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Conserved domains on  [gi|399288|sp|Q02318|]
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RecName: Full=Sterol 26-hydroxylase, mitochondrial; AltName: Full=5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase; AltName: Full=Cytochrome P-450C27/25; AltName: Full=Cytochrome P450 27; AltName: Full=Sterol 27-hydroxylase; AltName: Full=Vitamin D(3) 25-hydroxylase; Flags: Precursor

Protein Classification

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 ...
89-524 0e+00

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 cd20646:

Pssm-ID: 425388 [Multi-domain]  Cd Length: 430  Bit Score: 805.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20646   1 KKIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   169 AEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20646  81 KEVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   249 QNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaaGPDGIQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20646 161 KLSEIVTLLPKWTRPYLPFWKRYVDAWDTIFSFGKKLIDKKMEEIEERV---DRGEPVEGEYLTYLLSSGKLSPKEVYGS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRII- 407
Cdd:cd20646 238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIv 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20646 318 EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGG----LKHHPFGSIPFGYGVRACVGRRIAELEMY 393
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 399288   488 LLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20646 394 LALSRLIKRFEVRPDPSGGEVKAITRTLLVPNKPINL 430
 
Name Accession Description Interval E-value
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
89-524 0e+00

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


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 805.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20646   1 KKIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   169 AEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20646  81 KEVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   249 QNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaaGPDGIQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20646 161 KLSEIVTLLPKWTRPYLPFWKRYVDAWDTIFSFGKKLIDKKMEEIEERV---DRGEPVEGEYLTYLLSSGKLSPKEVYGS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRII- 407
Cdd:cd20646 238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIv 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20646 318 EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGG----LKHHPFGSIPFGYGVRACVGRRIAELEMY 393
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 399288   488 LLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20646 394 LALSRLIKRFEVRPDPSGGEVKAITRTLLVPNKPINL 430
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
61-526 4.44e-135

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: 399.35  E-value: 4.44e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288      61 PRLGQLRFFFQLFVQ-GYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQ 139
Cdd:pfam00067   1 PPGPPPLPLFGNLLQlGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     140 HDLTYGPFTTEGHHWYQLRQALNQRLLKPaEAALYTDAFNEVIDDFMTRLDQLRAEsasgNQVSDMAQLFYYFALEAICY 219
Cdd:pfam00067  81 PFLGKGIVFANGPRWRQLRRFLTPTFTSF-GKLSFEPRVEEEARDLVEKLRKTAGE----PGVIDITDLLFRAALNVICS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     220 ILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTrpVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQA 299
Cdd:pfam00067 156 ILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPI--LKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     300 AgpDGIQVSGYLHFLLAS-----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQV 374
Cdd:pfam00067 234 A--KKSPRDFLDALLLAKeeedgSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     375 PQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNS 453
Cdd:pfam00067 312 PTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDEN 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399288     454 QPatprIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLV-PNKKVGLQF 526
Cdd:pfam00067 392 GK----FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLlPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
147-518 8.11e-44

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 160.29  E-value: 8.11e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   147 FTTEGHHWYQLRQALNqRLLKPAEAALYTDAFNEVIDDFMTRLdqlraesaSGNQVSDMAQLFYYFALEAICYILfekri 226
Cdd:COG2124  92 LTLDGPEHTRLRKLLA-PAFTPRALRGYRPLIREIADRLLDDL--------WQGGADLVLDFAAELTLRVIAELL----- 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   227 gclqrSIP-EDTVTFVRSIGLMFQnslyaTFLPKWTRPvlPFWKRYLDGWNAIFSFGKKLIDEKLED-----MEAQLQAA 300
Cdd:COG2124 158 -----GVPlEDRPQLLRWSDALLL-----RLDPDLGPE--EPWRRARAARRELDAYLRALIAERRAAprddlLSLLLSAE 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   301 GPDGiqvsgylhfllasGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGvvpagqvpqhkdf 380
Cdd:COG2124 226 DDGG-------------GRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR------------- 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   381 ahmPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRnsqpatpri 460
Cdd:COG2124 280 ---PLLEAVVEETLRLYPPVPLARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN--------- 347
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 399288   461 QHpfgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELksVARIVLVP 518
Cdd:COG2124 348 AH----LPFGGGPHRCLGAALARLELKVALAELLRRFPLLLLAEPPPL--VRRPTLVP 399
PLN02687 PLN02687
flavonoid 3'-monooxygenase
318-502 1.41e-26

flavonoid 3'-monooxygenase


Pssm-ID: 215371  Cd Length: 517  Bit Score: 112.98  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    318 GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLY 397
Cdd:PLN02687 291 GRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLH 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    398 PVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQ-HPFGSVPFGYGVRA 475
Cdd:PLN02687 371 PSTPLSlPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKgSDFELIPFGAGRRI 450
                        170       180
                 ....*....|....*....|....*..
gi 399288    476 CLGRRIAELEMQLLLARLIQKYKVVLA 502
Cdd:PLN02687 451 CAGLSWGLRMVTLLTATLVHAFDWELA 477
 
Name Accession Description Interval E-value
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
89-524 0e+00

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


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 805.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20646   1 KKIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   169 AEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20646  81 KEVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   249 QNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaaGPDGIQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20646 161 KLSEIVTLLPKWTRPYLPFWKRYVDAWDTIFSFGKKLIDKKMEEIEERV---DRGEPVEGEYLTYLLSSGKLSPKEVYGS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRII- 407
Cdd:cd20646 238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIv 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20646 318 EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGG----LKHHPFGSIPFGYGVRACVGRRIAELEMY 393
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 399288   488 LLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20646 394 LALSRLIKRFEVRPDPSGGEVKAITRTLLVPNKPINL 430
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
91-522 1.12e-178

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


Pssm-ID: 410677 [Multi-domain]  Cd Length: 426  Bit Score: 509.38  E-value: 1.12e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd11054   3 KYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRPKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   171 AALYTDAFNEVIDDFMTRLDQLRAESasGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQN 250
Cdd:cd11054  83 VASYLPAINEVADDFVERIRRLRDED--GEEVPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIFES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   251 SLYATFLPKWTRPV-LPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGPDgiqvSGYLHFLLASGQLSPREAMGSL 329
Cdd:cd11054 161 SAKLMFGPPLWKYFpTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDEEE----DSLLEYLLSKPGLSKKEIVTMA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   330 PELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEK 409
Cdd:cd11054 237 LDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPK 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   410 EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpaTPRIQHPFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd11054 317 DIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDS--ENKNIHPFASLPFGFGPRMCIGRRFAELEMYLL 394
                       410       420       430
                ....*....|....*....|....*....|...
gi 399288   490 LARLIQKYKVVlaPETGELKSVARIVLVPNKKV 522
Cdd:cd11054 395 LAKLLQNFKVE--YHHEELKVKTRLILVPDKPL 425
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
89-524 3.35e-152

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


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 442.27  E-value: 3.35e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20648   2 KAKYGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSSWKDYRQLRGHAYGLLTAEGEEWQRLRSLLAKHMLKP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   169 AEAALYTDAFNEVIDDFMTRLDQLRAESaSGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20648  82 KAVEAYAGVLNAVVTDLIRRLRRQRSRS-SPGVVKDIAGEFYKFGLEGISSVLFESRIGCLEANVPEETETFIQSINTMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   249 QNSLYATFLPKWTRPVLPF-WKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaagPDGIQVSG-YLHFLLASGQLSPREAM 326
Cdd:cd20648 161 VMTLLTMAMPKWLHRLFPKpWQRFCRSWDQMFAFAKGHIDRRMAEVAAKL----PRGEAIEGkYLTYFLAREKLPMKSIY 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   327 GSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRI 406
Cdd:cd20648 237 GNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARV 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   407 IEK-EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAtpriqHPFGSVPFGYGVRACLGRRIAELE 485
Cdd:cd20648 317 IPDrDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTH-----HPYASLPFGFGKRSCIGRRIAELE 391
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 399288   486 MQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20648 392 VYLALARILTHFEVRPEPGGSPVKPMTRTLLVPERSINL 430
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
61-526 4.44e-135

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: 399.35  E-value: 4.44e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288      61 PRLGQLRFFFQLFVQ-GYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQ 139
Cdd:pfam00067   1 PPGPPPLPLFGNLLQlGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     140 HDLTYGPFTTEGHHWYQLRQALNQRLLKPaEAALYTDAFNEVIDDFMTRLDQLRAEsasgNQVSDMAQLFYYFALEAICY 219
Cdd:pfam00067  81 PFLGKGIVFANGPRWRQLRRFLTPTFTSF-GKLSFEPRVEEEARDLVEKLRKTAGE----PGVIDITDLLFRAALNVICS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     220 ILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTrpVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQA 299
Cdd:pfam00067 156 ILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPI--LKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     300 AgpDGIQVSGYLHFLLAS-----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQV 374
Cdd:pfam00067 234 A--KKSPRDFLDALLLAKeeedgSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288     375 PQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNS 453
Cdd:pfam00067 312 PTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDEN 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399288     454 QPatprIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLV-PNKKVGLQF 526
Cdd:pfam00067 392 GK----FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLlPPKPYKLKF 461
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
91-518 2.74e-131

