMSP 415
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
233-457 1.91e-26

Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is considerably larger than in other taxa. In individual plant genomes, CYPs form the third largest family of plant genes; the two largest gene families code for F-box proteins and receptor-like kinases. CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. However, there is a phenomenon called family creep, where a sequence (below 40% identity) is absorbed into a large family; this is seen in the plant CYP71 and CYP89 families. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP71 clan has expanded dramatically and represents 50% of all plant CYPs; it includes several families including CYP71, CYP73, CYP76, CYP81, CYP82, CYP89, and CYP93, among others. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410711 [Multi-domain]  Cd Length: 429  Bit Score: 111.49  E-value: 1.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 233 FFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSV 312
Cdd:cd20618  168 WLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAV 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 313 TLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVKRG 390
Cdd:cd20618  248 TIEWAMAELLRHPEVMRKAQEELDSVVGrERLVEESDLPKLPYLQAVVKETLRLHPPGPLlLPHESTEDCKVAGYDIPAG 327
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532691798 391 TNIILN---IGRMHKLefFPKPNEFS----LENFEKNVPSRYFQ--PFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd20618  328 TRVLVNvwaIGRDPKV--WEDPLEFKperfLESDIDDVKGQDFEllPFGSGRRMCPGMPLGLRMVQLTLANLLHGF 401
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
231-462 8.19e-26

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 109.63  E-value: 8.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 DIFFKISWL-YKKYEKSVK----DLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGEN-----VNQCVL 300
Cdd:cd20654  168 DAIPFLGWLdFGGHEKAMKrtakELDSILEEWLEEHRQKRSSSGKSKNDEDDDDVMMLSILEDSQISGYdadtvIKATCL 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 301 EMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMR-YQPVVDLVMRKALQ 378
Cdd:cd20654  248 ELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGkDRWVEESDIKNLVYLQAIVKETLRlYPPGPLLGPREATE 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 379 DDVIDGYPVKRGTNIILNIGRMHK--------LEFfpKPNEFSLENFEKNVPSRYFQ--PFGFGPRGCVGKFIAMVMMKA 448
Cdd:cd20654  328 DCTVGGYHVPKGTRLLVNVWKIQRdpnvwsdpLEF--KPERFLTTHKDIDVRGQNFEliPFGSGRRSCPGVSFGLQVMHL 405
                        250
                 ....*....|....
gi 532691798 449 ILVTLLRRYRVQTP 462
Cdd:cd20654  406 TLARLLHGFDIKTP 419
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
140-463 1.32e-25

cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 108.53  E-value: 1.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 140 WKEIRPFFTKALSGPGLVRMIAICVESTKDHLDRLEDVTAGLG--NINVLNFMRQITLDTSNTLFLGIPLDENA------ 211
Cdd:cd20615   60 WKRVRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNSGDGRrfVIDPAQALKFLPFRVIAEILYGELSPEEKeelwdl 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 212 IVLKIQNYFDAWQALLLKpdifFKIS-WLY-------KKYEKSVKDLKEAIeVLIEQKRQRLSTVEKLEEHMDfasqlif 283
Cdd:cd20615  140 APLREELFKYVIKGGLYR----FKISrYLPtaanrrlREFQTRWRAFNLKI-YNRARQRGQSTPIVKLYEAVE------- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 284 aqsRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDvqsndmsnlKVVENFI---- 359
Cdd:cd20615  208 ---KGDITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSG---------YPMEDYIlstd 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 360 -------NESMRYQPVVDL-VMRKALQDDVIDGYPVKRGTNIILNIGRMHKLEFFPKPN--EFSLENFEKNVPS--RY-F 426
Cdd:cd20615  276 tllaycvLESLRLRPLLAFsVPESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWGPDgeAYRPERFLGISPTdlRYnF 355
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 532691798 427 QPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPK 463
Cdd:cd20615  356 WRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPD 392
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
124-480 4.92e-25

cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 107.30  E-value: 4.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 124 IGMHENGIIFNNNPALWKEIRPFFTKAL-----SGPGLVRMIAicvESTKDHLDRLE-------DVTAGLGNInVLNFMR 191
Cdd:cd11027   46 FSRGGKDIAFGDYSPTWKLHRKLAHSALrlyasGGPRLEEKIA---EEAEKLLKRLAsqegqpfDPKDELFLA-VLNVIC 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 192 QITLDTSNTLflgipLDENaiVLKIQNYFDAWQALLLKPDIFFKISWLyKKYE-KSVKDLKEAIEVlieqkrqRLSTVEK 270
Cdd:cd11027  122 SITFGKRYKL-----DDPE--FLRLLDLNDKFFELLGAGSLLDIFPFL-KYFPnKALRELKELMKE-------RDEILRK 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 271 -LEEHM---------DFASQLIFAQS----RGD-----LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDM 331
Cdd:cd11027  187 kLEEHKetfdpgnirDLTDALIKAKKeaedEGDedsglLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKL 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 332 MKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVKRGTNIILNIGRMHK------- 402
Cdd:cd11027  267 HAELDDVIGrDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTLRGYTIPKGTTVLVNLWALHHdpkewdd 346
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532691798 403 -LEFfpKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNIQKSNDLSMHP 480
Cdd:cd11027  347 pDEF--RPERFLDENGKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPELEGIPGLVLYP 423
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
300-465 8.64e-25

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 106.53  E-value: 8.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 300 LEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKAL 377
Cdd:cd20651  231 LDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGrDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIgIPHRAL 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 378 QDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVT 452
Cdd:cd20651  311 KDTTLGGYRIPKDTTILASLYSVHMdPEYWGDPEEFRPERFldedGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTG 390
                        170
                 ....*....|...
gi 532691798 453 LLRRYRVQTPKGR 465
Cdd:cd20651  391 LLQNFTFSPPNGS 403
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
229-460 1.36e-24

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 106.11  E-value: 1.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 229 KPDIFFKISWLYK-KYEKSVKDLKEAIEVLIEQKRQRLSTVEK-LEEHMDFASQlifAQSRGDLTGENVNQCVLEMMIAA 306
Cdd:cd11068  166 RPPILNKLRRRAKrQFREDIALMRDLVDEIIAERRANPDGSPDdLLNLMLNGKD---PETGEKLSDENIRYQMITFLIAG 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 307 PDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDG-Y 385
Cdd:cd11068  243 HETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGkY 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 386 PVKRGTNIILNIGRMHK---------LEFfpKPNEFSLENFEKnVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11068  323 PLKKGDPVLVLLPALHRdpsvwgedaEEF--RPERFLPEEFRK-LPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQR 399

                 ....
gi 532691798 457 YRVQ 460
Cdd:cd11068  400 FDFE 403
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
129-457 2.32e-24

cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP714 enzymes are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels. They contribute to the production of diverse GA compounds through various oxidations of C and D rings in both monocots and eudicots. CYP714B1 and CYP714B2 encode the enzyme GA 13-oxidase, which is required for GA1 biosynthesis, while CYP714D1 encodes GA 16a,17-epoxidase, which inactivates the non-13-hydroxy GAs in rice. Arabidopsis CYP714A1 is an inactivation enzyme that catalyzes the conversion of GA12 to 16-carboxylated GA12 (16-carboxy-16beta,17-dihydro GA12). CYP714 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 105.19  E-value: 2.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 129 NGIIFNNNPAlW----KEIRP-FFTKALSGpglvrMIAICVESTKDHL----DRLEDVTAGLGNINVLNFMRQITLDT-S 198
Cdd:cd20640   60 GGILTSNGPH-WahqrKIIAPeFFLDKVKG-----MVDLMVDSAQPLLssweERIDRAGGMAADIVVDEDLRAFSADViS 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 199 NTLFLGIPLDENAIVLKIQnyfdAWQALLLKPDIFFKISWLY---KKYEKSVKDLKEAIEVLIEQ---KRQRLSTVEKle 272
Cdd:cd20640  134 RACFGSSYSKGKEIFSKLR----ELQKAVSKQSVLFSIPGLRhlpTKSNRKIWELEGEIRSLILEivkEREEECDHEK-- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 273 ehmDFASQLIFAQSRGDLTGENVNQCVLE----MMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSND 348
Cdd:cd20640  208 ---DLLQAILEGARSSCDKKAEAEDFIVDncknIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDADS 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 349 MSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMH--KLEFFPKPNEFSLENFEKNVPSRY- 425
Cdd:cd20640  285 LSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHldPEIWGPDANEFNPERFSNGVAAACk 364
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 532691798 426 ----FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd20640  365 pphsYMPFGAGARTCLGQNFAMAELKVLVSLILSKF 400
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
225-475 5.17e-24

cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 104.23  E-value: 5.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 225 ALLLKPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTveKLEEHMDFASQLIFA--------QSRGDLTGENVN 296
Cdd:cd11061  146 GVLGHAPWLRPLLLDLPLFPGATKARKRFLDFVRAQLKERLKA--EEEKRPDIFSYLLEAkdpetgegLDLEELVGEARL 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 297 qcvleMMIAAPDTLSVTL---FFMLvliAEHPKVEEDMMKEIQAVI--GDRDVQSNDMSNLKVVENFINESMR-YQPVVD 370
Cdd:cd11061  224 -----LIVAGSDTTATALsaiFYYL---ARNPEAYEKLRAELDSTFpsDDEIRLGPKLKSLPYLRACIDEALRlSPPVPS 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 371 LVMRKALQDDV-IDGYPVKRGTNI---ILNIGRMHKLefFPKPNEFslenfeknVPSR-------------YFQPFGFGP 433
Cdd:cd11061  296 GLPRETPPGGLtIDGEYIPGGTTVsvpIYSIHRDERY--FPDPFEF--------IPERwlsrpeelvrarsAFIPFSIGP 365
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 532691798 434 RGCVGKFIAMVMMKAILVTLLRRYRVQTPKGR-GLKNIQKSND 475
Cdd:cd11061  366 RGCIGKNLAYMELRLVLARLLHRYDFRLAPGEdGEAGEGGFKD 408
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
132-461 5.27e-24

cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome P450s from insects and crustaceans, including the CYP6, CYP9 and CYP310 subfamilies, which are involved in the metabolism of insect hormones and xenobiotic detoxification. The CYP6-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 104.16  E-value: 5.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 132 IFNNNPALWKEIR----PFFTkalsgPGLVRMIAICVESTKDHL-DRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIP 206
Cdd:cd11056   53 LFSLDGEKWKELRqkltPAFT-----SGKLKNMFPLMVEVGDELvDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 207 LD-----ENAIVLKIQNYFD---AWQALLLKPDIFFKISWL--YKKYEKSVKD-----LKEAIE--------------VL 257
Cdd:cd11056  128 ANslndpENEFREMGRRLFEpsrLRGLKFMLLFFFPKLARLlrLKFFPKEVEDffrklVRDTIEyreknnivrndfidLL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 258 IEQKRQRLSTVEKLEEHMDFasqlifaqsrGDLTGenvnQCVLeMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQA 337
Cdd:cd11056  208 LELKKKGKIEDDKSEKELTD----------EELAA----QAFV-FFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDE 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 338 VIGDRD--VQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDG--YPVKRGTNIILNIGRMHKL-EFFPKPNEF 412
Cdd:cd11056  273 VLEKHGgeLTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPVIIPVYALHHDpKYYPEPEKF 352
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 532691798 413 SLENF-EKNVPSRY---FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQT 461
Cdd:cd11056  353 DPERFsPENKKKRHpytYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEP 405
PLN02738 PLN02738
carotene beta-ring hydroxylase
232-464 6.05e-24

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 105.38  E-value: 6.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 232 IFFKISWLYKKYEKSVKDLKEAIEVLIEQKRqRLSTVEKLEEHMDFA-----SQLIFAQSRGD-LTGENVNQCVLEMMIA 305
Cdd:PLN02738 324 IWKDISPRQRKVAEALKLINDTLDDLIAICK-RMVEEEELQFHEEYMnerdpSILHFLLASGDdVSSKQLRDDLMTMLIA 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 306 APDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGY 385
Cdd:PLN02738 403 GHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGY 482
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 386 PVKRGTNIILNIGRMHK-------LEFF---------PKPNEfSLENFeknvpsRYFqPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:PLN02738 483 PIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNF------SYL-PFGGGPRKCVGDMFASFENVVA 554
                        250
                 ....*....|....*
gi 532691798 450 LVTLLRRYRVQTPKG 464
Cdd:PLN02738 555 TAMLVRRFDFQLAPG 569
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
75-457 2.81e-23

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 102.14  E-value: 2.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  75 YYNKMYGEFMRVWISGEETLIISKSSSIFHVM-KHGQYICRFGSK-LGLQCIGmheNGIifnnnPAL----WKEIRPFFT 148
Cdd:cd20639    6 HWRKIYGKTFLYWFGPTPRLTVADPELIREILlTRADHFDRYEAHpLVRQLEG---DGL-----VSLrgekWAHHRRVIT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 149 KALSGPGLVRMIAICVESTKDHLDRLEDV--TAGLGNINVLNFMRQITLDTSNTLFLGIPLDENAIVLKIQNyfdawQAL 226
Cdd:cd20639   78 PAFHMENLKRLVPHVVKSVADMLDKWEAMaeAGGEGEVDVAEWFQNLTEDVISRTAFGSSYEDGKAVFRLQA-----QQM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 227 LLKPDIFFKI-----SWLYKKYEKSVKDLKEAIEV----LIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQ 297
Cdd:cd20639  153 LLAAEAFRKVyipgyRFLPTKKNRKSWRLDKEIRKsllkLIERRQTAADDEKDDEDSKDLLGLMISAKNARNGEKMTVEE 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 298 CVLE---MMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSND-MSNLKVVENFINESMR-YQPVVDLV 372
Cdd:cd20639  233 IIEEcktFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDhLPKLKTLGMILNETLRlYPPAVATI 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 373 mRKALQDDVIDGYPVKRGTNIILNIGRMH--KLEFFPKPNEFSLENFEKNVPSRY-----FQPFGFGPRGCVGKFIAMVM 445
Cdd:cd20639  313 -RRAKKDVKLGGLDIPAGTELLIPIMAIHhdAELWGNDAAEFNPARFADGVARAAkhplaFIPFGLGPRTCVGQNLAILE 391
                        410
                 ....*....|..
gi 532691798 446 MKAILVTLLRRY 457
Cdd:cd20639  392 AKLTLAVILQRF 403
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
290-465 1.22e-22

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 100.22  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 290 LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG--DRDVQSNDMSNLKVVENFINESMRYQP 367
Cdd:cd20680  239 LSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGksDRPVTMEDLKKLRYLECVIKESLRLFP 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 368 VVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENF-EKNVPSRY---FQPFGFGPRGCVGKFIA 442
Cdd:cd20680  319 SVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRdPRYFPEPEEFRPERFfPENSSGRHpyaYIPFSAGPRNCIGQRFA 398
                        170       180
                 ....*....|....*....|...
gi 532691798 443 MVMMKAILVTLLRRYRVQTPKGR 465
Cdd:cd20680  399 LMEEKVVLSCILRHFWVEANQKR 421
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
219-458 3.08e-22

cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces cerevisiae cytochrome P450 56, also called cytochrome P450-DIT2, and similar fungal proteins. CYP56 is involved in spore wall maturation and is thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine-containing precursors of the spore wall. The CYP56-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 98.94  E-value: 3.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 219 YFDAWQALLLKPDIF-FKISWLYKKYE-----KSVKDLKEAIEVLIEQKRQRLSTVEKLEEHM--DFASQLIFAQSRGDL 290
Cdd:cd11070  140 TLNAIKLAIFPPLFLnFPFLDRLPWVLfpsrkRAFKDVDEFLSELLDEVEAELSADSKGKQGTesVVASRLKRARRSGGL 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 291 TGE----NVNQcvleMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSN---DMSNLKVVENFINESM 363
Cdd:cd11070  220 TEKellgNLFI----FFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDyeeDFPKLPYLLAVIYETL 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 364 RYQPVVDLVMRKALQDDVI-----DGYPVKRGTNIILNIGRMHK---------LEFFPK----PNEFSLENFEKNVPSRY 425
Cdd:cd11070  296 RLYPPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRdptiwgpdaDEFDPErwgsTSGEIGAATRFTPARGA 375
                        250       260       270
                 ....*....|....*....|....*....|...
gi 532691798 426 FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:cd11070  376 FIPFSAGPRACLGRKFALVEFVAALAELFRQYE 408
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
127-464 5.41e-22

