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Conserved domains on  [gi|15239310|ref|NP_198463|]
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cytochrome P450, family 716, subfamily A, polypeptide 2 [Arabidopsis thaliana]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

cytochrome P450 family protein may catalyze the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 65-311 1.46e-88

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.


The actual alignment was detected with superfamily member cd11043:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 408  Bit Score: 270.59  E-value: 1.46e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  65 RVRHFSSgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIF-PSSTQTSSKEEAIKTRMLLMPSMKPEAL 143
Cdd:cd11043   1 RIKRYGP-VFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRKLLgKSSLLTVSGEEHKRLRGLLLSFLGPEAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 144 R-RYVGVMDEIAQKHFETeWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFN 222
Cdd:cd11043  80 KdRLLGDIDELVRQHLDS-WWRGKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRKEFQAFLEGLLSFPLNLPGTTFH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 223 RAIKASRLLSKEVSTIIRQRKEELKAGkvSVEQDILSHMLMNIGETK----DEDLADKIIALLIGGHDTTSIVCTFVVNY 298
Cdd:cd11043 159 RALKARKRIRKELKKIIEERRAELEKA--SPKGDLLDVLLEEKDEDGdsltDEEILDNILTLLFAGHETTSTTLTLAVKF 236

                       250
                ....*....|...
gi 15239310 299 LAEFPHIYQRVLE 311
Cdd:cd11043 237 LAENPKVLQELLE 249
 
Name Accession Description Interval E-value
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 65-311 1.46e-88

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: 270.59  E-value: 1.46e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  65 RVRHFSSgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIF-PSSTQTSSKEEAIKTRMLLMPSMKPEAL 143
Cdd:cd11043   1 RIKRYGP-VFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRKLLgKSSLLTVSGEEHKRLRGLLLSFLGPEAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 144 R-RYVGVMDEIAQKHFETeWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFN 222
Cdd:cd11043  80 KdRLLGDIDELVRQHLDS-WWRGKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRKEFQAFLEGLLSFPLNLPGTTFH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 223 RAIKASRLLSKEVSTIIRQRKEELKAGkvSVEQDILSHMLMNIGETK----DEDLADKIIALLIGGHDTTSIVCTFVVNY 298
Cdd:cd11043 159 RALKARKRIRKELKKIIEERRAELEKA--SPKGDLLDVLLEEKDEDGdsltDEEILDNILTLLFAGHETTSTTLTLAVKF 236

                       250
                ....*....|...
gi 15239310 299 LAEFPHIYQRVLE 311
Cdd:cd11043 237 LAENPKVLQELLE 249
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 31-311 1.36e-45

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 161.03  E-value: 1.36e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   31 PNLPPGKIGFPLIGETLSFLSAGRQGHPEKFVTDRVRHF-SSGIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWwPD 109
Cdd:PLN02302  41 PPLPPGDLGWPVIGNMWSFLRAFKSSNPDSFIASFISRYgRTGIYKAFMFGQPTVLVTTPEACKRVLTDDDAFEPGW-PE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  110 SVNK-IFPSSTQTSSKEEAIKTRMLLMPSMK-PEALRRYVGVMDEIAQKHFEtEWANQDQLIVFPLTKKFTFSIACRLFL 187
Cdd:PLN02302 120 STVElIGRKSFVGITGEEHKRLRRLTAAPVNgPEALSTYIPYIEENVKSCLE-KWSKMGEIEFLTELRKLTFKIIMYIFL 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  188 SMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKVSVEQDILShMLMNIGE 267
Cdd:PLN02302 199 SSESELVMEALEREYTTLNYGVRAMAINLPGFAYHRALKARKKLVALFQSIVDERRNSRKQNISPRKKDMLD-LLLDAED 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15239310  268 TKDEDLADK-IIALLI----GGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:PLN02302 278 ENGRKLDDEeIIDLLLmylnAGHESSGHLTMWATIFLQEHPEVLQKAKA 326
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 73-312 4.55e-20

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: 89.57  E-value: 4.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  73 IFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSV---NKIFPSSTQTSSKEEAIKTRMLLMPSMKPEALRRYVGV 149
Cdd:COG2124  34 VFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVlrpLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPR 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 150 MDEIAQKHFEtEWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERvrkleEPFTTVMTGVFSIPIDLPGTRFNRAIKASR 229
Cdd:COG2124 114 IREIADELLD-RLAARGPVDLVEEFARPLPVIVICELLGVPEEDR-----DRLRRWSDALLDALGPLPPERRRRARRARA 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 230 LLSKEVSTIIRQRKEELKagkvsveQDILShMLMNIGETK----DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHI 305
Cdd:COG2124 188 ELDAYLRELIAERRAEPG-------DDLLS-ALLAARDDGerlsDEELRDELLLLLLAGHETTANALAWALYALLRHPEQ 259


                ....*..
gi 15239310 306 YQRVLEG 312
Cdd:COG2124 260 LARLRAE 266
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 34-311 4.90e-11

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: 63.07  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310    34 PPGKIGFPLIGetlSFLSAGRQGHPEKFVTDrVRHFSSGIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNK 113
Cdd:pfam00067   1 PPGPPPLPLFG---NLLQLGRKGNLHSVFTK-LQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   114 IFPSSTQT-----SSKEEAIKTRMLLMPSMKPEALRRYVGVMDEIAQKHFET--EWANQDQLI-VFPLTKKFTFSIACRL 185
Cdd:pfam00067  77 TSRGPFLGkgivfANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKlrKTAGEPGVIdITDLLFRAALNVICSI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   186 FLSM--------DDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFN------RAIKASRLLSKEVSTIIRQRKEELKAGKV 251
Cdd:pfam00067 157 LFGErfgsledpKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFpgphgrKLKRARKKIKDLLDKLIEERRETLDSAKK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239310   252 SvEQDILSHML---MNIGETK--DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:pfam00067 237 S-PRDFLDALLlakEEEDGSKltDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLRE 300
 
Name Accession Description Interval E-value
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 65-311 1.46e-88

