NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|3913375|sp|Q92112|]
View 

RecName: Full=Aromatase; AltName: Full=CYPXIX; AltName: Full=Cytochrome P-450AROM; AltName: Full=Cytochrome P450 19A1; AltName: Full=Estrogen synthase

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 72-485 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: 852.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   72 NACNYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKA 151
Cdd:cd20616   1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  152 LSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQNYFDAWQALLLKP 231
Cdd:cd20616  81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  232 DIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTL 311
Cdd:cd20616 161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  312 SVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKG 391
Cdd:cd20616 241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  392 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNI 471
Cdd:cd20616 321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400

                       410
                ....*....|....
gi 3913375  472 QKNNDLSMHPIERQ 485
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 ...
 72-485 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: 852.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   72 NACNYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKA 151
Cdd:cd20616   1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  152 LSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQNYFDAWQALLLKP 231
Cdd:cd20616  81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  232 DIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTL 311
Cdd:cd20616 161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  312 SVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKG 391
Cdd:cd20616 241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  392 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNI 471
Cdd:cd20616 321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400

                       410
                ....*....|....
gi 3913375  472 QKNNDLSMHPIERQ 485
Cdd:cd20616 401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 48-488 2.05e-123

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: 368.92  E-value: 2.05e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375     48 PGPGYCMGIGPLISHgrflWMGVGNACNYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHWHY--VSRFGSKLGLQCI 125
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefSGRPDEPWFATSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    126 GMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLG 205
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    206 VPLD------ENAIVLKIQNYFD-----AWQALLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKldE 274
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    275 HMDFASQLIFAQNRGD---LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD-RDIQSDDM 350
Cdd:pfam00067 238 PRDFLDALLLAKEEEDgskLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    351 PNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPS 424
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3913375    425 RYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNDLSMHPIERQPLL 488
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 81-459 7.92e-43

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: 156.98  E-value: 7.92e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   81 YGDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRM 160
Cdd:COG2124  31 YGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAAL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  161 IAICVESTTEHLDRLQEVttelGNINALNLMRRIMLDTSNKLFLGVPLDENAivlKIQNYFDAWQALLLKPDIFFKiswl 240
Cdd:COG2124 111 RPRIREIADELLDRLAAR----GPVDLVEEFARPLPVIVICELLGVPEEDRD---RLRRWSDALLDALGPLPPERR---- 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  241 cKKYKDAVKDLKGAMEILIEQKRQKLSTvekldehmDFASQLIFAQNRGD-LTAENV-NQCVLeMMIAAPDTLSVTLFFM 318
Cdd:COG2124 180 -RRARRARAELDAYLRELIAERRAEPGD--------DLLSALLAARDDGErLSDEELrDELLL-LLLAGHETTANALAWA 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  319 LILIAEHPTVEEEMMREIETVvgdrdiqsddmpnlkivENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNI 398
Cdd:COG2124 250 LYALLRHPEQLARLRAEPELL-----------------PAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSL 312

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3913375  399 GRMHKLE-FFPKPNEFSLEnfekNVPSRYFqPFGFGPRSCVGKFIAMVMMKAILVTLLRRCR 459
Cdd:COG2124 313 AAANRDPrVFPDPDRFDPD----RPPNAHL-PFGGGPHRCLGAALARLEARIALATLLRRFP 369
PLN02738 PLN02738
carotene beta-ring hydroxylase
 290-465 5.67e-21

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 96.52  E-value: 5.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   290 DLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:PLN02738 386 DVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQ 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   370 VDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-------LEFF---------PKPNEfSLENFeknvpsRYFqPFGFG 433
Cdd:PLN02738 466 PPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNF------SYL-PFGGG 537

                        170       180       190
                 ....*....|....*....|....*....|..
gi 3913375   434 PRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:PLN02738 538 PRKCVGDMFASFENVVATAMLVRRFDFQLAPG 569
 
Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 72-485 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: 852.81  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   72 NACNYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKA 151
Cdd:cd20616   1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  152 LSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQNYFDAWQALLLKP 231
Cdd:cd20616  81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  232 DIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTL 311
Cdd:cd20616 161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  312 SVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKG 391
Cdd:cd20616 241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  392 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNI 471
Cdd:cd20616 321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400

                       410
                ....*....|....
gi 3913375  472 QKNNDLSMHPIERQ 485
Cdd:cd20616 401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 48-488 2.05e-123

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: 368.92  E-value: 2.05e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375     48 PGPGYCMGIGPLISHgrflWMGVGNACNYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHWHY--VSRFGSKLGLQCI 125
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefSGRPDEPWFATSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    126 GMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLG 205
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    206 VPLD------ENAIVLKIQNYFD-----AWQALLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKldE 274
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    275 HMDFASQLIFAQNRGD---LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD-RDIQSDDM 350
Cdd:pfam00067 238 PRDFLDALLLAKEEEDgskLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    351 PNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPS 424
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3913375    425 RYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNDLSMHPIERQPLL 488
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 82-461 5.89e-65

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: 215.46  E-value: 5.89e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   82 GDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIiFNNNPAHWKEIRPFFTKALSGPGLVRMI 161
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGL-LTLDGPEHRRLRRLLAPAFTPRALAALR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  162 AICVESTTEHLDRLQEVTTELGNINALnlMRRIMLDTSNKLFLGVplDENAIVLKIQNYFDAWQALLLKPDIFFKISWLC 241
Cdd:cd00302  80 PVIREIARELLDRLAAGGEVGDDVADL--AQPLALDVIARLLGGP--DLGEDLEELAELLEALLKLLGPRLLRPLPSPRL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  242 KKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDfasqlifAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLIL 321
Cdd:cd00302 156 RRLRRARARLRDYLEELIARRRAEPADDLDLLLLAD-------ADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYL 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  322 IAEHPTVEEEMMREIETVVGDRDIqsDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRM 401
Cdd:cd00302 229 LARHPEVQERLRAEIDAVLGDGTP--EDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYAA 306

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3913375  402 HKLE-FFPKPNEFSLENF--EKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:cd00302 307 HRDPeVFPDPDEFDPERFlpEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFE 369
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 82-488 3.63e-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: 168.53  E-value: 3.63e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   82 GDFVRVWISGEETFIISKSSSVSHVM--KHWHYVS-----RFGSKLGlqcigmyeNGIIfNNNPAHWKEIR----PFFT- 149
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHVLvtNARNYVKggvyeRLKLLLG--------NGLL-TSEGDLWRRQRrlaqPAFHr 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  150 KALSGpglvrMIAICVESTTEHLDRLQEVTTElGNINALNLMRRIMLDTSNKLFLGVPLDE-------------NAIVLK 216
Cdd:cd20620  72 RRIAA-----YADAMVEATAALLDRWEAGARR-GPVDVHAEMMRLTLRIVAKTLFGTDVEGeadeigdaldvalEYAARR 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  217 IQNYFDAWQALLLKPDiffkiswlcKKYKDAVKDLKGAMEILIEQKRQklstvEKLDEHmDFASQLIFAQNRGDLTAENV 296
Cdd:cd20620 146 MLSPFLLPLWLPTPAN---------RRFRRARRRLDEVIYRLIAERRA-----APADGG-DLLSMLLAARDEETGEPMSD 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  297 NQC---VLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLI 373
Cdd:cd20620 211 QQLrdeVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTAEDLPQLPYTEMVLQESLRLYPPAWII 290

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  374 MRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENFEKNVPSR-----YFqPFGFGPRSCVGKFIAMVMM 447
Cdd:cd20620 291 GREAVEDDEIGGYRIPAGSTVLISPYVTHRDPrFWPDPEAFDPERFTPEREAArpryaYF-PFGGGPRICIGNHFAMMEA 369

                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 3913375  448 KAILVTLLRRCRVQTMKGrglnniqknndlsmHPIERQPLL 488
Cdd:cd20620 370 VLLLATIAQRFRLRLVPG--------------QPVEPEPLI 396
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 82-483 1.19e-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: 167.77  E-value: 1.19e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   82 GDFVRVWISGEETFIISKSSSV--SHVMKHWHYVSRFGSKLGLqcIGMYENGIIFNNNPaHWKEIRPFFTKALSGPGLVR 159
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIkeAFVKNGDNFSDRPLLPSFE--IISGGKGILFSNGD-YWKELRRFALSSLTKTKLKK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  160 MIAICVESTTEHL-DRLQEVTTELGNINALNLMRRIMLDTSNKLFLG--VPLDENAIVLKIQNYFDAWQALLLKPDIFFK 236
Cdd:cd20617  78 KMEELIEEEVNKLiESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGkrFPDEDDGEFLKLVKPIEEIFKELGSGNPSDF 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  237 ISWLC-------KKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPD 309
Cdd:cd20617 158 IPILLpfyflylKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLFLAGTD 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  310 TLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYP 387
Cdd:cd20617 238 TTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGnDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLpRVTTEDTEIGGYF 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  388 VKKGTNIILNIGRMHKLE-FFPKPNEFSLENF---EKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTM 463
Cdd:cd20617 318 IPKGTQIIINIYSLHRDEkYFEDPEEFNPERFlenDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFKSS 397

                       410       420
                ....*....|....*....|
gi 3913375  464 KGRgLNNIQKNNDLSMHPIE 483
Cdd:cd20617 398 DGL-PIDEKEVFGLTLKPKP 416
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 81-459 7.92e-43

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: 156.98  E-value: 7.92e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   81 YGDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRM 160
Cdd:COG2124  31 YGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAAL 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  161 IAICVESTTEHLDRLQEVttelGNINALNLMRRIMLDTSNKLFLGVPLDENAivlKIQNYFDAWQALLLKPDIFFKiswl 240
Cdd:COG2124 111 RPRIREIADELLDRLAAR----GPVDLVEEFARPLPVIVICELLGVPEEDRD---RLRRWSDALLDALGPLPPERR---- 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  241 cKKYKDAVKDLKGAMEILIEQKRQKLSTvekldehmDFASQLIFAQNRGD-LTAENV-NQCVLeMMIAAPDTLSVTLFFM 318
Cdd:COG2124 180 -RRARRARAELDAYLRELIAERRAEPGD--------DLLSALLAARDDGErLSDEELrDELLL-LLLAGHETTANALAWA 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  319 LILIAEHPTVEEEMMREIETVvgdrdiqsddmpnlkivENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNI 398
Cdd:COG2124 250 LYALLRHPEQLARLRAEPELL-----------------PAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSL 312

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3913375  399 GRMHKLE-FFPKPNEFSLEnfekNVPSRYFqPFGFGPRSCVGKFIAMVMMKAILVTLLRRCR 459
Cdd:COG2124 313 AAANRDPrVFPDPDRFDPD----RPPNAHL-PFGGGPHRCLGAALARLEARIALATLLRRFP 369
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 82-467 6.20e-41

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: 152.29  E-value: 6.20e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   82 GDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLQC-IGmyeNGIIFNNNPaHWKEIRPFFTKALSgpglVRM 160
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPwLG---DGLLTSTGE-KWRKRRKLLTPAFH----FKI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  161 IAICVESTTEHLDRLQEVTTEL---GNINALNLMRR----IMLDTSnklfLGVPLDENAIvlKIQNYFDAWQAL------ 227
Cdd:cd20628  73 LESFVEVFNENSKILVEKLKKKaggGEFDIFPYISLctldIICETA----MGVKLNAQSN--EDSEYVKAVKRIleiilk 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  228 -----LLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQ----------LIFAQNRGDLT 292
Cdd:cd20628 147 rifspWLRFDFIFRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDDEFGKkkrkafldllLEAHEDGGPLT 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  293 AENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD--RDIQSDDMPNLKIVENFIYESMRYQPVV 370
Cdd:cd20628 227 DEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVIKETLRLYPSV 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  371 DLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENFEK-NVPSRY---FQPFGFGPRSCVG-KFiAM 444
Cdd:cd20628 307 PFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNpEYFPDPEKFDPDRFLPeNSAKRHpyaYIPFSAGPRNCIGqKF-AM 385

                       410       420
                ....*....|....*....|...
gi 3913375  445 VMMKAILVTLLRRCRVQTMKGRG 467
Cdd:cd20628 386 LEMKTLLAKILRNFRVLPVPPGE 408
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 131-462 4.74e-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: 149.98  E-value: 4.74e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  131 GIIFNNNPaHWKEIRPFFTKALSGPGLVRMIAICVESTTEHL-DRLQEVTTELGNI--NALNLMRR--------IMLDTS 199
Cdd:cd11054  57 GLLNSNGE-EWHRLRSAVQKPLLRPKSVASYLPAINEVADDFvERIRRLRDEDGEEvpDLEDELYKwslesigtVLFGKR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  200 NKLFLGVPLDENAIVLK-IQNYFDAWQALLLKPDiFFKIsWLCKKYKDAVKDLKGAMEI---LIEQKRQKLSTVEKLDEH 275
Cdd:cd11054 136 LGCLDDNPDSDAQKLIEaVKDIFESSAKLMFGPP-LWKY-FPTPAWKKFVKAWDTIFDIaskYVDEALEELKKKDEEDEE 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  276 -MDFASQLIfaqNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD-IQSDDMPNL 353
Cdd:cd11054 214 eDSLLEYLL---SKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEpITAEDLKKM 290

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  354 KIVENFIYESMRYQPVVDLIMRKaLQDD-VIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLE-----NFEKNVPSRY 426
Cdd:cd11054 291 PYLKACIKESLRLYPVAPGNGRI-LPKDiVLSGYHIPKGTLVVLSNYVMGRDEeYFPDPEEFIPErwlrdDSENKNIHPF 369

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 3913375  427 -FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQT 462
Cdd:cd11054 370 aSLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEY 406
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 79-457 2.27e-36

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: 139.58  E-value: 2.27e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   79 KTYGDFVRVWISGEETFIISKSSSVSHVM------KHWHYVSRFGSKLGLQCIGmyeNGIIFNNNPAHWKEIRPFFTKAL 152
Cdd:cd20613   9 KEYGPVFVFWILHRPIVVVSDPEAVKEVLitlnlpKPPRVYSRLAFLFGERFLG---NGLVTEVDHEKWKKRRAILNPAF 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  153 SGPGLVRMIAICVESTTEHLDRLQEV---TTElgnINALNLMRRIMLDTSNKLFLGVPLD-----ENAIVLKIQNYFDAW 224
Cdd:cd20613  86 HRKYLKNLMDEFNESADLLVEKLSKKadgKTE---VNMLDEFNRVTLDVIAKVAFGMDLNsiedpDSPFPKAISLVLEGI 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  225 QALLLKPDIFFKIS--WLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEhmDFASQLI-FAQNRGDLTAENVNQCVL 301
Cdd:cd20613 163 QESFRNPLLKYNPSkrKYRREVREAIKFLRETGRECIEERLEALKRGEEVPN--DILTHILkASEEEPDFDMEELLDDFV 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  302 EMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDR-DIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQD 380
Cdd:cd20613 241 TFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKqYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKD 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  381 DVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENFEKNVPSR-----YFqPFGFGPRSCVGKFIAMVMMKAILVTL 454
Cdd:cd20613 321 IELGGYKIPAGTTVLVSTYVMGRMEeYFEDPLKFDPERFSPEAPEKipsyaYF-PFSLGPRSCIGQQFAQIEAKVILAKL 399


                ...
gi 3913375  455 LRR 457
Cdd:cd20613 400 LQN 402
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 84-465 1.47e-35

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: 137.34  E-value: 1.47e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   84 FVRVWISGEETFIISKSSSVSHVMKH--WHYV------SRFGSKLGlqcigmyeNGIiFNNNPAHWKEIRPFFTKALSGP 155
Cdd:cd11064   3 FRGPWPGGPDGIVTADPANVEHILKTnfDNYPkgpefrDLFFDLLG--------DGI-FNVDGELWKFQRKTASHEFSSR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  156 GLVRMIAICV-ESTTEHLDRLQEVTTELGN-INALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQNY---FDAWQALLLK 230
Cdd:cd11064  74 ALREFMESVVrEKVEKLLVPLLDHAAESGKvVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPEVPFakaFDDASEAVAK 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  231 ----PDIFFKI-SWLC----KKYKDAVKDLKG-AMEILIEQKRQKLSTVEKLDEHMDFASQLIFA--QNRGDLTAENVNQ 298
Cdd:cd11064 154 rfivPPWLWKLkRWLNigseKKLREAIRVIDDfVYEVISRRREELNSREEENNVREDLLSRFLASeeEEGEPVSDKFLRD 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  299 CVLEMMIAAPDTLSVTL--FFMLIliAEHPTVEEEMMREIETVVGDRDIQS------DDMPNLKIVENFIYESMRYQPVV 370
Cdd:cd11064 234 IVLNFILAGRDTTAAALtwFFWLL--SKNPRVEEKIREELKSKLPKLTTDEsrvptyEELKKLVYLHAALSESLRLYPPV 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  371 DLIMRKALQDDVI-DGYPVKKGTNIILNI---GRMHK------LEFfpKPNEF-SLENFEKNVPSRYFQPFGFGPRSCVG 439
Cdd:cd11064 312 PFDSKEAVNDDVLpDGTFVKKGTRIVYSIyamGRMESiwgedaLEF--KPERWlDEDGGLRPESPYKFPAFNAGPRICLG 389

                       410       420
                ....*....|....*....|....*.
gi 3913375  440 KFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:cd11064 390 KDLAYLQMKIVAAAILRRFDFKVVPG 415
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 133-462 5.64e-35

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: 135.81  E-value: 5.64e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  133 IFNNNPAHWKEIR-----PFFTKALSGpglvrMIAICVESTTEHLDRLQEVTTElGNINALNLMRRIMLDTSNKLFLGVP 207
Cdd:cd11057  47 LFSAPYPIWKLQRkalnpSFNPKILLS-----FLPIFNEEAQKLVQRLDTYVGG-GEFDILPDLSRCTLEMICQTTLGSD 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  208 LDENaiVLKIQNYFDAWQALL-----------LKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHM 276
Cdd:cd11057 121 VNDE--SDGNEEYLESYERLFeliakrvlnpwLHPEFIYRLTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLDSEE 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  277 D---------FASQLI-FAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD-- 344
Cdd:cd11057 199 DeengrkpqiFIDQLLeLARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGqf 278

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  345 IQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVID-GYPVKKGTNIILNIGRMHKLEFF--PKPNEFSLENFE-K 420
Cdd:cd11057 279 ITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIwgPDADQFDPDNFLpE 358

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 3913375  421 NVPSRY---FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQT 462
Cdd:cd11057 359 RSAQRHpyaFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKT 403
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 140-462 1.50e-32

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: 128.86  E-value: 1.50e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  140 HWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLD-----ENAIV 214
Cdd:cd11055  59 RWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDsqnnpDDPFL 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  215 LKIQNYFDAWQ-----ALLLKPDIFFKISWL-CKKYKDAVKDLKGAMEILIEQKRQKLSTVEKldehmDFASQLIFAQNR 288
Cdd:cd11055 139 KAAKKIFRNSIirlflLLLLFPLRLFLFLLFpFVFGFKSFSFLEDVVKKIIEQRRKNKSSRRK-----DLLQLMLDAQDS 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  289 GD------LTA-ENVNQCVLeMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS-DDMPNLKIVENFI 360
Cdd:cd11055 214 DEdvskkkLTDdEIVAQSFI-FLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTyDTVSKLKYLDMVI 292