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 98.02  E-value: 5.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 127 HENGIIFNNNPAlWKEIRPFFTKALSGPGLVRM---------IAICVESTKDHLDRLEDVTAGLGNI--NVLN---FMRQ 192
Cdd:cd11026   48 KGYGVVFSNGER-WKQLRRFSLTTLRNFGMGKRsieeriqeeAKFLVEAFRKTKGKPFDPTFLLSNAvsNVICsivFGSR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 193 itLDTSNTLFLGIpLDENAIVLKIQNYFdaWQALLlkpDIFFKISWL----YKKYEKSVKDLKEAIEVLIEQKRQRL--- 265
Cdd:cd11026  127 --FDYEDKEFLKL-LDLINENLRLLSSP--WGQLY---NMFPPLLKHlpgpHQKLFRNVEEIKSFIRELVEEHRETLdps 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 266 -------STVEKLEEHMDFASqlifaqsrGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAV 338
Cdd:cd11026  199 sprdfidCFLLKMEKEKDNPN--------SEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRV 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 339 IG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLE 415
Cdd:cd11026  271 IGrNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLgVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPkQWETPEEFNPG 350
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 532691798 416 NF-------EKNvpsRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKG 464
Cdd:cd11026  351 HFldeqgkfKKN---EAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVG 403
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
128-463 4.56e-21

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 95.39  E-value: 4.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 128 ENGIIFNNNPAlWKEIR----PFFT-KALSgpglvRMIAICVESTKDHLDRLEDVTAGLGN-INVLNFMRQITLDTSNTL 201
Cdd:cd11082   47 EDNLIFMFGEE-HKELRksllPLFTrKALG-----LYLPIQERVIRKHLAKWLENSKSGDKpIEMRPLIRDLNLETSQTV 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 202 FLGIPLDENAIVLKIqNYFDAWQALLLKPdIFFKISWLYKKYeKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQL 281
Cdd:cd11082  121 FVGPYLDDEARRFRI-DYNYFNVGFLALP-VDFPGTALWKAI-QARKRIVKTLEKCAAKSKKRMAAGEEPTCLLDFWTHE 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 282 IFA----------QSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRD--VQSNDM 349
Cdd:cd11082  198 ILEeikeaeeegePPPPHSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEppLTLDLL 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 350 SNLKVVENFINESMRYQPVVDLVMRKALQDDVI-DGYPVKRGTNIILNI-GRMHklEFFPKPNEFSLENF-----EKNVP 422
Cdd:cd11082  278 EEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLtEDYTVPKGTIVIPSIyDSCF--QGFPEPDKFDPDRFsperqEDRKY 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 532691798 423 SRYFQPFGFGPRGCVGKFIA----MVMMkAILVTLLRRYRVQTPK 463
Cdd:cd11082  356 KKNFLVFGAGPHQCVGQEYAinhlMLFL-ALFSTLVDWKRHRTPG 399
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
78-457 1.68e-20

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 93.75  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  78 KMYGEFMRVWISGEETLIISKSSSIFHVMK-HGQYICRFGSKLGLQCIGMHENGIIFNNNPALWKEIRP-FFTKALSGPG 155
Cdd:cd11073    2 KKYGPIMSLKLGSKTTVVVSSPEAAREVLKtHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKiCTTELFSPKR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 156 L-----VRMiaicvESTKDHLDRLEDVTAGLGNINV--------LNFMrqitldtSNTLF---LGIPLDENAIVLK--IQ 217
Cdd:cd11073   82 LdatqpLRR-----RKVRELVRYVREKAGSGEAVDIgraafltsLNLI-------SNTLFsvdLVDPDSESGSEFKelVR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 218 NYFDawqaLLLKPDI--------FFKISWLYKKYEKSVKDLKEAIEVLIEQK-RQRLSTVEKLEEHMDFASQLIFAQSRG 288
Cdd:cd11073  150 EIME----LAGKPNVadffpflkFLDLQGLRRRMAEHFGKLFDIFDGFIDERlAEREAGGDKKKDDDLLLLLDLELDSES 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 289 DLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQP 367
Cdd:cd11073  226 ELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGkDKIVEESDISKLPYLQAVVKETLRLHP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 368 VVD-LVMRKALQDDVIDGYPVKRGTNIILN---IGRMhkleffPK----PNEFSLENF---EKNVPSRYFQ--PFGFGPR 434
Cdd:cd11073  306 PAPlLLPRKAEEDVEVMGYTIPKGTQVLVNvwaIGRD------PSvwedPLEFKPERFlgsEIDFKGRDFEliPFGSGRR 379
                        410       420
                 ....*....|....*....|...
gi 532691798 435 GCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd11073  380 ICPGLPLAERMVHLVLASLLHSF 402
PLN02290 PLN02290
cytokinin trans-hydroxylase
76-458 1.86e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 94.11  E-value: 1.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  76 YNKMYGEFMRVWISGEETLIISKSSSI-----FHVMKHGQ-YICRFGSKlglQCIGmheNGIIFNNNpALWKEIRPFFTK 149
Cdd:PLN02290  89 WSKQYGKRFIYWNGTEPRLCLTETELIkelltKYNTVTGKsWLQQQGTK---HFIG---RGLLMANG-ADWYHQRHIAAP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 150 ALSGPGLVRMIAICVESTKDHLDRL-EDVTAGLGNINVLNFMRQITLDT-SNTLFlGIPLDENAIVLKIQNYFDAWQALL 227
Cdd:PLN02290 162 AFMGDRLKGYAGHMVECTKQMLQSLqKAVESGQTEVEIGEYMTRLTADIiSRTEF-DSSYEKGKQIFHLLTVLQRLCAQA 240
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 228 LKPDIFFKISWLYKKYEKSVKDLKEAIE-VLIE--QKRQRLSTVEKLEEH-MDFASQLIFAQSRGDLTGENVNqcvLEMM 303
Cdd:PLN02290 241 TRHLCFPGSRFFPSKYNREIKSLKGEVErLLMEiiQSRRDCVEIGRSSSYgDDLLGMLLNEMEKKRSNGFNLN---LQLI 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 304 I--------AAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRK 375
Cdd:PLN02290 318 MdecktfffAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRM 397
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 376 ALQDDVIDGYPVKRGTNIILNIGRMHKLE--FFPKPNEFSLENF--EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILV 451
Cdd:PLN02290 398 AFEDIKLGDLHIPKGLSIWIPVLAIHHSEelWGKDANEFNPDRFagRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILA 477

                 ....*..
gi 532691798 452 TLLRRYR 458
Cdd:PLN02290 478 MLISKFS 484
PLN02936 PLN02936
epsilon-ring hydroxylase
229-486 4.03e-20

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 92.93  E-value: 4.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 229 KPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKL---EEHMDFA--SQLIF-AQSRGDLTGENVNQCVLEM 302
Cdd:PLN02936 207 KVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGEViegEEYVNDSdpSVLRFlLASREEVSSVQLRDDLLSM 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 303 MIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVI 382
Cdd:PLN02936 287 LVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVL 366
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 383 -DGYPVKRGTNIILNIGRMHKL-EFFPKPNEFSLENF--------EKNVPSRYFqPFGFGPRGCVGKFIAMVMMKAILVT 452
Cdd:PLN02936 367 pGGYKVNAGQDIMISVYNIHRSpEVWERAEEFVPERFdldgpvpnETNTDFRYI-PFSGGPRKCVGDQFALLEAIVALAV 445
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 532691798 453 LLRRYRVQTPKGRGLK-----NIQKSNDLSMHPNERQPF 486
Cdd:PLN02936 446 LLQRLDLELVPDQDIVmttgaTIHTTNGLYMTVSRRRVP 484
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
246-460 4.51e-20

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 92.83  E-value: 4.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 246 SVKDLKEAIEV-------LIEQKRqrlstVEKLEEHMDFASQliFAQSRGDltGENVNQCVLEMMIAAPDTLS--VTLFF 316
Cdd:PLN02426 247 SERKLKEAIKLvdelaaeVIRQRR-----KLGFSASKDLLSR--FMASIND--DKYLRDIVVSFLLAGRDTVAsaLTSFF 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 317 MLVliAEHPKVEEDMMKEIQAVIGDRDVQSN--DMSNLKVVENFINESMRYQPVVDLVMRKALQDDVI-DGYPVKRGTNI 393
Cdd:PLN02426 318 WLL--SKHPEVASAIREEADRVMGPNQEAASfeEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLpDGTFVAKGTRV 395
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 394 ILN---IGRMHK------LEFFP----KPNEFSLENfeknvPSRY--FQPfgfGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:PLN02426 396 TYHpyaMGRMERiwgpdcLEFKPerwlKNGVFVPEN-----PFKYpvFQA---GLRVCLGKEMALMEMKSVAVAVVRRFD 467

                 ..
gi 532691798 459 VQ 460
Cdd:PLN02426 468 IE 469
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
290-484 5.21e-20

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 92.36  E-value: 5.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 290 LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPV 368
Cdd:cd11028  227 LTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGrERLPRLSDRPNLPYTEAFILETMRHSSF 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 369 VDLVM-RKALQDDVIDGYPVKRGTNIILNI-GRMHKLEFFPKPNEFSLENF---EKNV---PSRYFQPFGFGPRGCVGKF 440
Cdd:cd11028  307 VPFTIpHATTRDTTLNGYFIPKGTVVFVNLwSVNHDEKLWPDPSVFRPERFlddNGLLdktKVDKFLPFGAGRRRCLGEE 386
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 532691798 441 IAMVMMKAILVTLLRRYRVQTPKGRGLKNIQKSNdLSMHPNERQ 484
Cdd:cd11028  387 LARMELFLFFATLLQQCEFSVKPGEKLDLTPIYG-LTMKPKPFK 429
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
289-461 7.84e-20

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 91.90  E-value: 7.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 289 DLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQS-NDMSNLKVVENFINESMRYQP 367
Cdd:cd20647  232 ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTaEDVPKLPLIRALLKETLRLFP 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 368 VVDLVMRKALQDDVIDGYPVKRGTNIIL-NIGRMHKLEFFPKPNEFSlenfeknvPSRYFQ-------------PFGFGP 433
Cdd:cd20647  312 VLPGNGRVTQDDLIVGGYLIPKGTQLALcHYSTSYDEENFPRAEEFR--------PERWLRkdaldrvdnfgsiPFGYGI 383
                        170       180
                 ....*....|....*....|....*...
gi 532691798 434 RGCVGKFIAMVMMKAILVTLLRRYRVQT 461
Cdd:cd20647  384 RSCIGRRIAELEIHLALIQLLQNFEIKV 411
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
231-467 9.26e-20

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 91.61  E-value: 9.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 DIFfkiSWLYKKYEKSVKDLKEAIEVlieqkRQRLSTvEKLEEHM-----DFASQLIFAQSRGDLTGENVNQC------- 298
Cdd:cd20673  157 DIF---PWLQIFPNKDLEKLKQCVKI-----RDKLLQ-KKLEEHKekfssDSIRDLLDALLQAKMNAENNNAGpdqdsvg 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 299 ---------VLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPV 368
Cdd:cd20673  228 lsddhilmtVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGfSRTPTLSDRNHLPLLEATIREVLRIRPV 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 369 VDLVM-RKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLENF------EKNVPSRYFQPFGFGPRGCVGKF 440
Cdd:cd20673  308 APLLIpHVALQDSSIGEFTIPKGTRVVINLWALHHDEkEWDQPDQFMPERFldptgsQLISPSLSYLPFGAGPRVCLGEA 387
                        250       260
                 ....*....|....*....|....*..
gi 532691798 441 IAMVMMKAILVTLLRRYRVQTPKGRGL 467
Cdd:cd20673  388 LARQELFLFMAWLLQRFDLEVPDGGQL 414
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
237-486 1.12e-19

cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus cytochrome P450 64 (CYP64), also called O-methylsterigmatocystin (OMST) oxidoreductase or aflatoxin B synthase or aflatoxin biosynthesis protein Q, and similar fungal cytochrome P450s. CYP64 converts OMST to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway. The CYP64-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410688 [Multi-domain]  Cd Length: 425  Bit Score: 91.10  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 237 SWLYKKYEKSVKDLKEAIEVLIEQKRQR-LSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVL-EMMIAAPDTLSVTL 314
Cdd:cd11065  164 SWLGAPWKRKARELRELTRRLYEGPFEAaKERMASGTATPSFVKDLLEELDKEGGLSEEEIKYLAgSLYEAGSDTTASTL 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 315 FFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVKRGTN 392
Cdd:cd11065  244 QTFILAMALHPEVQKKAQEELDRVVGpDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKGTT 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 393 IILNI-GRMHKLEFFPKPNEFSLENFEKN------VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGR 465
Cdd:cd11065  324 VIPNAwAIHHDPEVYPDPEEFDPERYLDDpkgtpdPPDPPHFAFGFGRRICPGRHLAENSLFIAIARLLWAFDIKKPKDE 403
                        250       260
                 ....*....|....*....|....*
gi 532691798 466 GLKNIQKSNDLS----MHPNerqPF 486
Cdd:cd11065  404 GGKEIPDEPEFTdglvSHPL---PF 425
PTZ00404 PTZ00404
cytochrome P450; Provisional
233-488 2.76e-19

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 90.55  E-value: 2.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 233 FFKISW-LYKKY-EKSVKDLKEAIEVLIEQKRQRLSTVeKLEEHMDFASQLIfaQSRGDLTGE---NVNQCVLEMMIAAP 307
Cdd:PTZ00404 220 VIEITQpLYYQYlEHTDKNFKKIKKFIKEKYHEHLKTI-DPEVPRDLLDLLI--KEYGTNTDDdilSILATILDFFLAGV 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 308 DTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRD-VQSNDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVI-DG 384
Cdd:PTZ00404 297 DTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNkVLLSDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIgGG 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 385 YPVKRGTNIILN---IGRMHKleFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQT 461
Cdd:PTZ00404 377 HFIPKDAQILINyysLGRNEK--YFENPEQFDPSRFLNPDSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKS 454
                        250       260
                 ....*....|....*....|....*..
gi 532691798 462 PKGRGLKNIQKSNdLSMHPNERQPFLE 488
Cdd:PTZ00404 455 IDGKKIDETEEYG-LTLKPNKFKVLLE 480
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
302-464 5.04e-19