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: 270.59  E-value: 1.46e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  65 RVRHFSSgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIF-PSSTQTSSKEEAIKTRMLLMPSMKPEAL 143
Cdd:cd11043   1 RIKRYGP-VFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRKLLgKSSLLTVSGEEHKRLRGLLLSFLGPEAL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 144 R-RYVGVMDEIAQKHFETeWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFN 222
Cdd:cd11043  80 KdRLLGDIDELVRQHLDS-WWRGKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRKEFQAFLEGLLSFPLNLPGTTFH 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 223 RAIKASRLLSKEVSTIIRQRKEELKAGkvSVEQDILSHMLMNIGETK----DEDLADKIIALLIGGHDTTSIVCTFVVNY 298
Cdd:cd11043 159 RALKARKRIRKELKKIIEERRAELEKA--SPKGDLLDVLLEEKDEDGdsltDEEILDNILTLLFAGHETTSTTLTLAVKF 236

                       250
                ....*....|...
gi 15239310 299 LAEFPHIYQRVLE 311
Cdd:cd11043 237 LAENPKVLQELLE 249
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 44-309 2.43e-64

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: 208.68  E-value: 2.43e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  44 GETLSFLsagRQghPEKFVTDRVRHFSSgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIF-PSSTQTS 122
Cdd:cd11044   1 GETLEFL---RD--PEDFIQSRYQKYGP-VFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRYGWPRSVRRLLgENSLSLQ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 123 SKEEAIKTRMLLMPSMKPEALRRYVGVMDEIAQKHFETeWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPF 202
Cdd:cd11044  75 DGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRK-WLKAGEVALYPELRRLTFDVAARLLLGLDPEVEAEALSQDF 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 203 TTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKvsveQDILSHMLmnigETKDED--------LA 274
Cdd:cd11044 154 ETWTDGLFSLPVPLPFTPFGRAIRARNKLLARLEQAIRERQEEENAEA----KDALGLLL----EAKDEDgeplsmdeLK 225

                       250       260       270
                ....*....|....*....|....*....|....*
gi 15239310 275 DKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:cd11044 226 DQALLLLFAGHETTASALTSLCFELAQHPDVLEKL 260
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 31-311 1.36e-45

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 161.03  E-value: 1.36e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   31 PNLPPGKIGFPLIGETLSFLSAGRQGHPEKFVTDRVRHF-SSGIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWwPD 109
Cdd:PLN02302  41 PPLPPGDLGWPVIGNMWSFLRAFKSSNPDSFIASFISRYgRTGIYKAFMFGQPTVLVTTPEACKRVLTDDDAFEPGW-PE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  110 SVNK-IFPSSTQTSSKEEAIKTRMLLMPSMK-PEALRRYVGVMDEIAQKHFEtEWANQDQLIVFPLTKKFTFSIACRLFL 187
Cdd:PLN02302 120 STVElIGRKSFVGITGEEHKRLRRLTAAPVNgPEALSTYIPYIEENVKSCLE-KWSKMGEIEFLTELRKLTFKIIMYIFL 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  188 SMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKVSVEQDILShMLMNIGE 267
Cdd:PLN02302 199 SSESELVMEALEREYTTLNYGVRAMAINLPGFAYHRALKARKKLVALFQSIVDERRNSRKQNISPRKKDMLD-LLLDAED 277

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 15239310  268 TKDEDLADK-IIALLI----GGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:PLN02302 278 ENGRKLDDEeIIDLLLmylnAGHESSGHLTMWATIFLQEHPEVLQKAKA 326
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 16-303 4.79e-43

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 153.98  E-value: 4.79e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   16 PLLFFLGKHLSNFRYPNLPPGKIGFPLIGETLSFLSAGRQGHPEKFVTDRVRHFSSgIFKTHLFGSPFAVVTGASGNKFL 95
Cdd:PLN02987  14 AAIFFLLLRRTRYRRMRLPPGSLGLPLVGETLQLISAYKTENPEPFIDERVARYGS-LFMTHLFGEPTVFSADPETNRFI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   96 FTNENKLVISWWPDSVNKIFPSSTQTSSKEEAIKtRM--LLMPSMKPEALRRYVGV-MDEIAQKHFETeWAnqDQLIVFP 172
Cdd:PLN02987  93 LQNEGKLFECSYPGSISNLLGKHSLLLMKGNLHK-KMhsLTMSFANSSIIKDHLLLdIDRLIRFNLDS-WS--SRVLLME 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  173 LTKKFTFSIACRLFLSMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKvS 252
Cdd:PLN02987 169 EAKKITFELTVKQLMSFDPGEWTESLRKEYVLVIEGFFSVPLPLFSTTYRRAIQARTKVAEALTLVVMKRRKEEEEGA-E 247

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15239310  253 VEQDILSHMLMNIGETKDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFP 303
Cdd:PLN02987 248 KKKDMLAALLASDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETP 298
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 31-315 1.10e-38

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 141.80  E-value: 1.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   31 PNLPPGKIGFPLIGETLSFLSAGRQGHPEKFVTDRVRHFSSgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDS 110
Cdd:PLN03141   6 SRLPKGSLGWPVIGETLDFISCAYSSRPESFMDKRRSLYGK-VFKSHIFGTPTIVSTDAEVNKVVLQSDGNAFVPAYPKS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  111 VNKIFPSST------QTSSKEEAIKTRMLLMPSMKPEALR---RYVG-VMDEiaqkhfeteWANQDQLIVFPLTKKFTFS 180
Cdd:PLN03141  85 LTELMGKSSillingSLQRRVHGLIGAFLKSPHLKAQITRdmeRYVSeSLDS---------WRDDPPVLVQDETKKIAFE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  181 IACRLFLSMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKVSVEQ---DI 257
Cdd:PLN03141 156 VLVKALISLEPGEEMEFLKKEFQEFIKGLMSLPIKLPGTRLYRSLQAKKRMVKLVKKIIEEKRRAMKNKEEDETGipkDV 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  258 LSHMLMNIGETKDEDL-ADKIIALLIGGHDTTSIVCTFVVNYLAEFP-HIYQRVLEGMQI 315
Cdd:PLN03141 236 VDVLLRDGSDELTDDLiSDNMIDMMIPGEDSVPVLMTLAVKFLSDCPvALQQLTEENMKL 295
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 17-311 2.81e-34