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  361 YESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF---EKNVPSRY-FQPFGFGPR 435
Cdd:cd11055 293 NETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHdPEFWPDPEKFDPERFspeNKAKRHPYaYLPFGAGPR 372

                       330       340
                ....*....|....*....|....*..
gi 3913375  436 SCVGKFIAMVMMKAILVTLLRRCRVQT 462
Cdd:cd11055 373 NCIGMRFALLEVKLALVKILQKFRFVP 399
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 81-457 8.68e-32

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: 127.00  E-value: 8.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   81 YGDFVRVW-ISGEETFIISKSSSVSHVMKHWHYV---SRFGSKLGLQCIGmyeNGIIFNNNPAHwKEIRPFFTKALSGPG 156
Cdd:cd11069   1 YGGLIRYRgLFGSERLLVTDPKALKHILVTNSYDfekPPAFRRLLRRILG---DGLLAAEGEEH-KRQRKILNPAFSYRH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  157 LVRMIAICVESTTEHLDRLQEVTTELGN----INALNLMRRIMLDTSNKLFLGVplDENAIVLKIQNYFDAWQALL---- 228
Cdd:cd11069  77 VKELYPIFWSKAEELVDKLEEEIEESGDesisIDVLEWLSRATLDIIGLAGFGY--DFDSLENPDNELAEAYRRLFeptl 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  229 LKPDIFFKISWL------------CKKYKDAVKDLKGAMEILIEQKRQKLsTVEKLDEHMDFASQLI----FAQNRGDLT 292
Cdd:cd11069 155 LGSLLFILLLFLprwlvrilpwkaNREIRRAKDVLRRLAREIIREKKAAL-LEGKDDSGKDILSILLrandFADDERLSD 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  293 AENVNQcVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETV---VGDRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:cd11069 234 EELIDQ-ILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAAlpdPPDGDLSYDDLDRLPYLNAVCRETLRLYPP 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  370 VDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLEFF--PKPNEF-------SLENFEKNVPSRY--FQPFGFGPRSCV 438
Cdd:cd11069 313 VPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIwgPDAEEFnperwlePDGAASPGGAGSNyaLLTFLHGPRSCI 392

                       410
                ....*....|....*....
gi 3913375  439 GKFIAMVMMKAILVTLLRR 457
Cdd:cd11069 393 GKKFALAEMKVLLAALVSR 411
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 125-469 1.94e-31

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: 125.74  E-value: 1.94e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  125 IGMYENGIIFNNNPAHWKEIRPFFTKALSGP---------------GLVRMIAicVESTTEHLDRLQEVTTELgninALN 189
Cdd:cd20618  45 FSYNGQDIVFAPYGPHWRHLRKICTLELFSAkrlesfqgvrkeelsHLVKSLL--EESESGKPVNLREHLSDL----TLN 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  190 LMRRIMLdtsNKLFLGVPLDENAIVLKIQNYFDAWQALLLKPDI--------FFKISWLCKKYKDAVKDLKGAMEILIEQ 261
Cdd:cd20618 119 NITRMLF---GKRYFGESEKESEEAREFKELIDEAFELAGAFNIgdyipwlrWLDLQGYEKRMKKLHAKLDRFLQKIIEE 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  262 KRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLiliAE---HPTVEEEMMREIET 338
Cdd:cd20618 196 HREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAM---AEllrHPEVMRKAQEELDS 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  339 VVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILN---IGRMHKLefFPKPNEF 413
Cdd:cd20618 273 VVGrERLVEESDLPKLPYLQAVVKETLRLHPPGPLlLPHESTEDCKVAGYDIPAGTRVLVNvwaIGRDPKV--WEDPLEF 350

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3913375  414 S----LENFEKNVPSRYFQ--PFGFGPRSCVGKFIAMVMMKAILVTLLRRC--RVQTMKGRGLN 469
Cdd:cd20618 351 KperfLESDIDDVKGQDFEllPFGSGRRMCPGMPLGLRMVQLTLANLLHGFdwSLPGPKPEDID 414
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 130-466 1.02e-30

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: 123.52  E-value: 1.02e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  130 NGIIFNNNPAHWKEiRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTelgnINALNLMRRIMLDTSNKLFLGVPLD 209
Cdd:cd11049  60 NGLATCPGEDHRRQ-RRLMQPAFHRSRIPAYAEVMREEAEALAGSWRPGRV----VDVDAEMHRLTLRVVARTLFSTDLG 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  210 ENAIV-----LKIQNYFDAWQALLLKpdiffkisWLCK-------KYKDAVKDLKGAMEILIEQKRqklstvEKLDEHMD 277
Cdd:cd11049 135 PEAAAelrqaLPVVLAGMLRRAVPPK--------FLERlptpgnrRFDRALARLRELVDEIIAEYR------ASGTDRDD 200

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  278 FASQLIFA--QNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKI 355
Cdd:cd11049 201 LLSLLLAArdEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPATFEDLPRLTY 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  356 VENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFS----LENFEKNVPSRYFQPF 430
Cdd:cd11049 281 TRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDpEVYPDPERFDpdrwLPGRAAAVPRGAFIPF 360

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 3913375  431 GFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGR 466
Cdd:cd11049 361 GAGARKCIGDTFALTELTLALATIASRWRLRPVPGR 396
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 142-459 3.68e-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: 122.01  E-value: 3.68e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  142 KEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVttelGNINALNLMRRIMLDTSNKLFLGvpLDENAIVLKIQNYF 221
Cdd:cd11044  80 RRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLKA----GEVALYPELRRLTFDVAARLLLG--LDPEVEAEALSQDF 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  222 DAW-QALL-LKPDIFFKiswlckKYKDAVKD---LKGAMEILIEQKRQKLSTVEKldehmDFASQLIFAQ-NRG-DLTAE 294
Cdd:cd11044 154 ETWtDGLFsLPVPLPFT------PFGRAIRArnkLLARLEQAIRERQEEENAEAK-----DALGLLLEAKdEDGePLSMD 222

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  295 NVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM 374
Cdd:cd11044 223 ELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGF 302

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  375 RKALQDDVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENF------EKNVPSRYFqPFGFGPRSCVGKFIAMVMM 447
Cdd:cd11044 303 RKVLEDFELGGYQIPKGWLVYYSIRDTHRDpELYPDPERFDPERFsparseDKKKPFSLI-PFGGGPRECLGKEFAQLEM 381

                       330
                ....*....|..
gi 3913375  448 KAILVTLLRRCR 459
Cdd:cd11044 382 KILASELLRNYD 393
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 75-459 2.99e-29

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: 119.37  E-value: 2.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   75 NYYNKTYGDFVRVWISGEETFIISKSSSVSHVMKHwHYVSRFGSKLGLQCIGMYENGIIFNNNPaHWKEIRPFFTKALSG 154
Cdd:cd11052   5 YHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSK-KEGYFGKSPLQPGLKKLLGRGLVMSNGE-KWAKHRRIANPAFHG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  155 PGLVRMIAICVESTTEHLDRLQEVTTELGN-INALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQnyfDAWQALLLKPDI 233
Cdd:cd11052  83 EKLKGMVPAMVESVSDMLERWKKQMGEEGEeVDVFEEFKALTADIISRTAFGSSYEEGKEVFKLL---RELQKICAQANR 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  234 FFKIS-WLCKKYKDAVKDLKGAMEI------LIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDltaENVNQCVLEMM-- 304
Cdd:cd11052 160 DVGIPgSRFLPTKGNKKIKKLDKEIedslleIIKKREDSLKMGRGDDYGDDLLGLLLEANQSDD---QNKNMTVQEIVde 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  305 -----IAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMR-YQPVVDLImRKAL 378
Cdd:cd11052 237 cktffFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLRlYPPAVFLT-RKAK 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  379 QDDVIDGYPVKKGTNIILNIGRMHKLEFF--PKPNEFSLENFEKNVP-----SRYFQPFGFGPRSCVGKFIAMVMMKAIL 451
Cdd:cd11052 316 EDIKLGGLVIPKGTSIWIPVLALHHDEEIwgEDANEFNPERFADGVAkaakhPMAFLPFGLGPRNCIGQNFATMEAKIVL 395


                ....*...
gi 3913375  452 VTLLRRCR 459
Cdd:cd11052 396 AMILQRFS 403
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 129-465 1.04e-28

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: 117.67  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  129 ENGIIFNNNPAHwKEIRPFFTKALSGPGL-VRMIAICVESTTEHLDRLqevtTELGNINALNLMRRIMLDTSNKLFLGvp 207
Cdd:cd11043  52 KSSLLTVSGEEH-KRLRGLLLSFLGPEALkDRLLGDIDELVRQHLDSW----WRGKSVVVLELAKKMTFELICKLLLG-- 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  208 LDENAIVLKIQNYFDAWQALLLKpdifFKISWLCKKYKDAVKDLKGAMEIL---IEQKRQKLSTVEkldEHMDFASQLIF 284
Cdd:cd11043 125 IDPEEVVEELRKEFQAFLEGLLS----FPLNLPGTTFHRALKARKRIRKELkkiIEERRAELEKAS---PKGDLLDVLLE 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  285 AQNRGD--LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD----IQSDDMPNLKIVEN 358
Cdd:cd11043 198 EKDEDGdsLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKEegegLTWEDYKSMKYTWQ 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  359 FIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFEKN--VPSRYFQPFGFGPR 435
Cdd:cd11043 278 VINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLdPEYFPDPLKFNPWRWEGKgkGVPYTFLPFGGGPR 357

                       330       340       350
                ....*....|....*....|....*....|
gi 3913375  436 SCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:cd11043 358 LCPGAELAKLEILVFLHHLVTRFRWEVVPD 387
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 130-456 2.81e-28

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: 116.59  E-value: 2.81e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  130 NGIIFNNNPAhWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVttelgNINALNLMRRIMLDTSNKLFLGVPLD 209
Cdd:cd20621  49 KGLLFSEGEE-WKKQRKLLSNSFHFEKLKSRLPMINEITKEKIKKLDNQ-----NVNIIQFLQKITGEVVIRSFFGEEAK 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  210 E---------NAIVLKIQNYFDAWQA---LLLKPDIFFKISW---LCKKYKDA---VKDLKGAMEILIEQKR---QKLST 268
Cdd:cd20621 123 DlkingkeiqVELVEILIESFLYRFSspyFQLKRLIFGRKSWklfPTKKEKKLqkrVKELRQFIEKIIQNRIkqiKKNKD 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  269 VEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD-RDIQS 347
Cdd:cd20621 203 EIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNdDDITF 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  348 DDMPNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKKGTNI-ILNIGRMHKLEFFPKPNEFS----LENFEKN 421
Cdd:cd20621 283 EDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQIGDLKIKKGWIVnVGYIYNHFNPKYFENPDEFNperwLNQNNIE 362

                       330       340       350
                ....*....|....*....|....*....|....*
gi 3913375  422 VPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLR 456
Cdd:cd20621 363 DNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILK 397
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 126-457 9.64e-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: 115.47  E-value: 9.64e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  126 GMYENGIIFNNNPAHWKEIRPFFTKALsgPGLVRMIAicvESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLG 205
Cdd:cd11041  54 GFGTGGSVVLDSPLHVDVVRKDLTPNL--PKLLPDLQ---EELRAALDEELGSCTEWTEVNLYDTVLRIVARVSARVFVG 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  206 VPLDENAIVLKI-QNY----FDAWQALLLKPDIFFKI-SWL---CKKYKDAVKDLKGAMEILIEqKRQKLSTVEKLDEHM 276
Cdd:cd11041 129 PPLCRNEEWLDLtINYtidvFAAAAALRLFPPFLRPLvAPFlpePRRLRRLLRRARPLIIPEIE-RRRKLKKGPKEDKPN 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  277 DFASQLI-FAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDD-MPNLK 354
Cdd:cd11041 208 DLLQWLIeAAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAaLNKLK 287

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  355 IVENFIYESMRYQPVVDLIM-RKALQDDVI-DGYPVKKGTNIILNIGRMHKLE-FFPKPNEF---------SLENFEKN- 421
Cdd:cd11041 288 KLDSFMKESQRLNPLSLVSLrRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPdIYPDPETFdgfrfyrlrEQPGQEKKh 367

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 3913375  422 ---VPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11041 368 qfvSTSPDFLGFGHGRHACPGRFFASNEIKLILAHLLLN 406
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 80-459 3.16e-27

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: 113.96  E-value: 3.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   80 TYGDfVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKLGLqcIGMYENGIIFNNNPAhWKEIRPFFTKALSGPGLVR 159
Cdd:cd11070   1 KLGA-VKILFVSRWNILVTKPEYLTQIFRRRDDFPKPGNQYKI--PAFYGPNVISSEGED-WKRYRKIVAPAFNERNNAL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  160 MIAICVESTTEHLDRLQEVTTELGNIN--ALNLMRRIMLDTSNKLFLGVPLDE-NAIVLKIQNYFDAWQALLLKPDIF-F 235
Cdd:cd11070  77 VWEESIRQAQRLIRYLLEEQPSAKGGGvdVRDLLQRLALNVIGEVGFGFDLPAlDEEESSLHDTLNAIKLAIFPPLFLnF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  236 KIS-----WLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHM--DFASQLIFAQNRGDLTAE----NVNQcvleMM 304
Cdd:cd11070 157 PFLdrlpwVLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTesVVASRLKRARRSGGLTEKellgNLFI----FF 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  305 IAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQ---SDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 381
Cdd:cd11070 233 IAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDwdyEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPV 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  382 VI-----DGYPVKKGTNIILNIGRMHK---------LEFFPK----PNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIA 443
Cdd:cd11070 313 VVitglgQEIVIPKGTYVGYNAYATHRdptiwgpdaDEFDPErwgsTSGEIGAATRFTPARGAFIPFSAGPRACLGRKFA 392

                       410
                ....*....|....*.
gi 3913375  444 MVMMKAILVTLLRRCR 459
Cdd:cd11070 393 LVEFVAALAELFRQYE 408
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 228-495 6.33e-27

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: 112.74  E-value: 6.33e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  228 LLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMD------------FASQLIFA-QNRGDLTAE 294
Cdd:cd20660 152 WLWPDFIYSLTPDGREHKKCLKILHGFTNKVIQERKAELQKSLEEEEEDDedadigkrkrlaFLDLLLEAsEEGTKLSDE 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  295 NVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD--RDIQSDDMPNLKIVENFIYESMRYQPVVDL 372
Cdd:cd20660 232 DIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDsdRPATMDDLKEMKYLECVIKEALRLFPSVPM 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  373 IMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF-EKNVPSRY---FQPFGFGPRSCVGKFIAMVMM 447
Cdd:cd20660 312 FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRdPRQFPDPEKFDPDRFlPENSAGRHpyaYIPFSAGPRNCIGQKFALMEE 391

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3913375  448 KAILVTLLRRCRVQTMkgrglnniQKNNDLsmhpierQPLLEMVFTPR 495
Cdd:cd20660 392 KVVLSSILRNFRIESV--------QKREDL-------KPAGELILRPV 424
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 82-457 8.49e-27

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: 112.41  E-value: 8.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   82 GDFVRVWISGEETFIISKSSSVSHVMKHWHYVSRFGSKL--GLQCIGMyeNGIiFNNNPAHWKEIRPFFTKALSgPGLVR 159
Cdd:cd11083   1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFRRISSLesVFREMGI--NGV-FSAEGDAWRRQRRLVMPAFS-PKHLR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  160 MIAICVESTTEHL-DRLQEVTTELGNINALNLMRRIMLDTSNKLFLGV----------PLDEN------AIVLKIQNYFD 222
Cdd:cd11083  77 YFFPTLRQITERLrERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYdlntlerggdPLQEHlervfpMLNRRVNAPFP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  223 AWQALLLKPDiffkiswlcKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQN--RGDLTAENVNQCV 300
Cdd:cd11083 157 YWRYLRLPAD---------RALDRALVEVRALVLDIIAAARARLAANPALAEAPETLLAMMLAEDdpDARLTDDEIYANV 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  301 LEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQ--SDDMPNLKIVENFIYESMRYQPVVDLIMRKAL 378
Cdd:cd11083 228 LTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPplLEALDRLPYLEAVARETLRLKPVAPLLFLEPN 307

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  379 QDDVIDGYPVKKGTNIIL---NIGRmhKLEFFPKPNEFSLENFEKNVPSRY------FQPFGFGPRSCVGKFIAMVMMKA 449
Cdd:cd11083 308 EDTVVGDIALPAGTPVFLltrAAGL--DAEHFPDPEEFDPERWLDGARAAEphdpssLLPFGAGPRLCPGRSLALMEMKL 385


                ....*...
gi 3913375  450 ILVTLLRR 457
Cdd:cd11083 386 VFAMLCRN 393
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 80-481 2.80e-26

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: 111.30  E-value: 2.80e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   80 TYGDFVRVWISGEETFIISKSSSVSHVMK-HWHYVSRFGSKLG-LQCIgmYENGIIFNNNPAhWKEIRpfftKALSgPGL 157
Cdd:cd11046   9 EYGPIYKLAFGPKSFLVISDPAIAKHVLRsNAFSYDKKGLLAEiLEPI--MGKGLIPADGEI-WKKRR----RALV-PAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  158 --------VRMIAICVESTTEHLDRLQEVTTELgNINALnlMRRIMLDTSNKLFL----GVPLDENAIVLKIQN-YFDA- 223
Cdd:cd11046  81 hkdylemmVRVFGRCSERLMEKLDAAAETGESV-DMEEE--FSSLTLDIIGLAVFnydfGSVTEESPVIKAVYLpLVEAe 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  224 ----WQALLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIeQKRQKLSTVEKLD-EHMDF-----ASQLIF-AQNRG-DL 291
Cdd:cd11046 158 hrsvWEPPYWDIPAALFIVPRQRKFLRDLKLLNDTLDDLI-RKRKEMRQEEDIElQQEDYlneddPSLLRFlVDMRDeDV 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  292 TAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDR-DIQSDDMPNLKIVENFIYESMRYQPVV 370
Cdd:cd11046 237 DSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRlPPTYEDLKKLKYTRRVLNESLRLYPQP 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  371 DLIMRKALQDDVIDG--YPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENFE---KNVPSRY-----FQPFGFGPRSCVG 439
Cdd:cd11046 317 PVLIRRAVEDDKLPGggVKVPAGTDIFISVYNLHRSpELWEDPEEFDPERFLdpfINPPNEViddfaFLPFGGGPRKCLG 396

                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 3913375  440 KFIAMVMMKAILVTLLRRCRVQTMKGRGlnniqknnDLSMHP 481
Cdd:cd11046 397 DQFALLEATVALAMLLRRFDFELDVGPR--------HVGMTT 430
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 131-457 2.93e-26

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: 110.77  E-value: 2.93e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  131 GIIFNNNPaHWKEIRPFFTKALS--GPGLVRMIAICVESTTEHLDRLQEvtTELGNINALNLMRRIMLDTSNKLFLGVPL 208
Cdd:cd20651  50 GITFTDGP-FWKEQRRFVLRHLRdfGFGRRSMEEVIQEEAEELIDLLKK--GEKGPIQMPDLFNVSVLNVLWAMVAGERY 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  209 DENAIVL-KIQNY-------FDAWQALLlkpDIFFKISWLC------KKYKDAVKDLKGAMEILIEQKRQKLstveKLDE 274
Cdd:cd20651 127 SLEDQKLrKLLELvhllfrnFDMSGGLL---NQFPWLRFIApefsgyNLLVELNQKLIEFLKEEIKEHKKTY----DEDN 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  275 HMDFASQLIFAQNRGDLTAENVN--QCV---LEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSD 348
Cdd:cd20651 200 PRDLIDAYLREMKKKEPPSSSFTddQLVmicLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGrDRLPTLD 279