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


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 388.89  E-value: 2.74e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd20647   3 EYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWQEYRDLRGRSTGLISAEGEQWLKMRSVLRQKILRPRD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   171 AALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF-- 248
Cdd:cd20647  83 VAVYSGGVNEVVADLIKRIKTLRSQEDDGETVTNVNDLFFKYSMEGVATILYECRLGCLENEIPKQTVEYIEALELMFsm 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   249 -QNSLYATFLPKWTRPVLPF-WKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQaagpDGIQVSG-YLHFLLASGQLSPREA 325
Cdd:cd20647 163 fKTTMYAGAIPKWLRPFIPKpWEEFCRSWDGLFKFSQIHVDNRLREIQKQMD----RGEEVKGgLLTYLLVSKELTLEEI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   326 MGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSR 405
Cdd:cd20647 239 YANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNGR 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   406 IIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSqpATPRIQHpFGSVPFGYGVRACLGRRIAELE 485
Cdd:cd20647 319 VTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKD--ALDRVDN-FGSIPFGYGIRSCIGRRIAELE 395
                       410       420       430
                ....*....|....*....|....*....|...
gi 399288   486 MQLLLARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd20647 396 IHLALIQLLQNFEIKVSPQTTEVHAKTHGLLCP 428
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
91-522 1.47e-99

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


Pssm-ID: 410738  Cd Length: 419  Bit Score: 307.12  E-value: 1.47e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd20645   3 KFGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKPKE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   171 AALYTDAFNEVIDDFMTRLDQLRAESAsgnQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFqn 250
Cdd:cd20645  83 VMKLDGKINEVLADFMGRIDELCDETG---RVEDLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIKTMM-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   251 slyATFLPKWTRPV-------LPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAagpdgiqvsGYLHFLLASGQLSPR 323
Cdd:cd20645 158 ---STFGKMMVTPVelhkrlnTKVWQDHTEAWDNIFKTAKHCIDKRLQRYSQGPAN---------DFLCDIYHDNELSKK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   324 EAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN 403
Cdd:cd20645 226 ELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFT 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   404 SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAtpriqHPFGSVPFGYGVRACLGRRIAE 483
Cdd:cd20645 306 SRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHSI-----NPFAHVPFGIGKRMCIGRRLAE 380
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 399288   484 LEMQLLLARLIQKYKVVlAPETGELKSVARIVLVPNKKV 522
Cdd:cd20645 381 LQLQLALCWIIQKYQIV-ATDNEPVEMLHSGILVPSREL 418
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
91-520 1.77e-82

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


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 263.11  E-value: 1.77e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd20643   3 KYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAPKV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   171 AALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQN 250
Cdd:cd20643  83 IDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMFHT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   251 SLYATFLPkwtrPVL------PFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGpdgiQVSGYLHFLLASGQLSPRE 324
Cdd:cd20643 163 TSPMLYIP----PDLlrlintKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKGKNEH----EYPGILANLLLQDKLPIED 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   325 AMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS 404
Cdd:cd20643 235 IKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQ 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   405 RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSqpatprIQHpFGSVPFGYGVRACLGRRIAEL 484
Cdd:cd20643 315 RYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKD------ITH-FRNLGFGFGPRQCLGRRIAET 387
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 399288   485 EMQLLLARLIQKYKVVLAPETgELKSVARIVLVPNK 520
Cdd:cd20643 388 EMQLFLIHMLENFKIETQRLV-EVKTTFDLILVPEK 422
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
93-526 8.98e-73

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


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 237.82  E-value: 8.98e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    93 GPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAA 172
Cdd:cd20644   5 GPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSPAAVQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   173 LYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSL 252
Cdd:cd20644  85 RFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVMLKTTV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   253 YATFLP----KWTRPVLpfWKRYLDGWNAIFSFGKKLIDEKLEDMeaqlqAAGPDGiQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20644 165 PLLFMPrslsRWISPKL--WKEHFEAWDCIFQYADNCIQKIYQEL-----AFGRPQ-HYTGIVAELLLQAELSLEAIKAN 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVvpAGQVPQH--KDFAHMPLLKAVLKETLRLYPVVPTNSRI 406
Cdd:cd20644 237 ITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAA--AAQISEHpqKALTELPLLKAALKETLRLYPVGITVQRV 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   407 IEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpriqhPFGSVPFGYGVRACLGRRIAELEM 486
Cdd:cd20644 315 PSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGR-----NFKHLAFGFGMRQCLGRRLAEAEM 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 399288   487 QLLLARLIQKYKV-VLAPEtgELKSVARIVLVPNKKVGLQF 526
Cdd:cd20644 390 LLLLMHVLKNFLVeTLSQE--DIKTVYSFILRPEKPPLLTF 428
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
93-504 1.10e-67

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: 223.16  E-value: 1.10e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    93 GPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDqhdLTYGPFTTEGHHWYQLRQALnQRLLKPAEAA 172
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDF---LGDGLLTLDGPEHRRLRRLL-APAFTPRALA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   173 LYTDAFNEVIDDFMTRLDQLraesasGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFqnsl 252
Cdd:cd00302  77 ALRPVIREIARELLDRLAAG------GEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRL---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   253 yatflpkWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDmeaqlqaagPDGIQVSGYLHFLLASGQLSPREAMGSLPEL 332
Cdd:cd00302 147 -------LRPLPSPRLRRLRRARARLRDYLEELIARRRAE---------PADDLDLLLLADADDGGGLSDEEIVAELLTL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   333 LMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAgqvPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIE 412
Cdd:cd00302 211 LLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGD---GTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVE 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   413 VDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRnsqpatPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLAR 492
Cdd:cd00302 288 LGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLP------EREEPRYAHLPFGAGPHRCLGARLARLELKLALAT 361
                       410
                ....*....|..
gi 399288   493 LIQKYKVVLAPE 504
Cdd:cd00302 362 LLRRFDFELVPD 373
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
147-518 1.37e-62

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: 210.84  E-value: 1.37e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   147 FTTEGHHWYQLRQALN----QRLLKPaeaalYTDAFNEVIDDFMTRLDQLraesaSGNQVSDMAQLFYYFALEAICYILF 222
Cdd:cd20628  50 LTSTGEKWRKRRKLLTpafhFKILES-----FVEVFNENSKILVEKLKKK-----AGGGEFDIFPYISLCTLDIICETAM 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   223 EKRIGCLQrsipEDTVTFVRSIglmfqNSLYATFLPKWTRPVL---PFWKRYLDGW------NAIFSFGKKLIDEKLEDM 293
Cdd:cd20628 120 GVKLNAQS----NEDSEYVKAV-----KRILEIILKRIFSPWLrfdFIFRLTSLGKeqrkalKVLHDFTNKVIKERREEL 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   294 EAQLQAAGPDGIQVSG----YLHFLLAS----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEV 365
Cdd:cd20628 191 KAEKRNSEEDDEFGKKkrkaFLDLLLEAhedgGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEEL 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   366 VGVV-PAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESF 444
Cdd:cd20628 271 DEIFgDDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKF 350
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 399288   445 QPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd20628 351 DPDRFL----PENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGEDLKLIAEIVLRS 420
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
91-520 6.37e-61

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: 206.28  E-value: 6.37e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYLG--PQMHVnlaSAP-LLEQVMRQE-----GKYPVRNDMELWKEHRdqhdltygpFTTEGHHWYQLRQALN 162
Cdd:cd11055   1 KYGKVFGLYFGtiPVIVV---SDPeMIKEILVKEfsnftNRPLFILLDEPFDSSL---------LFLKGERWKRLRTTLS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   163 QRL----LKpaeaaLYTDAFNEVIDDFMTRLDQLraesASGNQVSDMAQLFYYFALEAICYILFEkrIGCLQRSIPEDTv 238
Cdd:cd11055  69 PTFssgkLK-----LMVPIINDCCDELVEKLEKA----AETGKPVDMKDLFQGFTLDVILSTAFG--IDVDSQNNPDDP- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   239 tFVRSIGLMFQNS---LYATFLPKWTRPVLPFWKRYLDGWNAIFSFG---KKLIDEKLEDMEAQ----LQA---AGPDGI 305
Cdd:cd11055 137 -FLKAAKKIFRNSiirLFLLLLLFPLRLFLFLLFPFVFGFKSFSFLEdvvKKIIEQRRKNKSSRrkdlLQLmldAQDSDE 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   306 QVSgylhfllaSGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPL 385
Cdd:cd11055 216 DVS--------KKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKY 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   386 LKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsqPATPRIQHPFG 465
Cdd:cd11055 288 LDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFS----PENKAKRHPYA 363
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 399288   466 SVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET-GELKSVARIVLVPNK 520
Cdd:cd11055 364 YLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETeIPLKLVGGATLSPKN 419
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
99-499 1.49e-58