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 130.06  E-value: 2.81e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   17 LLFFLGKHLSNFRYPN-----LPPGKIGFPLIGETLSFLSAgrqgHPEKFVTDRVRHFSSgIFKTHLFGSPFAVVTGASG 91
Cdd:PLN02196  15 LFLCLLRFLAGFRRSSstklpLPPGTMGWPYVGETFQLYSQ----DPNVFFASKQKRYGS-VFKTHVLGCPCVMISSPEA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   92 NKFLFTNENKLViswwpdsvNKIFPSSTQTSSKEEAI---------KTRMLLMPSMKPEALRRYVGVMDEIAQKHFETeW 162
Cdd:PLN02196  90 AKFVLVTKSHLF--------KPTFPASKERMLGKQAIffhqgdyhaKLRKLVLRAFMPDAIRNMVPDIESIAQESLNS-W 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  163 ANQdQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQR 242
Cdd:PLN02196 161 EGT-QINTYQEMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKGYNSMPINLPGTLFHKSMKARKELAQILAKILSKR 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239310  243 KEelkagKVSVEQDILSHMLMNIGETKDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:PLN02196 240 RQ-----NGSSHNDLLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTE 303
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 44-314 1.49e-29

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: 116.84  E-value: 1.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  44 GETLSFLSAGRqghpeKFVTDRVRHFSSgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIFPSSTQTSS 123
Cdd:cd20638   1 GETLQMVLQRR-----KFLQMKRQKYGY-IYKTHLFGRPTVRVMGAENVRQILLGEHKLVSVQWPASVRTILGSGCLSNL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 124 KEEAIKTR-MLLMPSMKPEALRRYVGVMDEIAQKHFEtEWANQDQ-LIVFPLTKKFTFSIACRLFLSMD----DLERVRK 197
Cdd:cd20638  75 HDSQHKHRkKVIMRAFSREALENYVPVIQEEVRSSVN-QWLQSGPcVLVYPEVKRLMFRIAMRILLGFEpqqtDREQEQQ 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 198 LEEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQR--KEELKAGKVSVEQDILSHMLMNIGETKDEDLAD 275
Cdd:cd20638 154 LVEAFEEMIRNLFSLPIDVPFSGLYRGLRARNLIHAKIEENIRAKiqREDTEQQCKDALQLLIEHSRRNGEPLNLQALKE 233

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15239310 276 KIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLEGMQ 314
Cdd:cd20638 234 SATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQ 272
PLN02500 PLN02500
cytochrome P450 90B1
 17-311 6.71e-28

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 112.65  E-value: 6.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   17 LLFFLGKHLSNFRYPNLPPGKIGFPLIGETLSFLSAGRQGHPEKFVTDRVRHFSSgIFKTHLFGSPFAVVTGASGNKFLF 96
Cdd:PLN02500  23 LVFILTKRRPKQKRFNLPPGNMGWPFLGETIGYLKPYSATSIGEFMEQHISRYGK-IYRSNLFGEPTIVSADAGLNRFIL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   97 TNENKLVISWWPDSVNKIFPSST------QTSSKEEAIKTRML----LMPSMKPEALRRYVGVMDEIAQkhfETEWANQD 166
Cdd:PLN02500 102 QNEGRLFECSYPRSIGGILGKWSmlvlvgDMHRDMRSISLNFLsharLRTHLLKEVERHTLLVLDSWKE---NSTFSAQD 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  167 QlivfplTKKFTFSIACRLFLSMD-DLERVRKLEEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEE 245
Cdd:PLN02500 179 E------AKKFTFNLMAKHIMSMDpGEEETEQLKKEYVTFMKGVVSAPLNFPGTAYRKALKSRATILKFIERKMEERIEK 252

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15239310  246 LKAGKVSVEQDILSHMLMNIGETKDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:PLN02500 253 LKEEDESVEEDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELRE 318
PLN02774 PLN02774
brassinosteroid-6-oxidase
 28-309 1.35e-26

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 108.71  E-value: 1.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   28 FRYPNLPPGKIGFPLIGETLSFLSAGrqghPEKFVTDRVRHFSsgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWW 107
Cdd:PLN02774  27 YSKKGLPPGTMGWPLFGETTEFLKQG----PDFMKNQRLRYGS--FFKSHILGCPTIVSMDPELNRYILMNEGKGLVPGY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  108 PDSVNKIFPS---STQTSSKEEAIKTRMLLM--PSMKPEALRRYVgvmDEIAQKHFeTEWANQDQLIVFPLTKKFTFSIA 182
Cdd:PLN02774 101 PQSMLDILGTcniAAVHGSTHRYMRGSLLSLisPTMIRDHLLPKI---DEFMRSHL-SGWDGLKTIDIQEKTKEMALLSA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  183 CRLFLSMDDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFNRAIKAsrllSKEVSTIIRQRKEELKAGKVsVEQDILSHmL 262
Cdd:PLN02774 177 LKQIAGTLSKPISEEFKTEFFKLVLGTLSLPIDLPGTNYRSGVQA----RKNIVRMLRQLIQERRASGE-THTDMLGY-L 250

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15239310  263 MNIGETK----DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:PLN02774 251 MRKEGNRykltDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQEL 301
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 60-314 5.35e-25

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: 103.55  E-value: 5.35e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  60 KFVTDRVRHFSSgIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISW--WPDSVNKIFPSSTQTSSKEEAIKTRMLLMPS 137
Cdd:cd11045   1 EFARQRYRRYGP-VSWTGMLGLRVVALLGPDANQLVLRNRDKAFSSKqgWDPVIGPFFHRGLMLLDFDEHRAHRRIMQQA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 138 MKPEALRRYVGVMDEIAQKHFeTEWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPF-TTVMTGVFSIPIDL 216
Cdd:cd11045  80 FTRSALAGYLDRMTPGIERAL-ARWPTGAGFQFYPAIKELTLDLATRVFLGVDLGPEADKVNKAFiDTVRASTAIIRTPI 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 217 PGTRFNRAIKASRLLSKEVSTIIRQRKEelKAGkvsveQDILSHMLMNIGET----KDEDLADKIIALLIGGHDTTSIVC 292
Cdd:cd11045 159 PGTRWWRGLRGRRYLEEYFRRRIPERRA--GGG-----DDLFSALCRAEDEDgdrfSDDDIVNHMIFLMMAAHDTTTSTL 231