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  349 DMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNV 422
Cdd:cd20651 280 DRSKLPYTEAVILEVLRIFTLVPIgIPHRALKDTTLGGYRIPKDTTILASLYSVHMdPEYWGDPEEFRPERFldedGKLL 359

                       330       340       350
                ....*....|....*....|....*....|....*
gi 3913375  423 PSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20651 360 KDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQN 394
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 227-460 3.58e-26

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: 110.34  E-value: 3.58e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  227 LLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTvEKLDE-----HMDFASQLIFAQNR-GD-LTAENVNQC 299
Cdd:cd20659 153 PLLHFDWIYYLTPEGRRFKKACDYVHKFAEEIIKKRRKELED-NKDEAlskrkYLDFLDILLTARDEdGKgLTDEEIRDE 231

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  300 VLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDR-DIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKAL 378
Cdd:cd20659 232 VDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLT 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  379 QDDVIDGYPVKKGTNIILNIGRMHK--------LEFfpKPNEFSLENFeKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAI 450
Cdd:cd20659 312 KPITIDGVTLPAGTLIAINIYALHHnptvwedpEEF--DPERFLPENI-KKRDPFAFIPFSAGPRNCIGQNFAMNEMKVV 388

                       250
                ....*....|
gi 3913375  451 LVTLLRRCRV 460
Cdd:cd20659 389 LARILRRFEL 398
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 232-455 4.17e-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: 110.78  E-value: 4.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  232 DIFFKISWL-----CKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAEN-----VNQCVL 301
Cdd:cd20654 168 DAIPFLGWLdfgghEKAMKRTAKELDSILEEWLEEHRQKRSSSGKSKNDEDDDDVMMLSILEDSQISGYdadtvIKATCL 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  302 EMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMR-YQPVVDLIMRKALQ 379
Cdd:cd20654 248 ELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGkDRWVEESDIKNLVYLQAIVKETLRlYPPGPLLGPREATE 327

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  380 DDVIDGYPVKKGTNIILNIGRMHK--------LEFfpKPNEFSLENFEKNVPSRYFQ--PFGFGPRSCVGKFIAMVMMKA 449
Cdd:cd20654 328 DCTVGGYHVPKGTRLLVNVWKIQRdpnvwsdpLEF--KPERFLTTHKDIDVRGQNFEliPFGSGRRSCPGVSFGLQVMHL 405


                ....*.
gi 3913375  450 ILVTLL 455
Cdd:cd20654 406 TLARLL 411
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 133-457 7.88e-26

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: 109.57  E-value: 7.88e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  133 IFNNNPAHWKE----IRPFFTKAlsgpglvrMIAIcVESTTEHLDRL-QEVTTELGNINALNLMRRIMLDTSNKLFLG-- 205
Cdd:cd11063  52 IFTSDGEEWKHsralLRPQFSRD--------QISD-LELFERHVQNLiKLLPRDGSTVDLQDLFFRLTLDSATEFLFGes 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  206 ----VPLDENAIVLKIQNYFDAWQALLLKPDIFFKISWLC--KKYKDAVKDLKGAMEILIEQ--KRQKLSTVEKLDEHMD 277
Cdd:cd11063 123 vdslKPGGDSPPAARFAEAFDYAQKYLAKRLRLGKLLWLLrdKKFREACKVVHRFVDPYVDKalARKEESKDEESSDRYV 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  278 FASQLI-FAQNRGDLTAEnvnqcVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD-RDIQSDDMPNLKI 355
Cdd:cd11063 203 FLDELAkETRDPKELRDQ-----LLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPePTPTYEDLKNMKY 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  356 VENFIYESMRYQPVVDLIMRKALQDDVI------DGYP---VKKGTNIILNIGRMHKLE--FFPKPNEFSLENFEKNVPS 424
Cdd:cd11063 278 LRAVINETLRLYPPVPLNSRVAVRDTTLprgggpDGKSpifVPKGTRVLYSVYAMHRRKdiWGPDAEEFRPERWEDLKRP 357

                       330       340       350
                ....*....|....*....|....*....|....
gi 3913375  425 RY-FQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11063 358 GWeYLPFNGGPRICLGQQFALTEASYVLVRLLQT 391
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 133-462 1.85e-25

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: 108.40  E-value: 1.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  133 IFNNNPAHWKEIR----PFFTKAlsgpglvRM------IAICVESTTEHLDRLQEVTTElgnINALNLMRRIMLDTSNKL 202
Cdd:cd11056  53 LFSLDGEKWKELRqkltPAFTSG-------KLknmfplMVEVGDELVDYLKKQAEKGKE---LEIKDLMARYTTDVIASC 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  203 FLGVPL----DENAIVLKIQNYFDAWQAL-LLKPDIFFKISWLCKKYK-------------DAVKDL------KGA---- 254
Cdd:cd11056 123 AFGLDAnslnDPENEFREMGRRLFEPSRLrGLKFMLLFFFPKLARLLRlkffpkevedffrKLVRDTieyrekNNIvrnd 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  255 -MEILIEQKRQKLSTVEKLDEHMDFasqlifaqnrGDLTAenvnQCVLeMMIAAPDTLSVTLFFMLILIAEHPTVEEEMM 333
Cdd:cd11056 203 fIDLLLELKKKGKIEDDKSEKELTD----------EELAA----QAFV-FFLAGFETSSSTLSFALYELAKNPEIQEKLR 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  334 REIETVVGDRD--IQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDG--YPVKKGTNIILNIGRMHKL-EFFP 408
Cdd:cd11056 268 EEIDEVLEKHGgeLTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPVIIPVYALHHDpKYYP 347

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3913375  409 KPNEFSLENF-EKNVPSRY---FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQT 462
Cdd:cd11056 348 EPEKFDPERFsPENKKKRHpytYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEP 405
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 79-461 2.06e-25

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: 108.05  E-value: 2.06e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   79 KTYGDFVRVWISGEETF-----------IISKSSSVSHVmkhwhyvsRFGSKLGLQCIGmyENGIIFNNNPAHwKEIRPF 147
Cdd:cd11053   9 ARYGDVFTLRVPGLGPVvvlsdpeaikqIFTADPDVLHP--------GEGNSLLEPLLG--PNSLLLLDGDRH-RRRRKL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  148 FTKALSGPGLVRMIAICVESTTEHLDRLQEVTTelgnINALNLMRRIMLDTSNKLFLGVplDENAIVLKIQNYFDAWQAL 227
Cdd:cd11053  78 LMPAFHGERLRAYGELIAEITEREIDRWPPGQP----FDLRELMQEITLEVILRVVFGV--DDGERLQELRRLLPRLLDL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  228 LLKPDIFFK------ISWL-CKKYKDAVKDLKGAMEILIEQKRQklstvEKLDEHMDFASQLIFAQ--NRGDLT-AENVN 297
Cdd:cd11053 152 LSSPLASFPalqrdlGPWSpWGRFLRARRRIDALIYAEIAERRA-----EPDAERDDILSLLLSARdeDGQPLSdEELRD 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  298 QcVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDiqSDDMPNLKIVENFIYESMRYQPVVDLIMRKA 377
Cdd:cd11053 227 E-LMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPD--PEDIAKLPYLDAVIKETLRLYPVAPLVPRRV 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  378 LQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENFEKNVPSRY-FQPFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd11053 304 KEPVELGGYTLPAGTTVAPSIYLTHHRPdLYPDPERFRPERFLGRKPSPYeYLPFGGGVRRCIGAAFALLEMKVVLATLL 383


                ....*.
gi 3913375  456 RRCRVQ 461
Cdd:cd11053 384 RRFRLE 389
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 116-464 2.16e-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: 108.14  E-value: 2.16e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  116 FGSKLGlQCIGMYengiifnnNPAHWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTELG--NINALNLMRR 193
Cdd:cd20615  44 FGQLLG-QCVGLL--------SGTDWKRVRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNSGDGRrfVIDPAQALKF 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  194 IMLDTSNKLFLGVPLDENA------IVLKIQNYFDAWQALLLKpdifFKIS-WLckkYKDAVKDLKG--------AMEIL 258
Cdd:cd20615 115 LPFRVIAEILYGELSPEEKeelwdlAPLREELFKYVIKGGLYR----FKISrYL---PTAANRRLREfqtrwrafNLKIY 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  259 -IEQKRQKLSTVEKLDEHMdfasqlifaqNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIE 337
Cdd:cd20615 188 nRARQRGQSTPIVKLYEAV----------EKGDITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEIS 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  338 TVvgdRDIQSDDMPNlKIVEN------FIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRMHKLEFFPKP 410
Cdd:cd20615 258 AA---REQSGYPMED-YILSTdtllayCVLESLRLRPLLAFsVPESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWGP 333

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3913375  411 N--EFSLENFEKNVPS--RY-FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMK 464
Cdd:cd20615 334 DgeAYRPERFLGISPTdlRYnFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPD 392
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 230-457 4.57e-25

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: 107.27  E-value: 4.57e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  230 KPDIFFKISWLCK-KYKDAVKDLKGAMEILIEQkRQKLSTVEKLD--EHMDFASQlifAQNRGDLTAENVNQCVLEMMIA 306
Cdd:cd11068 166 RPPILNKLRRRAKrQFREDIALMRDLVDEIIAE-RRANPDGSPDDllNLMLNGKD---PETGEKLSDENIRYQMITFLIA 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  307 APDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDG- 385
Cdd:cd11068 242 GHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGk 321

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  386 YPVKKGTNIILNIGRMHK---------LEFfpKPNEFSLENFEKnVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLR 456
Cdd:cd11068 322 YPLKKGDPVLVLLPALHRdpsvwgedaEEF--RPERFLPEEFRK-LPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQ 398


                .
gi 3913375  457 R 457
Cdd:cd11068 399 R 399
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 247-457 1.01e-23

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: 103.44  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  247 AVKDLKGAMEILIEQKRQKLST-VEKLDEHM--DFASQLIFAQ----NRGD-----LTAENVNQCVLEMMIAAPDTLSVT 314
Cdd:cd11027 169 ALRELKELMKERDEILRKKLEEhKETFDPGNirDLTDALIKAKkeaeDEGDedsglLTDDHLVMTISDIFGAGTETTATT 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  315 LFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGT 392
Cdd:cd11027 249 LRWAIAYLVNYPEVQAKLHAELDDVIGrDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTLRGYTIPKGT 328

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3913375  393 NIILNIGRMHK--------LEFfpKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11027 329 TVLVNLWALHHdpkewddpDEF--RPERFLDENGKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQK 399
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 294-457 1.90e-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: 99.56  E-value: 1.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  294 ENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS-DDMPNLKIVENFIYESMRYQPVVDL 372
Cdd:cd11026 225 ENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSlEDRAKMPYTDAVIHEVQRFGDIVPL 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  373 -IMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENF-------EKNvpsRYFQPFGFGPRSCVGKFIA 443
Cdd:cd11026 305 gVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPkQWETPEEFNPGHFldeqgkfKKN---EAFMPFSAGKRVCLGEGLA 381

                       170
                ....*....|....
gi 3913375  444 MVMMKAILVTLLRR 457
Cdd:cd11026 382 RMELFLFFTSLLQR 395
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 303-460 2.26e-22

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: 99.31  E-value: 2.26e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  303 MMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVvGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDV 382
Cdd:cd11045 219 LMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL-GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTE 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  383 IDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENF-----EKNVpSRY-FQPFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd11045 298 VLGYRIPAGTLVAVSPGVTHYMpEYWPNPERFDPERFsperaEDKV-HRYaWAPFGGGAHKCIGLHFAGMEVKAILHQML 376


                ....*
gi 3913375  456 RRCRV 460
Cdd:cd11045 377 RRFRW 381
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 290-462 2.80e-22

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: 99.22  E-value: 2.80e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  290 DLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS-DDMPNLKIVENFIYESMRYQP 368
Cdd:cd20647 232 ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTaEDVPKLPLIRALLKETLRLFP 311

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  369 VVDLIMRKALQDDVIDGYPVKKGTNIIL-NIGRMHKLEFFPKPNEFSlenfeknvPSRYFQ-------------PFGFGP 434
Cdd:cd20647 312 VLPGNGRVTQDDLIVGGYLIPKGTQLALcHYSTSYDEENFPRAEEFR--------PERWLRkdaldrvdnfgsiPFGYGI 383

                       170       180
                ....*....|....*....|....*...
gi 3913375  435 RSCVGKFIAMVMMKAILVTLLRRCRVQT 462
Cdd:cd20647 384 RSCIGRRIAELEIHLALIQLLQNFEIKV 411
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 291-466 7.34e-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: 97.91  E-value: 7.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  291 LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG--DRDIQSDDMPNLKIVENFIYESMRYQP 368
Cdd:cd20680 239 LSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGksDRPVTMEDLKKLRYLECVIKESLRLFP 318

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  369 VVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF-EKNVPSRY---FQPFGFGPRSCVGKFIA 443
Cdd:cd20680 319 SVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRdPRYFPEPEEFRPERFfPENSSGRHpyaYIPFSAGPRNCIGQRFA 398

                       170       180
                ....*....|....*....|...
gi 3913375  444 MVMMKAILVTLLRRCRVQTMKGR 466
Cdd:cd20680 399 LMEEKVVLSCILRHFWVEANQKR 421
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 291-485 1.08e-21

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: 97.37  E-value: 1.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  291 LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:cd11028 227 LTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGrERLPRLSDRPNLPYTEAFILETMRHSSF 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  370 VDL-IMRKALQDDVIDGYPVKKGTNIILNI-GRMHKLEFFPKPNEFSLENF---EKNV---PSRYFQPFGFGPRSCVGKF 441
Cdd:cd11028 307 VPFtIPHATTRDTTLNGYFIPKGTVVFVNLwSVNHDEKLWPDPSVFRPERFlddNGLLdktKVDKFLPFGAGRRRCLGEE 386

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 3913375  442 IAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNdLSMHPIERQ 485
Cdd:cd11028 387 LARMELFLFFATLLQQCEFSVKPGEKLDLTPIYG-LTMKPKPFK 429
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 130-455 4.04e-21

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: 95.56  E-value: 4.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  130 NGIIFNNNPaHW----KEIRP-FFTKALSGpglvrMIAICVESTT-------EHLDRLQEVTTElgnINALNLMRRIMLD 197
Cdd:cd20640  60 GGILTSNGP-HWahqrKIIAPeFFLDKVKG-----MVDLMVDSAQpllssweERIDRAGGMAAD---IVVDEDLRAFSAD 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  198 TSNKLFLGVPLDE-NAIVLKIQnyfdAWQALLLKPDIFFKIS---WLCKKYKDAVKDLKGAMEILIEQ---KRQKLSTVE 270
Cdd:cd20640 131 VISRACFGSSYSKgKEIFSKLR----ELQKAVSKQSVLFSIPglrHLPTKSNRKIWELEGEIRSLILEivkEREEECDHE 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  271 KldehmDFASQLIFAQNRGDL---TAEN--VNQCVlEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDI 345
Cdd:cd20640 207 K-----DLLQAILEGARSSCDkkaEAEDfiVDNCK-NIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPP 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  346 QSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMH--KLEFFPKPNEFSLENFEKNVP 423
Cdd:cd20640 281 DADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHldPEIWGPDANEFNPERFSNGVA 360

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 3913375  424 SRY-----FQPFGFGPRSCVGKFIAMVMMKaILVTLL 455
Cdd:cd20640 361 AACkpphsYMPFGAGARTCLGQNFAMAELK-VLVSLI 396
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 79-456 4.58e-21

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: 95.68  E-value: 4.58e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   79 KTYGDFVRVWISGEETFIISKSSSVSHVMK-HWHYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRP-FFTKALSGPG 156
Cdd:cd11073   2 KKYGPIMSLKLGSKTTVVVSSPEAAREVLKtHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKiCTTELFSPKR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  157 L-----VRMIaiCVEsttEHLDRLQEVTTELGNIN--------ALNLMrrimldtSNKLF---LGVPLDENAIVLK--IQ 218
Cdd:cd11073  82 LdatqpLRRR--KVR---ELVRYVREKAGSGEAVDigraafltSLNLI-------SNTLFsvdLVDPDSESGSEFKelVR 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  219 NYFDawqaLLLKPDI--------FFKISWLCKKYKDAVKDLKGAMEILIEQK-RQKLSTVEKLDEHMDFASQLIFAQNRG 289
Cdd:cd11073 150 EIME----LAGKPNVadffpflkFLDLQGLRRRMAEHFGKLFDIFDGFIDERlAEREAGGDKKKDDDLLLLLDLELDSES 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  290 DLTAENVNQCVLEMMIAAPDTLSVTLFFMLiliAE---HPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMR 365
Cdd:cd11073 226 ELTRNHIKALLLDLFVAGTDTTSSTIEWAM---AEllrNPEKMAKARAELDEVIGkDKIVEESDISKLPYLQAVVKETLR 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  366 YQPVVD-LIMRKALQDDVIDGYPVKKGTNIILN---IGRMhkleffPK----PNEFSLENF---EKNVPSRYFQ--PFGF 432
Cdd:cd11073 303 LHPPAPlLLPRKAEEDVEVMGYTIPKGTQVLVNvwaIGRD------PSvwedPLEFKPERFlgsEIDFKGRDFEliPFGS 376

                       410       420
                ....*....|....*....|....
gi 3913375  433 GPRSCVGKFIAMVMMKAILVTLLR 456
Cdd:cd11073 377 GRRICPGLPLAERMVHLVLASLLH 400
PLN02738 PLN02738
carotene beta-ring hydroxylase
 290-465 5.67e-21

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 96.52  E-value: 5.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   290 DLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:PLN02738 386 DVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQ 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   370 VDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-------LEFF---------PKPNEfSLENFeknvpsRYFqPFGFG 433
Cdd:PLN02738 466 PPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNF------SYL-PFGGG 537

                        170       180       190
                 ....*....|....*....|....*....|..
gi 3913375   434 PRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:PLN02738 538 PRKCVGDMFASFENVVATAMLVRRFDFQLAPG 569
PLN02655 PLN02655
ent-kaurene oxidase
 232-496 7.10e-21

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 95.19  E-value: 7.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   232 DIFFKISWL-CKKYKDAVKDL----KGAMEILIEQKRQKLSTVEKLDEHMDFASQlifaqNRGDLTAENVNQCVLEMMIA 306
Cdd:PLN02655 199 DFFPYLSWIpNKSFETRVQTTefrrTAVMKALIKQQKKRIARGEERDCYLDFLLS-----EATHLTDEQLMMLVWEPIIE 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   307 APDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMR-YQPVVDLIMRKALQDDVIDG 385
Cdd:PLN02655 274 AADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLPYLNAVFHETLRkYSPVPLLPPRFVHEDTTLGG 353

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   386 YPVKKGTNIILNI-GRMHKLEFFPKPNEFSLENF---EKNVPSRY-FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRV 460
Cdd:PLN02655 354 YDIPAGTQIAINIyGCNMDKKRWENPEEWDPERFlgeKYESADMYkTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEW 433