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 89.20  E-value: 5.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 302 MMI----AAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRD--VQSNDMSNLKVVENFINESMRYQPVVDLVMRK 375
Cdd:cd11042  216 LLIallfAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDdpLTYDVLKEMPLLHACIKETLRLHPPIHSLMRK 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 376 ALQD--DVIDGYPVKRGTNIILNIGRMHKL-EFFPKPNEFSLENFEKNVP------SRYFQPFGFGPRGCVGKFIAMVMM 446
Cdd:cd11042  296 ARKPfeVEGGGYVIPKGHIVLASPAVSHRDpEIFKNPDEFDPERFLKGRAedskggKFAYLPFGAGRHRCIGENFAYLQI 375
                        170
                 ....*....|....*...
gi 532691798 447 KAILVTLLRRYRVQTPKG 464
Cdd:cd11042  376 KTILSTLLRNFDFELVDS 393
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
233-454 7.68e-19

cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome P450 family 71 (CYP71) proteins, as well as some CYPs designated as belonging to a different family including CYP99A1, CYP83B1, and CYP84A1, among others. Characterized CYP71 enzymes include: parsnip (Pastinaca sativa) CYP71AJ4, also called angelicin synthase, that converts (+)-columbianetin to angelicin, an angular furanocumarin; periwinkle (Catharanthus roseus) CYP71D351, also called tabersonine 16-hydroxylase 2, that is involved in the foliar biosynthesis of vindoline; sorghum CYP71E1, also called 4-hydroxyphenylacetaldehyde oxime monooxygenase, that catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile; as well as maize CYP71C1, CYP71C2, and CYP71C4, which are monooxygenases catalyzing the oxidation of 3-hydroxyindolin-2-one, indolin-2-one, and indole, respectively. CYPs within a single CYP71 subfamily, such as the C subfamily, usually metabolize similar/related compounds. The CYP71-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410695 [Multi-domain]  Cd Length: 428  Bit Score: 88.67  E-value: 7.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 233 FFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRGD--LTGENVNQCVLEMMIAAPDTL 310
Cdd:cd11072  165 IDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEfpLTRDNIKAIILDMFLAGTDTS 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 311 SVTLFFMLVLIAEHPKVeedmMK----EIQAVIGDRD-VQSNDMSNLKVVENFINESMRYQPVVD-LVMRKALQDDVIDG 384
Cdd:cd11072  245 ATTLEWAMTELIRNPRV----MKkaqeEVREVVGGKGkVTEEDLEKLKYLKAVIKETLRLHPPAPlLLPRECREDCKING 320
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532691798 385 YPVKRGTNIILN---IGRMHKLefFPKPNEFSLENFEkNVPSRY----FQ--PFGFGPRGCVGKFIAMVMMKAILVTLL 454
Cdd:cd11072  321 YDIPAKTRVIVNawaIGRDPKY--WEDPEEFRPERFL-DSSIDFkgqdFEliPFGAGRRICPGITFGLANVELALANLL 396
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
171-460 8.31e-19

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 88.41  E-value: 8.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 171 LDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPL-------DENAIVLKIQNYFDAWQALLLKPDIffkISWLYKKY 243
Cdd:cd11060   88 VDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFgfleagtDVDGYIASIDKLLPYFAVVGQIPWL---DRLLLKNP 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 244 EKSVKDLKEAIEVLIE------QKRQRLSTVEKLEEHmDFASQLIFAQSRG--DLTGENVNQCVLEMMIAAPDTLSVTLF 315
Cdd:cd11060  165 LGPKRKDKTGFGPLMRfaleavAERLAEDAESAKGRK-DMLDSFLEAGLKDpeKVTDREVVAEALSNILAGSDTTAIALR 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 316 FMLVLIAEHPKVEEDMMKEIQAVIGD-------RDVQSNDMSNLKVVenfINESMRYQPVVDLVM-RKALQD-DVIDGYP 386
Cdd:cd11060  244 AILYYLLKNPRVYAKLRAEIDAAVAEgklsspiTFAEAQKLPYLQAV---IKEALRLHPPVGLPLeRVVPPGgATICGRF 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 387 VKRGTNIILNIGRMHKLE--FFPKPNEF----SLENFEKNVP--SRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:cd11060  321 IPGGTIVGVNPWVIHRDKevFGEDADVFrperWLEADEEQRRmmDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFD 400

                 ..
gi 532691798 459 VQ 460
Cdd:cd11060  401 FE 402
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
248-471 1.21e-18

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 88.24  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 248 KDLKEAIEvlieqkrQRLSTVEK-LEEH------------MDFASQLIFAQS----RGDLTGENVNQCVLEMMIAAPDTL 310
Cdd:cd20674  170 RRLKQAVE-------NRDHIVESqLRQHkeslvagqwrdmTDYMLQGLGQPRgekgMGQLLEGHVHMAVVDLFIGGTETT 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 311 SVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQS-NDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVK 388
Cdd:cd20674  243 ASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSyKDRARLPLLNATIAEVLRLRPVVPLaLPHRTTRDSSIAGYDIP 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 389 RGTNIILNI-GRMHKLEFFPKPNEFSLENF-EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRG 466
Cdd:cd20674  323 KGTVVIPNLqGAHLDETVWEQPHEFRPERFlEPGAANRALLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGA 402

                 ....*
gi 532691798 467 LKNIQ 471
Cdd:cd20674  403 LPSLQ 407
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
290-453 1.47e-18

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 88.04  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 290 LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPV 368
Cdd:cd20655  224 ITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGkTRLVQESDLPNLPYLQAVVKETLRLHPP 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 369 VDLVMRKALQDDVIDGYPVKRGTNIILN---IGRmhKLEFFPKPNEFSLENFEKNVPS--------RYFQ--PFGFGPRG 435
Cdd:cd20655  304 GPLLVRESTEGCKINGYDIPEKTTLFVNvyaIMR--DPNYWEDPLEFKPERFLASSRSgqeldvrgQHFKllPFGSGRRG 381
                        170
                 ....*....|....*...
gi 532691798 436 CVGKFIAMVMMKAILVTL 453
Cdd:cd20655  382 CPGASLAYQVVGTAIAAM 399
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
244-466 2.22e-18

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 86.59  E-value: 2.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 244 EKSVKDLKEAIEVLIEQKRQRLSTvekleehmDFASQLIFAQSRG-DLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIA 322
Cdd:cd20629  149 EAAAAELYDYVLPLIAERRRAPGD--------DLISRLLRAEVEGeKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLL 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 323 EHPKVeedmmkeIQAVIGDRDVqsndmsnlkvVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHK 402
Cdd:cd20629  221 QHPEQ-------LERVRRDRSL----------IPAAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANR 283
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532691798 403 LE-FFPKPNEFSLenFEKNVPSryfQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR-------VQTPKGRG 466
Cdd:cd20629  284 DEdVYPDPDVFDI--DRKPKPH---LVFGGGAHRCLGEHLARVELREALNALLDRLPnlrldpdAPAPEISG 350
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
238-446 4.98e-18

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 86.12  E-value: 4.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 238 WL-YKKYEKSVKDLKEAIEVLI-----EQKRQRLSTVEKLEEHMdfasqLIFAQSRGDL-TGENVNQCVLEMMIAAPDTL 310
Cdd:cd20653  169 WFdFQGLEKRVKKLAKRRDAFLqglidEHRKNKESGKNTMIDHL-----LSLQESQPEYyTDEIIKGLILVMLLAGTDTS 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 311 SVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVD-LVMRKALQDDVIDGYPVK 388
Cdd:cd20653  244 AVTLEWAMSNLLNHPEVLKKAREEIDTQVGqDRLIEESDLPKLPYLQNIISETLRLYPAAPlLVPHESSEDCKIGGYDIP 323
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 389 RGTNIILNIGRMHK-LEFFPKPNEFSLENFEKNVPSRY-FQPFGFGPRGCVGKFIAMVMM 446
Cdd:cd20653  324 RGTMLLVNAWAIHRdPKLWEDPTKFKPERFEGEEREGYkLIPFGLGRRACPGAGLAQRVV 383
PLN02655 PLN02655
ent-kaurene oxidase
231-485 5.84e-18

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 86.33  E-value: 5.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 DIFFKISWL-YKKYEKSVKDL---KEAI-EVLIEQKRQRLSTVEKLEEHMDFASQlifaqSRGDLTGENVNQCVLEMMIA 305
Cdd:PLN02655 199 DFFPYLSWIpNKSFETRVQTTefrRTAVmKALIKQQKKRIARGEERDCYLDFLLS-----EATHLTDEQLMMLVWEPIIE 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 306 APDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMR-YQPVVDLVMRKALQDDVIDG 384
Cdd:PLN02655 274 AADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLPYLNAVFHETLRkYSPVPLLPPRFVHEDTTLGG 353
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 385 YPVKRGTNIILNI-GRMHKLEFFPKPNEFSLENF---EKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRV 459
Cdd:PLN02655 354 YDIPAGTQIAINIyGCNMDKKRWENPEEWDPERFlgeKYESADMYkTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEW 433
                        250       260       270
                 ....*....|....*....|....*....|..
gi 532691798 460 QTPKGRGLK------NIQKSNDLSMHPNERQP 485
Cdd:PLN02655 434 RLREGDEEKedtvqlTTQKLHPLHAHLKPRGS 465
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
303-461 5.98e-18

cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 86.05  E-value: 5.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 303 MIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQaVIGDR--DVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDD 380
Cdd:cd20649  270 LIAGYETTTNTLSFATYLLATHPECQKKLLREVD-EFFSKheMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDC 348
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 381 VIDGYPVKRGTNIILNIGRMH-KLEFFPKPNEFSLENFEKNVPSRY----FQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd20649  349 VVLGQRIPAGAVLEIPVGFLHhDPEHWPEPEKFIPERFTAEAKQRRhpfvYLPFGAGPRSCIGMRLALLEIKVTLLHILR 428

                 ....*.
gi 532691798 456 RYRVQT 461
Cdd:cd20649  429 RFRFQA 434
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
291-464 7.42e-18

cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including insect cytochrome P450 306A1 (CYP306A1 or Cyp306a1) and CYP18A1. CYP306A1 functions as a carbon 25-hydroxylase and has an essential role in ecdysteroid biosynthesis during insect development. CYP18A1 is a 26-hydroxylase and plays a key role in steroid hormone inactivation. The CYP306A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 85.92  E-value: 7.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 291 TGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRD-VQSNDMSNLKVVENFINESMRYQPVV 369
Cdd:cd20652  231 TDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDlVTLEDLSSLPYLQACISESQRIRSVV 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 370 DL-VMRKALQDDVIDGYPVKRGTNIILNIGRMH-KLEFFPKPNEFSLENF----EKNVPSRYFQPFGFGPRGCVGKFIAM 443
Cdd:cd20652  311 PLgIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHmDPNLWEEPEEFRPERFldtdGKYLKPEAFIPFQTGKRMCLGDELAR 390
                        170       180
                 ....*....|....*....|.
gi 532691798 444 VMMKAILVTLLRRYRVQTPKG 464
Cdd:cd20652  391 MILFLFTARILRKFRIALPDG 411
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
252-455 2.25e-17

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 84.10  E-value: 2.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 252 EAIEVLIEQKRQRLSTveklEEHMDFASQLIFAQSRGDltGENVN-----QCVLEMMIAAPDTLSVTLFFMLVLIAEHPK 326
Cdd:cd20638  189 AKIEENIRAKIQREDT----EQQCKDALQLLIEHSRRN--GEPLNlqalkESATELLFGGHETTASAATSLIMFLGLHPE 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 327 VEEDMMKEIQ--AVIGDRDVQSNDMS-----NLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGR 399
Cdd:cd20638  263 VLQKVRKELQekGLLSTKPNENKELSmevleQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICD 342
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532691798 400 MHKL-EFFPKPNEFSLENFEKNVP---SRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd20638  343 THDVaDIFPNKDEFNPDRFMSPLPedsSRFsFIPFGGGSRSCVGKEFAKVLLKIFTVELAR 403
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
241-489 2.51e-17

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 84.49  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 241 KKYEKSVKDLKEAIevlIEQKRQRLSTVEKLEEHMDFASQLIfaqsrgDLTGEN---------VNQCVLEMMIAAPDTLS 311
Cdd:PLN03112 243 REVEKRVDEFHDKI---IDEHRRARSGKLPGGKDMDFVDVLL------SLPGENgkehmddveIKALMQDMIAAATDTSA 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 312 VTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVD-LVMRKALQDDVIDGYPVKR 389
Cdd:PLN03112 314 VTNEWAMAEVIKNPRVLRKIQEELDSVVGrNRMVQESDLVHLNYLRCVVRETFRMHPAGPfLIPHESLRATTINGYYIPA 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 390 GTNIILNI---GRMHKLefFPKPNEFSLENFEKNVPSRYFQ---------PFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:PLN03112 394 KTRVFINThglGRNTKI--WDDVEEFRPERHWPAEGSRVEIshgpdfkilPFSAGKRKCPGAPLGVTMVLMALARLFHCF 471
                        250       260       270
                 ....*....|....*....|....*....|..
gi 532691798 458 RVQTPKGRGLKNIQKSNDLSMHPNERQPFLEM 489
Cdd:PLN03112 472 DWSPPDGLRPEDIDTQEVYGMTMPKAKPLRAV 503
PLN02966 PLN02966
cytochrome P450 83A1
243-482 3.15e-17

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 84.41  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 243 YEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQsrgDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIA 322
Cdd:PLN02966 241 FERQDTYIQEVVNETLDPKRVKPETESMIDLLMEIYKEQPFAS---EFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLM 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 323 EHPKVEEDMMKEIQAVIGDRD---VQSNDMSNLKVVENFINESMRYQPVVDLVM-RKALQDDVIDGYPVKRGTNIILN-- 396
Cdd:PLN02966 318 KYPQVLKKAQAEVREYMKEKGstfVTEDDVKNLPYFRALVKETLRIEPVIPLLIpRACIQDTKIAGYDIPAGTTVNVNaw 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 397 -IGRMHKlEFFPKPNEFSLENF-EKNVPSR----YFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNI 470
Cdd:PLN02966 398 aVSRDEK-EWGPNPDEFRPERFlEKEVDFKgtdyEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPDDI 476
                        250
                 ....*....|....
gi 532691798 471 QKS--NDLSMHPNE 482
Cdd:PLN02966 477 NMDvmTGLAMHKSQ 490
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
217-473 4.30e-17

cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; Cytochrome P450 27A1 (CYP27A1, EC 1.14.15.15) is also called CYP27, cholestanetriol 26-monooxygenase, sterol 26-hydroxylase, 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase, cytochrome P-450C27/25, sterol 27-hydroxylase, or vitamin D(3) 25-hydroxylase. It catalyzes the first step in the oxidation of the side chain of sterol intermediates, the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, and the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. It also hydroxylates vitamin D3 at the 25-position, as well as cholesterol at positions 24 and 25. CYP27A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 83.56  E-value: 4.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 217 QNYFDAWQalllkpDIFfkiswlykKYEKSVKDLKeaievlIEQKRQRLSTVEKLEehmdfASQLIFAQSRGDLTGENVN 296
Cdd:cd20646  181 KRYVDAWD------TIF--------SFGKKLIDKK------MEEIEERVDRGEPVE-----GEYLTYLLSSGKLSPKEVY 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 297 QCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVI-GDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRK 375
Cdd:cd20646  236 GSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCpGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARV 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 376 ALQDDVIDG---YPVKrgTNIIL-NIGRMHKLEFFPKPNEFSLENFEKNVPSRY----FQPFGFGPRGCVGKFIAMVMMK 447
Cdd:cd20646  316 IVEKEVVVGdylFPKN--TLFHLcHYAVSHDETNFPEPERFKPERWLRDGGLKHhpfgSIPFGYGVRACVGRRIAELEMY 393
                        250       260
                 ....*....|....*....|....*..
gi 532691798 448 AILVTLLRRYRVQ-TPKGRGLKNIQKS 473
Cdd:cd20646  394 LALSRLIKRFEVRpDPSGGEVKAITRT 420
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
293-461 4.61e-17

cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain cleavage enzyme; Cytochrome P450 11A1 (CYP11A1, EC 1.14.15.6) is also called cholesterol side-chain cleavage enzyme, cholesterol desmolase, or cytochrome P450(scc). It catalyzes the side-chain cleavage reaction of cholesterol to form pregnenolone, the precursor of all steroid hormones. Missense or nonsense mutations of the CYP11A1 gene cause mild to severe early-onset adrenal failure depending on the severity of the enzyme dysfunction/deficiency. CYP11A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 83.23  E-value: 4.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAviGDRDVQSNDMSNLKVV---ENFINESMRYQPVV 369
Cdd:cd20643  233 EDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLA--ARQEAQGDMVKMLKSVpllKAAIKETLRLHPVA 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 370 DLVMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENFEKNvPSRYFQP--FGFGPRGCVGKFIAMVMM 446
Cdd:cd20643  311 VSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRdPTVFPKPEKYDPERWLSK-DITHFRNlgFGFGPRQCLGRRIAETEM 389
                        170
                 ....*....|....*
gi 532691798 447 KAILVTLLRRYRVQT 461
Cdd:cd20643  390 QLFLIHMLENFKIET 404
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
236-482 7.37e-17