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: 200.13  E-value: 1.49e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    99 YLGPQMHVNLASAPLLEQVMRQEGKYPV-RNDMELWKEHRDQHDLtygpFTTEGHHWYQLRQ-ALNQ-RLLKpaeaalYT 175
Cdd:cd20617   7 WLGDVPTVVLSDPEIIKEAFVKNGDNFSdRPLLPSFEIISGGKGI----LFSNGDYWKELRRfALSSlTKTK------LK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   176 DAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRsipEDTVTFVRSIGLMFQ--NSLY 253
Cdd:cd20617  77 KKMEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDD---GEFLKLVKPIEEIFKelGSGN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   254 ATFLPKWTRPVLPFWKRYLDGW-NAIFSFGKKLIDEKLEDMEAQlqaagpDGIQVSGYLHFLLASGQLSPREAMGSLP-- 330
Cdd:cd20617 154 PSDFIPILLPFYFLYLKKLKKSyDKIKDFIEKIIEEHLKTIDPN------NPRDLIDDELLLLLKEGDSGLFDDDSIIst 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   331 --ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRII 407
Cdd:cd20617 228 clDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGlPRVT 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpaTPRIQHpfgSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20617 308 TEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDG--NKLSEQ---FIPFGIGKRNCVGENLARDELF 382
                       410
                ....*....|..
gi 399288   488 LLLARLIQKYKV 499
Cdd:cd20617 383 LFFANLLLNFKF 394
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
156-507 1.21e-55

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: 192.05  E-value: 1.21e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   156 QLRQALNQRLlkpAEAAL--YTDAFNEVIDDFMTRLDQLRAESASGnqVSDMAQLFYYFALEAICYILFEKRIGCLQRS- 232
Cdd:cd11061  56 RRRRVWSHAF---SDKALrgYEPRILSHVEQLCEQLDDRAGKPVSW--PVDMSDWFNYLSFDVMGDLAFGKSFGMLESGk 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   233 ---IPEDTVTFVRSIGLMfqnsLYATFLPKWTRpVLPFWKRYLDGWNAIFSFGKKLIDEKLedmeaQLQAAGPDGIqvsg 309
Cdd:cd11061 131 dryILDLLEKSMVRLGVL----GHAPWLRPLLL-DLPLFPGATKARKRFLDFVRAQLKERL-----KAEEEKRPDI---- 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   310 yLHFLLAS------GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQ-VPQHKDFAH 382
Cdd:cd11061 197 -FSYLLEAkdpetgEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDeIRLGPKLKS 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   383 MPLLKAVLKETLRLYPVVPTN-SRIIEKE-IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpRI 460
Cdd:cd11061 276 LPYLRACIDEALRLSPPVPSGlPRETPPGgLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELV-RA 354
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 399288   461 QHPFgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP-ETGE 507
Cdd:cd11061 355 RSAF--IPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPgEDGE 400
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
145-520 3.74e-51

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: 180.54  E-value: 3.74e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   145 GPFTTEGHHWYQLRQALNqRLLKPAEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEK 224
Cdd:cd11069  52 GLLAAEGEEHKRQRKILN-PAFSYRHVKELYPIFWSKAEELVDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGY 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   225 RIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVLPFW-----KRYLDGWNAIFSFGKKLIDEKLEDMEAQLQA 299
Cdd:cd11069 131 DFDSLENPDNELAEAYRRLFEPTLLGSLLFILLLFLPRWLVRILpwkanREIRRAKDVLRRLAREIIREKKAALLEGKDD 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   300 AGPDGIQVsgylhfLLASGQ------LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPA-- 371
Cdd:cd11069 211 SGKDILSI------LLRANDfadderLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDpp 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   372 GQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWL 450
Cdd:cd11069 285 DGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWL 364
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 399288   451 RNSQPATPRIQHPFGS-VPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKsVARIVLVPNK 520
Cdd:cd11069 365 EPDGAASPGGAGSNYAlLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVER-PIGIITRPPV 434
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
164-499 1.68e-50

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


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 178.65  E-value: 1.68e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   164 RLLKPA--EAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDtvtfv 241
Cdd:cd11059  60 RLLSGVysKSSLLRAAMEPIIRERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDS----- 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   242 RSIGLMFqnsLYATFLPKWTRPVLPFWKR---------YLDGWNAIFSFGKKLIDEKLEDmeAQLQAAGPDGIQVSGYLH 312
Cdd:cd11059 135 RERELLR---RLLASLAPWLRWLPRYLPLatsrliigiYFRAFDEIEEWALDLCARAESS--LAESSDSESLTVLLLEKL 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   313 FLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGV-VPAGQVPQHKDFAHMPLLKAVLK 391
Cdd:cd11059 210 KGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLpGPFRGPPDLEDLDKLPYLNAVIR 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   392 ETLRLYPVVP-TNSRII-EKEIEVDGFLFPKNTQfVFCH-YVVSRDPTAFSEPESFQPHRWLrNSQPATPRIQHPFgSVP 468
Cdd:cd11059 290 ETLRLYPPIPgSLPRVVpEGGATIGGYYIPGGTI-VSTQaYSLHRDPEVFPDPEEFDPERWL-DPSGETAREMKRA-FWP 366
                       330       340       350
                ....*....|....*....|....*....|.
gi 399288   469 FGYGVRACLGRRIAELEMQLLLARLIQKYKV 499
Cdd:cd11059 367 FGSGSRMCIGMNLALMEMKLALAAIYRNYRT 397
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
99-503 2.03e-49

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: 175.07  E-value: 2.03e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    99 YLGPQMHVNLASAPLLEQVMRQE-GKYPVRNDMELWKEHrdqhdLTYGPFTTEGHHWyqLRQalnQRLLKPAEA----AL 173
Cdd:cd20620   7 RLGPRRVYLVTHPDHIQHVLVTNaRNYVKGGVYERLKLL-----LGNGLLTSEGDLW--RRQ---RRLAQPAFHrrriAA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   174 YTDAFNEVIDDFMTRLDQlRAESASGNQVSDMAQLfyyfALEAICYILFEKRIGCLQRSIPEDTVTFVRSIglmfqNSLY 253
Cdd:cd20620  77 YADAMVEATAALLDRWEA-GARRGPVDVHAEMMRL----TLRIVAKTLFGTDVEGEADEIGDALDVALEYA-----ARRM 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   254 ATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAqlqaaGPDGIQVsgylhfLLAS------GQLSPR---- 323
Cdd:cd20620 147 LSPFLLPLWLPTPANRRFRRARRRLDEVIYRLIAERRAAPAD-----GGDLLSM------LLAArdeetgEPMSDQqlrd 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   324 EAMGslpeLLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN 403
Cdd:cd20620 216 EVMT----LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVL-GGRPPTAEDLPQLPYTEMVLQESLRLYPPAWII 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   404 SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRiqhpFGSVPFGYGVRACLGRRIAE 483
Cdd:cd20620 291 GREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPR----YAYFPFGGGPRICIGNHFAM 366
                       410       420
                ....*....|....*....|
gi 399288   484 LEMQLLLARLIQKYKVVLAP 503
Cdd:cd20620 367 MEAVLLLATIAQRFRLRLVP 386
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
149-503 3.64e-49

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: 175.01  E-value: 3.64e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   149 TEGHH--WYQLRQALNqrllkPAEAALY----TDAFNEVIDDFMTRLDQLraesASGNQVSDMAQLFYYFALEAICYILF 222
Cdd:cd20613  67 TEVDHekWKKRRAILN-----PAFHRKYlknlMDEFNESADLLVEKLSKK----ADGKTEVNMLDEFNRVTLDVIAKVAF 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   223 ekriGCLQRSIPEDTVTFVRSIGLMFQnSLYATFLPKWTRPvLPF-WK---------RYLDGwnaifsFGKKLIDEKLED 292
Cdd:cd20613 138 ----GMDLNSIEDPDSPFPKAISLVLE-GIQESFRNPLLKY-NPSkRKyrrevreaiKFLRE------TGRECIEERLEA 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   293 MEAQLQAagPDGIqvsgyLHFLLASGQLSPREAMGSLPE----LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGV 368
Cdd:cd20613 206 LKRGEEV--PNDI-----LTHILKASEEEPDFDMEELLDdfvtFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEV 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   369 VPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHR 448
Cdd:cd20613 279 LGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPER 358
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 399288   449 WLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd20613 359 FS----PEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELVP 409
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
200-518 1.07e-48