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 3913375   461 QTMKGRGLN-NIQKNNDLSMHPierqplLEMVFTPRR 496
Cdd:PLN02655 434 RLREGDEEKeDTVQLTTQKLHP------LHAHLKPRG 464
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 278-444 8.03e-21

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: 94.57  E-value: 8.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  278 FASQLIFAQ-NRGDLTAENVNQCVLEMMIAAPDTLSVTL-FFMLILIAeHPTVEEEMMREIETVVG-DRDIQSDDMPNLK 354
Cdd:cd11065 205 FVKDLLEELdKEGGLSEEEIKYLAGSLYEAGSDTTASTLqTFILAMAL-HPEVQKKAQEELDRVVGpDRLPTFEDRPNLP 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  355 IVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNI-GRMHKLEFFPKPNEFSLENFEKN------VPSRY 426
Cdd:cd11065 284 YVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKGTTVIPNAwAIHHDPEVYPDPEEFDPERYLDDpkgtpdPPDPP 363

                       170
                ....*....|....*...
gi 3913375  427 FQPFGFGPRSCVGKFIAM 444
Cdd:cd11065 364 HFAFGFGRRICPGRHLAE 381
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 254-465 1.92e-20

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: 93.42  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  254 AMEILieQKRQKLSTVEKLDEHmDFASQLIFAQ--NRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEE 331
Cdd:cd11060 182 ALEAV--AERLAEDAESAKGRK-DMLDSFLEAGlkDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAK 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  332 MMREIETVVGDR---DIQSDD----MPNLKIVenfIYESMRYQPVVDLIM-RKALQD-DVIDGYPVKKGTNIILNIGRMH 402
Cdd:cd11060 259 LRAEIDAAVAEGklsSPITFAeaqkLPYLQAV---IKEALRLHPPVGLPLeRVVPPGgATICGRFIPGGTIVGVNPWVIH 335

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3913375  403 KLE--FFPKPNEF----SLENFEKNVP--SRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:cd11060 336 RDKevFGEDADVFrperWLEADEEQRRmmDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVDP 406
PLN02290 PLN02290
cytokinin trans-hydroxylase
 77-459 2.78e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 93.73  E-value: 2.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    77 YNKTYGDFVRVWISGEETFIISKSSSVSH-VMKHWH-----YVSRFGSKlglQCIGmyeNGIIFNNNpAHWKEIRPFFTK 150
Cdd:PLN02290  89 WSKQYGKRFIYWNGTEPRLCLTETELIKElLTKYNTvtgksWLQQQGTK---HFIG---RGLLMANG-ADWYHQRHIAAP 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   151 ALSGPGLVRMIAICVESTTEHLDRLQEVTTELGN-INALNLMRRIMLDTSNKLFLGVPLDENAIVLKIQNYFDAWQALLL 229
Cdd:PLN02290 162 AFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQTeVEIGEYMTRLTADIISRTEFDSSYEKGKQIFHLLTVLQRLCAQAT 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   230 KPDIFFKISWLCKKYKDAVKDLKGAME-ILIE--QKRQKLSTVEKLDEH-MDFASQLIfaqNRGDLTAENVNQCVLEMMI 305
Cdd:PLN02290 242 RHLCFPGSRFFPSKYNREIKSLKGEVErLLMEiiQSRRDCVEIGRSSSYgDDLLGMLL---NEMEKKRSNGFNLNLQLIM 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   306 --------AAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKA 377
Cdd:PLN02290 319 decktfffAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMA 398

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   378 LQDDVIDGYPVKKGTNIILNIGRMHKLE--FFPKPNEFSLENF--EKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVT 453
Cdd:PLN02290 399 FEDIKLGDLHIPKGLSIWIPVLAIHHSEelWGKDANEFNPDRFagRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAM 478


                 ....*.
gi 3913375   454 LLRRCR 459
Cdd:PLN02290 479 LISKFS 484
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 303-461 2.84e-20

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: 93.05  E-value: 2.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  303 MMI----AAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD--IQSDDMPNLKIVENFIYESMRYQPVVDLIMRK 376
Cdd:cd11042 216 LLIallfAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDdpLTYDVLKEMPLLHACIKETLRLHPPIHSLMRK 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  377 ALQD--DVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENFEKNVP------SRYFQPFGFGPRSCVGKFIAMVMM 447
Cdd:cd11042 296 ARKPfeVEGGGYVIPKGHIVLASPAVSHRDpEIFKNPDEFDPERFLKGRAedskggKFAYLPFGAGRHRCIGENFAYLQI 375

                       170
                ....*....|....
gi 3913375  448 KAILVTLLRRCRVQ 461
Cdd:cd11042 376 KTILSTLLRNFDFE 389
PLN02936 PLN02936
epsilon-ring hydroxylase
 234-485 1.22e-19

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 91.78  E-value: 1.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   234 FFKISWLCK------KYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFA-----SQLIF-AQNRGDLTAENVNQCVL 301
Cdd:PLN02936 205 YWKVDFLCKisprqiKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIEGEEYVndsdpSVLRFlLASREEVSSVQLRDDLL 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   302 EMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 381
Cdd:PLN02936 285 SMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVED 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   382 VI-DGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENF--------EKNVPSRYFqPFGFGPRSCVGKFIAMVMMKAIL 451
Cdd:PLN02936 365 VLpGGYKVNAGQDIMISVYNIHRSpEVWERAEEFVPERFdldgpvpnETNTDFRYI-PFSGGPRKCVGDQFALLEAIVAL 443

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 3913375   452 VTLLRRCRVQTMKGRGLN-----NIQKNNDLSMHPIERQ 485
Cdd:PLN02936 444 AVLLQRLDLELVPDQDIVmttgaTIHTTNGLYMTVSRRR 482
PTZ00404 PTZ00404
cytochrome P450; Provisional
 295-444 1.39e-19

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 91.32  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   295 NVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD-IQSDDMPNLKIVENFIYESMRYQPVVDL- 372
Cdd:PTZ00404 283 SILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNkVLLSDRQSTPYTVAIIKETLRYKPVSPFg 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3913375   373 IMRKALQDDVI-DGYPVKKGTNIILN---IGRMHKleFFPKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAM 444
Cdd:PTZ00404 363 LPRSTSNDIIIgGGHFIPKDAQILINyysLGRNEK--YFENPEQFDPSRFLNPDSNDAFMPFSIGPRNCVGQQFAQ 436
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 242-461 2.00e-19

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 90.91  E-value: 2.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   242 KKYKDAVKDLKGAMEILIEQKRqklstVEKLDEHMDFASQliFAQNRGDltAENVNQCVLEMMIAAPDTLS--VTLFFML 319
Cdd:PLN02426 249 RKLKEAIKLVDELAAEVIRQRR-----KLGFSASKDLLSR--FMASIND--DKYLRDIVVSFLLAGRDTVAsaLTSFFWL 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   320 IliAEHPTVEEEMMREIETVVGDRDIQS--DDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVI-DGYPVKKGTNIIL 396
Cdd:PLN02426 320 L--SKHPEVASAIREEADRVMGPNQEAAsfEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLpDGTFVAKGTRVTY 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   397 N---IGRMHK------LEFFP----KPNEFSLENfeknvPSRY--FQPfgfGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:PLN02426 398 HpyaMGRMERiwgpdcLEFKPerwlKNGVFVPEN-----PFKYpvFQA---GLRVCLGKEMALMEMKSVAVAVVRRFDIE 469
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 249-457 2.05e-19

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: 90.59  E-value: 2.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  249 KDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLE---MMIAAPDTLSVTLFFMLILIAEH 325
Cdd:cd20639 183 KEIRKSLLKLIERRQTAADDEKDDEDSKDLLGLMISAKNARNGEKMTVEEIIEEcktFFFAGKETTSNLLTWTTVLLAMH 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  326 PTVEEEMMREIETVVGDRDIQS-DDMPNLKIVENFIYESMR-YQPVVDLImRKALQDDVIDGYPVKKGTNIILNIGRMH- 402
Cdd:cd20639 263 PEWQERARREVLAVCGKGDVPTkDHLPKLKTLGMILNETLRlYPPAVATI-RRAKKDVKLGGLDIPAGTELLIPIMAIHh 341

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3913375  403 -KLEFFPKPNEFSLENFEKNVPSRY-----FQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20639 342 dAELWGNDAAEFNPARFADGVARAAkhplaFIPFGLGPRTCVGQNLAILEAKLTLAVILQR 402
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 291-454 2.39e-19

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: 90.35  E-value: 2.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  291 LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:cd20655 224 ITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGkTRLVQESDLPNLPYLQAVVKETLRLHPP 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  370 VDLIMRKALQDDVIDGYPVKKGTNIILN---IGRMHKleFFPKPNEFSLENFEKNVPS--------RYFQ--PFGFGPRS 436
Cdd:cd20655 304 GPLLVRESTEGCKINGYDIPEKTTLFVNvyaIMRDPN--YWEDPLEFKPERFLASSRSgqeldvrgQHFKllPFGSGRRG 381

                       170
                ....*....|....*...
gi 3913375  437 CVGKFIAMVMMKAILVTL 454
Cdd:cd20655 382 CPGASLAYQVVGTAIAAM 399
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 259-465 7.25e-19

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: 88.72  E-value: 7.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  259 IEQK-RQKLSTVEKLDEHMDfASQLIFAQNRGD---LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMR 334
Cdd:cd20638 191 IEENiRAKIQREDTEQQCKD-ALQLLIEHSRRNgepLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRK 269

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  335 EIETVV-------GDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKL-EF 406
Cdd:cd20638 270 ELQEKGllstkpnENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVaDI 349

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3913375  407 FPKPNEFSLENFEKNVP---SRY-FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:cd20638 350 FPNKDEFNPDRFMSPLPedsSRFsFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNG 412
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 226-457 7.86e-19

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: 88.43  E-value: 7.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  226 ALLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTveKLDEHMDFASQLIFAQN--------RGDLTAENVN 297
Cdd:cd11061 146 GVLGHAPWLRPLLLDLPLFPGATKARKRFLDFVRAQLKERLKA--EEEKRPDIFSYLLEAKDpetgegldLEELVGEARL 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  298 qcvleMMIAAPDTLSVTL---FFMLiliAEHPTVEEEMMREIETV--VGDRDIQSDDMPNLKIVENFIYESMR-YQPVVD 371
Cdd:cd11061 224 -----LIVAGSDTTATALsaiFYYL---ARNPEAYEKLRAELDSTfpSDDEIRLGPKLKSLPYLRACIDEALRlSPPVPS 295

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  372 LIMRKALQDDV-IDGYPVKKGTNI---ILNIGRMHKLefFPKPNEFslenfeknVPSR-------------YFQPFGFGP 434
Cdd:cd11061 296 GLPRETPPGGLtIDGEYIPGGTTVsvpIYSIHRDERY--FPDPFEF--------IPERwlsrpeelvrarsAFIPFSIGP 365

                       250       260
                ....*....|....*....|...
gi 3913375  435 RSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11061 366 RGCIGKNLAYMELRLVLARLLHR 388
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 129-447 1.24e-18

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: 88.07  E-value: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  129 ENGIIFNNNPAHwKEIR----PFFT-KALSgpglvRMIAICVESTTEHLDRLQEVTTELGN-INALNLMRRIMLDTSNKL 202
Cdd:cd11082  47 EDNLIFMFGEEH-KELRksllPLFTrKALG-----LYLPIQERVIRKHLAKWLENSKSGDKpIEMRPLIRDLNLETSQTV 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  203 FLGVPLDENAIVLKIqNYFDAWQALLLKPdIFFKISWLCKKYKdAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQL 282
Cdd:cd11082 121 FVGPYLDDEARRFRI-DYNYFNVGFLALP-VDFPGTALWKAIQ-ARKRIVKTLEKCAAKSKKRMAAGEEPTCLLDFWTHE 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  283 IFA----------QNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD--IQSDDM 350
Cdd:cd11082 198 ILEeikeaeeegePPPPHSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEppLTLDLL 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  351 PNLKIVENFIYESMRYQPVVDLIMRKALQDDVI-DGYPVKKGTNIILNI-GRMHklEFFPKPNEFSLENF-----EKNVP 423
Cdd:cd11082 278 EEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLtEDYTVPKGTIVIPSIyDSCF--QGFPEPDKFDPDRFsperqEDRKY 355

                       330       340       350
                ....*....|....*....|....*....|...
gi 3913375  424 SRYFQPFGFGPRSCVGK---------FIAMVMM 447
Cdd:cd11082 356 KKNFLVFGAGPHQCVGQeyainhlmlFLALFST 388
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 234-455 4.84e-18

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: 86.36  E-value: 4.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  234 FFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGD--LTAENVNQCVLEMMIAAPDTL 311
Cdd:cd11072 165 IDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEfpLTRDNIKAIILDMFLAGTDTS 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  312 SVTL-FFMLILIAeHPTVeeemMR----EIETVVGDRD-IQSDDMPNLKIVENFIYESMRYQPVVD-LIMRKALQDDVID 384
Cdd:cd11072 245 ATTLeWAMTELIR-NPRV----MKkaqeEVREVVGGKGkVTEEDLEKLKYLKAVIKETLRLHPPAPlLLPRECREDCKIN 319

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  385 GYPVKKGTNIILN---IGRMHKLefFPKPNEFSLENFEkNVPSRY----FQ--PFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd11072 320 GYDIPAKTRVIVNawaIGRDPKY--WEDPEEFRPERFL-DSSIDFkgqdFEliPFGAGRRICPGITFGLANVELALANLL 396
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 76-457 6.70e-18

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: 85.88  E-value: 6.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   76 YYNKTY---GDFVRVWISGEETFIISKSSSVSHVMKH------WHYVSRFGSKL-GLQCIGMYENGIIFNNNPAHwkEIR 145
Cdd:cd11040   3 RNGKKYfsgGPIFTIRLGGQKIYVITDPELISAVFRNpktlsfDPIVIVVVGRVfGSPESAKKKEGEPGGKGLIR--LLH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  146 PFFTKALSGP-GLVRMIAICVESTTEHLDRLQ-EVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAivLKIQNYFDA 223
Cdd:cd11040  81 DLHKKALSGGeGLDRLNEAMLENLSKLLDELSlSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPELD--PDLVEDFWT 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  224 WQALLLKpdIFFKI-SWLCKKYKDAVKDLKGAMEILIEQKRqklstvekldEHMDFASQLIFAQNR----GDLTAENVNQ 298
Cdd:cd11040 159 FDRGLPK--LLLGLpRLLARKAYAARDRLLKALEKYYQAAR----------EERDDGSELIRARAKvlreAGLSEEDIAR 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  299 CVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQ------SDDMPNLKIVENFIYESMRYQpVVDL 372
Cdd:cd11040 227 AELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTnaildlTDLLTSCPLLDSTYLETLRLH-SSST 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  373 IMRKALQDDV-IDGYPVKKGTNIILNIGRMHKL-EFFPK-PNEFSLENFEKNVP-------SRYFQPFGFGPRSCVGKFI 442
Cdd:cd11040 306 SVRLVTEDTVlGGGYLLRKGSLVMIPPRLLHMDpEIWGPdPEEFDPERFLKKDGdkkgrglPGAFRPFGGGASLCPGRHF 385

                       410
                ....*....|....*
gi 3913375  443 AMVMMKAILVTLLRR 457
Cdd:cd11040 386 AKNEILAFVALLLSR 400
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 304-462 1.28e-17

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: 85.28  E-value: 1.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  304 MIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIEtVVGDRDIQSD--DMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 381
Cdd:cd20649 270 LIAGYETTTNTLSFATYLLATHPECQKKLLREVD-EFFSKHEMVDyaNVQELPYLDMVIAETLRMYPPAFRFAREAAEDC 348

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  382 VIDGYPVKKGTNIILNIGRMH-KLEFFPKPNEFSLENFEKNVPSRY----FQPFGFGPRSCVGKFIAMVMMKAILVTLLR 456
Cdd:cd20649 349 VVLGQRIPAGAVLEIPVGFLHhDPEHWPEPEKFIPERFTAEAKQRRhpfvYLPFGAGPRSCIGMRLALLEIKVTLLHILR 428


                ....*.
gi 3913375  457 RCRVQT 462
Cdd:cd20649 429 RFRFQA 434
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 247-457 1.45e-17

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: 83.89  E-value: 1.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  247 AVKDLKGAMEILIEQKRQKLSTvekldehmDFASQLIFAQNRG-DLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEH 325
Cdd:cd20629 151 AAAELYDYVLPLIAERRRAPGD--------DLISRLLRAEVEGeKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQH 222

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  326 PtveEEMmreiETVVGDRDIqsddMPNLkivenfIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE 405
Cdd:cd20629 223 P---EQL----ERVRRDRSL----IPAA------IEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDE 285

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3913375  406 -FFPKPNEFSLenFEKNVPSryfQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20629 286 dVYPDPDVFDI--DRKPKPH---LVFGGGAHRCLGEHLARVELREALNALLDR 333
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 232-457 1.62e-17

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: 84.68  E-value: 1.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  232 DIFfkiSWLCKKYKDAVKDLKGAMEIlieqkRQKLSTvEKLDEHM-----DFASQLIFAQNRGDLTAENVNQC------- 299
Cdd:cd20673 157 DIF---PWLQIFPNKDLEKLKQCVKI-----RDKLLQ-KKLEEHKekfssDSIRDLLDALLQAKMNAENNNAGpdqdsvg 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  300 ---------VLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:cd20673 228 lsddhilmtVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGfSRTPTLSDRNHLPLLEATIREVLRIRPV 307

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  370 VD-LIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENF------EKNVPSRYFQPFGFGPRSCVGKF 441
Cdd:cd20673 308 APlLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEkEWDQPDQFMPERFldptgsQLISPSLSYLPFGAGPRVCLGEA 387

                       250
                ....*....|....*.
gi 3913375  442 IAMVMMKAILVTLLRR 457
Cdd:cd20673 388 LARQELFLFMAWLLQR 403
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 241-465 1.75e-17

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: 84.51  E-value: 1.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  241 CKKYKDAVKDLkgameILIEQKRQKLSTVEKLDEHMDF-ASQLIFAQNRGDLT--AENVNQCVLEMMIAAPDTLSVTLFF 317
Cdd:cd20667 173 IFAYHDAVRSF-----IKKEVIRHELRTNEAPQDFIDCyLAQITKTKDDPVSTfsEENMIQVVIDLFLGGTETTATTLHW 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  318 MLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNII 395
Cdd:cd20667 248 ALLYMVHHPEIQEKVQQELDEVLGaSQLICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCVTSTTMHGYYVEKGTIIL 327

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3913375  396 LNIGR-MHKLEFFPKPNEFSLENF-EKN---VPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:cd20667 328 PNLASvLYDPECWETPHKFNPGHFlDKDgnfVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQLPEG 402
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 291-462 4.10e-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: 83.61  E-value: 4.10e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  291 LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIetVVGDRDIQSDDMPNLK---IVENFIYESMRYQ 367
Cdd:cd20643 230 LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEV--LAARQEAQGDMVKMLKsvpLLKAAIKETLRLH 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  368 PVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFEKNvPSRYFQP--FGFGPRSCVGKFIAM 444
Cdd:cd20643 308 PVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRdPTVFPKPEKYDPERWLSK-DITHFRNlgFGFGPRQCLGRRIAE 386