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 83.20  E-value: 7.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 236 ISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRG-DLTGENVNQCVLEMMIAAPDTLSVTL 314
Cdd:PLN03234 229 LTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPFSiKFTHENVKAMILDIVVPGTDTAAAVV 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 315 FFMLVLIAEHPKVEEDMMKEIQAVIGDRD-VQSNDMSNLKVVENFINESMRYQPVVDLVM-RKALQDDVIDGYPVKRGTN 392
Cdd:PLN03234 309 VWAMTYLIKYPEAMKKAQDEVRNVIGDKGyVSEEDIPNLPYLKAVIKESLRLEPVIPILLhRETIADAKIGGYDIPAKTI 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 393 IILNIGRMHK--LEFFPKPNEFSLENFEKNVPSRYFQ-------PFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPK 463
Cdd:PLN03234 389 IQVNAWAVSRdtAAWGDNPNEFIPERFMKEHKGVDFKgqdfellPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPK 468
                        250       260
                 ....*....|....*....|.
gi 532691798 464 GRGLKNIQKS--NDLSMHPNE 482
Cdd:PLN03234 469 GIKPEDIKMDvmTGLAMHKKE 489
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
127-480 2.12e-16

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 81.38  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 127 HENGIIFNNNpALWKEIRPFFTKALSGPGLVR--MIAICVESTK---DHLD-------RLEDVTAGLGNINVL------- 187
Cdd:cd20671   48 HGNGVFFSSG-ERWRTTRRFTVRSMKSLGMGKrtIEDKILEELQflnGQIDsfngkpfPLRLLGWAPTNITFAmlfgrrf 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 188 -----NFMRQITLDTSNTLFLGIPLdenaivLKIQNYFdAWQALLLKPdiffkiswlYKKYEKSVKDLKEAIEVLIEQKR 262
Cdd:cd20671  127 dykdpTFVSLLDLIDEVMVLLGSPG------LQLFNLY-PVLGAFLKL---------HKPILDKVEEVCMILRTLIEARR 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 263 QRLSTvEKLEEHMDfasqLIFAQSRGDLTGE------NVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQ 336
Cdd:cd20671  191 PTIDG-NPLHSYIE----ALIQKQEEDDPKEtlfhdaNVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEID 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 337 AVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNII-LNIGRMHKLEFFPKPNEFSL 414
Cdd:cd20671  266 RVLGpGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIpLLSSVLLDKTQWETPYQFNP 345
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 415 ENF----EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRglkniqKSNDLSMHP 480
Cdd:cd20671  346 NHFldaeGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPGV------SPADLDATP 409
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
239-460 2.35e-16

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 81.52  E-value: 2.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 239 LYKKYEKSVKDLKEAIEVLIEQKRQRLStvekleEHMDFASQliFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFML 318
Cdd:PLN02196 217 LFHKSMKARKELAQILAKILSKRRQNGS------SHNDLLGS--FMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWIL 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 319 VLIAEHPKVEEDMMKEIQAVIGDRDVQSN----DMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNII 394
Cdd:PLN02196 289 KYLAENPSVLEAVTEEQMAIRKDKEEGESltweDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVL 368
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532691798 395 ---LNIgrMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQ 460
Cdd:PLN02196 369 plfRNI--HHSADIFSDPGKFDPSRFEVAPKPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWS 435
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
259-464 3.19e-16

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 80.65  E-value: 3.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 259 EQKRQRLSTVEKLEEHMDF-ASQLIFAQSRGDLT--GENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEI 335
Cdd:cd20667  187 EVIRHELRTNEAPQDFIDCyLAQITKTKDDPVSTfsEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQEL 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 336 QAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVKRGTNIILNIGR-MHKLEFFPKPNEF 412
Cdd:cd20667  267 DEVLGaSQLICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCVTSTTMHGYYVEKGTIILPNLASvLYDPECWETPHKF 346
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 532691798 413 SLENF-EKN---VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKG 464
Cdd:cd20667  347 NPGHFlDKDgnfVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQLPEG 402
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
305-463 3.43e-16

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 80.54  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 305 AAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSND----MSNLKVVenfINESMRYQPVVDLVMRKALQDD 380
Cdd:cd20650  239 AGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDtvmqMEYLDMV---VNETLRLFPIAGRLERVCKKDV 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 381 VIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENFEK----NVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd20650  316 EINGVFIPKGTVVMIPTYALHRdPQYWPEPEEFRPERFSKknkdNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQ 395

                 ....*...
gi 532691798 456 RYRVQTPK 463
Cdd:cd20650  396 NFSFKPCK 403
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
207-459 4.63e-16

cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4F subfamily show diverse specificities among its members: CYP4F2 and CYP4F3 metabolize pro- and anti-inflammatory leukotrienes; CYP4F8 and CYP4F12 metabolize prostaglandins, endoperoxides and arachidonic acid; CYP4F11 and CYP4F12 metabolize VLFA and are unique in the CYP4F subfamily since they also hydroxylate xenobiotics such as benzphetamine, ethylmorphine, erythromycin, and ebastine. CYP4F belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 80.12  E-value: 4.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 207 LDENAIVLKIQNYfdawqaLLLKPDIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEE--------HMDFA 278
Cdd:cd20679  153 LELSALVVKRQQQ------LLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFlkakakskTLDFI 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 279 SQLIFAQSR--GDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQS---NDMSNLK 353
Cdd:cd20679  227 DVLLLSKDEdgKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEiewDDLAQLP 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 354 VVENFINESMRYQPVVDLVMRKALQDDVI-DGYPVKRGTNIILNI-GRMHKLEFFPKPN-----EFSLENFEKNVPsRYF 426
Cdd:cd20679  307 FLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIyGTHHNPTVWPDPEvydpfRFDPENSQGRSP-LAF 385
                        250       260       270
                 ....*....|....*....|....*....|...
gi 532691798 427 QPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRV 459
Cdd:cd20679  386 IPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRV 418
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
300-463 6.84e-16

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 79.84  E-value: 6.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 300 LEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRKAL 377
Cdd:cd20668  232 LNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGrNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVT 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 378 QDDVIDGYPVKRGTNIILNIGR-MHKLEFFPKPNEFSLENF--EKNV--PSRYFQPFGFGPRGCVGKFIAMVMMKAILVT 452
Cdd:cd20668  312 KDTKFRDFFLPKGTEVFPMLGSvLKDPKFFSNPKDFNPQHFldDKGQfkKSDAFVPFSIGKRYCFGEGLARMELFLFFTT 391
                        170
                 ....*....|.
gi 532691798 453 LLRRYRVQTPK 463
Cdd:cd20668  392 IMQNFRFKSPQ 402
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
293-464 1.36e-15

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 78.69  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLV 372
Cdd:cd20664  224 DNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKNMPYTDAVIHEIQRFANIVPMN 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 373 MRKALQDDV-IDGYPVKRGTNII-LNIGRMHKLEFFPKPNEFSLENF----EKNVPSRYFQPFGFGPRGCVGKFIAMVMM 446
Cdd:cd20664  304 LPHATTRDVtFRGYFIPKGTYVIpLLTSVLQDKTEWEKPEEFNPEHFldsqGKFVKRDAFMPFSAGRRVCIGETLAKMEL 383
                        170
                 ....*....|....*...
gi 532691798 447 KAILVTLLRRYRVQTPKG 464
Cdd:cd20664  384 FLFFTSLLQRFRFQPPPG 401
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
141-500 1.40e-15

unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized fungal cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 78.50  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 141 KEIRPFFTK-ALSGPGLVRMIaicVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLG--IPLDENAIVLKIQ 217
Cdd:cd11059   60 RLLSGVYSKsSLLRAAMEPII---RERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGesFGTLLLGDKDSRE 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 218 NYFDAWQALLLKPDI-----FFKISWLY---KKYEKSVKDL-KEAIEvLIEQKRQRLSTVEKLEEHMDFASQLIFAQSRG 288
Cdd:cd11059  137 RELLRRLLASLAPWLrwlprYLPLATSRliiGIYFRAFDEIeEWALD-LCARAESSLAESSDSESLTVLLLEKLKGLKKQ 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 289 DLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSN--DMSNLKVVENFINESMRYQ 366
Cdd:cd11059  216 GLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPPDleDLDKLPYLNAVIRETLRLY 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 367 PVVDLVMRKALQDD--VIDGYPVKRGTNI-ILNIGrMHKL-EFFPKPNEFSLENFEKNVPS------RYFQPFGFGPRGC 436
Cdd:cd11059  296 PPIPGSLPRVVPEGgaTIGGYYIPGGTIVsTQAYS-LHRDpEVFPDPEEFDPERWLDPSGEtaremkRAFWPFGSGSRMC 374
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532691798 437 VGKFIAMVMMKAILVTLLRRYRVQTpkgrglkniqkSNDLSMHPnerqpflEMFFIPRRNIDKC 500
Cdd:cd11059  375 IGMNLALMEMKLALAAIYRNYRTST-----------TTDDDMEQ-------EDAFLAAPKGRRC 420
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
293-467 1.52e-15

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 78.69  E-value: 1.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD-RDVQSNDMSNLKVVENFINESMRYQPVVDL 371
Cdd:cd20662  224 ENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQkRQPSLADRESMPYTNAVIHEVQRMGNIIPL 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 372 -VMRKALQDDVIDGYPVKRGTNIILNIGRMHKlefFPK----PNEFSLENFEKNVPSR---YFQPFGFGPRGCVGKFIAM 443
Cdd:cd20662  304 nVPREVAVDTKLAGFHLPKGTMILTNLTALHR---DPKewatPDTFNPGHFLENGQFKkreAFLPFSMGKRACLGEQLAR 380
                        170       180
                 ....*....|....*....|....
gi 532691798 444 VMMKAILVTLLRRYRVQTPKGRGL 467
Cdd:cd20662  381 SELFIFFTSLLQKFTFKPPPNEKL 404
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
231-455 1.77e-15

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 78.47  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 231 DIFFKISWLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEE-----HMDFASQLIFAQ--SRGDLTGENVNQCVLEMM 303
Cdd:cd20678  169 DFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKikkkrHLDFLDILLFAKdeNGKSLSDEDLRAEVDTFM 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 304 IAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRD-VQSNDMSNLKVVENFINESMRYQPVVDLVMRKaLQDDVI 382
Cdd:cd20678  249 FEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDsITWEHLDQMPYTTMCIKEALRLYPPVPGISRE-LSKPVT 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 383 --DGYPVKRGTNIILNI-GRMHKLEFFPKPNEFSLENFEK-NVPSRY---FQPFGFGPRGCVGKFIAMVMMK-AILVTLL 454
Cdd:cd20678  328 fpDGRSLPAGITVSLSIyGLHHNPAVWPNPEVFDPLRFSPeNSSKRHshaFLPFSAGPRNCIGQQFAMNEMKvAVALTLL 407

                 .
gi 532691798 455 R 455
Cdd:cd20678  408 R 408
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
132-485 2.32e-15

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 77.68  E-value: 2.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 132 IFNNNPALWKEIRPFFTKALSGP---GLVRMIAICVESTKDHLDR---------LEDVTAGLgninvlnfmrqiTLDTSN 199
Cdd:cd11051   49 LISMEGEEWKRLRKRFNPGFSPQhlmTLVPTILDEVEIFAAILRElaesgevfsLEELTTNL------------TFDVIG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 200 TLFLGIPLDEnaivlkiQNYFDAWQALLLKPDIFFKISWLYKKYEKSVKDLKEAievlieQKRQRLSTVEKLEEHMDFAS 279
Cdd:cd11051  117 RVTLDIDLHA-------QTGDNSLLTALRLLLALYRSLLNPFKRLNPLRPLRRW------RNGRRLDRYLKPEVRKRFEL 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 280 QLIFAQSRGdltgenvnqcvleMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG---DRDVQ-----SNDMSN 351
Cdd:cd11051  184 ERAIDQIKT-------------FLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGpdpSAAAEllregPELLNQ 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 352 LKVVENFINESMRYQPVVdLVMRKA-----LQDDVIDGYPVKrGTNIILNIGRMHKLE-FFPKPNEFSLENF------EK 419
Cdd:cd11051  251 LPYTTAVIKETLRLFPPA-GTARRGppgvgLTDRDGKEYPTD-GCIVYVCHHAIHRDPeYWPRPDEFIPERWlvdeghEL 328
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532691798 420 NVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTP--------KGRGLKNIQKSNDLSMHPNERQP 485
Cdd:cd11051  329 YPPKSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFEKAydewdakgGYKGLKELFVTGQGTAHPVDGMP 402
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
288-483 3.99e-15

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 77.46  E-value: 3.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 288 GDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQ 366
Cdd:cd20657  222 ERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGrDRRLLESDIPNLPYLQAICKETFRLH 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 367 PVVDLVM-RKALQDDVIDGYPVKRGTNIILN---IGRMHKLefFPKPNEFSLENF--EKN----VPSRYFQ--PFGFGPR 434
Cdd:cd20657  302 PSTPLNLpRIASEACEVDGYYIPKGTRLLVNiwaIGRDPDV--WENPLEFKPERFlpGRNakvdVRGNDFEliPFGAGRR 379
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 532691798 435 GCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNI----------QKSNDLSMHPNER 483
Cdd:cd20657  380 ICAGTRMGIRMVEYILATLVHSFDWKLPAGQTPEELnmeeafglalQKAVPLVAHPTPR 438
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
254-475 4.29e-15

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 77.41  E-value: 4.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 254 IEVLIEQKRQRLSTVEklEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMK 333
Cdd:cd20658  199 IDERIKQWREGKKKEE--EDWLDVFITLKDENGNPLLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATE 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 334 EIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVM-RKALQDDVIDGYPVKRGTNIILN---IGRMHKleFFPK 408
Cdd:cd20658  277 ELDRVVGkERLVQESDIPNLNYVKACAREAFRLHPVAPFNVpHVAMSDTTVGGYFIPKGSHVLLSrygLGRNPK--VWDD 354
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532691798 409 PNEFSLE---NFEKNV----PSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNIQKSND 475
Cdd:cd20658  355 PLKFKPErhlNEDSEVtltePDLRFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPNVSSVDLSESKD 428
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
233-468 5.21e-15

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 77.51  E-value: 5.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 233 FFKISWLYKKY---------EKSVKDLKEAIEVLIEQKRQRLSTVEKLEEHM--DFASQLIFAQSRGD--LTGENVNQCV 299
Cdd:PLN03195 218 FIDPLWKLKKFlnigseallSKSIKVVDDFTYSVIRRRKAEMDEARKSGKKVkhDILSRFIELGEDPDsnFTDKSLRDIV 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 300 LEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDR----DVQSNDMSNLKVVE-----NF------------ 358
Cdd:PLN03195 298 LNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKALEKERakeeDPEDSQSFNQRVTQfagllTYdslgklqylhav 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 359 INESMRYQPVVDLVMRKALQDDVI-DGYPVKRG---TNIILNIGRMhKLEFFPKPNEFSLENFEKNVPSRYFQPFGF--- 431
Cdd:PLN03195 378 ITETLRLYPAVPQDPKGILEDDVLpDGTKVKAGgmvTYVPYSMGRM-EYNWGPDAASFKPERWIKDGVFQNASPFKFtaf 456
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 532691798 432 --GPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLK 468
Cdd:PLN03195 457 qaGPRICLGKDSAYLQMKMALALLCRFFKFQLVPGHPVK 495
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
74-464 8.27e-15