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: 173.54  E-value: 1.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   200 NQVSDMAQLFYYFALEAICYILF----EKRIGCLQRSIPeDTVTFVRSIGLMFqnslyaTFLPKWTRPVLPfWKRYLDGW 275
Cdd:cd11053 108 GQPFDLRELMQEITLEVILRVVFgvddGERLQELRRLLP-RLLDLLSSPLASF------PALQRDLGPWSP-WGRFLRAR 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   276 NAIfsfgKKLIDEKLEDMEAQLQAAGPDgiqvsgYLHFLLASG-----QLSPREAMGSLPELLMAGVDTTSNTLTWALYH 350
Cdd:cd11053 180 RRI----DALIYAEIAERRAEPDAERDD------ILSLLLSARdedgqPLSDEELRDELMTLLFAGHETTATALAWAFYW 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   351 LSKDPEIQEALHEEVVGVvpaGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYV 430
Cdd:cd11053 250 LHRHPEVLARLLAELDAL---GGDPDPEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYL 326
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   431 VSRDPTAFSEPESFQPHRWLrNSQPAtpriqhPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGElKS 510
Cdd:cd11053 327 THHRPDLYPDPERFRPERFL-GRKPS------PYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPE-RP 398

                ....*....
gi 399288   511 VAR-IVLVP 518
Cdd:cd11053 399 VRRgVTLAP 407
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
179-518 5.82e-48

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: 171.61  E-value: 5.82e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   179 NEVIDDFMTRLDqlraESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSipEDTVTFVRSIGLMFQNSLYATFLP 258
Cdd:cd11060  81 DECIDLLVDLLD----EKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLEAG--TDVDGYIASIDKLLPYFAVVGQIP 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   259 KWTRPV----LPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAqlqaagpDGIQVSGYLHFLLASGQ-----LSPREAMGSL 329
Cdd:cd11060 155 WLDRLLlknpLGPKRKDKTGFGPLMRFALEAVAERLAEDAE-------SAKGRKDMLDSFLEAGLkdpekVTDREVVAEA 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   330 PELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFA---HMPLLKAVLKETLRLYPVVPTN-SR 405
Cdd:cd11060 228 LSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKLSSPITFAeaqKLPYLQAVIKEALRLHPPVGLPlER 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   406 IIEKE-IEVDGFLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRnSQPATPRIQHPFgSVPFGYGVRACLGRRIAE 483
Cdd:cd11060 308 VVPPGgATICGRFIPGGTIVGVNPWVIHRDKEVFGEdADVFRPERWLE-ADEEQRRMMDRA-DLTFGAGSRTCLGKNIAL 385
                       330       340       350
                ....*....|....*....|....*....|....*
gi 399288   484 LEMQLLLARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd11060 386 LELYKVIPELLRRFDFELVDPEKEWKTRNYWFVKQ 420
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
93-498 2.56e-47

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: 170.09  E-value: 2.56e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    93 GPMWMSYLGPQMHVNLASAPLLEQVMrqegkypvrNDMElWKEHRDQHD---LTYGPFTTEGHHWYQLRQALN----QRL 165
Cdd:cd11057   1 GSPFRAWLGPRPFVITSDPEIVQVVL---------NSPH-CLNKSFFYDffrLGRGLFSAPYPIWKLQRKALNpsfnPKI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   166 LKPaeaalYTDAFNEVIDDFMTRLDQLraesASGNQVsDMAQLFYYFALEAICYILF-----------EKRIGCLQRSIp 234
Cdd:cd11057  71 LLS-----FLPIFNEEAQKLVQRLDTY----VGGGEF-DILPDLSRCTLEMICQTTLgsdvndesdgnEEYLESYERLF- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   235 edTVTFVRsiglMFQNSLYATFLPKWTrpvlPFWKRYLDGWNAIFSFGKKLIDEKL-EDMEAQLQAAGPDGIQVSGYLHF 313
Cdd:cd11057 140 --ELIAKR----VLNPWLHPEFIYRLT----GDYKEEQKARKILRAFSEKIIEKKLqEVELESNLDSEEDEENGRKPQIF 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   314 L-------LASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVP-AGQVPQHKDFAHMPL 385
Cdd:cd11057 210 IdqllelaRNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPdDGQFITYEDLQQLVY 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   386 LKAVLKETLRLYPVVPTNSRIIEKEIEVD-GFLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWLrnsqpaTPRIQ-- 461
Cdd:cd11057 290 LEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFL------PERSAqr 363
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 399288   462 HPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYK 498
Cdd:cd11057 364 HPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYR 400
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
91-507 2.11e-46

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


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 167.81  E-value: 2.11e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQegKYPVRNDMELWKE-----HRDQHDLTYGPFtteGHHWYQLRQALNQRL 165
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQ--KGSSFASRPPANPlrvlfSSNKHMVNSSPY---GPLWRTLRRNLVSEV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   166 LKPAEAALYTDAFNEVIDDFMTRLdqlRAESASGNQVSDMAQLFYYfaleAICYILFekrIGCLQRSIPEDTVTFVRSIG 245
Cdd:cd11075  76 LSPSRLKQFRPARRRALDNLVERL---REEAKENPGPVNVRDHFRH----ALFSLLL---YMCFGERLDEETVRELERVQ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   246 LMFQNSLYAT----FLPKWTRpvLPFWKRyldgWNAIFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFLLAS---- 317
Cdd:cd11075 146 RELLLSFTDFdvrdFFPALTW--LLNRRR----WKKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFLLLDLldlk 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   318 -----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKE 392
Cdd:cd11075 220 eeggeRKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLE 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   393 TLRLY-PVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATprIQHPFGSV---P 468
Cdd:cd11075 300 TLRRHpPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAAD--IDTGSKEIkmmP 377
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 399288   469 FGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd11075 378 FGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEGEEV 416
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
148-516 2.19e-45

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: 164.65  E-value: 2.19e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   148 TTEGHHWYQlrqalNQRLLKPA--EAAL--YTDAFNEVIDDFMTRLDQLraesASGNQVSDMAQLFYYFALEAICYILFE 223
Cdd:cd20659  51 LSNGKKWKR-----NRRLLTPAfhFDILkpYVPVYNECTDILLEKWSKL----AETGESVEVFEDISLLTLDIILRCAFS 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   224 KRIGCLQRSIPEDTVTFVRSIGLM----FQNSLY-ATFLPKWTrPVLPFWKRYLDGwnaIFSFGKKLIDEKLEdmeaQLQ 298
Cdd:cd20659 122 YKSNCQQTGKNHPYVAAVHELSRLvmerFLNPLLhFDWIYYLT-PEGRRFKKACDY---VHKFAEEIIKKRRK----ELE 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   299 AAGPDGIQVSGYLHFL----LA---SGQ-LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVP 370
Cdd:cd20659 194 DNKDEALSKRKYLDFLdillTArdeDGKgLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLG 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   371 AGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWL 450
Cdd:cd20659 274 DRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL 353
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 399288   451 R-NSQPatpriQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETgELKSVARIVL 516
Cdd:cd20659 354 PeNIKK-----RDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNH-PVEPKPGLVL 414
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
145-519 1.57e-44

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: 162.34  E-value: 1.57e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   145 GPFTTEGHHWYQLRQalnqrLLKPAEAALY---TDAFNEVIDDFMTRLDqlraesaSGNQVSDMAQLFYYFALEAICYIL 221
Cdd:cd11063  51 GIFTSDGEEWKHSRA-----LLRPQFSRDQisdLELFERHVQNLIKLLP-------RDGSTVDLQDLFFRLTLDSATEFL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   222 FEKRIGCLQ-RSIPEDTVTFVRSiglmFQNSLyaTFLPKWTR--PVLPFW--KRYLDGWNAIFSFGKKLIDEKLEDMEAQ 296
Cdd:cd11063 119 FGESVDSLKpGGDSPPAARFAEA----FDYAQ--KYLAKRLRlgKLLWLLrdKKFREACKVVHRFVDPYVDKALARKEES 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   297 LQAAGPDGIqvsGYLHFLLASGQlSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQ 376
Cdd:cd11063 193 KDEESSDRY---VFLDELAKETR-DPKELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPT 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   377 HKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKeievDGFL------------F-PKNTQFVFCHYVVSRDPTAFSE-PE 442
Cdd:cd11063 269 YEDLKNMKYLRAVINETLRLYPPVPLNSRVAVR----DTTLprgggpdgkspiFvPKGTRVLYSVYAMHRRKDIWGPdAE 344
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 399288   443 SFQPHRWLRNSQPatpriqhPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPN 519
Cdd:cd11063 345 EFRPERWEDLKRP-------GWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFDRIESRDVRPPEERLTLTLSNA 414
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
147-507 2.28e-44