                       170
                ....*....|....*...
gi 3913375  445 VMMKAILVTLLRRCRVQT 462
Cdd:cd20643 387 TEMQLFLIHMLENFKIET 404
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 300-447 6.11e-17

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: 83.04  E-value: 6.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  300 VLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKA 377
Cdd:cd20653 232 ILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGqDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVpHES 311

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3913375  378 LQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFEKNVPSRY-FQPFGFGPRSCVGKFIAMVMM 447
Cdd:cd20653 312 SEDCKIGGYDIPRGTMLLVNAWAIHRdPKLWEDPTKFKPERFEGEEREGYkLIPFGLGRRACPGAGLAQRVV 383
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 287-460 9.36e-17

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: 82.46  E-value: 9.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  287 NRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS-DDMPNLKIVENFIYESMR 365
Cdd:cd20652 226 FDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTlEDLSSLPYLQACISESQR 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  366 YQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRMH-KLEFFPKPNEFSLENF----EKNVPSRYFQPFGFGPRSCVG 439
Cdd:cd20652 306 IRSVVPLgIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHmDPNLWEEPEEFRPERFldtdGKYLKPEAFIPFQTGKRMCLG 385

                       170       180
                ....*....|....*....|.
gi 3913375  440 KFIAMVMMKAILVTLLRRCRV 460
Cdd:cd20652 386 DELARMILFLFTARILRKFRI 406
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 262-459 1.13e-16

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: 82.08  E-value: 1.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  262 KRQKLSTVEK-----LDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREI 336
Cdd:cd20674 188 RQHKESLVAGqwrdmTDYMLQGLGQPRGEKGMGQLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEEL 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  337 ETVVGDRDIQS-DDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNI-GRMHKLEFFPKPNEF 413
Cdd:cd20674 268 DRVLGPGASPSyKDRARLPLLNATIAEVLRLRPVVPLaLPHRTTRDSSIAGYDIPKGTVVIPNLqGAHLDETVWEQPHEF 347

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 3913375  414 SLENF-EKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCR 459
Cdd:cd20674 348 RPERFlEPGAANRALLPFGCGARVCLGEPLARLELFVFLARLLQAFT 394
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 242-455 2.84e-16

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: 80.87  E-value: 2.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  242 KKYKDAVKDLKgameilIEQKRQKLSTVEKldehmDFASQLIF---AQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFM 318
Cdd:cd20658 192 RKYHDPIIDER------IKQWREGKKKEEE-----DWLDVFITlkdENGNPLLTPDEIKAQIKELMIAAIDNPSNAVEWA 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  319 LILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYPVKKGTNIIL 396
Cdd:cd20658 261 LAEMLNQPEILRKATEELDRVVGkERLVQESDIPNLNYVKACAREAFRLHPVAPFNVpHVAMSDTTVGGYFIPKGSHVLL 340

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3913375  397 N---IGRMHKleFFPKPNEFSLE---NFEKNV----PSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd20658 341 SrygLGRNPK--VWDDPLKFKPErhlNEDSEVtltePDLRFISFSTGRRGCPGVKLGTAMTVMLLARLL 407
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 242-461 4.62e-16

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: 80.09  E-value: 4.62e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  242 KKYKDAVKDLKGAMEILIEQKRQKLStvEKLDEHMDFASQ-LIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLI 320
Cdd:cd20646 181 KRYVDAWDTIFSFGKKLIDKKMEEIE--ERVDRGEPVEGEyLTYLLSSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALY 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  321 LIAEHPTVEEEMMREIETVV-GDRDIQSDD---MPNLKIVenfIYESMRYQPVVDLIMRKALQDDVIDG-YPVKKGTNII 395
Cdd:cd20646 259 HLARDPEIQERLYQEVISVCpGDRIPTAEDiakMPLLKAV---IKETLRLYPVVPGNARVIVEKEVVVGdYLFPKNTLFH 335

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3913375  396 L-NIGRMHKLEFFPKPNEFSLENFEKNVPSRY----FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:cd20646 336 LcHYAVSHDETNFPEPERFKPERWLRDGGLKHhpfgSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVR 406
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 78-497 4.85e-16

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 80.51  E-value: 4.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    78 NKTYGDFVRVWISGEETFIISKSSSVSHVMK--HWHYVSRFGSKlGLQCIGMYENGIIFNNNPAHWKEIRPFFTKALSGP 155
Cdd:PLN03234  58 SKLYGPIFTMKIGGRRLAVISSAELAKELLKtqDLNFTARPLLK-GQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSP 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   156 GLVRMI-AICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAIVLK--IQNYFDAwQALL---- 228
Cdd:PLN03234 137 NRVASFrPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKrfIDILYET-QALLgtlf 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   229 ---LKPDIFF--KISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRG-DLTAENVNQCVLE 302
Cdd:PLN03234 216 fsdLFPYFGFldNLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKDQPFSiKFTHENVKAMILD 295

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   303 MMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD-IQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQD 380
Cdd:PLN03234 296 IVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGyVSEEDIPNLPYLKAVIKESLRLEPVIPILLhRETIAD 375

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   381 DVIDGYPVKKGTNIILNIGRMHK--LEFFPKPNEFSLENFEKNVPSRYFQ-------PFGFGPRSCVGKFIAMVMMKAIL 451
Cdd:PLN03234 376 AKIGGYDIPAKTIIQVNAWAVSRdtAAWGDNPNEFIPERFMKEHKGVDFKgqdfellPFGSGRRMCPAMHLGIAMVEIPF 455

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 3913375   452 VTLLRRCRVQTMKGRGLNNIQKN--NDLSMHPIErqpllEMVFTPRRN 497
Cdd:PLN03234 456 ANLLYKFDWSLPKGIKPEDIKMDvmTGLAMHKKE-----HLVLAPTKH 498
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 208-460 8.23e-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: 79.74  E-value: 8.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  208 LDENAIVLKIQNYfdawqaLLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDE--------HMDFA 279
Cdd:cd20679 153 LELSALVVKRQQQ------LLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFlkakakskTLDFI 226

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  280 SQLIFAQNR--GDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD---IQSDDMPNLK 354
Cdd:cd20679 227 DVLLLSKDEdgKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREpeeIEWDDLAQLP 306

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  355 IVENFIYESMRYQPVVDLIMRKALQDDVI-DGYPVKKGTNIILNI-GRMHKLEFFPKPN-----EFSLENFEKNVPsRYF 427
Cdd:cd20679 307 FLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIyGTHHNPTVWPDPEvydpfRFDPENSQGRSP-LAF 385

                       250       260       270
                ....*....|....*....|....*....|...
gi 3913375  428 QPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRV 460
Cdd:cd20679 386 IPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRV 418
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 245-461 9.45e-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: 79.46  E-value: 9.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  245 KDAVKDLKGAMEILIEQKRQKLSTVEkLDEHMDFA-SQLIFAQN-----RGDLTAENVNQCVLEMMIAAPDTLSVTLFFM 318
Cdd:cd20668 171 QQAFKELQGLEDFIAKKVEHNQRTLD-PNSPRDFIdSFLIRMQEekknpNTEFYMKNLVMTTLNLFFAGTETVSTTLRYG 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  319 LILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIIL 396
Cdd:cd20668 250 FLLLMKHPEVEAKVHEEIDRVIGrNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKDTKFRDFFLPKGTEVFP 329

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  397 NIGR-MHKLEFFPKPNEFSLENF--EKNV--PSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:cd20668 330 MLGSvLKDPKFFSNPKDFNPQHFldDKGQfkKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFK 399
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 131-465 1.12e-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: 79.08  E-value: 1.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  131 GIIFNNNpAHWKEIRPFFTKALS--GPGLVRMiaicVESTTEHLDRLQEVTTELGNiNALNLMRRIMLDTSN---KLFLG 205
Cdd:cd20664  51 GILFSNG-ENWKEMRRFTLTTLRdfGMGKKTS----EDKILEEIPYLIEVFEKHKG-KPFETTLSMNVAVSNiiaSIVLG 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  206 VPLD-ENAIVLKIQNYFDAWQALLLKPDI--FFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHM--DFAS 280
Cdd:cd20664 125 HRFEyTDPTLLRMVDRINENMKLTGSPSVqlYNMFPWLGPFPGDINKLLRNTKELNDFLMETFMKHLDVLEPNDqrGFID 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  281 QLIFAQNRGDLTA------ENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLK 354
Cdd:cd20664 205 AFLVKQQEEEESSdsffhdDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKNMP 284

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  355 IVENFIYESMRYQPVVDLIMRKALQDDV-IDGYPVKKGTNII-LNIGRMHKLEFFPKPNEFSLENF----EKNVPSRYFQ 428
Cdd:cd20664 285 YTDAVIHEIQRFANIVPMNLPHATTRDVtFRGYFIPKGTYVIpLLTSVLQDKTEWEKPEEFNPEHFldsqGKFVKRDAFM 364

                       330       340       350
                ....*....|....*....|....*....|....*..
gi 3913375  429 PFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:cd20664 365 PFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPPG 401
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 242-495 1.13e-15

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 79.48  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   242 KKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIfaqnrgDLTAEN---------VNQCVLEMMIAAPDTLS 312
Cdd:PLN03112 240 KKMREVEKRVDEFHDKIIDEHRRARSGKLPGGKDMDFVDVLL------SLPGENgkehmddveIKALMQDMIAAATDTSA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   313 VTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKK 390
Cdd:PLN03112 314 VTNEWAMAEVIKNPRVLRKIQEELDSVVGrNRMVQESDLVHLNYLRCVVRETFRMHPAGPfLIPHESLRATTINGYYIPA 393

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   391 GTNIILNI---GRMHKLefFPKPNEFSLENFEKNVPSRYFQ---------PFGFGPRSCVGKFIAMVMMKAILVTLLRRC 458
Cdd:PLN03112 394 KTRVFINThglGRNTKI--WDDVEEFRPERHWPAEGSRVEIshgpdfkilPFSAGKRKCPGAPLGVTMVLMALARLFHCF 471

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 3913375   459 RVQTMKGRGLNNIQKNNDLSMHPIERQPLLEMVfTPR 495
Cdd:PLN03112 472 DWSPPDGLRPEDIDTQEVYGMTMPKAKPLRAVA-TPR 507
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 252-455 1.41e-15

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: 78.68  E-value: 1.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  252 KGAMEILIEQKRQKLSTVEKLDehmdfasQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEE 331
Cdd:cd20656 194 KAIMEEHTLARQKSGGGQQHFV-------ALLTLKEQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEK 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  332 MMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYPVKKGTNIILN---IGRMHKLef 406
Cdd:cd20656 267 AQEELDRVVGsDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLpHKASENVKIGGYDIPKGANVHVNvwaIARDPAV-- 344

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3913375  407 FPKPNEFSLENF---EKNVPSRYFQ--PFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd20656 345 WKNPLEFRPERFleeDVDIKGHDFRllPFGAGRRVCPGAQLGINLVTLMLGHLL 398
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 257-455 1.42e-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: 78.62  E-value: 1.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  257 ILIEQKRQKLSTVEKLDEHmDFASQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMRE 335
Cdd:cd20657 190 ILEEHKATAQERKGKPDFL-DFVLLENDDNGEGErLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEE 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  336 IETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYPVKKGTNIILN---IGRMHKLefFPKP 410
Cdd:cd20657 269 MDQVIGrDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLpRIASEACEVDGYYIPKGTRLLVNiwaIGRDPDV--WENP 346

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3913375  411 NEFSLENF--EKN----VPSRYFQ--PFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd20657 347 LEFKPERFlpGRNakvdVRGNDFEliPFGAGRRICAGTRMGIRMVEYILATLV 399
PLN02966 PLN02966
cytochrome P450 83A1
 259-480 1.46e-15

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 79.02  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   259 IEQKRQKLSTVEKLDEHMDFASQLIFAQnrgDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIET 338
Cdd:PLN02966 256 LDPKRVKPETESMIDLLMEIYKEQPFAS---EFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVRE 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   339 VVGDRD---IQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYPVKKGTNIILN---IGRMHKlEFFPKPN 411
Cdd:PLN02966 333 YMKEKGstfVTEDDVKNLPYFRALVKETLRIEPVIPLLIpRACIQDTKIAGYDIPAGTTVNVNawaVSRDEK-EWGPNPD 411

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3913375   412 EFSLENF-EKNVPSR----YFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKN--NDLSMH 480
Cdd:PLN02966 412 EFRPERFlEKEVDFKgtdyEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPDDINMDvmTGLAMH 487
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 188-481 2.59e-15

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: 77.92  E-value: 2.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  188 LNLMRRIMLdtsnklFLGVPLdenaivLKIQNYFdAWQALLLKPD--IFFKISWLCKKYKDavkdlkgameiLIEQKRQK 265
Cdd:cd20671 137 LDLIDEVMV------LLGSPG------LQLFNLY-PVLGAFLKLHkpILDKVEEVCMILRT-----------LIEARRPT 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  266 LSTveklDEHMDFASQLIFaQNRGDLTAE------NVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETV 339
Cdd:cd20671 193 IDG----NPLHSYIEALIQ-KQEEDDPKEtlfhdaNVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRV 267

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  340 VG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNII-LNIGRMHKLEFFPKPNEFSLEN 417
Cdd:cd20671 268 LGpGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIpLLSSVLLDKTQWETPYQFNPNH 347

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3913375  418 F----EKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRglnniqKNNDLSMHP 481
Cdd:cd20671 348 FldaeGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPGV------SPADLDATP 409
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 306-464 2.94e-15

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: 77.84  E-value: 2.94e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  306 AAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDD----MPNLKIVENfiyESMRYQPVVDLIMRKALQDD 381
Cdd:cd20650 239 AGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDtvmqMEYLDMVVN---ETLRLFPIAGRLERVCKKDV 315

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  382 VIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFEK----NVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLR 456
Cdd:cd20650 316 EINGVFIPKGTVVMIPTYALHRdPQYWPEPEEFRPERFSKknkdNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQ 395


                ....*...
gi 3913375  457 RCRVQTMK 464
Cdd:cd20650 396 NFSFKPCK 403
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 240-461 3.77e-15

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 77.67  E-value: 3.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   240 LCKKYKDAVKDLKGAMEILIEQKRQKLStvekldEHMDFASQliFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFML 319
Cdd:PLN02196 217 LFHKSMKARKELAQILAKILSKRRQNGS------SHNDLLGS--FMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWIL 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   320 ILIAEHPTVEEEMMREIETVVGDRDIQS----DDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNII 395
Cdd:PLN02196 289 KYLAENPSVLEAVTEEQMAIRKDKEEGEsltwEDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVL 368

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3913375   396 ---LNIgrMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:PLN02196 369 plfRNI--HHSADIFSDPGKFDPSRFEVAPKPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWS 435
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 232-456 6.15e-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: 76.93  E-value: 6.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  232 DIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDE-----HMDFASQLIFAQ--NRGDLTAENVNQCVLEMM 304
Cdd:cd20678 169 DFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKikkkrHLDFLDILLFAKdeNGKSLSDEDLRAEVDTFM 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  305 IAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD-IQSDD---MPNLKIVenfIYESMRYQPVVDLIMRKaLQD 380
Cdd:cd20678 249 FEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDsITWEHldqMPYTTMC---IKEALRLYPPVPGISRE-LSK 324

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  381 DVI--DGYPVKKGTNIILNI-GRMHKLEFFPKPNEFSLENFEK-NVPSRY---FQPFGFGPRSCVGKFIAMVMMK-AILV 452
Cdd:cd20678 325 PVTfpDGRSLPAGITVSLSIyGLHHNPAVWPNPEVFDPLRFSPeNSSKRHshaFLPFSAGPRNCIGQQFAMNEMKvAVAL 404


                ....
gi 3913375  453 TLLR 456
Cdd:cd20678 405 TLLR 408
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 67-456 1.05e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 76.31  E-value: 1.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375    67 WMGVGNACNYYN-----KTYGDFVRVWIsGEETFIISKSSSVSHVMKHWHYVsRFGSKLGLQCIGMYE-NG--IIFNNNP 138
Cdd:PLN02394  44 WLQVGDDLNHRNlaemaKKYGDVFLLRM-GQRNLVVVSSPELAKEVLHTQGV-EFGSRTRNVVFDIFTgKGqdMVFTVYG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   139 AHWKEIR-----PFFTKAL---SGPGLVRMIAICV-------ESTTEHL---DRLQevttelgnINALNLMRRIMLDTSn 200
Cdd:PLN02394 122 DHWRKMRrimtvPFFTNKVvqqYRYGWEEEADLVVedvranpEAATEGVvirRRLQ--------LMMYNIMYRMMFDRR- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   201 klFLGVpldENAIVLKIQ---------------NYFDAWQalLLKPDI--FFKIswlCKKYKDavKDLKGAMEILIEQKR 263
Cdd:PLN02394 193 --FESE---DDPLFLKLKalngersrlaqsfeyNYGDFIP--ILRPFLrgYLKI---CQDVKE--RRLALFKDYFVDERK 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   264 QKLSTV----EKLDEHMDfasQLIFAQNRGDLTAENVNQCVLEMMIAAPDTlsvTLFFMLILIAE---HPTVEEEMMREI 336
Cdd:PLN02394 261 KLMSAKgmdkEGLKCAID---HILEAQKKGEINEDNVLYIVENINVAAIET---TLWSIEWGIAElvnHPEIQKKLRDEL 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   337 ETVVGDRD-IQSDDMPNLKIVENFIYESMRYQ-PVVDLIMRKALQDDVIDGYPVKKGTNIILN---IGrmHKLEFFPKPN 411
Cdd:PLN02394 335 DTVLGPGNqVTEPDTHKLPYLQAVVKETLRLHmAIPLLVPHMNLEDAKLGGYDIPAESKILVNawwLA--NNPELWKNPE 412

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 3913375   412 EFSLENF-------EKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLR 456
Cdd:PLN02394 413 EFRPERFleeeakvEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQ 464
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 302-456 1.20e-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: 75.97  E-value: 1.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  302 EMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQ 379
Cdd:cd20666 235 DLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGpDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLsIPHMASE 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  380 DDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFEKN----VPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTL 454
Cdd:cd20666 315 NTVLQGYTIPKGTVIVPNLWSVHRdPAIWEKPDDFMPSRFLDEngqlIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSL 394


                ..
gi 3913375  455 LR 456
Cdd:cd20666 395 MQ 396
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 133-457 1.52e-14

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: 75.37  E-value: 1.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  133 IFNNNPAHWKEIRPFFTKALSGP---GLVRMIAICVESTTEHLDRLQE--VTTELGNINAlnlmrRIMLDTSNKLFLGVP 207
Cdd:cd11051  49 LISMEGEEWKRLRKRFNPGFSPQhlmTLVPTILDEVEIFAAILRELAEsgEVFSLEELTT-----NLTFDVIGRVTLDID 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  208 LDEnaivlkiQNYFDAWQALLLKPDIFFKISWLCKKYKDAVKDLKgameilieqkRQKLSTveKLDEHMdfaSQLIFAQN 287
Cdd:cd11051 124 LHA-------QTGDNSLLTALRLLLALYRSLLNPFKRLNPLRPLR----------RWRNGR--RLDRYL---KPEVRKRF 181