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 76.25  E-value: 8.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798  74 NYYNKmyGEFMRVWISGEETLIISKSSSIFHVMKHGQYIC------RFGSKL-GLQCIGMHENGIIFNNNpaLWKEIRPF 146
Cdd:cd11040    7 KYFSG--GPIFTIRLGGQKIYVITDPELISAVFRNPKTLSfdpiviVVVGRVfGSPESAKKKEGEPGGKG--LIRLLHDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 147 FTKALSGP-GLVRMIAICVESTKDHLDRLE-DVTAGLGNINVLNFMRQ-ITLDTSNTLFlGIPLDENAivLKIQNYFDAW 223
Cdd:cd11040   83 HKKALSGGeGLDRLNEAMLENLSKLLDELSlSGGTSTVEVDLYEWLRDvLTRATTEALF-GPKLPELD--PDLVEDFWTF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 224 QALLLKpdIFFKISWLYKKYEKSVKD-LKEAIEVLIEQKRqrlstvekleEHMDFASQLIFA----QSRGDLTGENVNQC 298
Cdd:cd11040  160 DRGLPK--LLLGLPRLLARKAYAARDrLLKALEKYYQAAR----------EERDDGSELIRArakvLREAGLSEEDIARA 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 299 VLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQ------SNDMSNLKVVENFINESMRYQpVVDLV 372
Cdd:cd11040  228 ELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTnaildlTDLLTSCPLLDSTYLETLRLH-SSSTS 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 373 MRKALQDDV-IDGYPVKRGTNIILNIGRMHKL-EFFPK-PNEFSLENFEKNVP-------SRYFQPFGFGPRGCVGKFIA 442
Cdd:cd11040  307 VRLVTEDTVlGGGYLLRKGSLVMIPPRLLHMDpEIWGPdPEEFDPERFLKKDGdkkgrglPGAFRPFGGGASLCPGRHFA 386
                        410       420
                 ....*....|....*....|..
gi 532691798 443 MVMMKAILVTLLRRYRVQTPKG 464
Cdd:cd11040  387 KNEILAFVALLLSRFDVEPVGG 408
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
293-487 8.42e-15

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 76.39  E-value: 8.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQS-NDMSNLKVVENFINESMRYQPVVDL 371
Cdd:cd20661  237 ENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSfEDKCKMPYTEAVLHEVLRFCNIVPL 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 372 -VMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLENF----EKNVPSRYFQPFGFGPRGCVGKFIAMVM 445
Cdd:cd20661  317 gIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEkYWSDPEVFHPERFldsnGQFAKKEAFVPFSLGRRHCLGEQLARME 396
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 532691798 446 MKAILVTLLRRYRVQTPKGRgLKNIQKSNDLSMHPnerQPFL 487
Cdd:cd20661  397 MFLFFTALLQRFHLHFPHGL-IPDLKPKLGMTLQP---QPYL 434
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
261-464 1.40e-14

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 75.60  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 261 KRQRLsTVEKLEEHMD----------FASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEED 330
Cdd:cd20656  188 RRDRL-TKAIMEEHTLarqksgggqqHFVALLTLKEQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEK 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 331 MMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVM-RKALQDDVIDGYPVKRGTNIILN---IGRMHKLef 405
Cdd:cd20656  267 AQEELDRVVGsDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLpHKASENVKIGGYDIPKGANVHVNvwaIARDPAV-- 344
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532691798 406 FPKPNEFSLENF---EKNVPSRYFQ--PFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKG 464
Cdd:cd20656  345 WKNPLEFRPERFleeDVDIKGHDFRllPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPEG 408
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
258-460 1.41e-14

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 75.61  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 258 IEQKRQRLSTveklEEHMDFASQlIFAQSRgdLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQA 337
Cdd:cd20645  197 IDKRLQRYSQ----GPANDFLCD-IYHDNE--LSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQS 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 338 VIGDRDV-QSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNigrMHKL----EFFPKPNEF 412
Cdd:cd20645  270 VLPANQTpRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMIN---SQALgsseEYFEDGRQF 346
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 532691798 413 SLENF--EKNVPSRYFQ-PFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQ 460
Cdd:cd20645  347 KPERWlqEKHSINPFAHvPFGIGKRMCIGRRLAELQLQLALCWIIQKYQIV 397
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
232-480 3.96e-14

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 74.04  E-value: 3.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 232 IFFKISWLY-------KKYEKSVKDLKEAIEVLIEQKRQRLSTveklEEHMDF-------ASQLIFAQSRGDLTGENVNQ 297
Cdd:cd20666  156 LVNICPWLYylpfgpfRELRQIEKDITAFLKKIIADHRETLDP----ANPRDFidmyllhIEEEQKNNAESSFNEDYLFY 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 298 CVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL-VMRK 375
Cdd:cd20666  232 IIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGpDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLsIPHM 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 376 ALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENFEKN----VPSRYFQPFGFGPRGCVGKFIAMVMMKAIL 450
Cdd:cd20666  312 ASENTVLQGYTIPKGTVIVPNLWSVHRdPAIWEKPDDFMPSRFLDEngqlIKKEAFIPFGIGRRVCMGEQLAKMELFLMF 391
                        250       260       270
                 ....*....|....*....|....*....|
gi 532691798 451 VTLLRRYRVQTPKGRGLKNIQKSNDLSMHP 480
Cdd:cd20666  392 VSLMQSFTFLLPPNAPKPSMEGRFGLTLAP 421
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
251-460 4.25e-14

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 74.02  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 251 KEAIEVLIEQKRQRLSTVEKLEEHMdfasqLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEED 330
Cdd:cd20648  196 KGHIDRRMAEVAAKLPRGEAIEGKY-----LTYFLAREKLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTA 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 331 MMKEIQAVIGDRDVQS-NDMSNLKVVENFINESMRYQPVVDLVMRKALQDDV-IDGYPVKRGTNIIL-NIGRMHKLEFFP 407
Cdd:cd20648  271 LHREITAALKDNSVPSaADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDIqVGEYIIPKKTLITLcHYATSRDENQFP 350
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532691798 408 KPNEFSlenfeknvPSRYFQ-----------PFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQ 460
Cdd:cd20648  351 DPNSFR--------PERWLGkgdthhpyaslPFGFGKRSCIGRRIAELEVYLALARILTHFEVR 406
PLN02687 PLN02687
flavonoid 3'-monooxygenase
261-483 4.80e-14

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 74.46  E-value: 4.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 261 KRQRLSTVEKLEEHMDFASQLIFAQSRGDLTGEN-------VNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMK 333
Cdd:PLN02687 257 EEHKAAGQTGSEEHKDLLSTLLALKREQQADGEGgritdteIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQE 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 334 EIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVM-RKALQDDVIDGYPVKRGTNIILNI-GRMHKLEFFPKPN 410
Cdd:PLN02687 337 ELDAVVGrDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLpRMAAEECEINGYHIPKGATLLVNVwAIARDPEQWPDPL 416
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 411 EFSLENF-------EKNVPSRYFQ--PFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGR-----------GLkNI 470
Cdd:PLN02687 417 EFRPDRFlpggehaGVDVKGSDFEliPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQtpdklnmeeayGL-TL 495
                        250
                 ....*....|...
gi 532691798 471 QKSNDLSMHPNER 483
Cdd:PLN02687 496 QRAVPLMVHPRPR 508
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
241-464 8.18e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 73.61  E-value: 8.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 241 KKYEKSVKDLKEA-----IEVLIEQKRQRLSTV----EKLEEHMDfasQLIFAQSRGDLTGENVNQCVLEMMIAAPDTls 311
Cdd:PLN02394 234 RGYLKICQDVKERrlalfKDYFVDERKKLMSAKgmdkEGLKCAID---HILEAQKKGEINEDNVLYIVENINVAAIET-- 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 312 vTLFFMLVLIAE---HPKVEEDMMKEIQAVIGDRD-VQSNDMSNLKVVENFINESMRYQ-PVVDLVMRKALQDDVIDGYP 386
Cdd:PLN02394 309 -TLWSIEWGIAElvnHPEIQKKLRDELDTVLGPGNqVTEPDTHKLPYLQAVVKETLRLHmAIPLLVPHMNLEDAKLGGYD 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 387 VKRGTNIILNIGRM-HKLEFFPKPNEFSLENF-------EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:PLN02394 388 IPAESKILVNAWWLaNNPELWKNPEEFRPERFleeeakvEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFE 467

                 ....*.
gi 532691798 459 VQTPKG 464
Cdd:PLN02394 468 LLPPPG 473
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
291-457 8.36e-14

cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group includes CYP2C, and similar CYPs including mammalian CYP2E1, also called 4-nitrophenol 2-hydroxylase, as well as chicken CYP2H1 and CYP2H2. The CYP2C subfamily is composed of four human members (CYP2C8, CYP2C9, CYP2C18, CYP2C19) that metabolize approximately 20% of clinically used drugs, and all four exhibit genetic polymorphisms that results in toxicity or altered efficacy of some drugs in affected individuals. CYP2E1 participates in the metabolism of endogenous substrates, including acetone and fatty acids, and exogenous compounds such as anesthetics, ethanol, nicotine, acetaminophen, aspartame, and chlorzoxazone, among others. The CYP2C-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 73.06  E-value: 8.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 291 TGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYqpvV 369
Cdd:cd20665  223 TLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGrHRSPCMQDRSHMPYTDAVIHEIQRY---I 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 370 DLV----MRKALQDDVIDGYPVKRGTNIILNIGR-MHKLEFFPKPNEFSLE-------NFEKnvpSRYFQPFGFGPRGCV 437
Cdd:cd20665  300 DLVpnnlPHAVTCDTKFRNYLIPKGTTVITSLTSvLHDDKEFPNPEKFDPGhfldengNFKK---SDYFMPFSAGKRICA 376
                        170       180
                 ....*....|....*....|
gi 532691798 438 GKFIAMVMMKAILVTLLRRY 457
Cdd:cd20665  377 GEGLARMELFLFLTTILQNF 396
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
224-457 1.06e-13

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 73.00  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 224 QALLLKPDIFFKISWLYKKyeKSVKDLKEAIEVLIEQKRQRLstvEKLEEHMDFASQLIFAQS-RGDLTGENVNQCVLEM 302
Cdd:cd11058  151 QALRRYPWLLRLLRLLIPK--SLRKKRKEHFQYTREKVDRRL---AKGTDRPDFMSYILRNKDeKKGLTREELEANASLL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 303 MIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQ-AVIGDRDVQSNDMSNLKVVENFINESMR-YQPVVDLVMRKALQD- 379
Cdd:cd11058  226 IIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRsAFSSEDDITLDSLAQLPYLNAVIQEALRlYPPVPAGLPRVVPAGg 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 380 DVIDGYPVKRGTNI-ILNIGRMHKLEFFPKPNEFSLENFEKNVPSRY-------FQPFGFGPRGCVGKFIAMVMMKAILV 451
Cdd:cd11058  306 ATIDGQFVPGGTSVsVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFdndkkeaFQPFSVGPRNCIGKNLAYAEMRLILA 385

                 ....*.
gi 532691798 452 TLLRRY 457
Cdd:cd11058  386 KLLWNF 391
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
170-462 1.71e-13

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 72.17  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 170 HLDRLEDVT--------AGLGNINVLNFMRQITLDTSNTLFLGIPLDENAIVLKIQNYFDAWQALLLKP-DIFFkiSWLy 240
Cdd:cd20636   99 YLPRIQDVVrsevrgwcRGPGPVAVYTAAKSLTFRIAVRILLGLRLEEQQFTYLAKTFEQLVENLFSLPlDVPF--SGL- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 241 KKYEKSVKDLKEAIEVLIEQKRQRlstvEKLEEHMDFASQLIFAQSRGD--LTGENVNQCVLEMMIAAPDTLSVTLFFML 318
Cdd:cd20636  176 RKGIKARDILHEYMEKAIEEKLQR----QQAAEYCDALDYMIHSARENGkeLTMQELKESAVELIFAAFSTTASASTSLV 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 319 VLIAEHPKVEEDMMKEIQAVIGDRDVQS-------NDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGT 391
Cdd:cd20636  252 LLLLQHPSAIEKIRQELVSHGLIDQCQCcpgalslEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGW 331
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532691798 392 NIILNIGRMHKL-EFFPKPNEFSLENF----EKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLR--RYRVQTP 462
Cdd:cd20636  332 SVMYSIRDTHETaAVYQNPEGFDPDRFgverEESKSGRFnYIPFGGGVRSCIGKELAQVILKTLAVELVTtaRWELATP 410
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
236-457 2.68e-13

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 71.93  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 236 ISWLYKKYEKSVKDLKEAIEVLIEQKRQrlSTVEKLEEHMDFASQLIfaQSRGDLTGENVNQCVLEMMIAAPDTLSVTLF 315
Cdd:PLN02987 213 FSTTYRRAIQARTKVAEALTLVVMKRRK--EEEEGAEKKKDMLAALL--ASDDGFSDEEIVDFLVALLVAGYETTSTIMT 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 316 FMLVLIAEHP----KVEEDMmKEIQAVIGDRDV-QSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRG 390
Cdd:PLN02987 289 LAVKFLTETPlalaQLKEEH-EKIRAMKSDSYSlEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKG 367
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532691798 391 TNIILNIGRMH-KLEFFPKPNEFSLENFEKN----VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:PLN02987 368 WKVFASFRAVHlDHEYFKDARTFNPWRWQSNsgttVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRF 439
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
124-458 2.73e-13

cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 71.48  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 124 IGMHENGIIFNNNPALWKEIRPFFTKALSGP------GLVRmiAICVEstkdHLDRLEDvtAGLGNInVLNFMRQITLDT 197
Cdd:cd11078   56 AGFAPTPSLVNEDPPRHTRLRRLVSRAFTPRriaalePRIR--ELAAE----LLDRLAE--DGRADF-VADFAAPLPALV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 198 SNTLfLGIPLDEnaiVLKIQNYFDAWQALLLKPDIFFKISWLYKkyekSVKDLKEAIEVLIEQKRQRLSTvekleehmDF 277
Cdd:cd11078  127 IAEL-LGVPEED---MERFRRWADAFALVTWGRPSEEEQVEAAA----AVGELWAYFADLVAERRREPRD--------DL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 278 ASQLIFAQSRGD--LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVeedmMKEIQAvigDRDVqsndmsnlkvV 355
Cdd:cd11078  191 ISDLLAAADGDGerLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQ----WRRLRA---DPSL----------I 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 356 ENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRM-HKLEFFPKPNEFSL--ENFEKNVpsryfqPFGFG 432
Cdd:cd11078  254 PNAVEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSAnRDERVFPDPDRFDIdrPNARKHL------TFGHG 327
                        330       340
                 ....*....|....*....|....*.
gi 532691798 433 PRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:cd11078  328 IHFCLGAALARMEARIALEELLRRLP 353
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
293-464 5.24e-13

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 70.88  E-value: 5.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD-RDVQSNDMSNLKVVENFINESMRYQPVVDL 371
Cdd:cd20663  229 ENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQvRRPEMADQARMPYTNAVIHEVQRFGDIVPL 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 372 -VMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLENF----EKNVPSRYFQPFGFGPRGCVGKFIAMVM 445
Cdd:cd20663  309 gVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDEtVWEKPLRFHPEHFldaqGHFVKPEAFMPFSAGRRACLGEPLARME 388
                        170
                 ....*....|....*....
gi 532691798 446 MKAILVTLLRRYRVQTPKG 464
Cdd:cd20663  389 LFLFFTCLLQRFSFSVPAG 407
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
269-482 6.74e-13

cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) consists of only one functional member CYP2B6, which shows broad substrate specificity and plays a key role in the metabolism of many clinical drugs, environmental toxins, and endogenous compounds. Rodents have multiple functional CYP2B proteins; mouse subfamily members include CYP2B9, 2B10, 2B13, 2B19, and 2B23. CYP2B enzymes are highly inducible by chemicals that interact with the constitutive androstane receptor (CAR) and/or pregnane X receptor (PXR), such as rifampicin and phenobarbital. The CYP2B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 70.58  E-value: 6.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 269 EKLEEHMDFASQlifaqsrgdltgeNVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQS-N 347
Cdd:cd20672  214 EKSNHHTEFHHQ-------------NLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTlD 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 348 DMSNLKVVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVKRGTNI--ILNiGRMHKLEFFPKPNEFSLENF-EKN--- 420
Cdd:cd20672  281 DRAKMPYTDAVIHEIQRFSDLIPIgVPHRVTKDTLFRGYLLPKNTEVypILS-SALHDPQYFEQPDTFNPDHFlDANgal 359
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 532691798 421 VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGrglkniqkSNDLSMHPNE 482
Cdd:cd20672  360 KKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVASPVA--------PEDIDLTPKE 413
PLN02971 PLN02971
tryptophan N-hydroxylase
237-462 7.21e-13