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: 162.04  E-value: 2.28e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   147 FTTEGHHWYQLRQALnqrlLKPAEAALYTDAFNEVIDDFMTRL-DQLRAESASGNQVsDMAQLFYYFALEAICYILFEKR 225
Cdd:cd11062  47 FSTVDHDLHRLRRKA----LSPFFSKRSILRLEPLIQEKVDKLvSRLREAKGTGEPV-NLDDAFRALTADVITEYAFGRS 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   226 IGCL-QRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLD----GWNAIFSFGKKLIDEKLEDMEAQLQAA 300
Cdd:cd11062 122 YGYLdEPDFGPEFLDALRALAEMIHLLRHFPWLLKLLRSLPESLLKRLNpglaVFLDFQESIAKQVDEVLRQVSAGDPPS 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   301 GPDGIQVSGYLHFLLASGqLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVP-AGQVPQHKD 379
Cdd:cd11062 202 IVTSLFHALLNSDLPPSE-KTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPdPDSPPSLAE 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   380 FAHMPLLKAVLKETLRLYPVVPTNS-RIIEKE-IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNsqPAT 457
Cdd:cd11062 281 LEKLPYLTAVIKEGLRLSYGVPTRLpRVVPDEgLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGA--AEK 358
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 399288   458 PRIQHPFgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd11062 359 GKLDRYL--VPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYETTEE 406
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
91-526 3.72e-44

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: 161.73  E-value: 3.72e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYLGP-QMHVNLASAplLEQVMRQEGKYPVRNDMElwkehrdQHDLTYGP--FTTEGHHWYQLR----QALNQ 163
Cdd:cd11070   1 KLGAVKILFVSRwNILVTKPEY--LTQIFRRRDDFPKPGNQY-------KIPAFYGPnvISSEGEDWKRYRkivaPAFNE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   164 RLLK--PAEAALYTDAFNEVIddfmtrldqLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQ--RSIPEDTVT 239
Cdd:cd11070  72 RNNAlvWEESIRQAQRLIRYL---------LEEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDeeESSLHDTLN 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   240 FVRS-----IGLMFqnslyaTFLPKWTRPVLPFWKRYLDgwnAIFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFL 314
Cdd:cd11070 143 AIKLaifppLFLNF------PFLDRLPWVLFPSRKRAFK---DVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRA 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   315 LASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEV--VGVVPAGQVPQHKDFAHMPLLKAVLKE 392
Cdd:cd11070 214 RRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIdsVLGDEPDDWDYEEDFPKLPYLLAVIYE 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   393 TLRLYPVVPTNSRIIEKEIEV-----DGFLFPKNTQFVFCHYVVSRDPTA-FSEPESFQPHRWLRNSQP--ATPRIQHPF 464
Cdd:cd11070 294 TLRLYPPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWGSTSGEigAATRFTPAR 373
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 399288   465 GS-VPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQF 526
Cdd:cd11070 374 GAfIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRVDPEWEEGETPAGATRDSPAKLRLRF 436
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
147-518 8.11e-44

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 160.29  E-value: 8.11e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   147 FTTEGHHWYQLRQALNqRLLKPAEAALYTDAFNEVIDDFMTRLdqlraesaSGNQVSDMAQLFYYFALEAICYILfekri 226
Cdd:COG2124  92 LTLDGPEHTRLRKLLA-PAFTPRALRGYRPLIREIADRLLDDL--------WQGGADLVLDFAAELTLRVIAELL----- 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   227 gclqrSIP-EDTVTFVRSIGLMFQnslyaTFLPKWTRPvlPFWKRYLDGWNAIFSFGKKLIDEKLED-----MEAQLQAA 300
Cdd:COG2124 158 -----GVPlEDRPQLLRWSDALLL-----RLDPDLGPE--EPWRRARAARRELDAYLRALIAERRAAprddlLSLLLSAE 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   301 GPDGiqvsgylhfllasGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGvvpagqvpqhkdf 380
Cdd:COG2124 226 DDGG-------------GRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR------------- 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   381 ahmPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRnsqpatpri 460
Cdd:COG2124 280 ---PLLEAVVEETLRLYPPVPLARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN--------- 347
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 399288   461 QHpfgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELksVARIVLVP 518
Cdd:COG2124 348 AH----LPFGGGPHRCLGAALARLELKVALAELLRRFPLLLLAEPPPL--VRRPTLVP 399
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
164-503 6.73e-43

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


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 157.81  E-value: 6.73e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   164 RLLKPA----EAALYTDAfneviddfMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGclqrsiPEDTVT 239
Cdd:cd11049  75 RLMQPAfhrsRIPAYAEV--------MREEAEALAGSWRPGRVVDVDAEMHRLTLRVVARTLFSTDLG------PEAAAE 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   240 FVRSIGLMFQNSLYATFLPKWTRPV-LPFWKRYLDGWNAIFSfgkkLIDEkledMEAQLQAAGPDGiqvSGYLHFLLAS- 317
Cdd:cd11049 141 LRQALPVVLAGMLRRAVPPKFLERLpTPGNRRFDRALARLRE----LVDE----IIAEYRASGTDR---DDLLSLLLAAr 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   318 ----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKET 393
Cdd:cd11049 210 deegRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVL-GGRPATFEDLPRLTYTRRVVTEA 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   394 LRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRiqHPFgsVPFGYGV 473
Cdd:cd11049 289 LRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPR--GAF--IPFGAGA 364
                       330       340       350
                ....*....|....*....|....*....|
gi 399288   474 RACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11049 365 RKCIGDTFALTELTLALATIASRWRLRPVP 394
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
138-507 4.43e-40

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


Pssm-ID: 410711 [Multi-domain]  Cd Length: 429  Bit Score: 150.40  E-value: 4.43e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   138 DQHDLTYGPFtteGHHWYQLRQALNQRLLKPAEAALYTDAFNEVIDDFMTRLdqlRAESASGNQVsDMAQLFYYFALEAI 217
Cdd:cd20618  48 NGQDIVFAPY---GPHWRHLRKICTLELFSAKRLESFQGVRKEELSHLVKSL---LEESESGKPV-NLREHLSDLTLNNI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   218 CYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSL---YATFLPkWTRPVLPFW-KRYLDGWNAIF-SFGKKLIDEKLEd 292
Cdd:cd20618 121 TRMLFGKRYFGESEKESEEAREFKELIDEAFELAGafnIGDYIP-WLRWLDLQGyEKRMKKLHAKLdRFLQKIIEEHRE- 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   293 mEAQLQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAG 372
Cdd:cd20618 199 -KRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRE 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   373 QVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLr 451
Cdd:cd20618 278 RLVEESDLPKLPYLQAVVKETLRLHPPGPLLLpHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFL- 356
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 399288   452 NSQPATPRIQHpFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd20618 357 ESDIDDVKGQD-FELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFDWSLPGPKPE 411
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
139-503 4.55e-39

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: 147.74  E-value: 4.55e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   139 QHD-LTYGPFTTEGHHWYQlrqalnQRllKPAEAALYTDAFNevidDFMT---------RLDQLRAESASGNQVSDMAQL 208
Cdd:cd11064  43 FFDlLGDGIFNVDGELWKF------QR--KTASHEFSSRALR----EFMEsvvrekvekLLVPLLDHAAESGKVVDLQDV 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   209 FYYFALEAICYILFEKRIGCLQRSIPEdtVTFVRSIGLMFQNSLYATFLPKWtrpvlpFWK--RYL---------DGWNA 277
Cdd:cd11064 111 LQRFTFDVICKIAFGVDPGSLSPSLPE--VPFAKAFDDASEAVAKRFIVPPW------LWKlkRWLnigsekklrEAIRV 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   278 IFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFLLASGQLSPRE-----AMGslpeLLMAGVDTTSNTLTWALYHLS 352
Cdd:cd11064 183 IDDFVYEVISRRREELNSREEENNVREDLLSRFLASEEEEGEPVSDKflrdiVLN----FILAGRDTTAAALTWFFWLLS 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   353 KDPEIQEALHEEVVGVVPA-----GQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSR-IIEKEIEVDGFLFPKNTQFVF 426
Cdd:cd11064 259 KNPRVEEKIREELKSKLPKlttdeSRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKeAVNDDVLPDGTFVKKGTRIVY 338
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   427 CHYVVSRDPTAFSE-PESFQPHRWLRNSqpatPRIQH--PFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11064 339 SIYAMGRMESIWGEdALEFKPERWLDED----GGLRPesPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVP 414
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
332-518 9.74e-39