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  288 RGDLTAENVNQcvleMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRD-----IQSDD--MPNLKIVENF 359
Cdd:cd11051 182 ELERAIDQIKT----FLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGpDPSaaaelLREGPelLNQLPYTTAV 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  360 IYESMRYQPVVdLIMRKA-----LQDDVIDGYPVKkGTNIILNIGRMHKLE-FFPKPNEFSLENF------EKNVPSRYF 427
Cdd:cd11051 258 IKETLRLFPPA-GTARRGppgvgLTDRDGKEYPTD-GCIVYVCHHAIHRDPeYWPRPDEFIPERWlvdeghELYPPKSAW 335

                       330       340       350
                ....*....|....*....|....*....|
gi 3913375  428 QPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11051 336 RPFERGPRNCIGQELAMLELKIILAMTVRR 365
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 251-461 1.68e-14

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: 75.64  E-value: 1.68e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  251 LKGAMEILIEQKRQKlstvEKLDEHMDFASQLIFAQNRGD--LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTV 328
Cdd:cd20636 185 LHEYMEKAIEEKLQR----QQAAEYCDALDYMIHSARENGkeLTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSA 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  329 EEEMMREIETVVGDRDIQS-------DDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRM 401
Cdd:cd20636 261 IEKIRQELVSHGLIDQCQCcpgalslEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDT 340

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3913375  402 HKL-EFFPKPNEFSLENF----EKNVPSRY-FQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:cd20636 341 HETaAVYQNPEGFDPDRFgverEESKSGRFnYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWE 406
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 258-457 1.96e-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: 75.38  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  258 LIEQKRqklstvEKLDEHMDFasqlifaqnrgdlTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIE 337
Cdd:cd20665 208 LIKMEQ------EKHNQQSEF-------------TLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEID 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  338 TVVG--------DRdiqsDDMPNLKIVenfIYESMRYqpvVDLI----MRKALQDDVIDGYPVKKGTNIILNIGR-MHKL 404
Cdd:cd20665 269 RVIGrhrspcmqDR----SHMPYTDAV---IHEIQRY---IDLVpnnlPHAVTCDTKFRNYLIPKGTTVITSLTSvLHDD 338

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  405 EFFPKPNEFSLE-------NFEKnvpSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20665 339 KEFPNPEKFDPGhfldengNFKK---SDYFMPFSAGKRICAGEGLARMELFLFLTTILQN 395
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 300-443 2.37e-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: 74.79  E-value: 2.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  300 VLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS----DDMPNLKIVenfIYESMRYQPVVDLIMR 375
Cdd:cd20648 239 VTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSaadvARMPLLKAV---VKEVLRLYPVIPGNAR 315

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  376 KALQDDV-IDGYPVKKGTNIIL-NIGRMHKLEFFPKPNEFSlenfeknvPSRYFQ-----------PFGFGPRSCVGKFI 442
Cdd:cd20648 316 VIPDRDIqVGEYIIPKKTLITLcHYATSRDENQFPDPNSFR--------PERWLGkgdthhpyaslPFGFGKRSCIGRRI 387


                .
gi 3913375  443 A 443
Cdd:cd20648 388 A 388
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 306-459 2.82e-14

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: 74.79  E-value: 2.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  306 AAPDTLSVTLFFMLILIAEHP----TVEEEMMREIEtvvGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 381
Cdd:cd20641 246 AGHETTSNLLTWTMFLLSLHPdwqeKLREEVFRECG---KDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDM 322

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  382 VIDGYPVKKGTNIILNIGRMHKLE--FFPKPNEFSLENFEKNVPSRYFQP-----FGFGPRSCVGKFIAMVMMKAILVTL 454
Cdd:cd20641 323 KLGGLEIPKGTTIIIPIAKLHRDKevWGSDADEFNPLRFANGVSRAATHPnallsFSLGPRACIGQNFAMIEAKTVLAMI 402


                ....*
gi 3913375  455 LRRCR 459
Cdd:cd20641 403 LQRFS 407
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 292-457 3.92e-14

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: 74.47  E-value: 3.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  292 TAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS-DDMPNLKIVENFIYESMRYQPVV 370
Cdd:cd20661 235 SMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSfEDKCKMPYTEAVLHEVLRFCNIV 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  371 DL-IMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENF----EKNVPSRYFQPFGFGPRSCVGKFIAM 444
Cdd:cd20661 315 PLgIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEkYWSDPEVFHPERFldsnGQFAKKEAFVPFSLGRRHCLGEQLAR 394

                       170
                ....*....|...
gi 3913375  445 VMMKAILVTLLRR 457
Cdd:cd20661 395 MEMFLFFTALLQR 407
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 284-458 5.22e-14

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: 73.88  E-value: 5.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  284 FAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYE 362
Cdd:cd20675 224 SGDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGrDRLPCIEDQPNLPYVMAFLYE 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  363 SMRYQPVVDLIMRKALQDDV-IDGYPVKKGTNIILNIGRM-HKLEFFPKPNEFSlenfeknvPSRYFQPFGF-------- 432
Cdd:cd20675 304 AMRFSSFVPVTIPHATTADTsILGYHIPKDTVVFVNQWSVnHDPQKWPNPEVFD--------PTRFLDENGFlnkdlass 375

                       170       180       190
                ....*....|....*....|....*....|..
gi 3913375  433 ------GPRSCVGKFIAMVMMKAILVTLLRRC 458
Cdd:cd20675 376 vmifsvGKRRCIGEELSKMQLFLFTSILAHQC 407
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 294-443 6.06e-14

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: 73.68  E-value: 6.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  294 ENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD-RDIQSDDMPNLKIVENFIYESMRYQPVVDL 372
Cdd:cd20662 224 ENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQkRQPSLADRESMPYTNAVIHEVQRMGNIIPL 303

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3913375  373 -IMRKALQDDVIDGYPVKKGTNIILNIGRMHKlefFPK----PNEFSLENFEKNVPSR---YFQPFGFGPRSCVGKFIA 443
Cdd:cd20662 304 nVPREVAVDTKLAGFHLPKGTMILTNLTALHR---DPKewatPDTFNPGHFLENGQFKkreAFLPFSMGKRACLGEQLA 379
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 140-452 7.58e-14

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: 73.43  E-value: 7.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  140 HWKEIRPFFTKALSGPGLVRMIAICVESTTE-HLDRL-QEVTTELGNINALNLMRRIMLDTSNKLFLGVPLDENAI---- 213
Cdd:cd11075  63 LWRTLRRNLVSEVLSPSRLKQFRPARRRALDnLVERLrEEAKENPGPVNVRDHFRHALFSLLLYMCFGERLDEETVrele 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  214 -----VLKIQNYFDaWQALL--LKPdIFFKISWlcKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHMDF----ASQL 282
Cdd:cd11075 143 rvqreLLLSFTDFD-VRDFFpaLTW-LLNRRRW--KKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFllldLLDL 218

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  283 IFAQNRGDLT-AENVNQCVlEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDD----MPNLKIVe 357
Cdd:cd11075 219 KEEGGERKLTdEELVSLCS-EFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEdlpkMPYLKAV- 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  358 nfIYESMR-YQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK--------LEFfpKPNEFSLENFEKNVP--SRY 426
Cdd:cd11075 297 --VLETLRrHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRdpkvwedpEEF--KPERFLAGGEAADIDtgSKE 372

                       330       340       350
                ....*....|....*....|....*....|.
gi 3913375  427 FQ--PFGFGPRSCVGKFIAMV---MMKAILV 452
Cdd:cd11075 373 IKmmPFGAGRRICPGLGLATLhleLFVARLV 403
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 132-455 1.56e-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: 72.23  E-value: 1.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  132 IIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPLD-- 209
Cdd:cd11058  49 SISTADDEDHARLRRLLAHAFSEKALREQEPIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGESFGcl 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  210 EN-------AIVLKIqNYFDAW-QALLLKPDIFFKISWLCKKYkdAVKDLKGAMEILIEQKRQKLstvEKLDEHMDFASQ 281
Cdd:cd11058 129 ENgeyhpwvALIFDS-IKALTIiQALRRYPWLLRLLRLLIPKS--LRKKRKEHFQYTREKVDRRL---AKGTDRPDFMSY 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  282 LIFAQN-RGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREI-ETVVGDRDIQSDDMPNLKIVENF 359
Cdd:cd11058 203 ILRNKDeKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIrSAFSSEDDITLDSLAQLPYLNAV 282

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  360 IYESMR-YQPVVDLIMRKALQD-DVIDGYPVKKGTNI-ILNIGRMHKLEFFPKPNEFSLENFEKNVPSRY-------FQP 429
Cdd:cd11058 283 IQEALRlYPPVPAGLPRVVPAGgATIDGQFVPGGTSVsVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFdndkkeaFQP 362

                       330       340
                ....*....|....*....|....*.
gi 3913375  430 FGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd11058 363 FSVGPRNCIGKNLAYAEMRLILAKLL 388
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 262-455 1.60e-13

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 72.92  E-value: 1.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   262 KRQKLSTVEKLDEHMDFASQLI-------FAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMR 334
Cdd:PLN02687 257 EEHKAAGQTGSEEHKDLLSTLLalkreqqADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQE 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   335 EIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYPVKKGTNIILNI-GRMHKLEFFPKPN 411
Cdd:PLN02687 337 ELDAVVGrDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLpRMAAEECEINGYHIPKGATLLVNVwAIARDPEQWPDPL 416

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 3913375   412 EFSLENF-------EKNVPSRYFQ--PFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:PLN02687 417 EFRPDRFlpggehaGVDVKGSDFEliPFGAGRRICAGLSWGLRMVTLLTATLV 469
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 290-465 2.48e-13

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 72.12  E-value: 2.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   290 DLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDR----DIQSDDMPNLKIVE-----NF- 359
Cdd:PLN03195 287 NFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKALEKERakeeDPEDSQSFNQRVTQfagllTYd 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   360 -----------IYESMRYQPVVDLIMRKALQDDVI-DGYPVKKG---TNIILNIGRMhKLEFFPKPNEFSLENFEKNVPS 424
Cdd:PLN03195 367 slgklqylhavITETLRLYPAVPQDPKGILEDDVLpDGTKVKAGgmvTYVPYSMGRM-EYNWGPDAASFKPERWIKDGVF 445

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 3913375   425 RYFQPFGF-----GPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG 465
Cdd:PLN03195 446 QNASPFKFtafqaGPRICLGKDSAYLQMKMALALLCRFFKFQLVPG 491
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 103-459 4.46e-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: 70.71  E-value: 4.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  103 VSHVMKHWhyvSRFGSKLGLQ----CIGMYEN----GIIFNNNPAHwKEIRPFFTKALSGP------GLVRMIAicvest 168
Cdd:cd11078  30 VKAVLRDP---QTFSSAGGLTpespLWPEAGFaptpSLVNEDPPRH-TRLRRLVSRAFTPRriaalePRIRELA------ 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  169 TEHLDRLQE-----VTTELgninALNLMRRIMLDtsnklFLGVPLDEnaiVLKIQNYFDAWQALLLKPDIFFKISWLckk 243
Cdd:cd11078 100 AELLDRLAEdgradFVADF----AAPLPALVIAE-----LLGVPEED---MERFRRWADAFALVTWGRPSEEEQVEA--- 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  244 yKDAVKDLKGAMEILIEQKRQKLSTvekldehmDFASQLIfAQNRGD---LTAENVNQCVLEMMIAAPDTLSVTLFFMLI 320
Cdd:cd11078 165 -AAAVGELWAYFADLVAERRREPRD--------DLISDLL-AAADGDgerLTDEELVAFLFLLLVAGHETTTNLLGNAVK 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  321 LIAEHPTVEEEmmreietvvgdrdIQSDdmPNLkiVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGR 400
Cdd:cd11078 235 LLLEHPDQWRR-------------LRAD--PSL--IPNAVEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGS 297

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3913375  401 M-HKLEFFPKPNEFSL--ENFEKNVpsryfqPFGFGPRSCVGKFIAMVMMKAILVTLLRRCR 459
Cdd:cd11078 298 AnRDERVFPDPDRFDIdrPNARKHL------TFGHGIHFCLGAALARMEARIALEELLRRLP 353
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 259-461 4.83e-13

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: 70.99  E-value: 4.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  259 IEQKRQKLSTVEKldehMDFASQlIFAQNRgdLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIET 338
Cdd:cd20645 197 IDKRLQRYSQGPA----NDFLCD-IYHDNE--LSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQS 269

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  339 VVGD------RDIQSddMPNLKIVenfIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNigrMHKL----EFFP 408
Cdd:cd20645 270 VLPAnqtpraEDLKN--MPYLKAC---LKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMIN---SQALgsseEYFE 341

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3913375  409 KPNEFSLENF--EKNVPSRYFQ-PFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:cd20645 342 DGRQFKPERWlqEKHSINPFAHvPFGIGKRMCIGRRLAELQLQLALCWIIQKYQIV 397
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 142-483 7.09e-13

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: 70.41  E-value: 7.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  142 KEIRPFFTK-ALSGPGLVRMIaicVESTTEHLDRLQEVTTELGNINALNLMRRIMLDTSNKLFLG--VPLDENAIVLKIQ 218
Cdd:cd11059  60 RLLSGVYSKsSLLRAAMEPII---RERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGesFGTLLLGDKDSRE 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  219 NYFDAWQALLLKPDI-----FFKISWLC---KKYKDAVKDL-KGAMEiLIEQKRQKLSTVEKLDEHMDFASQLIFAQNRG 289
Cdd:cd11059 137 RELLRRLLASLAPWLrwlprYLPLATSRliiGIYFRAFDEIeEWALD-LCARAESSLAESSDSESLTVLLLEKLKGLKKQ 215

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  290 DLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD--RDIQSDDMPNLKIVENFIYESMRYQ 367
Cdd:cd11059 216 GLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPfrGPPDLEDLDKLPYLNAVIRETLRLY 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  368 PVVDLIMRKALQDD--VIDGYPVKKGTNI-ILNIGrMHKL-EFFPKPNEFSLENFEKNVPS------RYFQPFGFGPRSC 437
Cdd:cd11059 296 PPIPGSLPRVVPEGgaTIGGYYIPGGTIVsTQAYS-LHRDpEVFPDPEEFDPERWLDPSGEtaremkRAFWPFGSGSRMC 374

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 3913375  438 VGKFIAMVMMKAILVTLLRRCRVQTMkgrglnniqknNDLSMHPIE 483
Cdd:cd11059 375 IGMNLALMEMKLALAAIYRNYRTSTT-----------TDDDMEQED 409
PLN02971 PLN02971
tryptophan N-hydroxylase
 238-456 2.05e-12

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 69.30  E-value: 2.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   238 SWLCKKYKDAVKDLKgaMEILIEQKRQKLstveklDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFF 317
Cdd:PLN02971 278 SAIMDKYHDPIIDER--IKMWREGKRTQI------EDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEW 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   318 MLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNII 395
Cdd:PLN02971 350 AMAEMINKPEILHKAMEEIDRVVGkERFVQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVL 429

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3913375   396 LN---IGRMHK-----LEFFPKP--NEFSLENFEKNvpSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLR 456
Cdd:PLN02971 430 LSrygLGRNPKvwsdpLSFKPERhlNECSEVTLTEN--DLRFISFSTGKRGCAAPALGTAITTMMLARLLQ 498
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 270-443 2.20e-12

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: 68.65  E-value: 2.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  270 EKLDEHMDFASQlifaqnrgdltaeNVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS-D 348
Cdd:cd20672 214 EKSNHHTEFHHQ-------------NLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTlD 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  349 DMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNI--ILNiGRMHKLEFFPKPNEFSLENF-EKN--- 421
Cdd:cd20672 281 DRAKMPYTDAVIHEIQRFSDLIPIgVPHRVTKDTLFRGYLLPKNTEVypILS-SALHDPQYFEQPDTFNPDHFlDANgal 359

                       170       180
                ....*....|....*....|..
gi 3913375  422 VPSRYFQPFGFGPRSCVGKFIA 443
Cdd:cd20672 360 KKSEAFMPFSTGKRICLGEGIA 381
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 288-463 2.88e-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: 2.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  288 RGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVV--GDRDIQS--DDMPNLKIVenfIYES 363
Cdd:cd20644 225 QAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAaqISEHPQKalTELPLLKAA---LKET 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  364 MRYQPVVDLIMRKALQDDVIDGYPVKKGTNI---ILNIGRmhKLEFFPKPNEFSLENFEKNVPS-RYFQ--PFGFGPRSC 437
Cdd:cd20644 302 LRLYPVGITVQRVPSSDLVLQNYHIPAGTLVqvfLYSLGR--SAALFPRPERYDPQRWLDIRGSgRNFKhlAFGFGMRQC 379

                       170       180
                ....*....|....*....|....*.
gi 3913375  438 VGKFIAMVMMKAILVTLLRRCRVQTM 463
Cdd:cd20644 380 LGRRLAEAEMLLLLMHVLKNFLVETL 405
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 286-457 3.70e-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: 3.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  286 QNRGDLTAE----NVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQS-DDMPNLKIVENFI 360
Cdd:cd20670 213 QDKNNPHTEfnlkNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSvDDRVKMPYTDAVI 292

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  361 YESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLEN-------FEKNvpsRYFQPFG 431
Cdd:cd20670 293 HEIQRLTDIVPLgVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKdPKYFRYPEAFYPQHfldeqgrFKKN---EAFVPFS 369

                       170       180
                ....*....|....*....|....*.
gi 3913375  432 FGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20670 370 SGKRVCLGEAMARMELFLYFTSILQN 395
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 240-444 5.04e-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: 67.88  E-value: 5.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  240 LCKKYKDavKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIF-AQNRGDLTAENVNQCVLEMMIAAPDTlsvTLFFM 318
Cdd:cd11074 179 ICKEVKE--RRLQLFKDYFVDERKKLGSTKSTKNEGLKCAIDHILdAQKKGEINEDNVLYIVENINVAAIET---TLWSI 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  319 LILIAE---HPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYPVKKGTN 393
Cdd:cd11074 254 EWGIAElvnHPEIQKKLRDELDTVLGpGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVpHMNLHDAKLGGYDIPAESK 333

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  394 IILNIGRM-HKLEFFPKPNEFSLENF---EKNVPS-----RYFqPFGFGPRSCVGKFIAM 444
Cdd:cd11074 334 ILVNAWWLaNNPAHWKKPEEFRPERFleeESKVEAngndfRYL-PFGVGRRSCPGIILAL 392
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 130-461 8.43e-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: 67.09  E-value: 8.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  130 NGIIFNNNPaHWKEIRPFFTKALSGPGLVRmiaicveSTTEhlDRLQE---------VTTELGNINALNLMRRIMLDTSN 200
Cdd:cd20669  50 NGIAFSNGE-RWKILRRFALQTLRNFGMGK-------RSIE--ERILEeaqflleelRKTKGAPFDPTFLLSRAVSNIIC 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  201 KLFLGVPLD-ENAIVLKIQNYFDAWQALLLKP-----DIFFKI-SWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKlD 273
Cdd:cd20669 120 SVVFGSRFDyDDKRLLTILNLINDNFQIMSSPwgelyNIFPSVmDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDP-N 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  274 EHMDFASQLI--FAQNRGDLTA----ENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQ 346
Cdd:cd20669 199 SPRDFIDCFLtkMAEEKQDPLShfnmETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGrNRLPT 278

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  347 SDDMPNLKIVENFIYESMRYQPVVDLIMRKAL-QDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFE----- 419
Cdd:cd20669 279 LEDRARMPYTDAVIHEIQRFADIIPMSLPHAVtRDTNFRGFLIPKGTDVIPLLNSVHYdPTQFKDPQEFNPEHFLddngs 358