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 70.84  E-value: 7.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 237 SWLYKKYEKSVKDlkEAIEVLIEQKRQrlstveKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFF 316
Cdd:PLN02971 278 SAIMDKYHDPIID--ERIKMWREGKRT------QIEDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEW 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 317 MLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVM-RKALQDDVIDGYPVKRGTNII 394
Cdd:PLN02971 350 AMAEMINKPEILHKAMEEIDRVVGkERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLpHVALSDTTVAGYHIPKGSQVL 429
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 532691798 395 LN---IGRMHK-----LEFFPKP--NEFSLENFEKNvpSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTP 462
Cdd:PLN02971 430 LSrygLGRNPKvwsdpLSFKPERhlNECSEVTLTEN--DLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 505
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
305-458 8.45e-13

cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Arabidopsis thaliana CYP709B3 is involved in abscisic acid (ABA) and salt stress response. CYP709 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 70.17  E-value: 8.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 305 AAPDTLSVTLFFMLVLIAEHP----KVEEDMMKEIQaviGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDD 380
Cdd:cd20641  246 AGHETTSNLLTWTMFLLSLHPdwqeKLREEVFRECG---KDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDM 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 381 VIDGYPVKRGTNIILNIGRMHKLE--FFPKPNEFSLENFEKNVPSRYFQP-----FGFGPRGCVGKFIAMVMMKAILVTL 453
Cdd:cd20641  323 KLGGLEIPKGTTIIIPIAKLHRDKevWGSDADEFNPLRFANGVSRAATHPnallsFSLGPRACIGQNFAMIEAKTVLAMI 402

                 ....*
gi 532691798 454 LRRYR 458
Cdd:cd20641  403 LQRFS 407
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
308-470 1.59e-12

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 69.41  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 308 DTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKAL-QDDVIDGY 385
Cdd:cd20669  240 ETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGrNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVtRDTNFRGF 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 386 PVKRGTNIILNIGRMHK-LEFFPKPNEFSLENFE------KNVPSryFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:cd20669  320 LIPKGTDVIPLLNSVHYdPTQFKDPQEFNPEHFLddngsfKKNDA--FMPFSAGKRICLGESLARMELFLYLTAILQNFS 397
                        170       180
                 ....*....|....*....|..
gi 532691798 459 VQ----------TPKGRGLKNI 470
Cdd:cd20669  398 LQplgapedidlTPLSSGLGNV 419
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
293-476 3.43e-12

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 68.03  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDL 371
Cdd:cd20670  225 KNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGpHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 372 -VMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLEN-------FEKNvpsRYFQPFGFGPRGCVGKFIA 442
Cdd:cd20670  305 gVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKdPKYFRYPEAFYPQHfldeqgrFKKN---EAFVPFSSGKRVCLGEAMA 381
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 532691798 443 MVMMKAILVTLLRRYRVQ----------TPKGRGLKNIQKSNDL 476
Cdd:cd20670  382 RMELFLYFTSILQNFSLRslvppadidiTPKISGFGNIPPTYEL 425
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
287-461 3.51e-12

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 68.33  E-value: 3.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 287 RGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVI--GDRDVQSNdMSNLKVVENFINESMR 364
Cdd:cd20644  225 QAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAaqISEHPQKA-LTELPLLKAALKETLR 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 365 YQPVVDLVMRKALQDDVIDGYPVKRGTNI---ILNIGRmhKLEFFPKPNEFSLENFEKNVPS-RYFQ--PFGFGPRGCVG 438
Cdd:cd20644  304 LYPVGITVQRVPSSDLVLQNYHIPAGTLVqvfLYSLGR--SAALFPRPERYDPQRWLDIRGSgRNFKhlAFGFGMRQCLG 381
                        170       180
                 ....*....|....*....|...
gi 532691798 439 KFIAMVMMKAILVTLLRRYRVQT 461
Cdd:cd20644  382 RRLAEAEMLLLLMHVLKNFLVET 404
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
230-451 3.93e-12

cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 68.04  E-value: 3.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 230 PDIFFKISWL-YKKYEKSVKDL-KEAIEV---LIEQKRQRLSTVEKLEEHMDF----ASQLIFAQSRGDLT-GENVNQCV 299
Cdd:cd11075  158 RDFFPALTWLlNRRRWKKVLELrRRQEEVllpLIRARRKRRASGEADKDYTDFllldLLDLKEEGGERKLTdEELVSLCS 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 300 lEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSND----MSNLKVVenfINESMR-YQPVVDLVMR 374
Cdd:cd11075  238 -EFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEdlpkMPYLKAV---VLETLRrHPPGHFLLPH 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 375 KALQDDVIDGYPVKRGTNIILNIGRMHK--------LEFfpKPNEFSLENFEKNVP--SRYFQ--PFGFGPRGCVGKFIA 442
Cdd:cd11075  314 AVTEDTVLGGYDIPAGAEVNFNVAAIGRdpkvwedpEEF--KPERFLAGGEAADIDtgSKEIKmmPFGAGRRICPGLGLA 391
                        250
                 ....*....|..
gi 532691798 443 MV---MMKAILV 451
Cdd:cd11075  392 TLhleLFVARLV 403
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
291-457 6.84e-12

cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Characterized members, among others, include: Catharanthus roseus cytochrome P450 72A1 (CYP72A1), also called secologanin synthase (EC 1.3.3.9), that catalyzes the conversion of loganin into secologanin, the precursor of monoterpenoid indole alkaloids and ipecac alkaloids; Medicago truncatula CYP72A67 that catalyzes a key oxidative step in hemolytic sapogenin biosynthesis; and Arabidopsis thaliana CYP72C1, an atypical CYP that acts on brassinolide precursors and functions as a brassinosteroid-inactivating enzyme. This family also includes Panax ginseng CYP716A47 that catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis. CYP72 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 67.30  E-value: 6.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 291 TGENVNQCVLeMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMR-YQPVV 369
Cdd:cd20642  232 TEDVIEECKL-FYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPDFEGLNHLKVVTMILYEVLRlYPPVI 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 370 DLVmrKALQDDVIDG-YPVKRGTNIILNIGRMHK---------LEFfpKPNEFSlENFEKNVPSR--YFqPFGFGPRGCV 437
Cdd:cd20642  311 QLT--RAIHKDTKLGdLTLPAGVQVSLPILLVHRdpelwgddaKEF--NPERFA-EGISKATKGQvsYF-PFGWGPRICI 384
                        170       180
                 ....*....|....*....|
gi 532691798 438 GKFIAMVMMKAILVTLLRRY 457
Cdd:cd20642  385 GQNFALLEAKMALALILQRF 404
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
241-479 8.93e-12

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 67.11  E-value: 8.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 241 KKYEKSVKDLKEA-----IEVLIEQKRQRLSTVEKLEEHMDFASQLIF-AQSRGDLTGENVNQCVLEMMIAAPDTlsvTL 314
Cdd:cd11074  174 RGYLKICKEVKERrlqlfKDYFVDERKKLGSTKSTKNEGLKCAIDHILdAQKKGEINEDNVLYIVENINVAAIET---TL 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 315 FFMLVLIAE---HPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQ-PVVDLVMRKALQDDVIDGYPVKR 389
Cdd:cd11074  251 WSIEWGIAElvnHPEIQKKLRDELDTVLGpGVQITEPDLHKLPYLQAVVKETLRLRmAIPLLVPHMNLHDAKLGGYDIPA 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 390 GTNIILNIGRM-HKLEFFPKPNEFSLENF---EKNVPS-----RYFqPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQ 460
Cdd:cd11074  331 ESKILVNAWWLaNNPAHWKKPEEFRPERFleeESKVEAngndfRYL-PFGVGRRSCPGIILALPILGITIGRLVQNFELL 409
                        250       260
                 ....*....|....*....|
gi 532691798 461 TPKGRG-LKNIQKSNDLSMH 479
Cdd:cd11074  410 PPPGQSkIDTSEKGGQFSLH 429
PLN02500 PLN02500
cytochrome P450 90B1
243-458 2.05e-11

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 66.04  E-value: 2.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 243 YEKSVKDlKEAIEVLIEQK-RQRLSTVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLI 321
Cdd:PLN02500 228 YRKALKS-RATILKFIERKmEERIEKLKEEDESVEEDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFL 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 322 AEHPKVEEDMMKE------IQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIIL 395
Cdd:PLN02500 307 QGCPKAVQELREEhleiarAKKQSGESELNWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLP 386
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 532691798 396 NIGRMH-KLEFFPKPNEFSLENFEKNVPSR-----------YFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:PLN02500 387 VIAAVHlDSSLYDQPQLFNPWRWQQNNNRGgssgsssattnNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFN 461
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
272-490 2.13e-11

C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; This family contains Gaeumannomyces graminis linoleate diol synthase (LDS) and similar proteins including Ssp1 from the phytopathogenic basidiomycete Ustilago maydis. LDS, also called linoleate (8R)-dioxygenase, catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and the isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate. Ssp1 is expressed in mature teliospores, which are produced by U. maydis only after infection of its host plant, maize. Ssp1 is localized on lipid bodies in germinating teliospores, suggesting a role in the mobilization of storage lipids. LDS and Ssp1 contain an N-terminal dioxygenase domain related to animal heme peroxidases, and a C-terminal cytochrome P450 domain. The LDS-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 65.44  E-value: 2.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 272 EEHMDFASQL--IFAQSRGDLTGENVnqcvLEMMIAAPDTLSVTL-----FFMLVLIAEHpkveedmMKEIQavigdRDV 344
Cdd:cd20612  167 RAAQAAAARLgaLLDAAVADEVRDNV----LGTAVGGVPTQSQAFaqildFYLRRPGAAH-------LAEIQ-----ALA 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 345 QSNDMSNLKVVEnFINESMRYQPVVDLVMRKALQDDVID-----GYPVKRGTNIILNIGR-MHKLEFFPKPNEFSlenfe 418
Cdd:cd20612  231 RENDEADATLRG-YVLEALRLNPIAPGLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASaMRDPRAFPDPERFR----- 304
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532691798 419 knvPSRYFQP---FGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKG-RG-LKNIqksndlsmHPNERQPFLEMF 490
Cdd:cd20612  305 ---LDRPLESyihFGHGPHQCLGEEIARAALTEMLRVVLRLPNLRRAPGpQGeLKKI--------PRGGFKAYLRED 370
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
303-454 2.78e-11

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 65.78  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 303 MIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQ-----AVIGDRDVQSNDMSNLKV--VENFINESMRYQPVVDLVMRK 375
Cdd:cd20622  271 LIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYsahpeAVAEGRLPTAQEIAQARIpyLDAVIEEILRCANTAPILSRE 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 376 ALQDDVIDGYPVKRGTNIIL--NIG-----------------RMHKLEFFPKPNEFSLENFEknvPSR------------ 424
Cdd:cd20622  351 ATVDTQVLGYSIPKGTNVFLlnNGPsylsppieidesrrsssSAAKGKKAGVWDSKDIADFD---PERwlvtdeetgetv 427
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 532691798 425 ------YFQPFGFGPRGCVGKFIAMVMMKAILVTLL 454
Cdd:cd20622  428 fdpsagPTLAFGLGPRGCFGRRLAYLEMRLIITLLV 463
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
239-458 6.96e-11

3-epi-6-deoxocathasterone 23-monooxygenase; Provisional


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 64.38  E-value: 6.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 239 LYKKYeKSVKDLKEAIEVLIEQKRQRL-STVEKLEEHMDFASQLIFAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFM 317
Cdd:PLN03141 196 LYRSL-QAKKRMVKLVKKIIEEKRRAMkNKEEDETGIPKDVVDVLLRDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLA 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 318 LVLIAEHPK-----VEEDM-MKEIQAVIGDrDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGT 391
Cdd:PLN03141 275 VKFLSDCPValqqlTEENMkLKRLKADTGE-PLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGW 353
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 532691798 392 NIILNIGRMH-KLEFFPKPNEFSLENF-EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:PLN03141 354 CVLAYFRSVHlDEENYDNPYQFNPWRWqEKDMNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFR 422
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
244-457 8.24e-11

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 63.72  E-value: 8.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 244 EKSVKDLKEAIEVLIEQKRQRLSTvekleehmDFASQLIFAQSRGD-LTG-ENVNQCVLeMMIAAPDTlSVTLFF--MLV 319
Cdd:cd20625  158 NAAAAELAAYFRDLIARRRADPGD--------DLISALVAAEEDGDrLSEdELVANCIL-LLVAGHET-TVNLIGngLLA 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 320 LiAEHPkveeDMMKEIQAvigdrdvqsndmsNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIG- 398
Cdd:cd20625  228 L-LRHP----EQLALLRA-------------DPELIPAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGa 289
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 532691798 399 -----RMhklefFPKPNEFSlenfeknvPSRYFQP---FGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd20625  290 anrdpAV-----FPDPDRFD--------ITRAPNRhlaFGAGIHFCLGAPLARLEAEIALRALLRRF 343
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
290-464 1.29e-10

flavonoid 3',5'-hydroxylase (F3'5'H); Provisional


Pssm-ID: 177725  Cd Length: 504  Bit Score: 63.72  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 290 LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPV 368
Cdd:PLN00110 285 LTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGrNRRLVESDLPKLPYLQAICKESFRKHPS 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 369 VDLVM-RKALQDDVIDGYPVKRGTNIILN---IGRmhKLEFFPKPNEFSLENF--EKNVP----SRYFQ--PFGFGPRGC 436
Cdd:PLN00110 365 TPLNLpRVSTQACEVNGYYIPKNTRLSVNiwaIGR--DPDVWENPEEFRPERFlsEKNAKidprGNDFEliPFGAGRRIC 442
                        170       180
                 ....*....|....*....|....*...
gi 532691798 437 VGKFIAMVMMKAILVTLLRRYRVQTPKG 464
Cdd:PLN00110 443 AGTRMGIVLVEYILGTLVHSFDWKLPDG 470
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
302-455 2.42e-10

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 62.46  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 302 MMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAViGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDV 381
Cdd:cd20614  216 LVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA-GDVPRTPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIE 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 382 IDGYPVKRGTNII---LNIGRmhKLEFFPKPNEFSLENF----EKNVPSRYFQpFGFGPRGCVGKFIAMVMMKAILVTLL 454
Cdd:cd20614  295 LGGRRIPAGTHLGiplLLFSR--DPELYPDPDRFRPERWlgrdRAPNPVELLQ-FGGGPHFCLGYHVACVELVQFIVALA 371

                 .
gi 532691798 455 R 455
Cdd:cd20614  372 R 372
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
164-470 3.69e-10

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 61.95  E-value: 3.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 164 VESTKDHLDR---------LEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPLD--------------ENAIVL------ 214
Cdd:cd11066   80 VQSYAPIIDLesksfirelLRDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLDcvdddsllleiievESAISKfrstss 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 215 KIQNY------FDAWQALLLKPDIFFkiswlykkyEKSVKDLKEAIEVLIEQKRQRlstvekleEHMDFASQLIFAQSRG 288
Cdd:cd11066  160 NLQDYipilryFPKMSKFRERADEYR---------NRRDKYLKKLLAKLKEEIEDG--------TDKPCIVGNILKDKES 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 289 DLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVE--EDMMKEIQAVIG-DRDVQSNDMSNLKV--VENFINESM 363
Cdd:cd11066  223 KLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGQEiqEKAYEEILEAYGnDEDAWEDCAAEEKCpyVVALVKETL 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 364 RYQPVVDLVM-RKALQDDVIDGYPVKRGTNIILNI-GRMHKLEFFPKPNEFSlenfeknvPSRYFQP------------F 429
Cdd:cd11066  303 RYFTVLPLGLpRKTTKDIVYNGAVIPAGTILFMNAwAANHDPEHFGDPDEFI--------PERWLDAsgdlipgpphfsF 374
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 532691798 430 GFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGRGLKNI 470
Cdd:cd11066  375 GAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEEPMEL 415
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
238-457 5.31e-10

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 61.17  E-value: 5.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 238 WLYKKYEKSVKDLKEAievliEQKRQRLSTVekleehmdfasqlifAQSRGDLT-GENV-NQCVLEMMIAAPDTLSVTlF 315
Cdd:cd20635  173 WLLSLFEKVVPDAEKT-----KPLENNSKTL---------------LQHLLDTVdKENApNYSLLLLWASLANAIPIT-F 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 316 FMLVLIAEHPKVEEDMMKEIQAVIGDRD-----VQSNDMSNLKVVENFINESMRYQPvVDLVMRKALQDDVIDGYPVKRG 390
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGKAGkdkikISEDDLKKMPYIKRCVLEAIRLRS-PGAITRKVVKPIKIKNYTIPAG 310
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532691798 391 TNIILNIGRMHK-LEFFPKPNEFSLE-----NFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd20635  311 DMLMLSPYWAHRnPKYFPDPELFKPErwkkaDLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKY 383
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
200-462 5.88e-10

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 60.84  E-value: 5.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 200 TLFLGIPLDENAIVLkiqnyfdAWQAlllkpDIFFKISWLYK----KYEKSVKDLKEAIEVLIEQKRQrlstveklEEHM 275
Cdd:cd11038  135 CTLLGLPEEDWPRVH-------RWSA-----DLGLAFGLEVKdhlpRIEAAVEELYDYADALIEARRA--------EPGD 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 276 DFASQLIFAQSRGD-LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPkveeDMMKEIQAvigdrdvqsndmsNLKV 354
Cdd:cd11038  195 DLISTLVAAEQDGDrLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHP----DQWRALRE-------------DPEL 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 355 VENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKleffpKPNEFSLENFEknVPSRYFQPFGF--G 432
Cdd:cd11038  258 APAAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANR-----DPRVFDADRFD--ITAKRAPHLGFggG 330
                        250       260       270
                 ....*....|....*....|....*....|
gi 532691798 433 PRGCVGKFIAMVMMkAILVTLLRRyRVQTP 462
Cdd:cd11038  331 VHHCLGAFLARAEL-AEALTVLAR-RLPTP 358
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
283-451 1.53e-09

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 60.02  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 283 FAQSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINE 361
Cdd:cd20675  224 SGDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGrDRLPCIEDQPNLPYVMAFLYE 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 362 SMRYQPVVDLVMRKALQDDV-IDGYPVKRGTNIILNIGRM-HKLEFFPKPNEFSlenfeknvPSRYFQPFGF-------- 431
Cdd:cd20675  304 AMRFSSFVPVTIPHATTADTsILGYHIPKDTVVFVNQWSVnHDPQKWPNPEVFD--------PTRFLDENGFlnkdlass 375
                        170       180
                 ....*....|....*....|....*....
gi 532691798 432 ------GPRGCVGKFIAMV---MMKAILV 451
Cdd:cd20675  376 vmifsvGKRRCIGEELSKMqlfLFTSILA 404
PLN02774 PLN02774
brassinosteroid-6-oxidase
243-458 1.98e-09

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 59.79  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 243 YEKSVKDLKEAIEVLIEQKRQRLSTVEKleeHMDFASQLIFAQ-SRGDLTGENVNQCVLEMMIAAPDTLSVTLFFMLVLI 321
Cdd:PLN02774 215 YRSGVQARKNIVRMLRQLIQERRASGET---HTDMLGYLMRKEgNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYL 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 322 AEHPKVEEDMMKEIQAVIG----DRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNI 397
Cdd:PLN02774 292 HDHPKALQELRKEHLAIRErkrpEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYT 371
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 532691798 398 GRMHKLEF-FPKPNEFSLENF-EKNVPSR-YFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:PLN02774 372 REINYDPFlYPDPMTFNPWRWlDKSLESHnYFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYR 435
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
299-466 2.05e-09

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 59.65  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 299 VL-EMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD-RDVQSNDMSNLKVVENFINESMRYQPVVDLV--MR 374
Cdd:cd11076  228 VLwEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGsRRVADSDVAKLPYLQAVVKETLRLHPPGPLLswAR 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 375 KALQDDVIDGYPVKRGTNIILNigrM----HKLEFFPKPNEFSLENFEKNVPSRYFQ---------PFGFGPRGCVGKFI 441
Cdd:cd11076  308 LAIHDVTVGGHVVPAGTTAMVN---MwaitHDPHVWEDPLEFKPERFVAAEGGADVSvlgsdlrlaPFGAGRRVCPGKAL 384
                        170       180
                 ....*....|....*....|....*
gi 532691798 442 AMVMMKAILVTLLRRYRVQTPKGRG 466
Cdd:cd11076  385 GLATVHLWVAQLLHEFEWLPDDAKP 409
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
290-467 2.10e-09

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 59.34  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 290 LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPV 368
Cdd:cd20677  232 LSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGlSRLPRFEDRKSLHYTEAFINEVFRHSSF 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 369 VDLVMRK-ALQDDVIDGYPVKRGTNIILNIGRM-HKLEFFPKPNEFSLENF-------EKNVPSRYFQpFGFGPRGCVGK 439
Cdd:cd20677  312 VPFTIPHcTTADTTLNGYFIPKDTCVFINMYQVnHDETLWKDPDLFMPERFldengqlNKSLVEKVLI-FGMGVRKCLGE 390
                        170       180
                 ....*....|....*....|....*...
gi 532691798 440 FIAMVMMKAILVTLLRRYRVQTPKGRGL 467
Cdd:cd20677  391 DVARNEIFVFLTTILQQLKLEKPPGQKL 418
PLN03018 PLN03018
homomethionine N-hydroxylase
297-466 2.24e-09

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 59.64  E-value: 2.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 297 QCVlEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLV-MR 374
Cdd:PLN03018 318 QCV-EFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGkDRLVQESDIPNLNYLKACCRETFRIHPSAHYVpPH 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 375 KALQDDVIDGYPVKRGTNIIL---NIGRMHKLEFFP---KPNE-FSLENFEKNVP----SRYFQPFGFGPRGCVGKFIAM 443
Cdd:PLN03018 397 VARQDTTLGGYFIPKGSHIHVcrpGLGRNPKIWKDPlvyEPERhLQGDGITKEVTlvetEMRFVSFSTGRRGCVGVKVGT 476
                        170       180
                 ....*....|....*....|...
gi 532691798 444 VMMKAILVTLLRRYRVQTPKGRG 466
Cdd:PLN03018 477 IMMVMMLARFLQGFNWKLHQDFG 499
PLN02183 PLN02183
ferulate 5-hydroxylase
239-478 2.88e-09

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 59.48  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 239 LYKKYEKSVKDLKEAIEVLIE---QKRQRLSTVEKLEEH--------MDFASQLIFAQSRGDL------TGENVNQCVLE 301
Cdd:PLN02183 232 LNKRLVKARKSLDGFIDDIIDdhiQKRKNQNADNDSEEAetdmvddlLAFYSEEAKVNESDDLqnsiklTRDNIKAIIMD 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 302 MMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDD 380
Cdd:PLN02183 312 VMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDA 391
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 381 VIDGYPVKRGTNIILN---IGR---------MHKLEFFPKPN--EFSLENFEknvpsryFQPFGFGPRGCVGKFIAMVMM 446
Cdd:PLN02183 392 EVAGYFIPKRSRVMINawaIGRdknswedpdTFKPSRFLKPGvpDFKGSHFE-------FIPFGSGRRSCPGMQLGLYAL 464
                        250       260       270
                 ....*....|....*....|....*....|..
gi 532691798 447 KAILVTLLRRYRVQTPKGrglkniQKSNDLSM 478
Cdd:PLN02183 465 DLAVAHLLHCFTWELPDG------MKPSELDM 490
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
295-470 3.87e-09

fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 58.87  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 295 VNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIqavigDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMR 374
Cdd:PLN02169 302 IRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI-----NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHK 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 375 KALQDDVI-DGYPVKRGTNIILNI---GRMHK------LEFfpKPNEFSLENFE-KNVPSRYFQPFGFGPRGCVGKFIAM 443
Cdd:PLN02169 377 APAKPDVLpSGHKVDAESKIVICIyalGRMRSvwgedaLDF--KPERWISDNGGlRHEPSYKFMAFNSGPRTCLGKHLAL 454
                        170       180
                 ....*....|....*....|....*..
gi 532691798 444 VMMKAILVTLLRRYRVQTPKGRGLKNI 470
Cdd:PLN02169 455 LQMKIVALEIIKNYDFKVIEGHKIEAI 481
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
143-457 5.99e-09

cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410685 [Multi-domain]  Cd Length: 425  Bit Score: 58.03  E-value: 5.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 143 IRPFFTKAlSGPGLVRMIAICVESTKDHLDRLEDVTAGlgnINVLNFMRQITLDTSNTLFLGIPL------DENAIVLKI 216
Cdd:cd11062   62 LSPFFSKR-SILRLEPLIQEKVDKLVSRLREAKGTGEP---VNLDDAFRALTADVITEYAFGRSYgyldepDFGPEFLDA 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 217 QNYFDAWQALLLKPDIFFKI-SWLYKKYEKSVKDLKEAIEVLIEQKRQRLStvEKLEEHMDFASQLIFAQSRGDLTGENV 295
Cdd:cd11062  138 LRALAEMIHLLRHFPWLLKLlRSLPESLLKRLNPGLAVFLDFQESIAKQVD--EVLRQVSAGDPPSIVTSLFHALLNSDL 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 296 NQCVLE----------MMIAAPDT----LSVTLFFMLvliaEHPKVEEDMMKEIQAVIGDRDvQSNDMSNLkvvENF--- 358
Cdd:cd11062  216 PPSEKTlerladeaqtLIGAGTETtartLSVATFHLL----SNPEILERLREELKTAMPDPD-SPPSLAEL---EKLpyl 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 359 ---INESMRYQPVVdlVMR-------KALQddvIDGYPVKRGTNIILNIGRMH---KLefFPKPNEFS----LENFEKNV 421
Cdd:cd11062  288 tavIKEGLRLSYGV--PTRlprvvpdEGLY---YKGWVIPPGTPVSMSSYFVHhdeEI--FPDPHEFRperwLGAAEKGK 360
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 532691798 422 PSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd11062  361 LDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRF 396
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
239-460 6.94e-09

cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is an all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of similar metabolites as CYP26A1. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. In rats, CYP26B1 regulates sex-specific timing of meiotic initiation, independent of RA signaling. CYP26B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 57.94  E-value: 6.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 239 LYKKYEKSV---------KDLKEAIEVLIEQKRqrlstvekleEHmdfasqlifaqsRGDLTGENVNQCVLEMMIAAPDT 309
Cdd:cd20637  184 LQKSLEKAIreklqgtqgKDYADALDILIESAK----------EH------------GKELTMQELKDSTIELIFAAFAT 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 310 LSVTLFFMLVLIAEHPKVEEDMMKEIQA-------VIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRKALQDDVI 382
Cdd:cd20637  242 TASASTSLIMQLLKHPGVLEKLREELRSngilhngCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFEL 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 383 DGYPVKRGTNIILNIGRMH-------KLEFFpKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd20637  322 DGFQIPKGWSVLYSIRDTHdtapvfkDVDAF-DPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELAS 400

                 ....*
gi 532691798 456 RYRVQ 460
Cdd:cd20637  401 TSRFE 405
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
277-456 9.28e-09

cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 57.21  E-value: 9.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 277 FASQLIFAQSRGDLTGEnvnQCVLEMM---IAAPDTLSVTLFFMLVLIAEHPKveedmmkEIQAVIGDRdvqsndmsnlK 353
Cdd:cd11037  185 WGAAIFEAADRGEITED---EAPLLMRdylSAGLDTTISAIGNALWLLARHPD-------QWERLRADP----------S 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 354 VVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLEnfeKNvPSRYFQpFGFG 432
Cdd:cd11037  245 LAPNAFEEAVRLESPVQTFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPrKWDDPDRFDIT---RN-PSGHVG-FGHG 319
                        170       180
                 ....*....|....*....|....
gi 532691798 433 PRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11037  320 VHACVGQHLARLEGEALLTALARR 343
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
158-457 1.30e-08

cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 56.88  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 158 RMIAICVESTKDHLDRLEDVTAGLGNINVLNFMRQITLDTSNTLFLGIPLDENAIVLKIQNYFDAWQALLLKPDI----- 232
Cdd:cd11071   96 RFIPEFRSALSELFDKWEAELAKKGKASFNDDLEKLAFDFLFRLLFGADPSETKLGSDGPDALDKWLALQLAPTLslglp 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 233 --------------FFKISWLYKKYEKSVKdlKEAIEVLIEQKRQRLStveklEEhmDFASQLIFaqsrgdltgenvnqc 298
Cdd:cd11071  176 kileelllhtfplpFFLVKPDYQKLYKFFA--NAGLEVLDEAEKLGLS-----RE--EAVHNLLF--------------- 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 299 vlemMIAAPDTLSVTLFFMLVL--IAEH-PKVEEDMMKEIQAVIGDRDVQSND-MSNLKVVENFINESMRYQPVVDLVMR 374
Cdd:cd11071  232 ----MLGFNAFGGFSALLPSLLarLGLAgEELHARLAEEIRSALGSEGGLTLAaLEKMPLLKSVVYETLRLHPPVPLQYG 307
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 375 KALQDDVID----GYPVKRGTNIILNIGRMHK-LEFFPKPNEFslenfeknVPSRYFQPFGF---------GP------- 433
Cdd:cd11071  308 RARKDFVIEshdaSYKIKKGELLVGYQPLATRdPKVFDNPDEF--------VPDRFMGEEGKllkhliwsnGPeteeptp 379
                        330       340
                 ....*....|....*....|....*.
gi 532691798 434 --RGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd11071  380 dnKQCPGKDLVVLLARLFVAELFLRY 405
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
240-464 3.19e-08

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 55.79  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 240 YKKYEK-SVKDLKEAievLIEQKRQRlstveKLEEHmdfasqlifaqSRGDLTGENVNQCVLEMMIAAPDTLSVTLFFML 318
Cdd:cd20676  201 YQTFDKdNIRDITDS---LIEHCQDK-----KLDEN-----------ANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSL 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 319 VLIAEHPKVEEDMMKEIQAVIG-DRDVQSNDMSNLKVVENFINESMRYQPVVDLVM-RKALQDDVIDGYPVKRGTNIILN 396
Cdd:cd20676  262 MYLVTYPEIQKKIQEELDEVIGrERRPRLSDRPQLPYLEAFILETFRHSSFVPFTIpHCTTRDTSLNGYYIPKDTCVFIN 341
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532691798 397 IGRM-HKLEFFPKPNEFSLENF------EKN-VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKG 464
Cdd:cd20676  342 QWQVnHDEKLWKDPSSFRPERFltadgtEINkTESEKVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPPG 417
PLN00168 PLN00168
Cytochrome P450; Provisional
293-457 3.40e-08