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: 146.31  E-value: 9.74e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQ-HKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKE 410
Cdd:cd11083 230 LLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKPVAPLLFLEPNED 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPriQHPFGSVPFGYGVRACLGRRIAELEMQLLL 490
Cdd:cd11083 310 TVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEP--HDPSSLLPFGAGPRLCPGRSLALMEMKLVF 387
                       170       180
                ....*....|....*....|....*...
gi 399288   491 ARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd11083 388 AMLCRNFDIELPEPAPAVGEEFAFTMSP 415
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
135-518 2.02e-38

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


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 145.76  E-value: 2.02e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   135 EHRDqhDLTYGPFTTEGHHWYQLRQALnqrllkpaeAALYTDA--------FNEVIDDFMtrlDQLRAESASGNQVsDMA 206
Cdd:cd11056  44 EKDD--PLSANLFSLDGEKWKELRQKL---------TPAFTSGklknmfplMVEVGDELV---DYLKKQAEKGKEL-EIK 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   207 QLFYYFALEAICYILFEKRIGCLQRSIPEdtvtFVRSIGLMFQNSLYATFLpKWTRPVLPFWKRYLdgwnaifsfGKKLI 286
Cdd:cd11056 109 DLMARYTTDVIASCAFGLDANSLNDPENE----FREMGRRLFEPSRLRGLK-FMLLFFFPKLARLL---------RLKFF 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   287 DEKLED-----MEAQLQAAGPDGIQVSGYLHFLL---ASGQLSPREAMGSLPE---------LLMAGVDTTSNTLTWALY 349
Cdd:cd11056 175 PKEVEDffrklVRDTIEYREKNNIVRNDFIDLLLelkKKGKIEDDKSEKELTDeelaaqafvFFLAGFETSSSTLSFALY 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   350 HLSKDPEIQEALHEEVVGVVPA--GQVpQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDG--FLFPKNTQFV 425
Cdd:cd11056 255 ELAKNPEIQEKLREEIDEVLEKhgGEL-TYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPVI 333
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   426 FCHYVVSRDPTAFSEPESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:cd11056 334 IPVYALHHDPKYYPEPEKFDPERFS----PENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKT 409
                       410
                ....*....|....*
gi 399288   506 G-ELK-SVARIVLVP 518
Cdd:cd11056 410 KiPLKlSPKSFVLSP 424
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
88-515 2.98e-38

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: 145.59  E-value: 2.98e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    88 YKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYpvrndmelwkehRDQHDLTY---------GPFTTEGHHWYQLR 158
Cdd:cd11046   6 WFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFS------------YDKKGLLAeilepimgkGLIPADGEIWKKRR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   159 QALNQRLLKPAEAALyTDAFNEVIDDFMTRLDqlraESASGNQVSDMAQLFYYFALEAICYILFEKRIGclqrSIPEDTV 238
Cdd:cd11046  74 RALVPALHKDYLEMM-VRVFGRCSERLMEKLD----AAAETGESVDMEEEFSSLTLDIIGLAVFNYDFG----SVTEESP 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   239 TFVRSIGLMFQNSLYATF-LPKWTRP----VLPFWKRYLDGWNAIFSFGKKLIDEKLEDM-EAQLQAAGPDGIQV--SGY 310
Cdd:cd11046 145 VIKAVYLPLVEAEHRSVWePPYWDIPaalfIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRqEEDIELQQEDYLNEddPSL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   311 LHFLLASG--QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKA 388
Cdd:cd11046 225 LRFLVDMRdeDVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRR 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   389 VLKETLRLYPVVPTNSRIIEKEIEVDGFLF--PKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGS 466
Cdd:cd11046 305 VLNESLRLYPQPPVLIRRAVEDDKLPGGGVkvPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEVIDDFAF 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 399288   467 VPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLA--PETGELKSVARIV 515
Cdd:cd11046 385 LPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDvgPRHVGMTTGATIH 435
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
164-507 2.83e-37

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: 142.34  E-value: 2.83e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   164 RLLKPA--EAALYT--DAFNEVIDDFMtrlDQLRAESASGNQVsDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTV- 238
Cdd:cd11058  63 RLLAHAfsEKALREqePIIQRYVDLLV---SRLRERAGSGTPV-DMVKWFNFTTFDIIGDLAFGESFGCLENGEYHPWVa 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   239 ---TFVRSIGLMfQNSLYATFLPKWTRPVLP--FWKRYLDGWnaifsfgkKLIDEKLeDMEAQLQAAGPDgiqvsgYLHF 313
Cdd:cd11058 139 lifDSIKALTII-QALRRYPWLLRLLRLLIPksLRKKRKEHF--------QYTREKV-DRRLAKGTDRPD------FMSY 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   314 LLAS----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVvgvvpAGQVPQHKD-----FAHMP 384
Cdd:cd11058 203 ILRNkdekKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEI-----RSAFSSEDDitldsLAQLP 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   385 LLKAVLKETLRLYPVVPTN-SRIIEKE-IEVDGFLFPKNTQfVFC-HYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQ 461
Cdd:cd11058 278 YLNAVIQEALRLYPPVPAGlPRVVPAGgATIDGQFVPGGTS-VSVsQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNDK 356
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 399288   462 HPfGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd11058 357 KE-AFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESED 401
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
256-522 3.49e-37

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


Pssm-ID: 410667  Cd Length: 441  Bit Score: 142.43  E-value: 3.49e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   256 FLPKWTRPV----LPFWKRYldgwNAIFSFGKKLIDEKLEDMEAQlqAAGPDGIQVSGYLHFLL----ASGQLSPREAMG 327
Cdd:cd11041 157 LFPPFLRPLvapfLPEPRRL----RRLLRRARPLIIPEIERRRKL--KKGPKEDKPNDLLQWLIeaakGEGERTPYDLAD 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   328 SLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRI 406
Cdd:cd11041 231 RQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSlRRK 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   407 IEKEIEV-DGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSV-----PFGYGVRACLGRR 480
Cdd:cd11041 311 VLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKHQFVSTspdflGFGHGRHACPGRF 390
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 399288   481 IAELEMQLLLARLIQKYKVVLAPETGELKSV---ARIVLVPNKKV 522
Cdd:cd11041 391 FASNEIKLILAHLLLNYDFKLPEGGERPKNIwfgEFIMPDPNAKV 435
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
336-520 3.85e-37

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


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 142.02  E-value: 3.85e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   336 GVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAG-QVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD 414
Cdd:cd20660 244 GHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSdRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIG 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   415 GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd20660 324 GYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFL----PENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSIL 399
                       170       180
                ....*....|....*....|....*.
gi 399288   495 QKYKVVLAPETGELKSVARIVLVPNK 520
Cdd:cd20660 400 RNFRIESVQKREDLKPAGELILRPVD 425
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
256-494 5.61e-37

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: 141.56  E-value: 5.61e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   256 FLPKWtrpVLPFWKRYLDGWNAIFsfgKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMA 335
Cdd:cd11065 161 YLPSW---LGAPWKRKARELRELT---RRLYEGPFEAAKERMASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEA 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   336 GVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEKEIEVD 414
Cdd:cd11065 235 GSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIpHALTEDDEYE 314
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   415 GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSvpFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd11065 315 GYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPPHFA--FGFGRRICPGRHLAENSLFIAIARLL 392
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
276-503 1.09e-35

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: 137.80  E-value: 1.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   276 NAIFSFGKKLIDEKLEdmeaQLQAAGPDGIQVsgYLHFLLASGQ-LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKD 354
Cdd:cd11044 180 NKLLARLEQAIRERQE----EENAEAKDALGL--LLEAKDEDGEpLSMDELKDQALLLLFAGHETTASALTSLCFELAQH 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   355 PEIQEALHEEVVGVVPAGQVPQhKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRD 434
Cdd:cd11044 254 PDVLEKLRQEQDALGLEEPLTL-ESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRD 332
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 399288   435 PTAFSEPESFQPHRWlrnSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11044 333 PELYPDPERFDPERF---SPARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLP 398
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
91-505 2.68e-35

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: 136.54  E-value: 2.68e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    91 KYGPMWMSYL-GPQMHVnLASAPLLEQVMRQEGK-----YPvrndmelwkehRDQHDL--TYGPFTTEGHHWYQLRQALn 162
Cdd:cd11043   4 RYGPVFKTSLfGRPTVV-SADPEANRFILQNEGKlfvswYP-----------KSVRKLlgKSSLLTVSGEEHKRLRGLL- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   163 QRLLKPaEAAlyTDAFNEVIDDFMtrLDQLRAESASGNQ-VSDMAQLFyyfALEAICYILFekrigclqrSIpeDTVTFV 241
Cdd:cd11043  71 LSFLGP-EAL--KDRLLGDIDELV--RQHLDSWWRGKSVvVLELAKKM---TFELICKLLL---------GI--DPEEVV 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   242 RSIGLMFQNSLYATF-----LPkWTRpvlpFWkRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAagpdgiqvSGYLHFLLA 316
Cdd:cd11043 132 EELRKEFQAFLEGLLsfplnLP-GTT----FH-RALKARKRIRKELKKIIEERRAELEKASPK--------GDLLDVLLE 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   317 SGQ-----LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEAL---HEEVVGVVPAGQVPQHKDFAHMPLLKA 388
Cdd:cd11043 198 EKDedgdsLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELleeHEEIAKRKEEGEGLTWEDYKSMKYTWQ 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   389 VLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAtpriqhPFGSVP 468
Cdd:cd11043 278 VINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV------PYTFLP 351
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 399288   469 FGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:cd11043 352 FGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPDE 388
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
262-504 3.63e-35

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: 136.29  E-value: 3.63e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   262 RPVLPF--WKRYLDGWNAIFSFGKKLIDEKLE----DMEAQL-QAAGPDGiqvsgylhfllasGQLSPREAMGSLPELLM 334
Cdd:cd11045 155 RTPIPGtrWWRGLRGRRYLEEYFRRRIPERRAgggdDLFSALcRAEDEDG-------------DRFSDDDIVNHMIFLMM 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVvpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD 414
Cdd:cd11045 222 AAHDTTTSTLTSMAYFLARHPEWQERLREESLAL--GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVL 299
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   415 GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWlrnSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd11045 300 GYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERF---SPERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQML 376
                       250
                ....*....|
gi 399288   495 QKYKVVLAPE 504
Cdd:cd11045 377 RRFRWWSVPG 386
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
332-505 6.05e-35

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: 135.81  E-value: 6.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpaGQVPQHKDFAH---MPLLKAVLKETLRLYPVVPTNSRIIE 408
Cdd:cd11042 220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVL--GDGDDPLTYDVlkeMPLLHACIKETLRLHPPIHSLMRKAR 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   409 KEIEVD--GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFgsVPFGYGVRACLGRRIAELEM 486
Cdd:cd11042 298 KPFEVEggGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGGKFAY--LPFGAGRHRCIGENFAYLQI 375
                       170
                ....*....|....*....
gi 399288   487 QLLLARLIQKYKVVLAPET 505
Cdd:cd11042 376 KTILSTLLRNFDFELVDSP 394
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
326-520 9.55e-35

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


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 135.42  E-value: 9.55e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   326 MGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-S 404
Cdd:cd11027 231 VMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLAlP 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   405 RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsQPATPRIQHPFGSVPFGYGVRACLGRRIAEL 484
Cdd:cd11027 311 HKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFL---DENGKLVPKPESFLPFSAGRRVCLGESLAKA 387
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 399288   485 EMQLLLARLIQKYKVVLAPETG--ELKSVARIVLVPNK 520
Cdd:cd11027 388 ELFLFLARLLQKFRFSPPEGEPppELEGIPGLVLYPLP 425
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
228-499 9.41e-34

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: 132.76  E-value: 9.41e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   228 CLQRSIPEDTVTFVRSIGLMFQNSLY----ATFL--PKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAG 301
Cdd:cd20621 126 INGKEIQVELVEILIESFLYRFSSPYfqlkRLIFgrKSWKLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKNKDEIK 205
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   302 PDGIQVSGYLhflLASGQLSPREamgSLPELL-------MAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQV 374
Cdd:cd20621 206 DIIIDLDLYL---LQKKKLEQEI---TKEEIIqqfitffFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDD 279
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   375 PQHKDFAHMPLLKAVLKETLRLYPVVP-TNSRIIEKEIEVDGFLFPKNTqFVFCHY-VVSRDPTAFSEPESFQPHRWLrN 452
Cdd:cd20621 280 ITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQIGDLKIKKGW-IVNVGYiYNHFNPKYFENPDEFNPERWL-N 357
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 399288   453 SQPATpriQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKV 499
Cdd:cd20621 358 QNNIE---DNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEI 401
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
213-520 1.98e-33

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


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 131.81  E-value: 1.98e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   213 ALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLED 292
Cdd:cd20680 121 ALDIICETAMGKKIGAQSNKDSEYVQAVYRMSDIIQRRQKMPWLWLDLWYLMFKEGKEHNKNLKILHTFTDNVIAERAEE 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   293 MEAQLQAAGPDGIQVSG------YLHFLL-----ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEAL 361
Cdd:cd20680 201 MKAEEDKTGDSDGESPSkkkrkaFLDMLLsvtdeEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKV 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   362 HEEVVGVVPAGQVP-QHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSE 440
Cdd:cd20680 281 HKELDEVFGKSDRPvTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPE 360
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   441 PESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNK 520
Cdd:cd20680 361 PEEFRPERFF----PENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQKREELGLVGELILRPQN 436
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
331-495 6.42e-33

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


Pssm-ID: 410748  Cd Length: 433  Bit Score: 130.41  E-value: 6.42e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKE 410
Cdd:cd20655 235 DLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEG 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAT---PRIQHpFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20655 315 CKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQeldVRGQH-FKLLPFGSGRRGCPGASLAYQVVG 393

                ....*...
gi 399288   488 LLLARLIQ 495
Cdd:cd20655 394 TAIAAMVQ 401
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
333-525 9.10e-33

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


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 129.84  E-value: 9.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   333 LMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIE 412
Cdd:cd20650 237 IFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVE 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   413 VDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLR-NSQPATPRIQHPFGSVPfgygvRACLGRRIAELEMQLLLA 491
Cdd:cd20650 317 INGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKkNKDNIDPYIYLPFGSGP-----RNCIGMRFALMNMKLALV 391
                       170       180       190
                ....*....|....*....|....*....|....*
gi 399288   492 RLIQKYKVVLAPETG-ELKSVARIVLVPNKKVGLQ 525
Cdd:cd20650 392 RVLQNFSFKPCKETQiPLKLSLQGLLQPEKPIVLK 426
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
278-505 1.23e-32

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


Pssm-ID: 410759  Cd Length: 426  Bit Score: 129.51  E-value: 1.23e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   278 IFSFGKKLIdeklEDMEAQLQAAGP-DGIQVsgylhFLLASGQLSPREAMGSLPE---------LLMAGVDTTSNTLTWA 347
Cdd:cd20666 181 ITAFLKKII----ADHRETLDPANPrDFIDM-----YLLHIEEEQKNNAESSFNEdylfyiigdLFIAGTDTTTNTLLWC 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   348 LYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVP-TNSRIIEKEIEVDGFLFPKNTQFVF 426
Cdd:cd20666 252 LLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPlSIPHMASENTVLQGYTIPKGTVIVP 331
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   427 CHYVVSRDPTAFSEPESFQPHRWL-RNSQpatprIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:cd20666 332 NLWSVHRDPAIWEKPDDFMPSRFLdENGQ-----LIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNA 406
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
319-503 1.95e-31

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: 126.15  E-value: 1.95e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   319 QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYP 398
Cdd:cd11068 225 KLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVL-GDDPPPYEQVAKLRYIRRVLDETLRLWP 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   399 VVPTNSRIIEKEIEVDG-FLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRNSQPATPRiqHPFGsvPFGYGVRAC 476
Cdd:cd11068 304 TAPAFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWGEdAEEFRPERFLPEEFRKLPP--NAWK--PFGNGQRAC 379
                       170       180
                ....*....|....*....|....*..
gi 399288   477 LGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11068 380 IGRQFALQEATLVLAMLLQRFDFEDDP 406
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
253-504 2.08e-31

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


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 125.79  E-value: 2.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   253 YATFLPkWTRPVLPFWKRY---LDGWNAIFSFGKKLIDEKLEDMEaqlqaagPDGIQ--VSGYLHFLLASGQLSP---RE 324
Cdd:cd20651 153 LLNQFP-WLRFIAPEFSGYnllVELNQKLIEFLKEEIKEHKKTYD-------EDNPRdlIDAYLREMKKKEPPSSsftDD 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   325 --AMGSLpELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVP- 401
Cdd:cd20651 225 qlVMICL-DLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPi 303
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   402 TNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNsqpaTPRIQHPFGSVPFGYGVRACLGRRI 481
Cdd:cd20651 304 GIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDE----DGKLLKDEWFLPFGAGKRRCLGESL 379
                       250       260
                ....*....|....*....|...
gi 399288   482 AELEMQLLLARLIQKYKVVLAPE 504
Cdd:cd20651 380 ARNELFLFFTGLLQNFTFSPPNG 402
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
283-497 9.03e-31

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


Pssm-ID: 410750  Cd Length: 438  Bit Score: 124.46  E-value: 9.03e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   283 KKL---IDEKLEDMEAQLQAAGPDGIQVSGYLHFLLAS-------GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLS 352
Cdd:cd20657 177 KRLhkrFDALLTKILEEHKATAQERKGKPDFLDFVLLEnddngegERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELI 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   353 KDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVV 431
Cdd:cd20657 257 RHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNlPRIASEACEVDGYYIPKGTRLLVNIWAI 336
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 399288   432 SRDPTAFSEPESFQPHRWL--RNSQpATPRIQHpFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKY 497
Cdd:cd20657 337 GRDPDVWENPLEFKPERFLpgRNAK-VDVRGND-FELIPFGAGRRICAGTRMGIRMVEYILATLVHSF 402
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
278-495 1.87e-30

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


Pssm-ID: 410696  Cd Length: 435  Bit Score: 123.41  E-value: 1.87e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   278 IFSFGKKLIDEKLEDMEAQlQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEI 357
Cdd:cd11073 186 LFDIFDGFIDERLAEREAG-GDKKKDDDLLLLLDLELDSESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEK 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   358 QEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPT 436
Cdd:cd11073 265 MAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLpRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPS 344
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 399288   437 AFSEPESFQPHRWLRNSqpatprIQ---HPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQ 495
Cdd:cd11073 345 VWEDPLEFKPERFLGSE------IDfkgRDFELIPFGSGRRICPGLPLAERMVHLVLASLLH 400
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
92-516 3.34e-30

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: 122.52  E-value: 3.34e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    92 YGPMWMSYLGPQMHVNLASAPLLEQVM-RQEGKYPVRNDMELWK-EHRDQHDLTYGPFTTEghhWYQLRQALNQRLLKpa 169
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALvRKWADFAGRPHSYTGKlVSQGGQDLSLGDYSLL---WKAHRKLTRSALQL-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   170 eaalytdAFNEVIDDFMTRLDQLRAE--SASGNQVSDMAQLFYYFALEAICYILFEKRigclqrsipEDTVTFVRSIGLM 247
Cdd:cd20674  76 -------GIRNSLEPVVEQLTQELCErmRAQAGTPVDIQEEFSLLTCSIICCLTFGDK---------EDKDTLVQAFHDC 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   248 FQNslyatFLPKWTRP------VLPFWKRYLdgwNAIFSFGKKLIDEKLEDMEAQLQA------AGPDGIQVSGYLHFLL 315
Cdd:cd20674 140 VQE-----LLKTWGHWsiqaldSIPFLRFFP---NPGLRRLKQAVENRDHIVESQLRQhkeslvAGQWRDMTDYMLQGLG 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   316 ASGQLSPREAMG------SLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAV 389
Cdd:cd20674 212 QPRGEKGMGQLLeghvhmAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNAT 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   390 LKETLRLYPVVPTN--SRIIeKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpATPRIqhpfgsV 467
Cdd:cd20674 292 IAEVLRLRPVVPLAlpHRTT-RDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGA-ANRAL------L 363
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 399288   468 PFGYGVRACLGRRIAELEMQLLLARLIQKYKvVLAPETGELKS---VARIVL 516
Cdd:cd20674 364 PFGCGARVCLGEPLARLELFVFLARLLQAFT-LLPPSDGALPSlqpVAGINL 414
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
158-506 4.78e-30

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


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 122.04  E-value: 4.78e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   158 RQALNQRLLKPAEAAlYTDAFNEVIDDFMTrldQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGC-----LQRS 232
Cdd:cd11066  68 RKAAASALNRPAVQS-YAPIIDLESKSFIR---ELLRDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCvdddsLLLE 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   233 I--PEDTVTFVRSiglmfQNSLYATFLPkwtrpVLpfwkRYLDGWNAIFSFGKKLIDEKLEDME---AQLQAAGPDGIQV 307
Cdd:cd11066 144 IieVESAISKFRS-----TSSNLQDYIP-----IL----RYFPKMSKFRERADEYRNRRDKYLKkllAKLKEEIEDGTDK 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   308 SGYLHFLL--ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDP--EIQEALHEEVVGVVPAGQVPQHKDFAHM 383
Cdd:cd11066 210 PCIVGNILkdKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAEE 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   384 --PLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRI 460
Cdd:cd11066 290 kcPYVVALVKETLRYFTVLPLGlPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGP 369
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 399288   461 QHpFGsvpFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETG 506
Cdd:cd11066 370 PH-FS---FGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEE 411
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
144-508 1.11e-29

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


Pssm-ID: 410652  Cd Length: 425  Bit Score: 120.74  E-value: 1.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   144 YGPFTTEGHHWYQLRQ--------------ALNQRLLkpAEAALYTDAFNEviddfmtrldqlraesaSGNQVSDMAQLF 209
Cdd:cd11026  50 YGVVFSNGERWKQLRRfslttlrnfgmgkrSIEERIQ--EEAKFLVEAFRK-----------------TKGKPFDPTFLL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   210 YYFALEAICYILFEKRIGC-------LQRSIPEdTVTFVRSIGLMfqnsLYATFlPKWTRPVLPFWKRYLDGWNAIFSFG 282
Cdd:cd11026 111 SNAVSNVICSIVFGSRFDYedkeflkLLDLINE-NLRLLSSPWGQ----LYNMF-PPLLKHLPGPHQKLFRNVEEIKSFI 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   283 KKLIDEKLEDMEAQ----------LQAAGPDGIQVSGYlhfllasgqlSPREAMGSLPELLMAGVDTTSNTLTWALYHLS 352
Cdd:cd11026 185 RELVEEHRETLDPSsprdfidcflLKMEKEKDNPNSEF----------HEENLVMTVLDLFFAGTETTSTTLRWALLLLM 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   353 KDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVV 431
Cdd:cd11026 255 KYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGvPHAVTRDTKFRGYTIPKGTTVIPNLTSV 334
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 399288   432 SRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGEL 508
Cdd:cd11026 335 LRDPKQWETPEEFNPGHFLDEQG----KFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKDP 407
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
92-503 2.04e-28

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


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 117.44  E-value: 2.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288    92 YGPMWMSYLGPQMHVNLASAPLLEQVMRQ----EGKYPVRNDMELWkehrdqhdLTYGPFTTEGHHWYQLRqalnqRLLK 167
Cdd:cd11052  11 YGKNFLYWYGTDPRLYVTEPELIKELLSKkegyFGKSPLQPGLKKL--------LGRGLVMSNGEKWAKHR-----RIAN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   168 PAEAA----LYTDAfneVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKrigclqrSIPEDTVTF--V 241
Cdd:cd11052  78 PAFHGeklkGMVPA---MVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGS-------SYEEGKEVFklL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   242 RSIGLMFQNSLYATFLPKW----TRPVLPFWKryLDgwNAIFSFGKKLIDEKLEDMEAqlqaaGPDGIQVSGYLHFLLAS 317
Cdd:cd11052 148 RELQKICAQANRDVGIPGSrflpTKGNKKIKK--LD--KEIEDSLLEIIKKREDSLKM-----GRGDDYGDDLLGLLLEA 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   318 GQLSPREAMGSLPELL-------MAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKdFAHMPLLKAVL 390
Cdd:cd11052 219 NQSDDQNKNMTVQEIVdecktffFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDS-LSKLKTVSMVI 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   391 KETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRNSQPATpriQHPFGSVPF 469
Cdd:cd11052 298 NESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKAA---KHPMAFLPF 374
                       410       420       430
                ....*....|....*....|....*....|....
gi 399288   470 GYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11052 375 GLGPRNCIGQNFATMEAKIVLAMILQRFSFTLSP 408
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
147-502 2.24e-28

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


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 116.97  E-value: 2.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   147 FTTEGHHWYQLRQALNqrllkPAEAALY----TDAFNEVIDDFMTRLDQLrAESasgNQVSDMAQLFYYFALEAICYILF 222
Cdd:cd11051  50 ISMEGEEWKRLRKRFN-----PGFSPQHlmtlVPTILDEVEIFAAILREL-AES---GEVFSLEELTTNLTFDVIGRVTL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 399288   223 EKRIGClQRSIPEDTvTFVRSIGLMFQNSLyatFLPKWTRPVLPfWKRYLDGwNAIFSFG