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 3913375  420 -KNVPSryFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:cd20669 359 fKKNDA--FMPFSAGKRICLGESLARMELFLYLTAILQNFSLQ 399
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 306-457 1.07e-11

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: 66.53  E-value: 1.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  306 AAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMR-YQPVVDLImrKALQDDVID 384
Cdd:cd20642 245 AGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPDFEGLNHLKVVTMILYEVLRlYPPVIQLT--RAIHKDTKL 322

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  385 G-YPVKKGTNIILNIGRMHK---------LEFfpKPNEFSlENFEKNVPSR--YFqPFGFGPRSCVGKFIAMVMMKAILV 452
Cdd:cd20642 323 GdLTLPAGVQVSLPILLVHRdpelwgddaKEF--NPERFA-EGISKATKGQvsYF-PFGWGPRICIGQNFALLEAKMALA 398


                ....*
gi 3913375  453 TLLRR 457
Cdd:cd20642 399 LILQR 403
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 291-495 1.54e-11

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 66.41  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   291 LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:PLN00110 285 LTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGrNRRLVESDLPKLPYLQAICKESFRKHPS 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   370 VDL-IMRKALQDDVIDGYPVKKGTNIILN---IGRmhKLEFFPKPNEFSLENF--EKNVP----SRYFQ--PFGFGPRSC 437
Cdd:PLN00110 365 TPLnLPRVSTQACEVNGYYIPKNTRLSVNiwaIGR--DPDVWENPEEFRPERFlsEKNAKidprGNDFEliPFGAGRRIC 442

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 3913375   438 VGKFIAMVMMKAILVTLLRRCRVQTMKGRGLnNIQKNNDLSMHpiERQPLLEMVfTPR 495
Cdd:PLN00110 443 AGTRMGIVLVEYILGTLVHSFDWKLPDGVEL-NMDEAFGLALQ--KAVPLSAMV-TPR 496
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 294-457 1.78e-11

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: 65.87  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  294 ENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD-RDIQSDDMPNLKIVENFIYESMRYQPVVDL 372
Cdd:cd20663 229 ENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQvRRPEMADQARMPYTNAVIHEVQRFGDIVPL 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  373 -IMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENF----EKNVPSRYFQPFGFGPRSCVGKFIAMVM 446
Cdd:cd20663 309 gVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDEtVWEKPLRFHPEHFldaqGHFVKPEAFMPFSAGRRACLGEPLARME 388

                       170
                ....*....|.
gi 3913375  447 MKAILVTLLRR 457
Cdd:cd20663 389 LFLFFTCLLQR 399
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 259-440 3.19e-11

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: 65.04  E-value: 3.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  259 IEQKRQKLSTVEKLDEhmDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIET 338
Cdd:cd11076 190 IEEHRAKRSNRARDDE--DDVDVLLSLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDA 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  339 VVGDRDIQSD-DMPNLKIVENFIYESMRYQPVVDLI--MRKALQDDVIDGYPVKKGTNIILNigrM----HKLEFFPKPN 411
Cdd:cd11076 268 AVGGSRRVADsDVAKLPYLQAVVKETLRLHPPGPLLswARLAIHDVTVGGHVVPAGTTAMVN---MwaitHDPHVWEDPL 344

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 3913375  412 EFSLENFEKNVPSRYFQ---------PFGFGPRSCVGK 440
Cdd:cd11076 345 EFKPERFVAAEGGADVSvlgsdlrlaPFGAGRRVCPGK 382
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 127-457 4.57e-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: 64.49  E-value: 4.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  127 MYENGIIFNNNPAHwKEIRPFFTKALSGPGLVRMIAICVESTTEHLDRLQEVTtelgninALNLMR--------RIMLDt 198
Cdd:cd20625  52 LLSRSMLFLDPPDH-TRLRRLVSKAFTPRAVERLRPRIERLVDELLDRLAARG-------RVDLVAdfayplpvRVICE- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  199 snklFLGVPLDENAIVLKiqnYFDAWQALLlkpDIFFKISwLCKKYKDAVKDLKGAMEILIEQKRQKLSTvekldehmDF 278
Cdd:cd20625 123 ----LLGVPEEDRPRFRG---WSAALARAL---DPGPLLE-ELARANAAAAELAAYFRDLIARRRADPGD--------DL 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  279 ASQLIFAQNRGD-LT-AENVNQCVLeMMIAAPDTlSVTLFF--MLILiAEHPtveEEMmreiETVVGDRDIqsddMPNLk 354
Cdd:cd20625 184 ISALVAAEEDGDrLSeDELVANCIL-LLVAGHET-TVNLIGngLLAL-LRHP---EQL----ALLRADPEL----IPAA- 248

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  355 iVEnfiyESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIG------RMhklefFPKPNEFSlenfeknvPSRYFQ 428
Cdd:cd20625 249 -VE----ELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGaanrdpAV-----FPDPDRFD--------ITRAPN 310

                       330       340       350
                ....*....|....*....|....*....|..
gi 3913375  429 P---FGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20625 311 RhlaFGAGIHFCLGAPLARLEAEIALRALLRR 342
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 239-448 4.81e-11

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: 64.64  E-value: 4.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  239 WLCKKYKDAVKDLKGAMeilieQKRQKLSTVekldehmdfaSQLIFAQNRGDLTAenvNQCVLEMMIAAPDTLSVTlFFM 318
Cdd:cd20635 173 WLLSLFEKVVPDAEKTK-----PLENNSKTL----------LQHLLDTVDKENAP---NYSLLLLWASLANAIPIT-FWT 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  319 LILIAEHPTVEEEMMREIETVVGDRD-----IQSDDMPNLKIVENFIYESMRYQPvVDLIMRKALQDDVIDGYPVKKGTN 393
Cdd:cd20635 234 LAFILSHPSVYKKVMEEISSVLGKAGkdkikISEDDLKKMPYIKRCVLEAIRLRS-PGAITRKVVKPIKIKNYTIPAGDM 312

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  394 IILNIGRMHK-LEFFPKPNEFSLE-----NFEKNVPSRYFQPFGFGPRSCVGK---------FIAMVMMK 448
Cdd:cd20635 313 LMLSPYWAHRnPKYFPDPELFKPErwkkaDLEKNVFLEGFVAFGGGRYQCPGRwfalmeiqmFVAMFLYK 382
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 245-469 5.09e-11

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: 64.65  E-value: 5.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  245 KDAVKDLKGAmeiLIEQKRQKlstveKLDEHmdfasqlifaqNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAE 324
Cdd:cd20676 206 KDNIRDITDS---LIEHCQDK-----KLDEN-----------ANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVT 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  325 HPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRM- 401
Cdd:cd20676 267 YPEIQKKIQEELDEVIGrERRPRLSDRPQLPYLEAFILETFRHSSFVPFtIPHCTTRDTSLNGYYIPKDTCVFINQWQVn 346

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3913375  402 HKLEFFPKPNEFSLENF------EKN-VPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLN 469
Cdd:cd20676 347 HDEKLWKDPSSFRPERFltadgtEINkTESEKVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPPGVKVD 421
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 304-455 7.34e-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: 64.24  E-value: 7.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  304 MIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-----DR-----DIQSDDMPNLkivENFIYESMRYQPVVDLI 373
Cdd:cd20622 271 LIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPeavaeGRlptaqEIAQARIPYL---DAVIEEILRCANTAPIL 347

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  374 MRKALQDDVIDGYPVKKGTNIIL--NIG-----------------RMHKLEFFPKPNEFSLENFEknvPSR--------- 425
Cdd:cd20622 348 SREATVDTQVLGYSIPKGTNVFLlnNGPsylsppieidesrrsssSAAKGKKAGVWDSKDIADFD---PERwlvtdeetg 424

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 3913375  426 ---------YFQPFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd20622 425 etvfdpsagPTLAFGLGPRGCFGRRLAYLEMRLIITLLV 463
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 289-457 1.62e-10

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: 62.74  E-value: 1.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  289 GDLTAENVNQCVLEMMI--AAPDTLSVTLFFMLILiaehptveEEMMREietvvGDR----DIQSDDMPNLKI---VENF 359
Cdd:cd20612 177 GALLDAAVADEVRDNVLgtAVGGVPTQSQAFAQIL--------DFYLRR-----PGAahlaEIQALARENDEAdatLRGY 243

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  360 IYESMRYQPVVDLIMRKALQDDVID-----GYPVKKGTNIILNIGR-MHKLEFFPKPNEFSlenfeknvPSRYFQP---F 430
Cdd:cd20612 244 VLEALRLNPIAPGLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASaMRDPRAFPDPERFR--------LDRPLESyihF 315

                       170       180
                ....*....|....*....|....*..
gi 3913375  431 GFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20612 316 GHGPHQCLGEEIARAALTEMLRVVLRL 342
PLN02500 PLN02500
cytochrome P450 90B1
 249-447 5.87e-10

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 61.42  E-value: 5.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   249 KDLKGAMEIL--IEQK-RQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEH 325
Cdd:PLN02500 230 KALKSRATILkfIERKmEERIEKLKEEDESVEEDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGC 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   326 PTVEEEMMRE------IETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIG 399
Cdd:PLN02500 310 PKAVQELREEhleiarAKKQSGESELNWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIA 389

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   400 RMH-KLEFFPKPNEFSLENFEKNVPSR-----------YFQPFGFGPRSCVGKFIAMVMM 447
Cdd:PLN02500 390 AVHlDSSLYDQPQLFNPWRWQQNNNRGgssgsssattnNFMPFGGGPRLCAGSELAKLEM 449
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 249-461 6.39e-10

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: 61.02  E-value: 6.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  249 KDLKGAMEILIEQKRQklstvekldehmdfasqlifaqNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTV 328
Cdd:cd20637 202 KDYADALDILIESAKE----------------------HGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGV 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  329 EEEMMREI-------ETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRM 401
Cdd:cd20637 260 LEKLREELrsngilhNGCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDT 339

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3913375  402 H-------KLEFFpKPNEFSLENFEKNVPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQ 461
Cdd:cd20637 340 HdtapvfkDVDAF-DPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFE 405
PLN02183 PLN02183
ferulate 5-hydroxylase
 240-439 7.13e-10

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 61.40  E-value: 7.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   240 LCKKYKDAVKDLKGAMEILIE---QKRQKLSTVEK--------LDEHMDFASQLIFA------QNRGDLTAENVNQCVLE 302
Cdd:PLN02183 232 LNKRLVKARKSLDGFIDDIIDdhiQKRKNQNADNDseeaetdmVDDLLAFYSEEAKVnesddlQNSIKLTRDNIKAIIMD 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   303 MMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 381
Cdd:PLN02183 312 VMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDA 391

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3913375   382 VIDGYPVKKGTNIILN---IGR---------MHKLEFFPKPN--EFSLENFEknvpsryFQPFGFGPRSCVG 439
Cdd:PLN02183 392 EVAGYFIPKRSRVMINawaIGRdknswedpdTFKPSRFLKPGvpDFKGSHFE-------FIPFGSGRRSCPG 456
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 146-496 1.86e-09

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: 59.76  E-value: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  146 PFFTKALSGPGLVRMIAICVESttehldRLQEVTTElGNINALNLMRRIMLDTSNKLfLGVPLDEnaivlkiqnyFDAWQ 225
Cdd:cd20614  76 SFTPKGLSAAGVGALIAEVIEA------RIRAWLSR-GDVAVLPETRDLTLEVIFRI-LGVPTDD----------LPEWR 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  226 ---------ALLLKPDIFFKISWLCKKYKDAVKdlkgameiliEQKRQKLSTVEKLDEHMDFASQLIFAQNRGD--LTAE 294
Cdd:cd20614 138 rqyrelflgVLPPPVDLPGMPARRSRRARAWID----------ARLSQLVATARANGARTGLVAALIRARDDNGagLSEQ 207

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  295 NVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVvGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIM 374
Cdd:cd20614 208 ELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA-GDVPRTPAELRRFPLAEALFRETLRLHPPVPFVF 286

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  375 RKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPSRYFQpFGFGPRSCVGKFIAMVMMKA 449
Cdd:cd20614 287 RRVLEEIELGGRRIPAGTHLGIPLLLFSRdPELYPDPDRFRPERWlgrdRAPNPVELLQ-FGGGPHFCLGYHVACVELVQ 365

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 3913375  450 ILVTLLRrcrvqtmkgrglnniqknndlSMHPIERQPLLEMVFTPRR 496
Cdd:cd20614 366 FIVALAR---------------------ELGAAGIRPLLVGVLPGRR 391
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 244-471 2.61e-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: 59.13  E-value: 2.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  244 YKDAVKDLKGAMEILIEQ-KRQKLSTvekldehmD-FASQLIFAQNRGDLTAEnvnQCVLEMM---IAAPDTLSVTLFFM 318
Cdd:cd11037 157 TRAALPRLKELRDWVAEQcARERLRP--------GgWGAAIFEAADRGEITED---EAPLLMRdylSAGLDTTISAIGNA 225

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  319 LILIAEHPTvEEEMMREietvvgDRdiqsddmpnlKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNI 398
Cdd:cd11037 226 LWLLARHPD-QWERLRA------DP----------SLAPNAFEEAVRLESPVQTFSRTTTRDTELAGVTIPAGSRVLVFL 288

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3913375  399 GRMHKLE-FFPKPNEFSLEnfeKNvPSRYFQpFGFGPRSCVGKFIAMVMMKAILVTLLRRCRVQTMKG---RGLNNI 471
Cdd:cd11037 289 GSANRDPrKWDDPDRFDIT---RN-PSGHVG-FGHGVHACVGQHLARLEGEALLTALARRVDRIELAGppvRALNNT 360
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 291-481 2.82e-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: 58.95  E-value: 2.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  291 LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPV 369
Cdd:cd20677 232 LSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGlSRLPRFEDRKSLHYTEAFINEVFRHSSF 311

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  370 VDL-IMRKALQDDVIDGYPVKKGTNIILNIGRM-HKLEFFPKPNEFSLENF-------EKNVPSRYFQpFGFGPRSCVGK 440
Cdd:cd20677 312 VPFtIPHCTTADTTLNGYFIPKDTCVFINMYQVnHDETLWKDPDLFMPERFldengqlNKSLVEKVLI-FGMGVRKCLGE 390

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3913375  441 FIAMVMMKAILVTLLRRCRVQTMKGRGLnNIQKNNDLSMHP 481
Cdd:cd20677 391 DVARNEIFVFLTTILQQLKLEKPPGQKL-DLTPVYGLTMKP 430
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 234-457 3.00e-09

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 59.22  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   234 FFKISW--LCKKYKDAVK---DLKGAMEILIEQKRQKlsTVEKLDEHMDFASQLIFAQNrgDLTAENVNQCVLEMMIAAP 308
Cdd:PLN02987 205 FFSVPLplFSTTYRRAIQartKVAEALTLVVMKRRKE--EEEGAEKKKDMLAALLASDD--GFSDEEIVDFLVALLVAGY 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   309 DTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRD----IQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVID 384
Cdd:PLN02987 281 ETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSdsysLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVK 360

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3913375   385 GYPVKKGTNIILNIGRMH-KLEFFPKPNEFSLENFEKN----VPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:PLN02987 361 GYTIPKGWKVFASFRAVHlDHEYFKDARTFNPWRWQSNsgttVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTR 438
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 296-471 3.06e-09

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 59.25  E-value: 3.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   296 VNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETvvgdrDIQSDDMPNLKIVENFIYESMRYQPVVDLIMR 375
Cdd:PLN02169 302 IRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINT-----KFDNEDLEKLVYLHAALSESMRLYPPLPFNHK 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   376 KALQDDVI-DGYPVKKGTNIILNI---GRMHK------LEFfpKPNEFSLENFE-KNVPSRYFQPFGFGPRSCVGKFIAM 444
Cdd:PLN02169 377 APAKPDVLpSGHKVDAESKIVICIyalGRMRSvwgedaLDF--KPERWISDNGGlRHEPSYKFMAFNSGPRTCLGKHLAL 454

                        170       180
                 ....*....|....*....|....*..
gi 3913375   445 VMMKAILVTLLRRCRVQTMKGRGLNNI 471
Cdd:PLN02169 455 LQMKIVALEIIKNYDFKVIEGHKIEAI 481
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 203-443 3.52e-09

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: 58.37  E-value: 3.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  203 FLGVPLDEnaivlkiQNYFDAWQALLLKPDiffkiswlckkykDAVKDLKGAMEI------LIEQKRQklstveklDEHM 276
Cdd:cd11035 119 LMGLPLED-------LDRFLEWEDAMLRPD-------------DAEERAAAAQAVldyltpLIAERRA--------NPGD 170

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  277 DFASQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVgdrdiqsddmpnlki 355
Cdd:cd11035 171 DLISAILNAEIDGRpLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLREDPELIP--------------- 235

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  356 veNFIYESMRYQPVVDLImRKALQDDVIDGYPVKKGTNIILNIGrMHKL--EFFPKPNEFSLEnfekNVPSRYFQpFGFG 433
Cdd:cd11035 236 --AAVEELLRRYPLVNVA-RIVTRDVEFHGVQLKAGDMVLLPLA-LANRdpREFPDPDTVDFD----RKPNRHLA-FGAG 306

                       250
                ....*....|
gi 3913375  434 PRSCVGKFIA 443
Cdd:cd11035 307 PHRCLGSHLA 316
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 95-457 4.02e-09

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: 58.50  E-value: 4.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   95 FIISKSSSVSHVMKHWHYVSRFGSKLGLQCIGMYENGIIfNNNPAHWKEIR----PFFTkalsgPGLVRMIAICVESTTe 170
Cdd:cd11034  16 WVLTRYAEVQAVARDTDTFSSKGVTFPRPELGEFRLMPI-ETDPPEHKKYRkllnPFFT-----PEAVEAFRPRVRQLT- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  171 hlDRLQEVTTELGNINALN-----LMRRIMLDtsnklFLGVPldenaiVLKIQNYFDAWQALLLKPDiffkiswlCKKYK 245
Cdd:cd11034  89 --NDLIDAFIERGECDLVTelanpLPARLTLR-----LLGLP------DEDGERLRDWVHAILHDED--------PEEGA 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  246 DAVKDLKGAMEILIEQKRQklstvEKLDehmDFASQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAE 324
Cdd:cd11034 148 AAFAELFGHLRDLIAERRA-----NPRD---DLISRLIEGEIDGKpLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQ 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  325 HPTVEEEMMREietvvgdrdiqsddmPNL--KIVENFIyesmRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRM- 401
Cdd:cd11034 220 HPEDRRRLIAD---------------PSLipNAVEEFL----RFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASAn 280

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3913375  402 HKLEFFPKPNEFSLENFeknvPSRYFQpFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11034 281 RDEEKFEDPDRIDIDRT----PNRHLA-FGSGVHRCLGSHLARVEARVALTEVLKR 331
PLN02774 PLN02774
brassinosteroid-6-oxidase
 247-459 4.23e-09

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 58.63  E-value: 4.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   247 AVKDLKGAMEILIEQKRQKLSTvekldeHMDFASQLIFAQ-NRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEH 325
Cdd:PLN02774 221 ARKNIVRMLRQLIQERRASGET------HTDMLGYLMRKEgNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDH 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   326 PTVEEEMMRE----IETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRM 401
Cdd:PLN02774 295 PKALQELRKEhlaiRERKRPEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREI 374