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 55.73  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 293 ENVNQCVlEMMIAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGD-------RDVQsnDMSNLKVVenfINESMRY 365
Cdd:PLN00168 306 EIVNLCS-EFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDdqeevseEDVH--KMPYLKAV---VLEGLRK 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 366 QPVVDLVM-RKALQDDVIDGYPVKRGTNIILNIGRMHKLEF-FPKPNEFSLENFEKN--------VPSRYFQ--PFGFGP 433
Cdd:PLN00168 380 HPPAHFVLpHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEReWERPMEFVPERFLAGgdgegvdvTGSREIRmmPFGVGR 459
                        170       180
                 ....*....|....*....|....
gi 532691798 434 RGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:PLN00168 460 RICAGLGIAMLHLEYFVANMVREF 483
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
259-458 3.81e-08

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 55.17  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 259 EQKRQRLSTVEKLEEHM-------------DFASQLIFAQSRGD-LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEH 324
Cdd:cd11080  144 EARAHGLRCAEQLSQYLlpvieerrvnpgsDLISILCTAEYEGEaLSDEDIKALILNVLLAATEPADKTLALMIYHLLNN 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 325 PKveedmmkEIQAVIGDRdvqsndmsnlKVVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE 404
Cdd:cd11080  224 PE-------QLAAVRADR----------SLVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDP 286
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 532691798 405 F-FPKPNEFSLeNFEKNVPSRYFQP------FGFGPRGCVGKFIAMVMMKAILVTLLRRYR 458
Cdd:cd11080  287 AaFEDPDTFNI-HREDLGIRSAFSGaadhlaFGSGRHFCVGAALAKREIEIVANQVLDALP 346
PLN02302 PLN02302
ent-kaurenoic acid oxidase
141-460 4.42e-08

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 55.49  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 141 KEIRPFFTKALSGP-GLVRMIAICVESTKDHLDRLEDvtagLGNINVLNFMRQITLDTSNTLFLGiplDENAIVLK---- 215
Cdd:PLN02302 139 KRLRRLTAAPVNGPeALSTYIPYIEENVKSCLEKWSK----MGEIEFLTELRKLTFKIIMYIFLS---SESELVMEaler 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 216 ---IQNYfdAWQALLLKPDIFfkiswLYKKYEKSVKDLKEAIEVLIEQKRQRLSTVEKLEEhMDFASQLIFAQSRG--DL 290
Cdd:PLN02302 212 eytTLNY--GVRAMAINLPGF-----AYHRALKARKKLVALFQSIVDERRNSRKQNISPRK-KDMLDLLLDAEDENgrKL 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 291 TGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKV-------EEDMMKEI---QAVIGDRDVQSndMSNLKVVenfIN 360
Cdd:PLN02302 284 DDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVlqkakaeQEEIAKKRppgQKGLTLKDVRK--MEYLSQV---ID 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 361 ESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMH-KLEFFPKPNEFSLENFEKNVPSRY-FQPFGFGPRGCVG 438
Cdd:PLN02302 359 ETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHmDPEVYPNPKEFDPSRWDNYTPKAGtFLPFGLGSRLCPG 438
                        330       340
                 ....*....|....*....|..
gi 532691798 439 KFIAMVMMKAILVTLLRRYRVQ 460
Cdd:PLN02302 439 NDLAKLEISIFLHHFLLGYRLE 460
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
257-459 6.69e-08

P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Pseudomonas putida P450cam and Cyp101 proteins from Novosphingobium aromaticivorans such as CYP101C1 and CYP101D2. P450cam catalyzes the hydroxylation of camphor in a process that involves two electron transfers from the iron-sulfur protein, putidaredoxin. CYP101D2 is capable of oxidizing camphor while CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives such as alpha- and beta-ionone and beta-damascone. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 54.52  E-value: 6.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 257 LIEQKRQrlstveklEEHMDFASQLIFAQSRGD-LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPkveedmmkEI 335
Cdd:cd11035  160 LIAERRA--------NPGDDLISAILNAEIDGRpLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHP--------ED 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 336 QAVIGDRDvqsndmsnlKVVENFINESMRYQPVVdLVMRKALQDDVIDGYPVKRGTNIILNIGrMHKL--EFFPKPNEFS 413
Cdd:cd11035  224 RRRLREDP---------ELIPAAVEELLRRYPLV-NVARIVTRDVEFHGVQLKAGDMVLLPLA-LANRdpREFPDPDTVD 292
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 532691798 414 LEnfekNVPSRYFQpFGFGPRGCVGKFIAMVMMKAILVTLLRR---YRV 459
Cdd:cd11035  293 FD----RKPNRHLA-FGAGPHRCLGSHLARLELRIALEEWLKRipdFRL 336
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
290-456 1.58e-07

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 53.49  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 290 LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKveedmmkeiqavigDRDVQSNDMSNLKV-VENFInesmRYQPV 368
Cdd:cd11034  186 LSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPE--------------DRRRLIADPSLIPNaVEEFL----RFYSP 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 369 VDLVMRKALQDDVIDGYPVKRGTNIILNIGRM-HKLEFFPKPNEFSLENFeknvPSRYFQpFGFGPRGCVGKFIAMVMMK 447
Cdd:cd11034  248 VAGLARTVTQEVEVGGCRLKPGDRVLLAFASAnRDEEKFEDPDRIDIDRT----PNRHLA-FGSGVHRCLGSHLARVEAR 322

                 ....*....
gi 532691798 448 AILVTLLRR 456
Cdd:cd11034  323 VALTEVLKR 331
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
257-459 1.70e-07

cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and bacterial CYPs including Saccharopolyspora erythraea P450 EryK, Saccharolobus solfataricus cytochrome P450 119 (CYP119), Picrophilus torridus CYP231A2, Bacillus subtilis CYP109, Streptomyces himastatinicus HmtT and HmtN, and Bacillus megaterium CYP106A2, among others. EryK, also called erythromycin C-12 hydroxylase, is active during the final steps of erythromycin A (ErA) biosynthesis. CYP106A2 catalyzes the hydroxylation of a variety of 3-oxo-delta(4)-steroids such as progesterone and deoxycorticosterone, mainly in the 15beta-position. It is also capable of hydroxylating a variety of terpenoids. HmtT and HmtN is involved in the post-tailoring of the cyclohexadepsipeptide backbone during the biosynthesis of the himastatin antibiotic. The EryK-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 53.37  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 257 LIEQKRQRLSTvekleehmDFASQLIFAQSRGD-LT-GENVNQCVLeMMIAAPDTLSVTLFFMLVLIAEHPKVEedmmke 334
Cdd:cd11032  168 HLEERRRNPRD--------DLISRLVEAEVDGErLTdEEIVGFAIL-LLIAGHETTTNLLGNAVLCLDEDPEVA------ 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 335 iQAVIGDRDVqsndmsnlkvVENFINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRM-HKLEFFPKPNEFs 413
Cdd:cd11032  233 -ARLRADPSL----------IPGAIEEVLRYRPPVQRTARVTTEDVELGGVTIPAGQLVIAWLASAnRDERQFEDPDTF- 300
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 532691798 414 lenfeknVPSRyfQP-----FGFGPRGCVGKFIAMVMMKAILVTLLRRYRV 459
Cdd:cd11032  301 -------DIDR--NPnphlsFGHGIHFCLGAPLARLEARIALEALLDRFPR 342
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
203-457 2.65e-07

cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is a heme-containing monooxygenase which participates in epothilone biosynthesis where it catalyzes the epoxidation of epothilones C and D into epothilones A and B, respectively. This subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 52.81  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 203 LGIPLDENAIVLKIQNYFDAWQALLLKPDIFFKISwlykkyEKSVKDLkEAIEVLIEQKRQRLstvekLEEhmDFASQLI 282
Cdd:cd20630  125 LGVPAEWDEQFRRFGTATIRLLPPGLDPEELETAA------PDVTEGL-ALIEEVIAERRQAP-----VED--DLLTTLL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 283 FAQSRGD-LTGENVNQCVLEMMIAAPDTLSVTLFFMLVLIAEHPKVEEdmmkEIQAvigDRDVQSNDmsnlkvvenfINE 361
Cdd:cd20630  191 RAEEDGErLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALR----KVKA---EPELLRNA----------LEE 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 362 SMRYQPVVDL-VMRKALQDDVIDGYPVKRGTNIILNIG-RMHKLEFFPKPNEFSlenfeknvPSRYFQP---FGFGPRGC 436
Cdd:cd20630  254 VLRWDNFGKMgTARYATEDVELCGVTIRKGQMVLLLLPsALRDEKVFSDPDRFD--------VRRDPNAniaFGYGPHFC 325
                        250       260
                 ....*....|....*....|.
gi 532691798 437 VGKFIAMVMMKAILVTLLRRY 457
Cdd:cd20630  326 IGAALARLELELAVSTLLRRF 346
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
257-456 6.03e-07

cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 51.75  E-value: 6.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 257 LIEQKRQRLSTvekleehmDFASQLIFAQSR-GDLT-GENVNQCVLeMMIAAPDTLSVTLFFMLVLIAEHPKveedmmkE 334
Cdd:cd11030  178 LVARKRREPGD--------DLLSRLVAEHGApGELTdEELVGIAVL-LLVAGHETTANMIALGTLALLEHPE-------Q 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 335 IQAVIGDRDVqsndmsnlkvVENFINESMRYQPVVDL-VMRKALQDDVIDGYPVKRGTNIILNIGRM-HKLEFFPKPNEF 412
Cdd:cd11030  242 LAALRADPSL----------VPGAVEELLRYLSIVQDgLPRVATEDVEIGGVTIRAGEGVIVSLPAAnRDPAVFPDPDRL 311
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 532691798 413 SLENfeknvPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11030  312 DITR-----PARRHLAFGHGVHQCLGQNLARLELEIALPTLFRR 350
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
359-472 3.86e-06

cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial metabolism of the military explosive, hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX). XplA has an unusual structural organization comprising a heme domain that is fused to its flavodoxin redox partner. XplA, along with its partner reductase XplB, are plasmid encoded and the xplA gene has now been found in divergent genera across the globe with near sequence identity. It has only been detected at explosive-contaminated sites, suggesting rapid dissemination of this novel catabolic activity, possibly within a 50-year period since the introduction of RDX into the environment. XplA belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 48.97  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 359 INESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFsleNFEKNVPSRYFQPFGFGPRGCV 437
Cdd:cd20619  238 INEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRdPEVFDDPDVF---DHTRPPAASRNLSFGLGPHSCA 314
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 532691798 438 GKFIAMVMMKAILVTLLRR-YRVQTPKGRGLKNIQK 472
Cdd:cd20619  315 GQIISRAEATTVFAVLAERyERIELAEEPTVAHNDF 350
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
254-456 1.90e-04

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 43.71  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 254 IEVLIEQKRQrlstveklEEHMDFASQLIFAQSRGD-LT-GENVNQCVLeMMIAAPDTLSVTLFFMLVLIAEHPkveeDM 331
Cdd:cd11031  173 MAELVAARRA--------EPGDDLLSALVAARDDDDrLSeEELVTLAVG-LLVAGHETTASQIGNGVLLLLRHP----EQ 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 332 MKEIQAvigdrdvqsndmsNLKVVENFINESMRYQPV--VDLVMRKALQDDVIDGYPVKRGTNIILNIGRM-HKLEFFPK 408
Cdd:cd11031  240 LARLRA-------------DPELVPAAVEELLRYIPLgaGGGFPRYATEDVELGGVTIRAGEAVLVSLNAAnRDPEVFPD 306
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 532691798 409 PNEFSLENFEKnvpsryfqP---FGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11031  307 PDRLDLDREPN--------PhlaFGHGPHHCLGAPLARLELQVALGALLRR 349
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
327-465 1.03e-03

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 41.34  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 327 VEEDMMKEIQAVIGDRDVQSNDMSNLKVVENFINESMRYQPVVDLVMRkaLQD--DVIDGYPVKRGTNIILNIGRM-HKL 403
Cdd:cd20627  235 VQKKLYKEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSAR--LQEleGKVDQHIIPKETLVLYALGVVlQDN 312
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 532691798 404 EFFPKPNEFSLENFEKNVPSRYFQPFGF-GPRGCVGKFIAMVMMKAILVTLLRRYRVQTPKGR 465
Cdd:cd20627  313 TTWPLPYRFDPDRFDDESVMKSFSLLGFsGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQ 375
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
358-464 2.02e-03

AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis proteins including anthracycline biosynthesis proteins DnrQ and AknT, and macrolide antibiotic biosynthesis proteins TylM3 and DesVIII. Streptomyces peucetius DnrQ is involved in the biosynthesis of carminomycin and daunorubicin (daunomycin) while Streptomyces galilaeus AknT functions in the biosynthesis of aclacinomycin A. Streptomyces fradiae TylM3 is involved in the biosynthesis of tylosin derived from the polyketide lactone tylactone, and Streptomyces venezuelae functions in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin. These proteins are required for the glycosylation of specific substrates during the biosynthesis of specific anthracyclines and macrolide antibiotics. Although members of this family belong to the large cytochrome P450 (P450, CYP) superfamily and show significant similarity to cytochrome P450s, they lack heme-binding sites and are not functional cytochromes.


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 40.55  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 358 FINESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENfeknvPSRYFQPFGFGPRGC 436
Cdd:cd11036  224 AVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRdPEAFPDPDRFDLGR-----PTARSAHFGLGRHAC 298
                         90       100
                 ....*....|....*....|....*...
gi 532691798 437 VGKFIAMVMMKAILVTLLRRYRVQTPKG 464
Cdd:cd11036  299 LGAALARAAAAAALRALAARFPGLRAAG 326
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
344-454 2.99e-03

P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Agrobacterium tumefaciens P450-pinF2, whose expression is induced by the presence of wounded plant tissue and by plant phenolic compounds such as acetosyringone. P450-pinF2 may be involved in the detoxification of plant protective agents at the site of wounding. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 39.79  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 344 VQSNDMSNLKVVEnfinESMRYQPVVDLVMRKALQDDVIDGYPVKRGTNIILNIGRMHKLE-FFPKPNEFSLenFEKNVP 422
Cdd:cd11039  239 VMAGDVHWLRAFE----EGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEaRFENPDRFDV--FRPKSP 312
                         90       100       110
                 ....*....|....*....|....*....|..
gi 532691798 423 SryfQPFGFGPRGCVGKFIAMVMMKAILVTLL 454
Cdd:cd11039  313 H---VSFGAGPHFCAGAWASRQMVGEIALPEL 341
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
304-456 3.96e-03

unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 39.37  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 304 IAAPDTLSVTLFFMLVLIAEHPKVEEDMMKEIQAVIGDRDVqsndmSNLKVVenfINESMRYQPVVDLVMRKALQDDVID 383
Cdd:cd20624  201 LFAFDAAGMALLRALALLAAHPEQAARAREEAAVPPGPLAR-----PYLRAC---VLDAVRLWPTTPAVLRESTEDTVWG 272
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 532691798 384 GYPVKRGTNIILNIGRMHK-LEFFPKPNEFSLENFEKN--VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd20624  273 GRTVPAGTGFLIFAPFFHRdDEALPFADRFVPEIWLDGraQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRR 348
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
345-457 4.16e-03

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 39.67  E-value: 4.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 532691798 345 QSNDMSNLKVVenfINESMRYQPVvDLVMRKALQD-----DVIDGYPVKRGTNIILNIGRMH-KLEFFPKPNEFSLENF- 417
Cdd:cd20631  292 QLDDMPVLGSI---IKEALRLSSA-SLNIRVAKEDftlhlDSGESYAIRKDDIIALYPQLLHlDPEIYEDPLTFKYDRYl 367
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 532691798 418 -----EKNVPSR-------YFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRY 457
Cdd:cd20631  368 dengkEKTTFYKngrklkyYYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYF 419
 
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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