                       250       260
                ....*....|....*....|..
gi 15239310 293 TFVVNYLAEFPHIYQRVLEGMQ 314
Cdd:cd11045 232 TSMAYFLARHPEWQERLREESL 253
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 73-311 5.28e-24

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: 100.67  E-value: 5.28e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  73 IFKTHLFGSPFAVVTGASGNKFLFTNE--NKLVISWWPDSVNKIFPSSTQTSSKEEAIKTRMLLMPSMKPEALRRYVGVM 150
Cdd:cd00302   3 VFRVRLGGGPVVVVSDPELVREVLRDPrdFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 151 DEIAQKHFETEWAN-QDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTTVMTGVFSIPI-DLPGTRFNRAIKAS 228
Cdd:cd00302  83 REIARELLDRLAAGgEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRLLrPLPSPRLRRLRRAR 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 229 RLLSKEVSTIIRQRKEELKAGkvsvEQDILSHMLMNIGETKDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQR 308
Cdd:cd00302 163 ARLRDYLEELIARRRAEPADD----LDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPEVQER 238


                ...
gi 15239310 309 VLE 311
Cdd:cd00302 239 LRA 241
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 43-309 1.67e-23

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: 99.91  E-value: 1.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  43 IGETLSFLSAGRQGHPEKfvtdRVRHfsSGIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIFPSSTQTS 122
Cdd:cd20636   1 FGETLHWLVQGSSFHSSR----REKY--GNVFKTHLLGRPVIRVTGAENIRKILLGEHTLVSTQWPQSTRILLGSNTLLN 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 123 SKEEAIKT-RMLLMPSMKPEALRRYVGVMDEIAQKHFETEWANQDQLIVFPLTKKFTFSIACRLFLSMD-DLERVRKLEE 200
Cdd:cd20636  75 SVGELHRQrRKVLARVFSRAALESYLPRIQDVVRSEVRGWCRGPGPVAVYTAAKSLTFRIAVRILLGLRlEEQQFTYLAK 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 201 PFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRqrkEELKAGKVSVEQDILSHMLMNIGETKDE----DLADK 276
Cdd:cd20636 155 TFEQLVENLFSLPLDVPFSGLRKGIKARDILHEYMEKAIE---EKLQRQQAAEYCDALDYMIHSARENGKEltmqELKES 231

                       250       260       270
                ....*....|....*....|....*....|...
gi 15239310 277 IIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:cd20636 232 AVELIFAAFSTTASASTSLVLLLLQHPSAIEKI 264
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 73-311 5.11e-23

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: 98.04  E-value: 5.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  73 IFKTHLFGS-PFAVVTGASGNKFLFTNENKLvisWWPDSVNKIF-----PSSTQTSSKEEAIKTRMLLMPSMKPEALRRY 146
Cdd:cd11053  14 VFTLRVPGLgPVVVLSDPEAIKQIFTADPDV---LHPGEGNSLLepllgPNSLLLLDGDRHRRRRKLLMPAFHGERLRAY 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 147 VGVMDEIAQKHFETeWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTTvMTGVFSIPI---------DLP 217
Cdd:cd11053  91 GELIAEITEREIDR-WPPGQPFDLRELMQEITLEVILRVVFGVDDGERLQELRRLLPR-LLDLLSSPLasfpalqrdLGP 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 218 GTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKvsveQDILShMLMnigETKDED--------LADKIIALLIGGHDTTS 289
Cdd:cd11053 169 WSPWGRFLRARRRIDALIYAEIAERRAEPDAER----DDILS-LLL---SARDEDgqplsdeeLRDELMTLLFAGHETTA 240

                       250       260
                ....*....|....*....|..
gi 15239310 290 IVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11053 241 TALAWAFYWLHRHPEVLARLLA 262
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 73-312 4.55e-20

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: 89.57  E-value: 4.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  73 IFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSV---NKIFPSSTQTSSKEEAIKTRMLLMPSMKPEALRRYVGV 149
Cdd:COG2124  34 VFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVlrpLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPR 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 150 MDEIAQKHFEtEWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERvrkleEPFTTVMTGVFSIPIDLPGTRFNRAIKASR 229
Cdd:COG2124 114 IREIADELLD-RLAARGPVDLVEEFARPLPVIVICELLGVPEEDR-----DRLRRWSDALLDALGPLPPERRRRARRARA 187

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 230 LLSKEVSTIIRQRKEELKagkvsveQDILShMLMNIGETK----DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHI 305
Cdd:COG2124 188 ELDAYLRELIAERRAEPG-------DDLLS-ALLAARDDGerlsDEELRDELLLLLLAGHETTANALAWALYALLRHPEQ 259


                ....*..
gi 15239310 306 YQRVLEG 312
Cdd:COG2124 260 LARLRAE 266
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 44-311 9.95e-20

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: 89.14  E-value: 9.95e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  44 GETLSFLSAGRQGHPEKfvtdrvRHFSSGIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIF-PSSTQTS 122
Cdd:cd20637   1 GETFHWLLQGSGFQSSR------REKYGNVFKTHLLGRPLIRVTGAENVRKILMGEHSLVSTEWPRSTRMLLgPNSLVNS 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 123 SKEEAIKTRMLLMPSMKPEALRRYVGVMDEIAQKHFETEWANQDQLIVFPLTKKFTFSIACRLFLSMD-DLERVRKLEEP 201
Cdd:cd20637  75 IGDIHRHKRKVFSKLFSHEALESYLPKIQQVIQDTLRVWSSNPEPINVYQEAQKLTFRMAIRVLLGFRvSEEELSHLFSV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 202 FTTVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKVSVEQDILSHMLMNIG-ETKDEDLADKIIAL 280
Cdd:cd20637 155 FQQFVENVFSLPLDLPFSGYRRGIRARDSLQKSLEKAIREKLQGTQGKDYADALDILIESAKEHGkELTMQELKDSTIEL 234

                       250       260       270
                ....*....|....*....|....*....|.
gi 15239310 281 LIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd20637 235 IFAAFATTASASTSLIMQLLKHPGVLEKLRE 265
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 73-311 2.78e-16

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: 78.80  E-value: 2.78e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  73 IFKTHLFGSPFAVVTGASGNKFLFtNENKLVISW---WPDSVNKIFPSSTQTSSKEEAIKTRMLLMPSMKPEALRRYVGV 149
Cdd:cd11042   8 VFTFNLLGKKVTVLLGPEANEFFF-NGKDEDLSAeevYGFLTPPFGGGVVYYAPFAEQKEQLKFGLNILRRGKLRGYVPL 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 150 MDEIAQKHFETeWANQDQLIVFPLTKKFTFSIACRLFL------SMDD--LERVRKLEEPFTTVMtgVFSIPIDLPgtRF 221
Cdd:cd11042  87 IVEEVEKYFAK-WGESGEVDLFEEMSELTILTASRCLLgkevreLLDDefAQLYHDLDGGFTPIA--FFFPPLPLP--SF 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 222 NRAIKASRLLSKEVSTIIRQRKEElkagKVSVEQDILShMLMN----IGE-TKDEDLADKIIALLIGGHDTTSIVCTFVV 296
Cdd:cd11042 162 RRRDRARAKLKEIFSEIIQKRRKS----PDKDEDDMLQ-TLMDakykDGRpLTDDEIAGLLIALLFAGQHTSSATSAWTG 236

                       250
                ....*....|....*
gi 15239310 297 NYLAEFPHIYQRVLE 311
Cdd:cd11042 237 LELLRNPEHLEALRE 251
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 129-311 2.03e-13

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: 70.24  E-value: 2.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 129 KTRMLLMPSMKPEALRRYVGVMDEIAQ---KHFETEwANQDQLIVFPLTKKFTFSIACRL-------FLSMDDLERVRKL 198
Cdd:cd20628  59 KRRKLLTPAFHFKILESFVEVFNENSKilvEKLKKK-AGGGEFDIFPYISLCTLDIICETamgvklnAQSNEDSEYVKAV 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 199 EEPFTTVMTGVFSIPIDLP--------GTRFNRAIKasrLLSKEVSTIIRQRKEELKAGKVSVEQ-------------DI 257
Cdd:cd20628 138 KRILEIILKRIFSPWLRFDfifrltslGKEQRKALK---VLHDFTNKVIKERREELKAEKRNSEEddefgkkkrkaflDL 214

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15239310 258 LSHMLMNIGETKDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd20628 215 LLEAHEDGGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYE 268
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 131-311 1.17e-12

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: 67.99  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 131 RMLLMPSMKPEALRRYVGVMDEIAQKHFEtEWANQDQLIVFPLTKKF---TFSIACRLFLSMDDLERVRKLEEPFTTVM- 206
Cdd:cd20620  62 RRLAQPAFHRRRIAAYADAMVEATAALLD-RWEAGARRGPVDVHAEMmrlTLRIVAKTLFGTDVEGEADEIGDALDVALe 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 207 --TGVFSIPIDLPG---TRFNRAI-KASRLLSKEVSTIIRQRKEELKAGKvsveqDILShMLMNigETKDED-------- 272
Cdd:cd20620 141 yaARRMLSPFLLPLwlpTPANRRFrRARRRLDEVIYRLIAERRAAPADGG-----DLLS-MLLA--ARDEETgepmsdqq 212

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15239310 273 LADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd20620 213 LRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRA 251
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 129-311 5.88e-12

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: 65.93  E-value: 5.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 129 KTRMLLMPSMKPEAL-RRYVG--VMDEIAQKhfETEWANQDQLIVFPLTKKFTFSIACRLF-LSMDDLER-VRKLEEpft 203
Cdd:cd20614  68 RARAASNPSFTPKGLsAAGVGalIAEVIEAR--IRAWLSRGDVAVLPETRDLTLEVIFRILgVPTDDLPEwRRQYRE--- 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 204 tVMTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRqrkeELKAGKvsvEQDILSHMLMNIGETKDE-----DLADKII 278
Cdd:cd20614 143 -LFLGVLPPPVDLPGMPARRSRRARAWIDARLSQLVA----TARANG---ARTGLVAALIRARDDNGAglseqELVDNLR 214

                       170       180       190
                ....*....|....*....|....*....|...
gi 15239310 279 ALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd20614 215 LLVLAGHETTASIMAWMVIMLAEHPAVWDALCD 247
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 34-311 4.90e-11

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: 63.07  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310    34 PPGKIGFPLIGetlSFLSAGRQGHPEKFVTDrVRHFSSGIFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNK 113
Cdd:pfam00067   1 PPGPPPLPLFG---NLLQLGRKGNLHSVFTK-LQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   114 IFPSSTQT-----SSKEEAIKTRMLLMPSMKPEALRRYVGVMDEIAQKHFET--EWANQDQLI-VFPLTKKFTFSIACRL 185
Cdd:pfam00067  77 TSRGPFLGkgivfANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKlrKTAGEPGVIdITDLLFRAALNVICSI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310   186 FLSM--------DDLERVRKLEEPFTTVMTGVFSIPIDLPGTRFN------RAIKASRLLSKEVSTIIRQRKEELKAGKV 251
Cdd:pfam00067 157 LFGErfgsledpKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFpgphgrKLKRARKKIKDLLDKLIEERRETLDSAKK 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15239310   252 SvEQDILSHML---MNIGETK--DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:pfam00067 237 S-PRDFLDALLlakEEEDGSKltDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLRE 300
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 131-309 5.46e-11

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: 63.06  E-value: 5.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 131 RMLLMPSMKPEALRRYVGVMDEIA-------QKHFETEWANQDQLIVFPLTKKFTFSIACRLFLSMDdLERVRKLEEPFT 203
Cdd:cd11069  65 RKILNPAFSYRHVKELYPIFWSKAeelvdklEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYD-FDSLENPDNELA 143

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 204 TVMTGVFSIPID------------------LPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGKVSVEQDILSHML--- 262
Cdd:cd11069 144 EAYRRLFEPTLLgsllfilllflprwlvriLPWKANREIRRAKDVLRRLAREIIREKKAALLEGKDDSGKDILSILLran 223

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15239310 263 MNIGETK--DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:cd11069 224 DFADDERlsDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERL 272
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 133-309 1.46e-09

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: 58.74  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 133 LLMPSMKPEALRRYVGVMDEIAQKHFeTEWA--NQDQLI-VFPLTKKFTF-SIA-C---RLFLSMDDLERvrkleEPFTT 204
Cdd:cd11068  78 ILMPAFGPLAMRGYFPMMLDIAEQLV-LKWErlGPDEPIdVPDDMTRLTLdTIAlCgfgYRFNSFYRDEP-----HPFVE 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 205 VMTGVFSIPID---LPGTRFNRAIKASR-------LLSKEVSTIIRQRKeelkAGKVSVEQDILSHMLMNI----GET-K 269
Cdd:cd11068 152 AMVRALTEAGRranRPPILNKLRRRAKRqfrediaLMRDLVDEIIAERR----ANPDGSPDDLLNLMLNGKdpetGEKlS 227

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15239310 270 DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:cd11068 228 DENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKA 267
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 222-311 1.55e-09

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: 58.68  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 222 NRAIKASRLLSKEVSTIIRQRKEELKAGKvSVEQDILSHMLMNIGETKD---EDLADKIIALLIGGHDTTSIVCTFVVNY 298
Cdd:cd20613 182 REVREAIKFLRETGRECIEERLEALKRGE-EVPNDILTHILKASEEEPDfdmEELLDDFVTFFIAGQETTANLLSFTLLE 260

                        90
                ....*....|...
gi 15239310 299 LAEFPHIYQRVLE 311
Cdd:cd20613 261 LGRHPEILKRLQA 273
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 73-311 1.43e-08

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: 55.72  E-value: 1.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  73 IFKTHLFGSPFAVVTGASGNKFLFTNENKLVISWWPDSVNKIFPSSTQTSSKEEAIKTRMLLMPSMKPEALRRYVGVMDE 152
Cdd:cd20621   5 IIVSNLGSKPLISLVDPEYIKEFLQNHHYYKKKFGPLGIDRLFGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINE 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 153 IAQKHFetewaNQDQLIVFP---LTKKFTFSIACRLFL--SMDDL---------ERVRKLEEPFTTVMTGVFSIP----- 213
Cdd:cd20621  85 ITKEKI-----KKLDNQNVNiiqFLQKITGEVVIRSFFgeEAKDLkingkeiqvELVEILIESFLYRFSSPYFQLkrlif 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 214 ----IDLPGTRFNRAI-KASRLLSKEVSTIIRQRKEELKAGKVSVEQDILSHMLMNIGETKD------EDLADKIIALLI 282
Cdd:cd20621 160 grksWKLFPTKKEKKLqKRVKELRQFIEKIIQNRIKQIKKNKDEIKDIIIDLDLYLLQKKKLeqeitkEEIIQQFITFFF 239

                       250       260
                ....*....|....*....|....*....
gi 15239310 283 GGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd20621 240 AGTDTTGHLVGMCLYYLAKYPEIQEKLRQ 268
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 131-311 3.14e-08

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: 54.56  E-value: 3.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 131 RMLLMPSMKPEALRRYVGVMDEIAQKHFeTEW-----ANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTTV 205
Cdd:cd11082  62 RKSLLPLFTRKALGLYLPIQERVIRKHL-AKWlenskSGDKPIEMRPLIRDLNLETSQTVFVGPYLDDEARRFRIDYNYF 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 206 MTGVFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEELKAGkvsvEQ-----DILSHMLMN------------IGET 268
Cdd:cd11082 141 NVGFLALPVDFPGTALWKAIQARKRIVKTLEKCAAKSKKRMAAG----EEptcllDFWTHEILEeikeaeeegeppPPHS 216

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15239310 269 KDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11082 217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVRE 259
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 131-311 3.02e-07

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: 51.45  E-value: 3.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 131 RMLLMPSMKPEALRRYVGVMDEIAQK---HFETeWANQDQLIVFPLTKKFTFSIACR-------LFLSMDDLERVRKLEE 200
Cdd:cd11057  59 RKALNPSFNPKILLSFLPIFNEEAQKlvqRLDT-YVGGGEFDILPDLSRCTLEMICQttlgsdvNDESDGNEEYLESYER 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 201 PFTTVMTGVFSI--PIDLpgtrFNRAIKASRLLSKEVS-------TIIRQRKEELKAGKVSVEQDILSH----------- 260
Cdd:cd11057 138 LFELIAKRVLNPwlHPEF----IYRLTGDYKEEQKARKilrafseKIIEKKLQEVELESNLDSEEDEENgrkpqifidql 213

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15239310 261 --MLMNIGETKDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11057 214 leLARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYE 266
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 129-311 5.10e-07

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: 50.66  E-value: 5.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 129 KTRMLLMPSMKPEALRRYVGVMDEIAQ---KHFETEWANQDQLIVFPLTKKFTFSIACRL-------FLSMDDLERVRKL 198
Cdd:cd11055  62 RLRTTLSPTFSSGKLKLMVPIINDCCDelvEKLEKAAETGKPVDMKDLFQGFTLDVILSTafgidvdSQNNPDDPFLKAA 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 199 EEPFTTVMTGVFSIPIDLPGTRFNRAIKASRLLSK---EVSTIIRQRKEELKAGKVSVEQDILSHMLmNIGETKDEDLAD 275
Cdd:cd11055 142 KKIFRNSIIRLFLLLLLFPLRLFLFLLFPFVFGFKsfsFLEDVVKKIIEQRRKNKSSRRKDLLQLML-DAQDSDEDVSKK 220

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15239310 276 K-----IIA----LLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11055 221 KltddeIVAqsfiFLLAGYETTSNTLSFASYLLATNPDVQEKLIE 265
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 175-309 5.85e-07

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: 50.67  E-value: 5.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 175 KKFTFSIACRLFLSM-----DDLER---VRKLEEPFTTVMTG----VFSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQR 242
Cdd:cd20617 111 KKFVLNIINQFLFGKrfpdeDDGEFlklVKPIEEIFKELGSGnpsdFIPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEH 190

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15239310 243 KEELKAGKvsvEQDILSHMLMNIGETKDEDLADK------IIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:cd20617 191 LKTIDPNN---PRDLIDDELLLLLKEGDSGLFDDdsiistCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKI 260
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 216-308 4.76e-06

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: 47.55  E-value: 4.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 216 LPGTRFNRAIKASRllsKEVSTIIRQRKEELKAGKVSVEQD--ILSHMLMNigETKD-EDLADKIIALLIGGHDTTSIVC 292
Cdd:cd11063 162 LRDKKFREACKVVH---RFVDPYVDKALARKEESKDEESSDryVFLDELAK--ETRDpKELRDQLLNILLAGRDTTASLL 236

                        90
                ....*....|....*.
gi 15239310 293 TFVVNYLAEFPHIYQR 308
Cdd:cd11063 237 SFLFYELARHPEVWAK 252
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 233-311 1.49e-05

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: 46.09  E-value: 1.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 233 KEVSTIIRQRKEELKAGKVSVEQDILSHMLMN----IGETKDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQR 308
Cdd:cd11062 181 ESIAKQVDEVLRQVSAGDPPSIVTSLFHALLNsdlpPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILER 260


                ...
gi 15239310 309 VLE 311
Cdd:cd11062 261 LRE 263
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 226-311 2.58e-05

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: 45.66  E-value: 2.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 226 KASRLLSKEVSTIIRQRKEELKA--GKVSVEQDILShMLMNIGE-----TKDEDLADKIIALLIGGHDTTSIVCTFVVNY 298
Cdd:cd11064 178 EAIRVIDDFVYEVISRRREELNSreEENNVREDLLS-RFLASEEeegepVSDKFLRDIVLNFILAGRDTTAAALTWFFWL 256

                        90
                ....*....|...
gi 15239310 299 LAEFPHIYQRVLE 311
Cdd:cd11064 257 LSKNPRVEEKIRE 269
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 131-311 4.11e-05

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: 45.00  E-value: 4.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 131 RMLLMPSMKPEALRRYVGVMDEIA---QKHFETEWANQDQLIVFPLTKKFTFSIACRL-F-LSMDDLER-----VRKLEE 200
Cdd:cd11083  63 RRLVMPAFSPKHLRYFFPTLRQITerlRERWERAAAEGEAVDVHKDLMRYTVDVTTSLaFgYDLNTLERggdplQEHLER 142

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 201 PFTTVMTGVFS-IP----IDLPGTR-FNRAIKASRllsKEVSTIIRQRKEELKAGKVSVEQ--DILSHMLM---NIGETK 269
Cdd:cd11083 143 VFPMLNRRVNApFPywryLRLPADRaLDRALVEVR---ALVLDIIAAARARLAANPALAEApeTLLAMMLAeddPDARLT 219

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15239310 270 DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11083 220 DDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVRE 261
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 129-311 5.23e-05

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: 44.47  E-value: 5.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 129 KTRMLLMPSMKPEALRRYVGVMDEIAQ---KHFETEWANQDQLIVFPLTKKFTFSIACRLFLSMDDLERVRKLEEPFTT- 204
Cdd:cd20659  59 RNRRLLTPAFHFDILKPYVPVYNECTDillEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNCQQTGKNHPYVAa 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 205 -------VMTGVFSIPIDLP--------GTRFNRAIKASRLLSKEvstIIRQRKEELKAGKVSVEQ-----DILSHMLMn 264
Cdd:cd20659 139 vhelsrlVMERFLNPLLHFDwiyyltpeGRRFKKACDYVHKFAEE---IIKKRRKELEDNKDEALSkrkylDFLDILLT- 214

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15239310 265 igeTKDED--------LADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd20659 215 ---ARDEDgkgltdeeIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCRE 266
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 221-309 5.78e-05

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: 44.52  E-value: 5.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 221 FNRAIKASRLLSKEVSTIIRQRKEELKAGKvsveQDILSHML------MNIGETKDEDLADkIIALLIGGHDTTSIVCTF 294
Cdd:cd11061 164 FPGATKARKRFLDFVRAQLKERLKAEEEKR----PDIFSYLLeakdpeTGEGLDLEELVGE-ARLLIVAGSDTTATALSA 238

                        90
                ....*....|....*
gi 15239310 295 VVNYLAEFPHIYQRV 309
Cdd:cd11061 239 IFYYLARNPEAYEKL 253
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 238-311 7.55e-05

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: 43.74  E-value: 7.55e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15239310 238 IIRQRKEELKagkvsveQDILSHmLMNI---GET-KDEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11032 168 HLEERRRNPR-------DDLISR-LVEAevdGERlTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRA 237
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 225-303 1.02e-04

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: 43.83  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 225 IKASRLLSKEVSTIIRQ--RKEELKAGKVSVEQDILSHMLMnigetkdedlaDKIIALLIGGHDTTSIVCTFVVNYLAEF 302
Cdd:cd20622 224 SLERKGDEGEVRSAVDHmvRRELAAAEKEGRKPDYYSQVIH-----------DELFGYLIAGHDTTSTALSWGLKYLTAN 292


                .
gi 15239310 303 P 303
Cdd:cd20622 293 Q 293
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 225-309 2.21e-04

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 42.84  E-value: 2.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  225 IKASRLLSKEVSTI-------IRQRKEELKAGKVS---VEQDILSHmLMNIGETKDEDLADK-----IIALLIGGHDTTS 289
Cdd:PLN03195 231 IGSEALLSKSIKVVddftysvIRRRKAEMDEARKSgkkVKHDILSR-FIELGEDPDSNFTDKslrdiVLNFVIAGRDTTA 309

                         90       100
                 ....*....|....*....|
gi 15239310  290 IVCTFVVNYLAEFPHIYQRV 309
Cdd:PLN03195 310 TTLSWFVYMIMMNPHVAEKL 329
PLN02290 PLN02290
cytokinin trans-hydroxylase
 216-309 2.56e-04

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 42.49  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310  216 LPGTRF-----NRAIKAsrlLSKEVST----IIRQRKEELKAGKVSVEQDILSHMLMNIGETKDED--------LADKII 278
Cdd:PLN02290 246 FPGSRFfpskyNREIKS---LKGEVERllmeIIQSRRDCVEIGRSSSYGDDLLGMLLNEMEKKRSNgfnlnlqlIMDECK 322

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15239310  279 ALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:PLN02290 323 TFFFAGHETTALLLTWTLMLLASNPTWQDKV 353
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 131-308 2.77e-04

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: 42.18  E-value: 2.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 131 RMLLMPSMKPEALRRYVGVMD-EIAQ--KHFETEWANqdqliVFPLTKKFTFSIACRL-----FLSMDD--LERVRKLEE 200
Cdd:cd11065  66 RRLFHQLLNPSAVRKYRPLQElESKQllRDLLESPDD-----FLDHIRRYAASIILRLaygyrVPSYDDplLRDAEEAME 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 201 PFTTVMTG----VFSIPI-----DLPGTRFNRAIKASRLLSKEVSTIIRQR-KEELKAGKV--SVEQDILSHMLMNIGET 268
Cdd:cd11065 141 GFSEAGSPgaylVDFFPFlrylpSWLGAPWKRKARELRELTRRLYEGPFEAaKERMASGTAtpSFVKDLLEELDKEGGLS 220

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15239310 269 kDEDLADKIIALLIGGHDTT-SIVCTFVVnYLAEFPHIYQR 308
Cdd:cd11065 221 -EEEIKYLAGSLYEAGSDTTaSTLQTFIL-AMALHPEVQKK 259
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 238-311 4.19e-04

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: 41.80  E-value: 4.19e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15239310 238 IIRQRKEELKAGKVSvEQDILSHmLMNIGETK-----DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11060 185 AVAERLAEDAESAKG-RKDMLDS-FLEAGLKDpekvtDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRA 261
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 239-311 9.39e-04

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: 40.47  E-value: 9.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 239 IRQRKEELKAGKVsveQDILSHMLMNIGETKDEDLADK---------IIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRV 309
Cdd:cd20674 187 LRQHKESLVAGQW---RDMTDYMLQGLGQPRGEKGMGQlleghvhmaVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRL 263


                ..
gi 15239310 310 LE 311
Cdd:cd20674 264 QE 265
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 235-311 2.73e-03

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: 39.05  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 235 VSTIIRQRKEELKAGKVSVEQDILSHMLMNIGETKD--------EDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIY 306
Cdd:cd20667 180 VRSFIKKEVIRHELRTNEAPQDFIDCYLAQITKTKDdpvstfseENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQ 259


                ....*
gi 15239310 307 QRVLE 311
Cdd:cd20667 260 EKVQQ 264
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 131-311 2.91e-03

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: 39.11  E-value: 2.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 131 RMLLMP--------SMKPEALRRYVGVMDEIAQK---HFETEWANqdqliVFPltkkftfsiaCRLFLSM-----DDLER 194
Cdd:cd11035  65 RRLLNPlfspkavaALEPRIRERAVELIESFAPRgecDFVADFAE-----PFP----------TRVFLELmglplEDLDR 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 195 VRKLEEPFTTvmtgvfsipidlpGTRFNRAIKASRLLSKEVSTIIRQRKEElkagkvsVEQDILSHML-MNIGETK--DE 271
Cdd:cd11035 130 FLEWEDAMLR-------------PDDAEERAAAAQAVLDYLTPLIAERRAN-------PGDDLISAILnAEIDGRPltDD 189

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15239310 272 DLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11035 190 ELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRE 229
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 216-311 3.93e-03

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: 38.50  E-value: 3.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 216 LPGTR-FNRAIKasrLLSKEVSTIIRQRKEELKAGKVSVEQDILS-----HMLMNIGETKDEDLADK-----IIALLIGG 284
Cdd:cd11046 176 VPRQRkFLRDLK---LLNDTLDDLIRKRKEMRQEEDIELQQEDYLneddpSLLRFLVDMRDEDVDSKqlrddLMTMLIAG 252

                        90       100
                ....*....|....*....|....*..
gi 15239310 285 HDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11046 253 HETTAAVLTWTLYELSQNPELMAKVQA 279
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 256-311 4.17e-03

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: 38.72  E-value: 4.17e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15239310 256 DILSHMLMNIGETK---DEDLADKIIALLIGGHDTTSIVCTFVVNYLAEFPHIYQRVLE 311
Cdd:cd11058 198 DFMSYILRNKDEKKgltREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVD 256
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 210-314 5.52e-03

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: 38.08  E-value: 5.52e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 210 FSIPIDLPGTRFNRAIKASRLLSKEVSTIIRQRKEEL------KAGKVSVEQDILShMLMNIGETKDEDLADKIIALLIG 283
Cdd:cd11070 156 FPFLDRLPWVLFPSRKRAFKDVDEFLSELLDEVEAELsadskgKQGTESVVASRLK-RARRSGGLTEKELLGNLFIFFIA 234

                        90       100       110
                ....*....|....*....|....*....|.
gi 15239310 284 GHDTTSIVCTFVVNYLAEFPHIYQRVLEGMQ 314
Cdd:cd11070 235 GHETTANTLSFALYLLAKHPEVQDWLREEID 265
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 218-307 9.88e-03

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: 37.36  E-value: 9.88e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239310 218 GTRFNRAikaSRLLSKEVSTIIRQRK---------EELKAGKVSVEQDILSHMLMnigeTKDED---LADKII-----AL 280
Cdd:cd20679 180 GRRFRRA---CRLVHDFTDAVIQERRrtlpsqgvdDFLKAKAKSKTLDFIDVLLL----SKDEDgkeLSDEDIraeadTF 252

                        90       100
                ....*....|....*....|....*..
gi 15239310 281 LIGGHDTTSIVCTFVVNYLAEFPHiYQ 307
Cdd:cd20679 253 MFEGHDTTASGLSWILYNLARHPE-YQ 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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