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3913375   402 HKLEF-FPKPNEFSLENF-EKNVPSR-YFQPFGFGPRSCVGKFIAMVMMKAILVTLLRRCR 459
Cdd:PLN02774 375 NYDPFlYPDPMTFNPWRWlDKSLESHnYFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYR 435
PLN03018 PLN03018
homomethionine N-hydroxylase
 298-456 5.29e-09

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 58.48  E-value: 5.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   298 QCVlEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVG-DRDIQSDDMPNLKIVENFIYESMRYQPVVDLI-MR 375
Cdd:PLN03018 318 QCV-EFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGkDRLVQESDIPNLNYLKACCRETFRIHPSAHYVpPH 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   376 KALQDDVIDGYPVKKGTNIIL---NIGRMHKLEFFP---KPNE-FSLENFEKNVP----SRYFQPFGFGPRSCVGKFIAM 444
Cdd:PLN03018 397 VARQDTTLGGYFIPKGSHIHVcrpGLGRNPKIWKDPlvyEPERhLQGDGITKEVTlvetEMRFVSFSTGRRGCVGVKVGT 476

                        170
                 ....*....|..
gi 3913375   445 VMMKAILVTLLR 456
Cdd:PLN03018 477 IMMVMMLARFLQ 488
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 144-457 8.33e-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: 57.65  E-value: 8.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  144 IRPFFTKAlsgpGLVRMIAIcVESTTEHL-DRLQEVTTELGNINALNLMRRIMLDTSNKLFLGVPL------DENAIVLK 216
Cdd:cd11062  62 LSPFFSKR----SILRLEPL-IQEKVDKLvSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYgyldepDFGPEFLD 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  217 IQNYFDAWQALLLKPDIFFKI-----SWLCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDE----HMDFASQLIFAQN 287
Cdd:cd11062 137 ALRALAEMIHLLRHFPWLLKLlrslpESLLKRLNPGLAVFLDFQESIAKQVDEVLRQVSAGDPpsivTSLFHALLNSDLP 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  288 RGDLTAENVNQCVLEMMIAAPDT----LSVTLFFMLiliaEHPTVEEEMMREIETVVGDRDiqsdDMPNLKIVENF---- 359
Cdd:cd11062 217 PSEKTLERLADEAQTLIGAGTETtartLSVATFHLL----SNPEILERLREELKTAMPDPD----SPPSLAELEKLpylt 288

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  360 --IYESMRYQPVVDLIM-RKALQDD-VIDGYPVKKGTNIILNIGRMH---KLefFPKPNEFS----LENFEKNVPSRYFQ 428
Cdd:cd11062 289 avIKEGLRLSYGVPTRLpRVVPDEGlYYKGWVIPPGTPVSMSSYFVHhdeEI--FPDPHEFRperwLGAAEKGKLDRYLV 366

                       330       340
                ....*....|....*....|....*....
gi 3913375  429 PFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11062 367 PFSKGSRSCLGINLAYAELYLALAALFRR 395
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 260-443 1.19e-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: 57.10  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  260 EQKRQKLSTVEKLDEHM-------------DFASQLIFAQ-NRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEH 325
Cdd:cd11080 144 EARAHGLRCAEQLSQYLlpvieerrvnpgsDLISILCTAEyEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNN 223

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  326 PtveeemmREIETVVGDRdiqsddmpnlKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE 405
Cdd:cd11080 224 P-------EQLAAVRADR----------SLVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDP 286

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 3913375  406 F-FPKPNEFSLeNFEKNVPSRYFQP------FGFGPRSCVGKFIA 443
Cdd:cd11080 287 AaFEDPDTFNI-HREDLGIRSAFSGaadhlaFGSGRHFCVGAALA 330
PLN00168 PLN00168
Cytochrome P450; Provisional
 294-456 1.20e-08

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 57.27  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   294 ENVNQCVlEMMIAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGD-------RDIQsdDMPNLKIVenfIYESMRY 366
Cdd:PLN00168 306 EIVNLCS-EFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDdqeevseEDVH--KMPYLKAV---VLEGLRK 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   367 QPVVDLIM-RKALQDDVIDGYPVKKGTNIILNIGRMHKLEF-FPKPNEFSLENFEKN--------VPSRYFQ--PFGFGP 434
Cdd:PLN00168 380 HPPAHFVLpHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEReWERPMEFVPERFLAGgdgegvdvTGSREIRmmPFGVGR 459

                        170       180
                 ....*....|....*....|..
gi 3913375   435 RSCVGKFIAMVMMKAILVTLLR 456
Cdd:PLN00168 460 RICAGLGIAMLHLEYFVANMVR 481
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 133-458 2.51e-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: 56.11  E-value: 2.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  133 IFNNNPAHWKeIRPFFTKALSGPGLvRMIAICVESTTEHLDRL--QEVTTELGNINALNLmrRIMLDTSNKLFLGVPLDE 210
Cdd:cd11071  72 LDTSEPKHAK-LKAFLFELLKSRSS-RFIPEFRSALSELFDKWeaELAKKGKASFNDDLE--KLAFDFLFRLLFGADPSE 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  211 NAIVLKIQNYFDAWQALLLKPDI-------------------FFKISWLCKKYKDAVKDlkgameilieqkrqklSTVEK 271
Cdd:cd11071 148 TKLGSDGPDALDKWLALQLAPTLslglpkileelllhtfplpFFLVKPDYQKLYKFFAN----------------AGLEV 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  272 LDEhmdfasqlifAQNRGDLTAENVNQCVLEMMIAApdTLSVTLFFMLIL--IAEHPT-VEEEMMREIETVVGDRDIQS- 347
Cdd:cd11071 212 LDE----------AEKLGLSREEAVHNLLFMLGFNA--FGGFSALLPSLLarLGLAGEeLHARLAEEIRSALGSEGGLTl 279

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  348 DDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVI---DG-YPVKKGTNIILNIGRMHK-LEFFPKPNEFslenfeknV 422
Cdd:cd11071 280 AALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIeshDAsYKIKKGELLVGYQPLATRdPKVFDNPDEF--------V 351

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 3913375  423 PSRYFQPFGF---------GP---------RSCVGKFIAMVMMKAILVTLLRRC 458
Cdd:cd11071 352 PDRFMGEEGKllkhliwsnGPeteeptpdnKQCPGKDLVVLLARLFVAELFLRY 405
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 247-439 2.63e-08

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 56.29  E-value: 2.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   247 AVKDLKGAMEILIEQKRQKL-STVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEH 325
Cdd:PLN03141 202 AKKRMVKLVKKIIEEKRRAMkNKEEDETGIPKDVVDVLLRDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDC 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   326 PT-----VEEEM-MREIETVVGDrDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIG 399
Cdd:PLN03141 282 PValqqlTEENMkLKRLKADTGE-PLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFR 360

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 3913375   400 RMH-KLEFFPKPNEFSLENF-EKNVPSRYFQPFGFGPRSCVG 439
Cdd:PLN03141 361 SVHlDEENYDNPYQFNPWRWqEKDMNNSSFTPFGGGQRLCPG 402
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 204-457 1.23e-07

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: 53.91  E-value: 1.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  204 LGVPLDENAIVLkiqnyfdAWQAlllkpDIFFKISWLCKKYKD----AVKDLKGAMEILIEQKRqklstVEKLDehmDFA 279
Cdd:cd11038 138 LGLPEEDWPRVH-------RWSA-----DLGLAFGLEVKDHLPrieaAVEELYDYADALIEARR-----AEPGD---DLI 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  280 SQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAEHPTvEEEMMREietvvgdrdiqsddmpNLKIVEN 358
Cdd:cd11038 198 STLVAAEQDGDrLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALRE----------------DPELAPA 260

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  359 FIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKleffpKPNEFSLENFEknVPSRYFQPFGF--GPRS 436
Cdd:cd11038 261 AVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANR-----DPRVFDADRFD--ITAKRAPHLGFggGVHH 333

                       250       260
                ....*....|....*....|.
gi 3913375  437 CVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11038 334 CLGAFLARAELAEALTVLARR 354
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 255-457 1.93e-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: 53.30  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  255 MEILIEQKRQKLSTvekldehmDFASQLIFAQNR-GDLT-AENVNQCVLeMMIAAPDT------LSVTLFFmliliaEHP 326
Cdd:cd11030 175 LDELVARKRREPGD--------DLLSRLVAEHGApGELTdEELVGIAVL-LLVAGHETtanmiaLGTLALL------EHP 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  327 TVEEEMMREietvvgdrdiqsddmPNLkiVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRM-HKL 404
Cdd:cd11030 240 EQLAALRAD---------------PSL--VPGAVEELLRYLSIVQDgLPRVATEDVEIGGVTIRAGEGVIVSLPAAnRDP 302

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3913375  405 EFFPKPNEFSLENfeknvPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11030 303 AVFPDPDRLDITR-----PARRHLAFGHGVHQCLGQNLARLELEIALPTLFRR 350
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 241-457 2.36e-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: 2.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  241 CKKYKDAVKDLKGAMEIL---IEQKRQKLstVEKldehmDFASQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLF 316
Cdd:cd20630 152 PEELETAAPDVTEGLALIeevIAERRQAP--VED-----DLLTTLLRAEEDGErLSEDELMALVAALIVAGTDTTVHLIT 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  317 FMLILIAEHPTVEEEMMREIETVvgdrdiqsddmpnlkivENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNII 395
Cdd:cd20630 225 FAVYNLLKHPEALRKVKAEPELL-----------------RNALEEVLRWDNFGKMgTARYATEDVELCGVTIRKGQMVL 287

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3913375  396 LNIG-RMHKLEFFPKPNEFSlenfeknvPSRYFQP---FGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20630 288 LLLPsALRDEKVFSDPDRFD--------VRRDPNAniaFGYGPHFCIGAALARLELELAVSTLLRR 345
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 204-457 5.32e-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: 51.83  E-value: 5.32e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  204 LGVPLDENAivlkiqnYFDAW-QALLLKPDIFFKISWLCKKYKDAVKDLKGAMEILIEQKRQKLSTvekldehmDFASQL 282
Cdd:cd11032 120 LGVPAEDRE-------LFKKWsDALVSGLGDDSFEEEEVEEMAEALRELNAYLLEHLEERRRNPRD--------DLISRL 184

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  283 IFAQNRGD-LT-AENVNQCVLeMMIAAPDTLSVTLFFMLILIAEHPTVEEEmmreietVVGDRDiqsdDMPNlkivenFI 360
Cdd:cd11032 185 VEAEVDGErLTdEEIVGFAIL-LLIAGHETTTNLLGNAVLCLDEDPEVAAR-------LRADPS----LIPG------AI 246

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  361 YESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRM-HKLEFFPKPNEFslenfeknVPSRyfQP-----FGFGP 434
Cdd:cd11032 247 EEVLRYRPPVQRTARVTTEDVELGGVTIPAGQLVIAWLASAnRDERQFEDPDTF--------DIDR--NPnphlsFGHGI 316

                       250       260
                ....*....|....*....|...
gi 3913375  435 RSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11032 317 HFCLGAPLARLEARIALEALLDR 339
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 310-459 1.66e-06

cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 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: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 50.22  E-value: 1.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  310 TLSVTLF--FMLILIAEHPTVEEemmreietvvgdrDIQSDDmpnLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYP 387
Cdd:cd11067 233 TVAVARFvtFAALALHEHPEWRE-------------RLRSGD---EDYAEAFVQEVRRFYPFFPFVGARARRDFEWQGYR 296

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3913375  388 VKKGTNIILNI-GRMHKLEFFPKPNEFSLENFEKNVPSRY-FQPFGFGPRS----CVGKFIAMVMMKAILVTLLRRCR 459
Cdd:cd11067 297 FPKGQRVLLDLyGTNHDPRLWEDPDRFRPERFLGWEGDPFdFIPQGGGDHAtghrCPGEWITIALMKEALRLLARRDY 374
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 246-457 9.53e-06

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: 47.95  E-value: 9.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  246 DAVKDLKGAMEILIEQKRQklstveklDEHMDFASQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLFFMLILIAE 324
Cdd:cd11031 164 AARQELRGYMAELVAARRA--------EPGDDLLSALVAARDDDDrLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLR 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  325 HPtveeEMMREIetvVGDRDIqsddMPNlkIVEnfiyESMRYQPV--VDLIMRKALQDDVIDGYPVKKGTNIILNIGRM- 401
Cdd:cd11031 236 HP----EQLARL---RADPEL----VPA--AVE----ELLRYIPLgaGGGFPRYATEDVELGGVTIRAGEAVLVSLNAAn 298

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3913375  402 HKLEFFPKPNEFSLENFEKnvpsryfqP---FGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11031 299 RDPEVFPDPDRLDLDREPN--------PhlaFGHGPHHCLGAPLARLELQVALGALLRR 349
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 244-443 1.08e-05

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 47.79  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   244 YKDAVKDLKGAMEIL--IEQKRQKLSTVEKLDEHMDFASQLIFAQNRG--DLTAENVNQCVLEMMIAAPDTLSVTLFFML 319
Cdd:PLN02302 232 YHRALKARKKLVALFqsIVDERRNSRKQNISPRKKDMLDLLLDAEDENgrKLDDEEIIDLLLMYLNAGHESSGHLTMWAT 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   320 ILIAEHPTV-------EEEMMREIEtvVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGT 392
Cdd:PLN02302 312 IFLQEHPEVlqkakaeQEEIAKKRP--PGQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGW 389

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 3913375   393 NIILNIGRMH-KLEFFPKPNEFSLENFEKNVPSRY-FQPFGFGPRSCVGKFIA 443
Cdd:PLN02302 390 KVLAWFRQVHmDPEVYPNPKEFDPSRWDNYTPKAGtFLPFGLGSRLCPGNDLA 442
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
 360-473 1.24e-05

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: 47.43  E-value: 1.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  360 IYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFsleNFEKNVPSRYFQPFGFGPRSCV 438
Cdd:cd20619 238 INEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRdPEVFDDPDVF---DHTRPPAASRNLSFGLGPHSCA 314

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 3913375  439 GKFIAMVMMKAILVTLLRRC-RVQTMKGRGLNNIQK 473
Cdd:cd20619 315 GQIISRAEATTVFAVLAERYeRIELAEEPTVAHNDF 350
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 328-498 2.67e-05

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: 46.35  E-value: 2.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  328 VEEEMMREIETVVGDRDIQSDDMPNLKIVENFIYESMRYQPVVDLIMRkaLQD--DVIDGYPVKKGTNIILNIGRM-HKL 404
Cdd:cd20627 235 VQKKLYKEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSAR--LQEleGKVDQHIIPKETLVLYALGVVlQDN 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  405 EFFPKPNEFSLENFEKNVPSRYFQPFGF-GPRSCVGKFIAMVMMKAILVTLLRRcrvqtmkgrglnniqknndLSMHPIE 483
Cdd:cd20627 313 TTWPLPYRFDPDRFDDESVMKSFSLLGFsGSQECPELRFAYMVATVLLSVLVRK-------------------LRLLPVD 373

                       170
                ....*....|....*...
gi 3913375  484 RQPL---LEMVFTPRRNA 498
Cdd:cd20627 374 GQVMetkYELVTSPREEA 391
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 349-457 3.32e-04

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: 42.86  E-value: 3.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  349 DMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENfeknvPSRYF 427
Cdd:cd11036 214 LRPDPELAAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRdPEAFPDPDRFDLGR-----PTARS 288

                        90       100       110
                ....*....|....*....|....*....|
gi 3913375  428 QPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd11036 289 AHFGLGRHACLGAALARAAAAAALRALAAR 318
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 79-455 6.76e-04

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: 41.98  E-value: 6.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375   79 KTYGDFVRVWISGEETFIISKSSSVSHVMKHWHYV--SRFGSKLGLQCIGMYEngiiFNNNPAH-WKEIRPFFTKALSGP 155
Cdd:cd20631   7 KKYGHIFTCKIAGKYVHFITDPFSYHSVIRHGKHLdwKKFHFATSAKAFGHVS----FDPSDGNtTENIHDTFIKTLQGS 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  156 GLVRMIaicvESTTEHL------DRLQEVTTELGNINAL-NLMRRIMLDTSNKLFLGVPLDENAIV--------LKIQNY 220
Cdd:cd20631  83 ALDSLT----ESMMENLqyvmlqDKSSSSSTKAWVTEGLySFCYRVMFEAGYLTLFGKELTAREDKnarleaqrALILNA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  221 FDAWQALLLK-PDIFFKISW-LCKKYKDAVKDLKGAMEILIEQKRQKLSTVEKLDEHM-DFASQLifaqnrGDLTAENVN 297
Cdd:cd20631 159 LENFKEFDKVfPALVAGLPIhMFKTAKSAREALAERLLHENLQKRENISELISLRMLLnDTLSTL------DEMEKARTH 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  298 qcvLEMMIAA-PDTLSVTlFFMLILIAEHPTVEEEMMREIETVVGD-----RDIQS---------DDMPNLKIVenfIYE 362
Cdd:cd20631 233 ---VAMLWASqANTLPAT-FWSLFYLLRCPEAMKAATKEVKRTLEKtgqkvSDGGNpivltreqlDDMPVLGSI---IKE 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  363 SMRYQPVvDLIMRKALQD-----DVIDGYPVKKGTNIILNIGRMH-KLEFFPKPNEFSLENF------EKNVPSR----- 425
Cdd:cd20631 306 ALRLSSA-SLNIRVAKEDftlhlDSGESYAIRKDDIIALYPQLLHlDPEIYEDPLTFKYDRYldengkEKTTFYKngrkl 384

                       410       420       430
                ....*....|....*....|....*....|..
gi 3913375  426 --YFQPFGFGPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd20631 385 kyYYMPFGSGTSKCPGRFFAINEIKQFLSLML 416
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 294-455 1.09e-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: 41.33  E-value: 1.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  294 ENVNQCVLEMMIAAPDTLSVTLFFMLILIA--------------------EHPTVEEEMMREietvvgdrdiqsdDMPNL 353
Cdd:cd11039 181 SNPNPSLLSVMLNAGMPMSLEQIRANIKVAiggglneprdaiagtcwgllSNPEQLAEVMAG-------------DVHWL 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  354 KIVEnfiyESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLenFEKNVPSryfQPFGF 432
Cdd:cd11039 248 RAFE----EGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEaRFENPDRFDV--FRPKSPH---VSFGA 318

                       170       180
                ....*....|....*....|...
gi 3913375  433 GPRSCVGKFIAMVMMKAILVTLL 455
Cdd:cd11039 319 GPHFCAGAWASRQMVGEIALPEL 341
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 305-457 1.44e-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: 40.91  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3913375  305 IAAPDTLSVTLFFMLILIAEHPTVEEEMMREIETVVGDRDiqsddMPNLKIVenfIYESMRYQPVVDLIMRKALQDDVID 384
Cdd:cd20624 201 LFAFDAAGMALLRALALLAAHPEQAARAREEAAVPPGPLA-----RPYLRAC---VLDAVRLWPTTPAVLRESTEDTVWG 272

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3913375  385 GYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFEKN--VPSRYFQPFGFGPRSCVGKFIAMVMMKAILVTLLRR 457
Cdd:cd20624 273 GRTVPAGTGFLIFAPFFHRdDEALPFADRFVPEIWLDGraQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRR 348
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH