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Conserved domains on  [gi|568941360|ref|XP_006505943|]
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thromboxane-A synthase isoform X6 [Mus musculus]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 2-409 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 cd20649:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 457  Bit Score: 678.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   2 VADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQV 81
Cdd:cd20649   48 MSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  82 DSQNSPEDPFVQHCRRASTFCIPRPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFL 161
Cdd:cd20649  128 DSQKNPDDPFVKNCKRFFEFSFFRPILILFLAFPFIMIPLARILPNKSRDELNSFFTQCIRNMIAFRDQQSPEERRRDFL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 162 QMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPTSTS---KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYL 238
Cdd:cd20649  208 QLMLDARTSAKFLSVEHFDIVNDADESAYDGHPNSPANEQTKPSkqkRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYL 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVG 318
Cdd:cd20649  288 LATHPECQKKLLREVDEFFSKHEMVDYANVQE-LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVG 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 319 ALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLES 398
Cdd:cd20649  367 FLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLKS 446

                        410
                 ....*....|.
gi 568941360 399 KSALGPKNGVY 409
Cdd:cd20649  447 KSTLGPKNGVY 457
 
Name Accession Description Interval E-value
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 2-409 0e+00

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


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 678.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   2 VADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQV 81
Cdd:cd20649   48 MSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  82 DSQNSPEDPFVQHCRRASTFCIPRPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFL 161
Cdd:cd20649  128 DSQKNPDDPFVKNCKRFFEFSFFRPILILFLAFPFIMIPLARILPNKSRDELNSFFTQCIRNMIAFRDQQSPEERRRDFL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 162 QMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPTSTS---KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYL 238
Cdd:cd20649  208 QLMLDARTSAKFLSVEHFDIVNDADESAYDGHPNSPANEQTKPSkqkRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYL 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVG 318
Cdd:cd20649  288 LATHPECQKKLLREVDEFFSKHEMVDYANVQE-LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVG 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 319 ALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLES 398
Cdd:cd20649  367 FLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLKS 446

                        410
                 ....*....|.
gi 568941360 399 KSALGPKNGVY 409
Cdd:cd20649  447 KSTLGPKNGVY 457
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 6-412 5.83e-81

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: 256.44  E-value: 5.83e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360    6 VLLLRDRRWEEVRGALMSSF-SPEKLdEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQ 84
Cdd:pfam00067  87 IVFANGPRWRQLRRFLTPTFtSFGKL-SFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFGSL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   85 NSPEDP----FVQHcrRASTFCIPRPLLVLILsfpsimvPLARILPNKNRDELNGFFNT---LIRNVIALRDQ--QAAEE 155
Cdd:pfam00067 166 EDPKFLelvkAVQE--LSSLLSSPSPQLLDLF-------PILKYFPGPHGRKLKRARKKikdLLDKLIEERREtlDSAKK 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  156 RRRDFLQMVLDAQHSMNSVGvegfdmvpeslsssectkeppqrchptstskpFTVDEIVGQAFLFLIAGHEVITNTLSFI 235
Cdd:pfam00067 237 SPRDFLDALLLAKEEEDGSK--------------------------------LTDEELRATVLELFFAGTDTTSSTLSWA 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  236 TYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLE 314
Cdd:pfam00067 285 LYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQN-MPYLDAVIKETLRLHPVVpLLLPREVTKDTVIPGYLIPKGTLVI 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  315 IAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPL 394
Cdd:pfam00067 364 VNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443

                         410
                  ....*....|....*...
gi 568941360  395 QLESKSALGPKNGVYIKI 412
Cdd:pfam00067 444 IDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 1-395 7.49e-56

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


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 189.33  E-value: 7.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   1 MVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLkryaASRDAFNIQRCYCCYTIDVVASVAFGtq 80
Cdd:COG2124   78 LLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRL----AARGPVDLVEEFARPLPVIVICELLG-- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  81 VDSQNspEDPFVQHCRRASTFCIPRPLLvlilsfpsimvPLARILpnKNRDELNGFFNTLIrnvialrdqqaaEERRR-- 158
Cdd:COG2124  152 VPEED--RDRLRRWSDALLDALGPLPPE-----------RRRRAR--RARAELDAYLRELI------------AERRAep 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 159 --DFLQMVLDAQHsmnsvgvegfdmvpeslsssectkeppqrchptsTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFIT 236
Cdd:COG2124  205 gdDLLSALLAARD----------------------------------DGERLSDEELRDELLLLLLAGHETTANALAWAL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 237 YLLATHPDCQERLlkevdlfmgkhpapeyhslQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIA 316
Cdd:COG2124  251 YALLRHPEQLARL-------------------RAEPELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLS 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 317 VGALHHDPEHWPNPETFDPErftaearlqRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFR-FEASPETQVPLQ 395
Cdd:COG2124  312 LAAANRDPRVFPDPDRFDPD---------RPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLAPPEELRWR 382
PLN02290 PLN02290
cytokinin trans-hydroxylase
 220-410 2.09e-29

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 119.53  E-value: 2.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 220 FLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPaPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQD 299
Cdd:PLN02290 324 FFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGET-PSVDHLSK-LTLLNMVINESLRLYPPATLLPRMAFED 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 300 CEVLGQRIPAGTVLEIAVGALHHDPEHW-PNPETFDPERFTAEARLQRRPFtyLPFGAGPRSCLGVRLGLLVVKLTILQV 378
Cdd:PLN02290 402 IKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHF--IPFAAGPRNCIGQAFAMMEAKIILAML 479

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568941360 379 LHKFRFEASPETQ-VPLQLESksaLGPKNGVYI 410
Cdd:PLN02290 480 ISKFSFTISDNYRhAPVVVLT---IKPKYGVQV 509
 
Name Accession Description Interval E-value
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 2-409 0e+00

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


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 678.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   2 VADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQV 81
Cdd:cd20649   48 MSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  82 DSQNSPEDPFVQHCRRASTFCIPRPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFL 161
Cdd:cd20649  128 DSQKNPDDPFVKNCKRFFEFSFFRPILILFLAFPFIMIPLARILPNKSRDELNSFFTQCIRNMIAFRDQQSPEERRRDFL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 162 QMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPTSTS---KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYL 238
Cdd:cd20649  208 QLMLDARTSAKFLSVEHFDIVNDADESAYDGHPNSPANEQTKPSkqkRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYL 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVG 318
Cdd:cd20649  288 LATHPECQKKLLREVDEFFSKHEMVDYANVQE-LPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVG 366

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 319 ALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLES 398
Cdd:cd20649  367 FLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLKS 446

                        410
                 ....*....|.
gi 568941360 399 KSALGPKNGVY 409
Cdd:cd20649  447 KSTLGPKNGVY 457
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 5-409 2.35e-169

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: 480.93  E-value: 2.35e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   5 SVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQ 84
Cdd:cd11055   51 SLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQ 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  85 NSPEDPFVQHCRRAstFCIPRPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQaAEERRRDFLQMV 164
Cdd:cd11055  131 NNPDDPFLKAAKKI--FRNSIIRLFLLLLLFPLRLFLFLLFPFVFGFKSFSFLEDVVKKIIEQRRKN-KSSRRKDLLQLM 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 165 LDAQHSmnsvgvegfdmvpeslsssectkeppqrcHPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPD 244
Cdd:cd11055  208 LDAQDS-----------------------------DEDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPD 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 245 CQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDP 324
Cdd:cd11055  259 VQEKLIEEIDEVLPDDGSPTYDTVSK-LKYLDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDP 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 325 EHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSALGP 404
Cdd:cd11055  338 EFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSP 417


                 ....*
gi 568941360 405 KNGVY 409
Cdd:cd11055  418 KNGIY 422
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 8-409 1.55e-118

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: 351.84  E-value: 1.55e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   8 LLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSP 87
Cdd:cd11056   55 SLDGEKWKELRQKLTPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDP 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  88 EDPFVQHCRRASTfciPRPLLVLILSFPSIMVPLARILPNK-NRDELNGFFNTLIRNVIALRdqQAAEERRRDFLQMVLD 166
Cdd:cd11056  135 ENEFREMGRRLFE---PSRLRGLKFMLLFFFPKLARLLRLKfFPKEVEDFFRKLVRDTIEYR--EKNNIVRNDFIDLLLE 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 167 AQHSmnsvgvegfdmvpESLSSSECTKEppqrchptstskpFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQ 246
Cdd:cd11056  210 LKKK-------------GKIEDDKSEKE-------------LTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQ 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 247 ERLLKEVDLFMGKHPAP-EYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQR--IPAGTVLEIAVGALHHD 323
Cdd:cd11056  264 EKLREEIDEVLEKHGGElTYEALQE-MKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvvIEKGTPVIIPVYALHHD 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 324 PEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSA-L 402
Cdd:cd11056  343 PKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKLSPKSFvL 422


                 ....*..
gi 568941360 403 GPKNGVY 409
Cdd:cd11056  423 SPKGGIW 429
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 3-411 1.46e-98

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: 300.49  E-value: 1.46e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   3 ADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVD 82
Cdd:cd20650   49 KSAISIAEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNID 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  83 SQNSPEDPFVQHCRRASTFCIPRPLLVLILSFPSimvpLARILPNKN-----RDELNgFFNTLIRNVIA--LRDQQaaeE 155
Cdd:cd20650  129 SLNNPQDPFVENTKKLLKFDFLDPLFLSITVFPF----LTPILEKLNisvfpKDVTN-FFYKSVKKIKEsrLDSTQ---K 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 156 RRRDFLQMVLDAQHSMNsvgvegfdmvpeslsssectkeppqrchpTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFI 235
Cdd:cd20650  201 HRVDFLQLMIDSQNSKE-----------------------------TESHKALSDLEILAQSIIFIFAGYETTSSTLSFL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 236 TYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEI 315
Cdd:cd20650  252 LYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQ-MEYLDMVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTVVMI 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 316 AVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQ 395
Cdd:cd20650  331 PTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPLK 410

                        410
                 ....*....|....*.
gi 568941360 396 LESKSALGPKNGVYIK 411
Cdd:cd20650  411 LSLQGLLQPEKPIVLK 426
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 4-410 3.06e-81

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: 255.91  E-value: 3.06e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   4 DSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASrDAFNIQRCYCCYTIDVVASVAFGTQVDS 83
Cdd:cd20628   47 DGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNENSKILVEKLKKKAGG-GEFDIFPYISLCTLDIICETAMGVKLNA 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  84 QNSPEDPFVQHCRRASTfCIPRPLLVLILSFPSI--MVPLARILpNKNRDELNGFFNTLIRNVIALRDQQAAEE------ 155
Cdd:cd20628  126 QSNEDSEYVKAVKRILE-IILKRIFSPWLRFDFIfrLTSLGKEQ-RKALKVLHDFTNKVIKERREELKAEKRNSeeddef 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 156 ---RRRDFLQMVLDAqhsmnsvgvegfdmvpeslsssectkeppqrchpTSTSKPFTVDEIVGQAFLFLIAGHEVITNTL 232
Cdd:cd20628  204 gkkKRKAFLDLLLEA----------------------------------HEDGGPLTDEDIREEVDTFMFAGHDTTASAI 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 233 SFITYLLATHPDCQERLLKEVDLFMGKHP-APEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGT 311
Cdd:cd20628  250 SFTLYLLGLHPEVQEKVYEELDEIFGDDDrRPTLEDLNK-MKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGT 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 312 VLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQ 391
Cdd:cd20628  329 TVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGE 408

                        410
                 ....*....|....*....
gi 568941360 392 vPLQLESKSALGPKNGVYI 410
Cdd:cd20628  409 -DLKLIAEIVLRSKNGIRV 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 6-412 5.83e-81

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: 256.44  E-value: 5.83e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360    6 VLLLRDRRWEEVRGALMSSF-SPEKLdEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQ 84
Cdd:pfam00067  87 IVFANGPRWRQLRRFLTPTFtSFGKL-SFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFGSL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   85 NSPEDP----FVQHcrRASTFCIPRPLLVLILsfpsimvPLARILPNKNRDELNGFFNT---LIRNVIALRDQ--QAAEE 155
Cdd:pfam00067 166 EDPKFLelvkAVQE--LSSLLSSPSPQLLDLF-------PILKYFPGPHGRKLKRARKKikdLLDKLIEERREtlDSAKK 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  156 RRRDFLQMVLDAQHSMNSVGvegfdmvpeslsssectkeppqrchptstskpFTVDEIVGQAFLFLIAGHEVITNTLSFI 235
Cdd:pfam00067 237 SPRDFLDALLLAKEEEDGSK--------------------------------LTDEELRATVLELFFAGTDTTSSTLSWA 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  236 TYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLE 314
Cdd:pfam00067 285 LYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQN-MPYLDAVIKETLRLHPVVpLLLPREVTKDTVIPGYLIPKGTLVI 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  315 IAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPL 394
Cdd:pfam00067 364 VNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443

                         410
                  ....*....|....*...
gi 568941360  395 QLESKSALGPKNGVYIKI 412
Cdd:pfam00067 444 IDETPGLLLPPKPYKLKF 461
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 4-411 1.82e-69

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: 225.51  E-value: 1.82e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   4 DSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDS 83
Cdd:cd20659   47 DGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVYNECTDILLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNC 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  84 QNS-PEDPFVQHCRRASTFCIPRpLLVLILSFPSI--MVPLARILpNKNRDELNGFFNTLI---RNVIALRDQQAAEERR 157
Cdd:cd20659  127 QQTgKNHPYVAAVHELSRLVMER-FLNPLLHFDWIyyLTPEGRRF-KKACDYVHKFAEEIIkkrRKELEDNKDEALSKRK 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 158 R-DFLQMVLDAQhsmnsvgvegfdmvpeslsssectkeppqrchpTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFIT 236
Cdd:cd20659  205 YlDFLDILLTAR---------------------------------DEDGKGLTDEEIRDEVDTFLFAGHDTTASGISWTL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 237 YLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIA 316
Cdd:cd20659  252 YSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSK-LPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAIN 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 317 VGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQL 396
Cdd:cd20659  331 IYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKP 410

                        410
                 ....*....|....*
gi 568941360 397 EskSALGPKNGVYIK 411
Cdd:cd20659  411 G--LVLRSKNGIKLK 423
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 1-408 2.08e-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: 219.31  E-value: 2.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   1 MVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFN--IQRcyccYTIDVVASVAFG 78
Cdd:cd00302   46 FLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIREIARELLDRLAAGGEVGDDVAdlAQP----LALDVIARLLGG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  79 TQVDSQNspeDPFVQHCRRastfciprpllvLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRR 158
Cdd:cd00302  122 PDLGEDL---EELAELLEA------------LLKLLGPRLLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDL 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 159 DFLQMVLDAQhsmnsvgvegfdmvpeslsssectkeppqrchptstskPFTVDEIVGQAFLFLIAGHEVITNTLSFITYL 238
Cdd:cd00302  187 LLLADADDGG--------------------------------------GLSDEEIVAELLTLLLAGHETTASLLAWALYL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPapeyHSLQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVG 318
Cdd:cd00302  229 LARHPEVQERLRAEIDAVLGDGT----PEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLY 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 319 ALHHDPEHWPNPETFDPERFTAEARlqRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLES 398
Cdd:cd00302  305 AAHRDPEVFPDPDEFDPERFLPERE--EPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRPSL 382

                        410
                 ....*....|
gi 568941360 399 KSaLGPKNGV 408
Cdd:cd00302  383 GT-LGPASLP 391
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 13-408 7.78e-64

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: 210.84  E-value: 7.78e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPF- 91
Cdd:cd20613   73 KWKKRRAILNPAFHRKYLKNLMDEFNESADLLVEKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDSPFp 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  92 --VQHCRRASTFCIPRPLLVLIlsfpsimvPLARILPNKNRDELNgFFNTLIRNVIALR--DQQAAEERRRDFLQMVLDA 167
Cdd:cd20613  153 kaISLVLEGIQESFRNPLLKYN--------PSKRKYRREVREAIK-FLRETGRECIEERleALKRGEEVPNDILTHILKA 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 168 qhsmnSVGVEGFDMvpESLsssectkeppqrchptstskpftVDEIVgqafLFLIAGHEVITNTLSFITYLLATHPDCQE 247
Cdd:cd20613  224 -----SEEEPDFDM--EEL-----------------------LDDFV----TFFIAGQETTANLLSFTLLELGRHPEILK 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 248 RLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHW 327
Cdd:cd20613  270 RLQAEVDEVLGSKQYVEYEDLGK-LEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYF 348

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 328 PNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPeTQvPLQLESKSALGPKNG 407
Cdd:cd20613  349 EDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELVP-GQ-SFGILEEVTLRPKDG 426


                 .
gi 568941360 408 V 408
Cdd:cd20613  427 V 427
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 14-410 2.05e-63

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: 208.97  E-value: 2.05e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  14 WEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAAsRDAFNIQRCYCCYTIDVVASVAFGTQVDSQnspedpfVQ 93
Cdd:cd20620   58 WRRQRRLAQPAFHRRRIAAYADAMVEATAALLDRWEAGAR-RGPVDVHAEMMRLTLRIVAKTLFGTDVEGE-------AD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  94 HCRRASTFCIPRpLLVLILSFpsIMVPLARILP-----NKNRDELNGFFNTLIRnvialrDQQAAEERRRDFLQMVLDAQ 168
Cdd:cd20620  130 EIGDALDVALEY-AARRMLSP--FLLPLWLPTPanrrfRRARRRLDEVIYRLIA------ERRAAPADGGDLLSMLLAAR 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 169 HSmnsvgvegfdmvpeslsssectkeppqrchptSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQER 248
Cdd:cd20620  201 DE--------------------------------ETGEPMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAAR 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 249 LLKEVDLFMG-KHPAPEyhSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHW 327
Cdd:cd20620  249 LRAEVDRVLGgRPPTAE--DLPQ-LPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFW 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 328 PNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVplQLESKSALGPKNG 407
Cdd:cd20620  326 PDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPV--EPEPLITLRPKNG 403


                 ...
gi 568941360 408 VYI 410
Cdd:cd20620  404 VRM 406
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 18-393 6.61e-63

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: 208.66  E-value: 6.61e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  18 RGALMSSFSPEKLDEMTPLIS----QACELLVAHLKRYAASRDAFNIQ----RCyccyTIDVVASVAFGTQVDSQNSPED 89
Cdd:cd11069   65 RKILNPAFSYRHVKELYPIFWskaeELVDKLEEEIEESGDESISIDVLewlsRA----TLDIIGLAGFGYDFDSLENPDN 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  90 PFVQHCRRAstFCIPRPLLVLILSFPSIMVPLARILPNKNRDELN---GFFNTLIRNVIALRDQQAAEERR---RDFLQM 163
Cdd:cd11069  141 ELAEAYRRL--FEPTLLGSLLFILLLFLPRWLVRILPWKANREIRrakDVLRRLAREIIREKKAALLEGKDdsgKDILSI 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 164 VLdaqhsmnsvgvegfdmvpeslsssectkeppqRCHPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHP 243
Cdd:cd11069  219 LL--------------------------------RANDFADDERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHP 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 244 DCQERLLKEV-DLFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHH 322
Cdd:cd11069  267 DVQERLREEIrAALPDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINR 346

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941360 323 DPEHW-PNPETFDPERF-----TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVP 393
Cdd:cd11069  347 SPEIWgPDAEEFNPERWlepdgAASPGGAGSNYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVE 423
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 9-387 5.69e-59

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: 198.21  E-value: 5.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   9 LRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAaSRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPE 88
Cdd:cd11057   50 APYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQKLVQRLDTYV-GGGEFDILPDLSRCTLEMICQTTLGSDVNDESDGN 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  89 DPFVQHCRRASTFCIPRPLLV-LILSFPSIMVPLARiLPNKNRDELNGFFNTLI---RNVIALRDQQAAEE------RRR 158
Cdd:cd11057  129 EEYLESYERLFELIAKRVLNPwLHPEFIYRLTGDYK-EEQKARKILRAFSEKIIekkLQEVELESNLDSEEdeengrKPQ 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 159 DFLQMVLDAQHSmnsvgvegfdmvpeslsssectkeppqrchptstSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYL 238
Cdd:cd11057  208 IFIDQLLELARN----------------------------------GEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLL 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEV-DLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEV-LGQRIPAGTVLEIA 316
Cdd:cd11057  254 LAMHPEVQEKVYEEImEVFPDDGQFITYEDLQQ-LVYLEMVLKETMRLFPVGPLVGRETTADIQLsNGVVIPKGTTIVID 332

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568941360 317 VGALHHDPEHW-PNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEAS 387
Cdd:cd11057  333 IFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTS 404
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 1-395 7.49e-56

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


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 189.33  E-value: 7.49e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   1 MVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLkryaASRDAFNIQRCYCCYTIDVVASVAFGtq 80
Cdd:COG2124   78 LLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRL----AARGPVDLVEEFARPLPVIVICELLG-- 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  81 VDSQNspEDPFVQHCRRASTFCIPRPLLvlilsfpsimvPLARILpnKNRDELNGFFNTLIrnvialrdqqaaEERRR-- 158
Cdd:COG2124  152 VPEED--RDRLRRWSDALLDALGPLPPE-----------RRRRAR--RARAELDAYLRELI------------AERRAep 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 159 --DFLQMVLDAQHsmnsvgvegfdmvpeslsssectkeppqrchptsTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFIT 236
Cdd:COG2124  205 gdDLLSALLAARD----------------------------------DGERLSDEELRDELLLLLLAGHETTANALAWAL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 237 YLLATHPDCQERLlkevdlfmgkhpapeyhslQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIA 316
Cdd:COG2124  251 YALLRHPEQLARL-------------------RAEPELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLS 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 317 VGALHHDPEHWPNPETFDPErftaearlqRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFR-FEASPETQVPLQ 395
Cdd:COG2124  312 LAAANRDPRVFPDPDRFDPD---------RPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLAPPEELRWR 382
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 5-408 4.09e-53

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: 182.40  E-value: 4.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   5 SVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHL---KRYAASRDAFNIqrcyccyTIDVVASVAFGTQV 81
Cdd:cd11053   62 SLLLLDGDRHRRRRKLLMPAFHGERLRAYGELIAEITEREIDRWppgQPFDLRELMQEI-------TLEVILRVVFGVDD 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  82 DSQnspEDPFVQHCRRASTFcIPRPLLvlilSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAEERRrDFL 161
Cdd:cd11053  135 GER---LQELRRLLPRLLDL-LSSPLA----SFPALQRDLGPWSPWGRFLRARRRIDALIYAEIAERRAEPDAERD-DIL 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 162 QMVLDAQHSMNSvgvegfdmvpeslsssectkeppqrchptstskPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLAT 241
Cdd:cd11053  206 SLLLSARDEDGQ---------------------------------PLSDEELRDELMTLLFAGHETTATALAWAFYWLHR 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 242 HPDCQERLLKEVDLFMGKHPAPEYhslqEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALH 321
Cdd:cd11053  253 HPEVLARLLAELDALGGDPDPEDI----AKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTH 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 322 HDPEHWPNPETFDPERFtaearLQRR--PFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESK 399
Cdd:cd11053  329 HRPDLYPDPERFRPERF-----LGRKpsPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPERPVRRGV 403


                 ....*....
gi 568941360 400 sALGPKNGV 408
Cdd:cd11053  404 -TLAPSRGV 411
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 1-388 4.40e-52

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: 179.84  E-value: 4.40e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   1 MVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDA-FNIQRCYCCYTIDVVASVAFGT 79
Cdd:cd11052   56 LLGRGLVMSNGEKWAKHRRIANPAFHGEKLKGMVPAMVESVSDMLERWKKQMGEEGEeVDVFEEFKALTADIISRTAFGS 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  80 qvdSQNSPEDPFvqHCRRASTFCIPRpllvlilSFPSIMVPLARILP---NKNRDELNGFFNTLIRNVIALRDQQAAEER 156
Cdd:cd11052  136 ---SYEEGKEVF--KLLRELQKICAQ-------ANRDVGIPGSRFLPtkgNKKIKKLDKEIEDSLLEIIKKREDSLKMGR 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 157 RR----DFLQMVLDAQHSmnsvgvegfdmvpeslsssectkeppqrchpTSTSKPFTVDEIVGQAFLFLIAGHEVITNTL 232
Cdd:cd11052  204 GDdygdDLLGLLLEANQS-------------------------------DDQNKNMTVQEIVDECKTFFFAGHETTALLL 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 233 SFITYLLATHPDCQERLLKEVDLFMGKHpAPEYHSLQeGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTV 312
Cdd:cd11052  253 TWTTMLLAIHPEWQEKAREEVLEVCGKD-KPPSDSLS-KLKTVSMVINESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTS 330

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941360 313 LEIAVGALHHDPEHWPN-PETFDPERFTAE-ARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:cd11052  331 IWIPVLALHHDEEIWGEdANEFNPERFADGvAKAAKHPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTLSP 408
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 199-407 1.01e-51

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: 178.67  E-value: 1.01e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 199 CHPTSTS-KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfMGKhPAPEYHSLqEGLPYLDM 277
Cdd:cd11045  197 CRAEDEDgDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLA-LGK-GTLDYEDL-GQLEVTDW 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 278 VISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRR-PFTYLPFGA 356
Cdd:cd11045  274 VFKEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVhRYAWAPFGG 353

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568941360 357 GPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSAlgPKNG 407
Cdd:cd11045  354 GAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGYYPPWWQSPLPA--PKDG 402
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 11-410 1.04e-51

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: 179.00  E-value: 1.04e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  11 DRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAaSRDAFN----IQRCyccyTIDVVASVAFGTQVDSQNS 86
Cdd:cd20660   54 GEKWHSRRKMLTPTFHFKILEDFLDVFNEQSEILVKKLKKEV-GKEEFDifpyITLC----ALDIICETAMGKSVNAQQN 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  87 PEDPFVQHCRRASTFCIPR---PLLVLILSFPsiMVPLARiLPNKNRDELNGFFNTLIRNVIALR----DQQAAEE---- 155
Cdd:cd20660  129 SDSEYVKAVYRMSELVQKRqknPWLWPDFIYS--LTPDGR-EHKKCLKILHGFTNKVIQERKAELqkslEEEEEDDedad 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 156 ----RRRDFLQMVLDAQHSMNSVGVEgfDMVPEslsssectkeppqrchptstskpftVDeivgqAFLFliAGHEVITNT 231
Cdd:cd20660  206 igkrKRLAFLDLLLEASEEGTKLSDE--DIREE-------------------------VD-----TFMF--EGHDTTAAA 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 232 LSFITYLLATHPDCQERLLKEVDLFMGKHP-APEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAG 310
Cdd:cd20660  252 INWALYLIGSHPEVQEKVHEELDRIFGDSDrPATMDDLKE-MKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKG 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 311 TVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEaSPET 390
Cdd:cd20660  331 TTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIE-SVQK 409

                        410       420
                 ....*....|....*....|
gi 568941360 391 QVPLQLESKSALGPKNGVYI 410
Cdd:cd20660  410 REDLKPAGELILRPVDGIRV 429
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 2-389 2.22e-51

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: 177.80  E-value: 2.22e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   2 VADSVLLLRD-----RRweevRGALMSSFSPEKLDEMTPLISQACELLVAHLKR--YAASRDAFNIQRCYCCYTIDVVAS 74
Cdd:cd11061   41 SASLTFTTRDkaehaRR----RRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDraGKPVSWPVDMSDWFNYLSFDVMGD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  75 VAFGTQVDSQNSPEDPFVQHCRRASTfciprpLLVLILSFPSIMVPLARILP-----NKNRDELNGFFNTLIRNVIalrd 149
Cdd:cd11061  117 LAFGKSFGMLESGKDRYILDLLEKSM------VRLGVLGHAPWLRPLLLDLPlfpgaTKARKRFLDFVRAQLKERL---- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 150 qQAAEERRRDFLQMVLDAqhsmnsvgvegfdmvpeslsssectKEPpqrchptSTSKPFTVDEIVGQAFLFLIAGHEVIT 229
Cdd:cd11061  187 -KAEEEKRPDIFSYLLEA-------------------------KDP-------ETGEGLDLEELVGEARLLIVAGSDTTA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 230 NTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPAFRFT-REA-AQDCEVLGQRI 307
Cdd:cd11061  234 TALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGLpRETpPGGLTIDGEYI 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 308 PAGTVLEIAVGALHHDPEHWPNPETFDPERFTAE---ARLQRRPFTylPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRF 384
Cdd:cd11061  314 PGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRpeeLVRARSAFI--PFSIGPRGCIGKNLAYMELRLVLARLLHRYDF 391


                 ....*
gi 568941360 385 EASPE 389
Cdd:cd11061  392 RLAPG 396
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 21-415 1.58e-50

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: 175.84  E-value: 1.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  21 LMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDaFNIQRCYCCYTIDVVASVAFGTQVDSQNSPE-DPFVQHCRRAS 99
Cdd:cd11068   79 LMPAFGPLAMRGYFPMMLDIAEQLVLKWERLGPDEP-IDVPDDMTRLTLDTIALCGFGYRFNSFYRDEpHPFVEAMVRAL 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 100 TFCIPRPllvlilSFPSIMVPLaRILPNKNRDELNGFFNTLIRNVIALRdQQAAEERRRDFLQMVLDAqhsmnsvgvegf 179
Cdd:cd11068  158 TEAGRRA------NRPPILNKL-RRRAKRQFREDIALMRDLVDEIIAER-RANPDGSPDDLLNLMLNG------------ 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 180 dmvpeslsssectkeppqrCHPTsTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGK 259
Cdd:cd11068  218 -------------------KDPE-TGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGD 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 260 HPAPeYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDcEVLGQR--IPAGTVLEIAVGALHHDPEHW-PNPETFDPE 336
Cdd:cd11068  278 DPPP-YEQVAK-LRYIRRVLDETLRLWPTAPAFARKPKED-TVLGGKypLKKGDPVLVLLPALHRDPSVWgEDAEEFRPE 354

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 337 RFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPetqvPLQLESKSALGPK-NGVYIKIVSR 415
Cdd:cd11068  355 RFLPEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDP----DYELDIKETLTLKpDGFRLKARPR 430
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 13-385 1.91e-50

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: 175.48  E-value: 1.91e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSSFSPEKL-DEMTPLISQACELLVAHLKRYAASRDAFNIQRcYC-CYTIDVVASVAFGTQVDSQNSPE-- 88
Cdd:cd20617   58 YWKELRRFALSSLTKTKLkKKMEELIEEEVNKLIESLKKHSKSGEPFDPRP-YFkKFVLNIINQFLFGKRFPDEDDGEfl 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  89 ---DPFVQHCRRASTfciprPLLVLILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRDQQAAeerrRDFLQMVL 165
Cdd:cd20617  137 klvKPIEEIFKELGS-----GNPSDFIPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNP----RDLIDDEL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 166 DAQHSMNSvgvegfdmvpeslsssectkeppqrchptstSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDC 245
Cdd:cd20617  208 LLLLKEGD-------------------------------SGLFDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEI 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 246 QERLLKEVDLFMGKHPAP--EYHSLqegLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHH 322
Cdd:cd20617  257 QEKIYEEIDNVVGNDRRVtlSDRSK---LPYLNAVIKEVLRLRPILpLGLPRVTTEDTEIGGYFIPKGTQIIINIYSLHR 333

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941360 323 DPEHWPNPETFDPERFTaEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE 385
Cdd:cd20617  334 DEKYFEDPEEFNPERFL-ENDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFK 395
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 67-389 4.04e-50

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: 175.21  E-value: 4.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  67 YTIDVVASVAFGTQVDSQNSPEDPFVQHCRRASTFCIPRpllvLILSFPSIMVPLARILPnknrdelngffntlirnvia 146
Cdd:cd11070  113 LALNVIGEVGFGFDLPALDEEESSLHDTLNAIKLAIFPP----LFLNFPFLDRLPWVLFP-------------------- 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 147 lRDQQAAEERRRdFLQMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRchptstskpFTVDEIVGQAFLFLIAGHE 226
Cdd:cd11070  169 -SRKRAFKDVDE-FLSELLDEVEAELSADSKGKQGTESVVASRLKRARRSGG---------LTEKELLGNLFIFFIAGHE 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 227 VITNTLSFITYLLATHPDCQERLLKEVD-LFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPA---FRFTREAAQDCEV 302
Cdd:cd11070  238 TTANTLSFALYLLAKHPEVQDWLREEIDsVLGDEPDDWDYEEDFPKLPYLLAVIYETLRLYPPVqllNRKTTEPVVVITG 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 303 LGQR--IPAGTVLEIAVGALHHDPEHW-PNPETFDPERF-------TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVK 372
Cdd:cd11070  318 LGQEivIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWgstsgeiGAATRFTPARGAFIPFSAGPRACLGRKFALVEFV 397

                        330
                 ....*....|....*..
gi 568941360 373 LTILQVLHKFRFEASPE 389
Cdd:cd11070  398 AALAELFRQYEWRVDPE 414
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 1-388 6.43e-50

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


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 174.18  E-value: 6.43e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   1 MVADSVLLLRDRRWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQ--RCYCCYTIDVVASVAFG 78
Cdd:cd20639   56 LEGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVVKSVADMLDKWEAMAEAGGEGEVDvaEWFQNLTEDVISRTAFG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  79 TQVDSQnspedpfvqhcrrASTFCIPRPLLVL-ILSFPSIMVPLARILPN-KNRD--ELNGFFNTLIRNVIALR----DQ 150
Cdd:cd20639  136 SSYEDG-------------KAVFRLQAQQMLLaAEAFRKVYIPGYRFLPTkKNRKswRLDKEIRKSLLKLIERRqtaaDD 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 151 QAAEERRRDFLQMVLDAQHSMNSVgvegfdmvpeslsssectkeppqrchptstskPFTVDEIVGQAFLFLIAGHEVITN 230
Cdd:cd20639  203 EKDDEDSKDLLGLMISAKNARNGE--------------------------------KMTVEEIIEECKTFFFAGKETTSN 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 231 TLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAG 310
Cdd:cd20639  251 LLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPK-LKTLGMILNETLRLYPPAVATIRRAKKDVKLGGLDIPAG 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 311 TVLEIAVGALHHDPEHW-PNPETFDPERFTA-EARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:cd20639  330 TELLIPIMAIHHDAELWgNDAAEFNPARFADgVARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLSP 409
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 13-390 2.07e-49

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: 172.89  E-value: 2.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPFV 92
Cdd:cd11083   58 AWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPLQ 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  93 QHCRRAstfciprpllvlilsFPSIM------VPLARILP-------NKNRDELNGFFNTLI---RNVIALRDQQAaeER 156
Cdd:cd11083  138 EHLERV---------------FPMLNrrvnapFPYWRYLRlpadralDRALVEVRALVLDIIaaaRARLAANPALA--EA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 157 RRDFLQMVLDAQHsmnsvgvegfdmvPESlsssectkeppqrchptstskPFTVDEIVGQAFLFLIAGHEVITNTLSFIT 236
Cdd:cd11083  201 PETLLAMMLAEDD-------------PDA---------------------RLTDDEIYANVLTLLLAGEDTTANTLAWML 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 237 YLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIA 316
Cdd:cd11083  247 YYLASRPDVQARVREEVDAVLGGARVPPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLL 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941360 317 VGALHHDPEHWPNPETFDPERF--TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPET 390
Cdd:cd11083  327 TRAAGLDAEHFPDPEEFDPERWldGARAAEPHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPA 402
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 14-389 2.28e-46

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: 164.62  E-value: 2.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  14 WEEVRGALMSSF-SPEKLDEMTPLISQACELLVAHLKRYAASRDAF--NIQRCYCCYTIDVVASVAFGTQVDSQNSPEDP 90
Cdd:cd11054   66 WHRLRSAVQKPLlRPKSVASYLPAINEVADDFVERIRRLRDEDGEEvpDLEDELYKWSLESIGTVLFGKRLGCLDDNPDS 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  91 ----FVQHCRRASTfciprplLVLILSFpsiMVPLARILPNK-------NRDELNGFFNTLIRNVIA-LRDQQAAEERRR 158
Cdd:cd11054  146 daqkLIEAVKDIFE-------SSAKLMF---GPPLWKYFPTPawkkfvkAWDTIFDIASKYVDEALEeLKKKDEEDEEED 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 159 DFLQMVLdaqhsmnsvgvegfdmvpeslsssectkeppqrchptsTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYL 238
Cdd:cd11054  216 SLLEYLL--------------------------------------SKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYH 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVG 318
Cdd:cd11054  258 LAKNPEVQEKLYEEIRSVLPDGEPITAEDLKK-MPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNY 336

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941360 319 ALHHDPEHWPNPETFDPERF--TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPE 389
Cdd:cd11054  337 VMGRDEEYFPDPEEFIPERWlrDDSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE 409
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 17-412 3.58e-46

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: 163.89  E-value: 3.58e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  17 VRGALMSSFSPEKLDEMtpLISQACELLVAHLKRYAASRDaFNIQRCYCCYTIDVVASVAFGtqvdsqNSPE---DPFVQ 93
Cdd:cd11043   66 LRGLLLSFLGPEALKDR--LLGDIDELVRQHLDSWWRGKS-VVVLELAKKMTFELICKLLLG------IDPEevvEELRK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  94 HCRRastfciprpLLVLILSFPsIMVP---LARILpnKNRDELNGFFNTLIRnviALRDQQAAEERRRDFLQMVLDAqhs 170
Cdd:cd11043  137 EFQA---------FLEGLLSFP-LNLPgttFHRAL--KARKRIRKELKKIIE---ERRAELEKASPKGDLLDVLLEE--- 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 171 mnsvgvegfdmvpeslsSSEctkeppqrchptsTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLL 250
Cdd:cd11043  199 -----------------KDE-------------DGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 251 KEVDLFMGKHPAPEYHSLQE--GLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWP 328
Cdd:cd11043  249 EEHEEIAKRKEEGEGLTWEDykSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFP 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 329 NPETFDPERFtaEARLQRRPFTYLPFGAGPRSCLGVRLGllvvKLTILQVLH----KFRFEASPETQVPLQLesksALGP 404
Cdd:cd11043  329 DPLKFNPWRW--EGKGKGVPYTFLPFGGGPRLCPGAELA----KLEILVFLHhlvtRFRWEVVPDEKISRFP----LPRP 398


                 ....*...
gi 568941360 405 KNGVYIKI 412
Cdd:cd11043  399 PKGLPIRL 406
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 18-389 3.77e-46

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: 163.91  E-value: 3.77e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  18 RGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDS-QNSPEDPFVqhcr 96
Cdd:cd11058   62 RRLLAHAFSEKALREQEPIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGESFGClENGEYHPWV---- 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  97 rASTFCIPR--PLLVLILSFPSIMVPLARILPNKNRDELNGFFNtLIRNVIALRDQQAAEerRRDFLQMVLDAQhsmnsv 174
Cdd:cd11058  138 -ALIFDSIKalTIIQALRRYPWLLRLLRLLIPKSLRKKRKEHFQ-YTREKVDRRLAKGTD--RPDFMSYILRNK------ 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 175 gvegfdmvpeslsssectkeppqrchptSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEV- 253
Cdd:cd11058  208 ----------------------------DEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIr 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 254 DLFmgkhPAPE---YHSLQEgLPYLDMVISETLRMYPPA----FRFTREAAQDceVLGQRIPAGTVLEIAVGALHHDPEH 326
Cdd:cd11058  260 SAF----SSEDditLDSLAQ-LPYLNAVIQEALRLYPPVpaglPRVVPAGGAT--IDGQFVPGGTSVSVSQWAAYRSPRN 332

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941360 327 WPNPETFDPERFTAEARL-----QRRPFTylPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPE 389
Cdd:cd11058  333 FHDPDEFIPERWLGDPRFefdndKKEAFQ--PFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPE 398
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 18-385 8.13e-46

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: 163.24  E-value: 8.13e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  18 RGALMSSFSPE--KLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPFVQHC 95
Cdd:cd11059   59 RRLLSGVYSKSslLRAAMEPIIRERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSRERE 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  96 RRASTFCIPRPLLVLILSFPsimvPLARILPnknrdelngffntlirnvIALRDQQAAEERRRDFLQMVLDAQHSMNSVG 175
Cdd:cd11059  139 LLRRLLASLAPWLRWLPRYL----PLATSRL------------------IIGIYFRAFDEIEEWALDLCARAESSLAESS 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 176 VEGFDMVPESLSssectkeppqrcHPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEV-D 254
Cdd:cd11059  197 DSESLTVLLLEK------------LKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELaG 264

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 255 LFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDCEVL-GQRIPAGTVLEIAVGALHHDPEHWPNPET 332
Cdd:cd11059  265 LPGPFRGPPDLEDLDK-LPYLNAVIRETLRLYPPIpGSLPRVVPEGGATIgGYYIPGGTIVSTQAYSLHRDPEVFPDPEE 343

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941360 333 FDPERF----TAEARLQRRPFtyLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE 385
Cdd:cd11059  344 FDPERWldpsGETAREMKRAF--WPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTS 398
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 9-385 4.54e-45

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: 161.27  E-value: 4.54e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   9 LRDRRweevRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPE 88
Cdd:cd11062   54 LHRLR----RKALSPFFSKRSILRLEPLIQEKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  89 DPFVQHcrraSTFCIPRPLLVLILSFPSIMVPLARILPNKNRdelngffnTLIRNVIALRD-QQAAEERRRDFLQMVlda 167
Cdd:cd11062  130 FGPEFL----DALRALAEMIHLLRHFPWLLKLLRSLPESLLK--------RLNPGLAVFLDfQESIAKQVDEVLRQV--- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 168 qhsMNSVGVEGFDMVPESLSSSECTKEPPqrchptstskpfTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQE 247
Cdd:cd11062  195 ---SAGDPPSIVTSLFHALLNSDLPPSEK------------TLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 248 RLLKEVD-LFMGKHPAPEYHSLqEGLPYLDMVISETLRMYPPAF-RFTREA-AQDCEVLGQRIPAGTVLEIAVGALHHDP 324
Cdd:cd11062  260 RLREELKtAMPDPDSPPSLAEL-EKLPYLTAVIKEGLRLSYGVPtRLPRVVpDEGLYYKGWVIPPGTPVSMSSYFVHHDE 338

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941360 325 EHWPNPETFDPERF---TAEARLQRrpftYL-PFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE 385
Cdd:cd11062  339 EIFPDPHEFRPERWlgaAEKGKLDR----YLvPFSKGSRSCLGINLAYAELYLALAALFRRFDLE 399
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 4-389 4.10e-44

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: 158.51  E-value: 4.10e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   4 DSVLLLRDRRW-EEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQ-- 80
Cdd:cd11060   46 DNLFSERDEKRhAALRRKVASGYSMSSLLSLEPFVDECIDLLVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPfg 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  81 -VDsQNSPEDPFVQHCRRASTFciprplLVLILSFPSIMVPLARILPNKNRDELNGF--FNTLIRNVIALRDQQAAEER- 156
Cdd:cd11060  126 fLE-AGTDVDGYIASIDKLLPY------FAVVGQIPWLDRLLLKNPLGPKRKDKTGFgpLMRFALEAVAERLAEDAESAk 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 157 -RRDFLQMVLDAQhsmnsvgvegfdmvpeslsssectKEPPQrchptstskPFTVDEIVGQAFLFLIAGHEVITNTLSFI 235
Cdd:cd11060  199 gRKDMLDSFLEAG------------------------LKDPE---------KVTDREVVAEALSNILAGSDTTAIALRAI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 236 TYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQE--GLPYLDMVISETLRMYPP-AFRFTREA-AQDCEVLGQRIPAGT 311
Cdd:cd11060  246 LYYLLKNPRVYAKLRAEIDAAVAEGKLSSPITFAEaqKLPYLQAVIKEALRLHPPvGLPLERVVpPGGATICGRFIPGGT 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 312 VLEIAVGALHHDPEHW-PNPETFDPERF--TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE-AS 387
Cdd:cd11060  326 IVGVNPWVIHRDKEVFgEDADVFRPERWleADEEQRRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFElVD 405


                 ..
gi 568941360 388 PE 389
Cdd:cd11060  406 PE 407
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 203-392 9.23e-44

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: 157.42  E-value: 9.23e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 203 STSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPA-PEYHSlqeGLPYLDMVISE 281
Cdd:cd11049  211 EEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPAtFEDLP---RLTYTRRVVTE 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 282 TLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSC 361
Cdd:cd11049  288 ALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKC 367

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568941360 362 LGVRLGLLVVKLTILQVLHKFRFEASPETQV 392
Cdd:cd11049  368 IGDTFALTELTLALATIASRWRLRPVPGRPV 398
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 207-385 6.39e-42

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: 152.76  E-value: 6.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 207 PFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAP-EYHSLQEgLPYLDMVISETLRM 285
Cdd:cd11042  207 PLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDPlTYDVLKE-MPLLHACIKETLRL 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 286 YPPAFRFTREAAQDCEVLGQ--RIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQR--RPFTYLPFGAGPRSC 361
Cdd:cd11042  286 HPPIHSLMRKARKPFEVEGGgyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSkgGKFAYLPFGAGRHRC 365

                        170       180
                 ....*....|....*....|....*
gi 568941360 362 LGVRLGLLVVKlTILQVL-HKFRFE 385
Cdd:cd11042  366 IGENFAYLQIK-TILSTLlRNFDFE 389
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 14-409 8.91e-42

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: 152.90  E-value: 8.91e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  14 WEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSpEDP--- 90
Cdd:cd11046   69 WKKRRRALVPALHKDYLEMMVRVFGRCSERLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTE-ESPvik 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  91 -----FVQHCRRaSTFCIPRPLLVLILsfpsIMVPLARILpNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFLQM-- 163
Cdd:cd11046  148 avylpLVEAEHR-SVWEPPYWDIPAAL----FIVPRQRKF-LRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLNEdd 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 164 --VLDAQHSMNSvgvegfdmvpeslsssectkeppqrchPTSTSKPFTvDEIVGqaflFLIAGHEVITNTLSFITYLLAT 241
Cdd:cd11046  222 psLLRFLVDMRD---------------------------EDVDSKQLR-DDLMT----MLIAGHETTAAVLTWTLYELSQ 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 242 HPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDcEVLGQ---RIPAGTVLEIAVG 318
Cdd:cd11046  270 NPELMAKVQAEVDAVLGDRLPPTYEDLKK-LKYTRRVLNESLRLYPQPPVLIRRAVED-DKLPGggvKVPAGTDIFISVY 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 319 ALHHDPEHWPNPETFDPERF----TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQvPL 394
Cdd:cd11046  348 NLHRSPELWEDPEEFDPERFldpfINPPNEVIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPR-HV 426

                        410
                 ....*....|....*
gi 568941360 395 QLESKSALGPKNGVY 409
Cdd:cd11046  427 GMTTGATIHTKNGLK 441
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 18-388 1.21e-41

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: 152.05  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  18 RGALMSSFSPEKLDEMTPLISQaceLLVAHLKRYAaSRDAFNIQRCYCCYTIDVVASVAFGTQvdsqnsPEDPFVQHCRR 97
Cdd:cd11044   83 RKLLAPAFSREALESYVPTIQA---IVQSYLRKWL-KAGEVALYPELRRLTFDVAARLLLGLD------PEVEAEALSQD 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  98 ASTFCipRPLLVLILSFPsiMVPLARILpnKNRDELNGFFNTLIRnviaLRDQQAAEERRrDFLQMVLDAQHSMNsvgve 177
Cdd:cd11044  153 FETWT--DGLFSLPVPLP--FTPFGRAI--RARNKLLARLEQAIR----ERQEEENAEAK-DALGLLLEAKDEDG----- 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 178 gfdmvpeslsssectkeppqrchptstsKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFM 257
Cdd:cd11044  217 ----------------------------EPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALG 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 258 GKHPAPEYHslQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPER 337
Cdd:cd11044  269 LEEPLTLES--LKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPER 346

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568941360 338 FTAEARLQRR-PFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:cd11044  347 FSPARSEDKKkPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLP 398
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 14-385 1.84e-41

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: 151.25  E-value: 1.84e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  14 WEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPfvq 93
Cdd:cd11051   57 WKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAAILRELAESGEVFSLEELTTNLTFDVIGRVTLDIDLHAQTGDNSL--- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  94 hcrraSTFciprpLLVLILSFPSIMVPLARILPNKNRdelngffntlirnvialrdQQAAEERRRD-FLQMVLDAQHSMn 172
Cdd:cd11051  134 -----LTA-----LRLLLALYRSLLNPFKRLNPLRPL-------------------RRWRNGRRLDrYLKPEVRKRFEL- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 173 svgvegfdmvpeslsssectkeppqrchptstskpftvDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKE 252
Cdd:cd11051  184 --------------------------------------ERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAE 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 253 VDLFMGKHPAPEYHSLQEG------LPYLDMVISETLRMYPPA--FRFTREAAQDCEVLGQRIP-AGTVLEIAVGALHHD 323
Cdd:cd11051  226 HDEVFGPDPSAAAELLREGpellnqLPYTTAVIKETLRLFPPAgtARRGPPGVGLTDRDGKEYPtDGCIVYVCHHAIHRD 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568941360 324 PEHWPNPETFDPERFTAEARLQRRPFT--YLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE 385
Cdd:cd11051  306 PEYWPRPDEFIPERWLVDEGHELYPPKsaWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFE 369
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 101-391 5.15e-41

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


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 150.25  E-value: 5.15e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 101 FCIPRPLLVLIlSFPSIM--VPLARILP---NKNRDELNGFFNTLIRNVIALRDQQAAEERrrDFLQMVLDAqhsmnsvg 175
Cdd:cd20640  148 FSKLRELQKAV-SKQSVLfsIPGLRHLPtksNRKIWELEGEIRSLILEIVKEREEECDHEK--DLLQAILEG-------- 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 176 vegfdmvpeslSSSECTKeppqrchpTSTSKPFTVDEIVGQAFlfliAGHEVITNTLSFITYLLATHPDCQERLLKEVDL 255
Cdd:cd20640  217 -----------ARSSCDK--------KAEAEDFIVDNCKNIYF----AGHETTAVTAAWCLMLLALHPEWQDRVRAEVLE 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 256 FMGKHPaPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHW-PNPETFD 334
Cdd:cd20640  274 VCKGGP-PDADSLSR-MKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFN 351

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941360 335 PERFT-AEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQ 391
Cdd:cd20640  352 PERFSnGVAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSFTLSPEYQ 409
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 14-389 4.17e-40

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 147.98  E-value: 4.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  14 WEEVRGALMSSFSPEKLDEMT-PLISQACELLVAHLKRYAASRDA---FNIQRCYCCYTIDVVASVAFGTqvdsqNSPED 89
Cdd:cd20641   69 WVRHRRVLNPAFSMDKLKSMTqVMADCTERMFQEWRKQRNNSETErieVEVSREFQDLTADIIATTAFGS-----SYAEG 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  90 PFVQHCRRASTFCiprpllvLILSFPSIMVPLARILP---NKNRDELNGFFNTLIRNVIALRDQQAAEERRRDFLQMVLD 166
Cdd:cd20641  144 IEVFLSQLELQKC-------AAASLTNLYIPGTQYLPtprNLRVWKLEKKVRNSIKRIIDSRLTSEGKGYGDDLLGLMLE 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 167 AqhsmnsvgvegfdmvpeslssseCTKEPPQRchptSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQ 246
Cdd:cd20641  217 A-----------------------ASSNEGGR----RTERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQ 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 247 ERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEH 326
Cdd:cd20641  270 EKLREEVFRECGKDKIPDADTLSK-LKLMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEV 348

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941360 327 W-PNPETFDPERFT-AEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPE 389
Cdd:cd20641  349 WgSDADEFNPLRFAnGVSRAATHPNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPE 413
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 13-410 6.10e-40

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: 147.98  E-value: 6.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAaSRDAFNiqrCYCCYTI---DVVASVAFGTQVDSQNSPED 89
Cdd:cd20680   67 KWRSRRKMLTPTFHFTILSDFLEVMNEQSNILVEKLEKHV-DGEAFN---CFFDITLcalDIICETAMGKKIGAQSNKDS 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  90 PFVQHCRRASTFCIPR---PLLVLILSFpsIMVPLARiLPNKNRDELNGFFNTLIRNVI-----------ALRDQQAAEE 155
Cdd:cd20680  143 EYVQAVYRMSDIIQRRqkmPWLWLDLWY--LMFKEGK-EHNKNLKILHTFTDNVIAERAeemkaeedktgDSDGESPSKK 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 156 RRRDFLQMVLDAQHSmnsvgvEGfdmvpESLSSSECTKEppqrchptstskpftVDEivgqaflFLIAGHEVITNTLSFI 235
Cdd:cd20680  220 KRKAFLDMLLSVTDE------EG-----NKLSHEDIREE---------------VDT-------FMFEGHDTTAAAMNWS 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 236 TYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEI 315
Cdd:cd20680  267 LYLLGSHPEVQRKVHKELDEVFGKSDRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVI 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 316 AVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASpETQVPLQ 395
Cdd:cd20680  347 IPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEAN-QKREELG 425

                        410
                 ....*....|....*
gi 568941360 396 LESKSALGPKNGVYI 410
Cdd:cd20680  426 LVGELILRPQNGIWI 440
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 132-382 1.70e-39

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: 146.16  E-value: 1.70e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 132 ELNGFFNtlIRNVI-ALR--DQQAAEERRRD-------FLQMVLDaQHSMNSVGVEGFDMVPESLSSSEctkeppqrchP 201
Cdd:cd20618  152 ELAGAFN--IGDYIpWLRwlDLQGYEKRMKKlhakldrFLQKIIE-EHREKRGESKKGGDDDDDLLLLL----------D 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 202 TSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHpapeyHSLQE----GLPYLDM 277
Cdd:cd20618  219 LDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRE-----RLVEEsdlpKLPYLQA 293

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 278 VISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF--TAEARLQRRPFTYLPF 354
Cdd:cd20618  294 VVKETLRLHPPGpLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFleSDIDDVKGQDFELLPF 373

                        250       260
                 ....*....|....*....|....*...
gi 568941360 355 GAGPRSCLGVRLGLLVVKLTILQVLHKF 382
Cdd:cd20618  374 GSGRRMCPGMPLGLRMVQLTLANLLHGF 401
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 143-411 2.30e-39

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 146.27  E-value: 2.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 143 NVIALRDQQAAEE---------RRRDFLQMVLDAQhsmnsvgvegfDMVPESLSSSECTKEppqrchptstskpftVDEi 213
Cdd:cd20678  194 KVIQQRKEQLQDEgelekikkkRHLDFLDILLFAK-----------DENGKSLSDEDLRAE---------------VDT- 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 214 vgqaflFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFT 293
Cdd:cd20678  247 ------FMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQ-MPYTTMCIKEALRLYPPVPGIS 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 294 REAAQ-----DcevlGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGL 368
Cdd:cd20678  320 RELSKpvtfpD----GRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAM 395

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 568941360 369 L----VVKLTILqvlhkfRFEASPETQVPLQLESKSALGPKNGVYIK 411
Cdd:cd20678  396 NemkvAVALTLL------RFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 222-392 9.41e-38

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


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 141.98  E-value: 9.41e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 222 IAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDC 300
Cdd:cd20654  251 LGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKN-LVYLQAIVKETLRLYPPGpLLGPREATEDC 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 301 EVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-TAEARLQRR--PFTYLPFGAGPRSCLGVRLGLLVVKLTILQ 377
Cdd:cd20654  330 TVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFlTTHKDIDVRgqNFELIPFGSGRRSCPGVSFGLQVMHLTLAR 409

                        170
                 ....*....|....*
gi 568941360 378 VLHKFRFEASPETQV 392
Cdd:cd20654  410 LLHGFDIKTPSNEPV 424
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 35-405 1.11e-37

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: 141.19  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  35 PLISQACELLVAHLKRYAASRD-AFNIQRCYCCYTIDVVASVAFGTQVDsqnsPEDPFVQHCRRASTFCIPRPLLVLILS 113
Cdd:cd11027   82 RLEEKIAEEAEKLLKRLASQEGqPFDPKDELFLAVLNVICSITFGKRYK----LDDPEFLRLLDLNDKFFELLGAGSLLD 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 114 FpsimVPLARILPNKnrdelngffntlirnviALRDQQAAEERRRDFLQMVLDaQHsmnsvgVEGFD----------MVP 183
Cdd:cd11027  158 I----FPFLKYFPNK-----------------ALRELKELMKERDEILRKKLE-EH------KETFDpgnirdltdaLIK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 184 ESLSSSECTKEPpqrchptstSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAP 263
Cdd:cd11027  210 AKKEAEDEGDED---------SGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLP 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 264 EYhSLQEGLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-TAE 341
Cdd:cd11027  281 TL-SDRKRLPYLEATIAEVLRLSSVVpLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFlDEN 359

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941360 342 ARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVP-LQLESKSALGPK 405
Cdd:cd11027  360 GKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPeLEGIPGLVLYPL 424
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 13-392 1.30e-37

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: 141.23  E-value: 1.30e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSS-FSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTI-DVVASVAFGTQVDsqnspEDP 90
Cdd:cd11075   63 LWRTLRRNLVSEvLSPSRLKQFRPARRRALDNLVERLREEAKENPGPVNVRDHFRHALfSLLLYMCFGERLD-----EET 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  91 F--VQHcrrastfcIPRPLLVLILSF-PSIMVPLARILPNKNRDelngffntliRNVIALRdqqaaeERRRDFLQMVLDA 167
Cdd:cd11075  138 VreLER--------VQRELLLSFTDFdVRDFFPALTWLLNRRRW----------KKVLELR------RRQEEVLLPLIRA 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 168 QHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPTStskpftvDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQE 247
Cdd:cd11075  194 RRKRRASGEADKDYTDFLLLDLLDLKEEGGERKLTD-------EELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQE 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 248 RLLKEVDLFMGKHPAPEYHSLQeGLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEH 326
Cdd:cd11075  267 KLYEEIKEVVGDEAVVTEEDLP-KMPYLKAVVLETLRRHPPGhFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKV 345

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568941360 327 WPNPETFDPERF-----TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQV 392
Cdd:cd11075  346 WEDPEEFKPERFlaggeAADIDTGSKEIKMMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEGEEV 416
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 208-412 3.31e-37

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: 140.08  E-value: 3.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYP 287
Cdd:cd20621  225 ITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQK-LNYLNAFIKEVLRLYN 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 288 PAFR-FTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRL 366
Cdd:cd20621  304 PAPFlFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHL 383

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568941360 367 GLLVVKLTILQVLHKFRFEASPEtqVPLQLESKSALGPKNGVYIKI 412
Cdd:cd20621  384 ALMEAKIILIYILKNFEIEIIPN--PKLKLIFKLLYEPVNDLLLKL 427
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 13-388 3.79e-36

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


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 137.41  E-value: 3.79e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSSFSPEKLDEMTPLISQACELLVAHLKRYAASR-----DAFN-IQRcyccYTIDVVASVAFGTqvdsqnS 86
Cdd:cd20642   66 KWAKHRKIINPAFHLEKLKNMLPAFYLSCSEMISKWEKLVSSKgscelDVWPeLQN----LTSDVISRTAFGS------S 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  87 PEDPfvqhcrrASTFCIPRPLLVLIL-SFPSIMVPLARILP---NKNRDELNGFFNTLIRNVIALRDQ--QAAEERRRDF 160
Cdd:cd20642  136 YEEG-------KKIFELQKEQGELIIqALRKVYIPGWRFLPtkrNRRMKEIEKEIRSSLRGIINKREKamKAGEATNDDL 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 161 LQMVLDAQHSMN-SVGVEGFDMvpeslsssectkeppqrchptstskpfTVDEIVGQAFLFLIAGHEVITNTLSFITYLL 239
Cdd:cd20642  209 LGILLESNHKEIkEQGNKNGGM---------------------------STEDVIEECKLFYFAGQETTSVLLVWTMVLL 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 240 ATHPDCQERLLKEVDLFMGKHpAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEvLGQ-RIPAGTVLEIAVG 318
Cdd:cd20642  262 SQHPDWQERAREEVLQVFGNN-KPDFEGLNH-LKVVTMILYEVLRLYPPVIQLTRAIHKDTK-LGDlTLPAGVQVSLPIL 338

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941360 319 ALHHDPEHWPN-PETFDPERFtAE--ARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:cd20642  339 LVHRDPELWGDdAKEFNPERF-AEgiSKATKGQVSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFELSP 410
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 13-408 4.28e-36

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: 136.92  E-value: 4.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSSFSPE---KLDEMTPLISQacelLVAHLKRYAASRDafnIQRCYCCYTIDVVASVAFGTQVDSQ----- 84
Cdd:cd11063   59 EWKHSRALLRPQFSRDqisDLELFERHVQN----LIKLLPRDGSTVD---LQDLFFRLTLDSATEFLFGESVDSLkpggd 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  85 NSPEDPFVQHCRRASTFCIPR----PLLVLILSFPSimvplarilpNKNRDELNGFFNTLIRNVIALRDQQAAEERRRDF 160
Cdd:cd11063  132 SPPAARFAEAFDYAQKYLAKRlrlgKLLWLLRDKKF----------REACKVVHRFVDPYVDKALARKEESKDEESSDRY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 161 LqmVLDAqhsmnsvgvegfdMVPEslsssecTKEPpqrchptstskpftvDEIVGQAFLFLIAGHEVITNTLSFITYLLA 240
Cdd:cd11063  202 V--FLDE-------------LAKE-------TRDP---------------KELRDQLLNILLAGRDTTASLLSFLFYELA 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 241 THPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCeVL-------GQR---IPAG 310
Cdd:cd11063  245 RHPEVWAKLREEVLSLFGPEPTPTYEDLKN-MKYLRAVINETLRLYPPVPLNSRVAVRDT-TLprgggpdGKSpifVPKG 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 311 TVLEIAVGALHHDPEHW-PNPETFDPERFtaeARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKF-RFEASP 388
Cdd:cd11063  323 TRVLYSVYAMHRRKDIWgPDAEEFRPERW---EDLKRPGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFdRIESRD 399

                        410       420
                 ....*....|....*....|
gi 568941360 389 ETqvPLQLESKSALGPKNGV 408
Cdd:cd11063  400 VR--PPEERLTLTLSNANGV 417
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 206-393 2.32e-35

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


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 135.20  E-value: 2.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 206 KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEV-DLFMGKHPAP-EYHSLQEgLPYLDMVISETL 283
Cdd:cd20679  238 KELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVqELLKDREPEEiEWDDLAQ-LPFLTMCIKESL 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 284 RMYPPAFRFTREAAQDCEVLGQR-IPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCL 362
Cdd:cd20679  317 RLHPPVTAISRCCTQDIVLPDGRvIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCI 396

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568941360 363 GVRLGLLVVKLTILQVLHKFRFeaSPETQVP 393
Cdd:cd20679  397 GQTFAMAEMKVVLALTLLRFRV--LPDDKEP 425
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 41-382 6.47e-34

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


Pssm-ID: 410695 [Multi-domain]  Cd Length: 428  Bit Score: 131.05  E-value: 6.47e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  41 CELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNspEDPFVQHCRRASTfciprpllvLILSFP-SIMV 119
Cdd:cd11072   91 VSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKD--QDKFKELVKEALE---------LLGGFSvGDYF 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 120 PLARILpnknrDELNGFFNTLIRNvialrdqqaaeeRRR--DFLQMVLDAQHSMNSVGVEGFDMVPESLSSSECTKeppq 197
Cdd:cd11072  160 PSLGWI-----DLLTGLDRKLEKV------------FKEldAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEG---- 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 198 rchptSTSKPFTVDEIvgQAFLF--LIAGHEVITNTLSFI-TYLLAtHPDCQERLLKEV-DLFMGKHPAPEYHSlqEGLP 273
Cdd:cd11072  219 -----DLEFPLTRDNI--KAIILdmFLAGTDTSATTLEWAmTELIR-NPRVMKKAQEEVrEVVGGKGKVTEEDL--EKLK 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 274 YLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF---TAEARLQRrpF 349
Cdd:cd11072  289 YLKAVIKETLRLHPPApLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFldsSIDFKGQD--F 366

                        330       340       350
                 ....*....|....*....|....*....|...
gi 568941360 350 TYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKF 382
Cdd:cd11072  367 ELIPFGAGRRICPGITFGLANVELALANLLYHF 399
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 4-386 6.77e-34

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: 130.78  E-value: 6.77e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360   4 DSVLLLR-DRRWEEVRGALMSSFSPEKLDEMTPLISQ-ACELL----------VAHLKRYAASrdafniqrcyccytidV 71
Cdd:cd11065   51 MRLLLMPyGPRWRLHRRLFHQLLNPSAVRKYRPLQELeSKQLLrdllespddfLDHIRRYAAS----------------I 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  72 VASVAFGTQVDSQNSPEDPFVQHCRRASTFCIPrPLLVLILSFPSIM-VPLARILPNKN-----RDELNGFFNTLIRNVi 145
Cdd:cd11065  115 ILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGS-PGAYLVDFFPFLRyLPSWLGAPWKRkarelRELTRRLYEGPFEAA- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 146 alRDQQAAEERRRDFLQMVLDAQHSMNSvgvegfdmvpeslsssectkeppqrchptstskpFTVDEIVGQAFLFLIAGH 225
Cdd:cd11065  193 --KERMASGTATPSFVKDLLEELDKEGG----------------------------------LSEEEIKYLAGSLYEAGS 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 226 EVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLG 304
Cdd:cd11065  237 DTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPN-LPYVNAIVKEVLRWRPVApLGIPHALTEDDEYEG 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 305 QRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAE---ARLQRRPFTYlPFGAGPRSCLGVRLGLLVVKLTILQVLHK 381
Cdd:cd11065  316 YFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDpkgTPDPPDPPHF-AFGFGRRICPGRHLAENSLFIAIARLLWA 394


                 ....*
gi 568941360 382 FRFEA 386
Cdd:cd11065  395 FDIKK 399
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 208-395 9.48e-33

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: 127.72  E-value: 9.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPeyhSLQE--GLPYLDMVISETLRM 285
Cdd:cd20651  221 FTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLP---TLDDrsKLPYTEAVILEVLRI 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 286 YPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLG- 363
Cdd:cd20651  298 FTLVpIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGe 377

                        170       180       190
                 ....*....|....*....|....*....|....
gi 568941360 364 --VRLGLLVVKLTILQvlhKFRFEASPETQVPLQ 395
Cdd:cd20651  378 slARNELFLFFTGLLQ---NFTFSPPNGSLPDLE 408
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 209-402 6.41e-32

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


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 125.49  E-value: 6.41e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGqaflfliAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYhSLQEGLPYLDMVISETLR---M 285
Cdd:cd11028  235 TVQDLFG-------AGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRL-SDRPNLPYTEAFILETMRhssF 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 286 YPpaFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-TAEARLQRRPF-TYLPFGAGPRSCLG 363
Cdd:cd11028  307 VP--FTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFlDDNGLLDKTKVdKFLPFGAGRRRCLG 384

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568941360 364 VRLGLLVVKLTILQVLHKFRFEASPEtqVPLQLESKSAL 402
Cdd:cd11028  385 EELARMELFLFFATLLQQCEFSVKPG--EKLDLTPIYGL 421
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 118-393 6.42e-32

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


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 125.51  E-value: 6.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 118 MVPLARILPNKNRDelngffntLIRNVIALRD---QQAAEERRRDF----LQMVLDA--QHSMNSvgvegfdmvpESLSS 188
Cdd:cd20673  158 IFPWLQIFPNKDLE--------KLKQCVKIRDkllQKKLEEHKEKFssdsIRDLLDAllQAKMNA----------ENNNA 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 189 SectkeppqrchPTSTSKPFTVDEI---VGQAFlflIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEY 265
Cdd:cd20673  220 G-----------PDQDSVGLSDDHIlmtVGDIF---GAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTL 285

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 266 hSLQEGLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARL 344
Cdd:cd20673  286 -SDRNHLPLLEATIREVLRIRPVApLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGS 364

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568941360 345 QRR--PFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVP 393
Cdd:cd20673  365 QLIspSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGGQLP 415
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 13-388 1.57e-31

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: 124.63  E-value: 1.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  13 RWEEVRGALMSSFSPEKL-DEMTPLI-SQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNS--PE 88
Cdd:cd11064   58 LWKFQRKTASHEFSSRALrEFMESVVrEKVEKLLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPslPE 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  89 DPFVQHCRRASTFCIPRpllvliLSFPS--------IMVPLARILpNKNRDELNGFFNTLIRNVIA-LRDQQAAEERRRD 159
Cdd:cd11064  138 VPFAKAFDDASEAVAKR------FIVPPwlwklkrwLNIGSEKKL-REAIRVIDDFVYEVISRRREeLNSREEENNVRED 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 160 FLQMVldaqhsMNSVGVEGFDMVPESLsssectkeppqRchptstskpftvDEIVGqaflFLIAGHEVITNTLSFITYLL 239
Cdd:cd11064  211 LLSRF------LASEEEEGEPVSDKFL-----------R------------DIVLN----FILAGRDTTAAALTWFFWLL 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 240 ATHPDCQERLLKEVD-----LFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDcEVL--GQRIPAGTV 312
Cdd:cd11064  258 SKNPRVEEKIREELKsklpkLTTDESRVPTYEELKK-LVYLHAALSESLRLYPPVPFDSKEAVND-DVLpdGTFVKKGTR 335

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941360 313 LEIAVGALHHDPEHW-PNPETFDPERF-TAEARLQRR-PFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:cd11064  336 IVYSIYAMGRMESIWgEDALEFKPERWlDEDGGLRPEsPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVP 414
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 217-375 9.17e-31

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


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 122.32  E-value: 9.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 217 AFL--FLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHpapeyHSLQEG----LPYLDMVISETLRMYPPAF 290
Cdd:cd20655  231 AFIldLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKT-----RLVQESdlpnLPYLQAVVKETLRLHPPGP 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 291 RFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQ------RRPFTYLPFGAGPRSCLGV 364
Cdd:cd20655  306 LLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGqeldvrGQHFKLLPFGSGRRGCPGA 385

                        170
                 ....*....|.
gi 568941360 365 RLGLLVVKLTI 375
Cdd:cd20655  386 SLAYQVVGTAI 396
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 57-397 1.13e-30

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


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 121.90  E-value: 1.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  57 AFNIQRCYCCYTIDVVASVAFGTQVDSqnspEDPFVQHC--------RRASTFCIprpllVLILSFPSIMvplaRILPnk 128
Cdd:cd11026  103 PFDPTFLLSNAVSNVICSIVFGSRFDY----EDKEFLKLldlinenlRLLSSPWG-----QLYNMFPPLL----KHLP-- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 129 nrdelnGFFNTLIRNVIALRD--QQAAEERR--------RDFLQMVLD--AQHSMNsvgvegfdmvpeslsssectkepp 196
Cdd:cd11026  168 ------GPHQKLFRNVEEIKSfiRELVEEHRetldpsspRDFIDCFLLkmEKEKDN------------------------ 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 197 qrchPTSTskpFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLD 276
Cdd:cd11026  218 ----PNSE---FHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLED-RAKMPYTD 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 277 MVISETLRM---YPPAFrfTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-TAEARLQRRPfTYL 352
Cdd:cd11026  290 AVIHEVQRFgdiVPLGV--PHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFlDEQGKFKKNE-AFM 366

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 568941360 353 PFGAGPRSCLGVRLG-----LLVVklTILQvlhKFRFeASPETQVPLQLE 397
Cdd:cd11026  367 PFSAGKRVCLGEGLArmelfLFFT--SLLQ---RFSL-SSPVGPKDPDLT 410
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 205-391 3.25e-30

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: 120.79  E-value: 3.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 205 SKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLR 284
Cdd:cd20647  230 SKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPK-LPLIRALLKETLR 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 285 MYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQR-RPFTYLPFGAGPRSCLG 363
Cdd:cd20647  309 LFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRvDNFGSIPFGYGIRSCIG 388

                        170       180
                 ....*....|....*....|....*...
gi 568941360 364 VRLGLLVVKLTILQVLHKFRFEASPETQ 391
Cdd:cd20647  389 RRIAELEIHLALIQLLQNFEIKVSPQTT 416
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 17-412 6.25e-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: 119.83  E-value: 6.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  17 VRGALMSSFSpeklDEMTPLISQACELLVAHLKRYAASrdAFNIQRCYCCYTIDVVASVAFGTQVDsqnspEDPFVQhcr 96
Cdd:cd20674   69 TRSALQLGIR----NSLEPVVEQLTQELCERMRAQAGT--PVDIQEEFSLLTCSIICCLTFGDKED-----KDTLVQ--- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  97 rASTFCIPRplLVLILSFPSI----MVPLARILPNKnrdelngffntlirnviALRDQQAAEERRRDFLQMVLDaQHSMN 172
Cdd:cd20674  135 -AFHDCVQE--LLKTWGHWSIqaldSIPFLRFFPNP-----------------GLRRLKQAVENRDHIVESQLR-QHKES 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 173 SVGVEGFDMVPESLSSSECTKEppqrchpTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKE 252
Cdd:cd20674  194 LVAGQWRDMTDYMLQGLGQPRG-------EKGMGQLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEE 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 253 VDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPE 331
Cdd:cd20674  267 LDRVLGPGASPSYKDRAR-LPLLNATIAEVLRLRPVVpLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPH 345

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 332 TFDPERFTAEARLQRRpftYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPlqlesksALGPKNGVYIK 411
Cdd:cd20674  346 EFRPERFLEPGAANRA---LLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGALP-------SLQPVAGINLK 415


                 .
gi 568941360 412 I 412
Cdd:cd20674  416 V 416
PLN02290 PLN02290
cytokinin trans-hydroxylase
 220-410 2.09e-29

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 119.53  E-value: 2.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 220 FLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPaPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQD 299
Cdd:PLN02290 324 FFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGET-PSVDHLSK-LTLLNMVINESLRLYPPATLLPRMAFED 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 300 CEVLGQRIPAGTVLEIAVGALHHDPEHW-PNPETFDPERFTAEARLQRRPFtyLPFGAGPRSCLGVRLGLLVVKLTILQV 378
Cdd:PLN02290 402 IKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHF--IPFAAGPRNCIGQAFAMMEAKIILAML 479

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568941360 379 LHKFRFEASPETQ-VPLQLESksaLGPKNGVYI 410
Cdd:PLN02290 480 ISKFSFTISDNYRhAPVVVLT---IKPKYGVQV 509
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 207-382 3.86e-29

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


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 117.63  E-value: 3.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 207 PFTVDEIvgQAFLF--LIAGHEVITNTLSF-ITYLLaTHPDCQERLLKEVDLFMGKHPAPEyHSLQEGLPYLDMVISETL 283
Cdd:cd11073  226 ELTRNHI--KALLLdlFVAGTDTTSSTIEWaMAELL-RNPEKMAKARAELDEVIGKDKIVE-ESDISKLPYLQAVVKETL 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 284 RMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFtaearLQR------RPFTYLPFGA 356
Cdd:cd11073  302 RLHPPApLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERF-----LGSeidfkgRDFELIPFGS 376

                        170       180
                 ....*....|....*....|....*.
gi 568941360 357 GPRSCLGVRLGLLVVKLTILQVLHKF 382
Cdd:cd11073  377 GRRICPGLPLAERMVHLVLASLLHSF 402
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 155-375 4.42e-28

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


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 114.62  E-value: 4.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 155 ERRRDFLQMVLDaQHSMNSVGVEGfDMVPESLSSSEctKEPPqrchptstskpFTVDEIV-GQAFLFLIAGHEVITNTLS 233
Cdd:cd20653  184 KRRDAFLQGLID-EHRKNKESGKN-TMIDHLLSLQE--SQPE-----------YYTDEIIkGLILVMLLAGTDTSAVTLE 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 234 FITYLLATHPDC-------------QERLLKEVDLfmgkhpapeyhslqEGLPYLDMVISETLRMYPPA-FRFTREAAQD 299
Cdd:cd20653  249 WAMSNLLNHPEVlkkareeidtqvgQDRLIEESDL--------------PKLPYLQNIISETLRLYPAApLLVPHESSED 314

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941360 300 CEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRpftYLPFGAGPRSCLGVRLGLLVVKLTI 375
Cdd:cd20653  315 CKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREGYK---LIPFGLGRRACPGAGLAQRVVGLAL 387
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 212-389 6.82e-28

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 115.09  E-value: 6.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 212 EIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKE-VDLFMGKHPAPEYHSLQE----GLPYLDMVISETLRMY 286
Cdd:cd20622  262 VIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKAlYSAHPEAVAEGRLPTAQEiaqaRIPYLDAVIEEILRCA 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 287 PPAFRFTREAAQDCEVLGQRIPAGT-VLEIAVG------ALHHDPE-------------HW---PNPETFDPERF----- 338
Cdd:cd20622  342 NTAPILSREATVDTQVLGYSIPKGTnVFLLNNGpsylspPIEIDESrrssssaakgkkaGVwdsKDIADFDPERWlvtde 421

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568941360 339 -TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPE 389
Cdd:cd20622  422 eTGETVFDPSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPE 473
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 201-404 1.39e-27

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


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 113.35  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 201 PTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVIS 280
Cdd:cd20662  214 YPDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLAD-RESMPYTNAVIH 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 281 ETLRM---YPpaFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPfTYLPFGAG 357
Cdd:cd20662  293 EVQRMgniIP--LNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQFKKRE-AFLPFSMG 369

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568941360 358 PRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSALGP 404
Cdd:cd20662  370 KRACLGEQLARSELFIFFTSLLQKFTFKPPPNEKLSLKFRMGITLSP 416
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 239-397 5.05e-27

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 111.74  E-value: 5.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAV 317
Cdd:cd20657  255 LIRHPDILKKAQEEMDQVIGRDRRLLESDIPN-LPYLQAICKETFRLHPSTpLNLPRIASEACEVDGYYIPKGTRLLVNI 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 318 GALHHDPEHWPNPETFDPERFTAEARLQRRP----FTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE-ASPETQV 392
Cdd:cd20657  334 WAIGRDPDVWENPLEFKPERFLPGRNAKVDVrgndFELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKlPAGQTPE 413


                 ....*
gi 568941360 393 PLQLE 397
Cdd:cd20657  414 ELNME 418
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 239-394 5.80e-27

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


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 111.65  E-value: 5.80e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA--FRFTREAAQDCEVLGQRIPAGTVLEIA 316
Cdd:cd11076  251 MVLHPDIQSKAQAEIDAAVGGSRRVADSDVAK-LPYLQAVVKETLRLHPPGplLSWARLAIHDVTVGGHVVPAGTTAMVN 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 317 VGALHHDPEHWPNPETFDPERFTAEA------------RLQrrpftylPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRF 384
Cdd:cd11076  330 MWAITHDPHVWEDPLEFKPERFVAAEggadvsvlgsdlRLA-------PFGAGRRVCPGKALGLATVHLWVAQLLHEFEW 402

                        170
                 ....*....|
gi 568941360 385 EASPETQVPL 394
Cdd:cd11076  403 LPDDAKPVDL 412
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 219-403 1.95e-26

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 111.06  E-value: 1.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 219 LFlIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAA 297
Cdd:PLN02687 305 LF-TAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQ-LTYLQAVIKETFRLHPSTpLSLPRMAA 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 298 QDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFT-----AEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVK 372
Cdd:PLN02687 383 EECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpggehAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVT 462

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568941360 373 LTILQVLHKFRFEAsPETQVPLQLESKSALG 403
Cdd:PLN02687 463 LLTATLVHAFDWEL-ADGQTPDKLNMEEAYG 492
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 206-382 3.13e-26

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 110.19  E-value: 3.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 206 KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYH-SLQE--GLPYLDMVISET 282
Cdd:PLN02302 281 RKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKRPPGQKGlTLKDvrKMEYLSQVIDET 360

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 283 LRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFtaeARLQRRPFTYLPFGAGPRSCL 362
Cdd:PLN02302 361 LRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW---DNYTPKAGTFLPFGLGSRLCP 437

                        170       180
                 ....*....|....*....|
gi 568941360 363 GVRLGllvvKLTILQVLHKF 382
Cdd:PLN02302 438 GNDLA----KLEISIFLHHF 453
PLN02936 PLN02936
epsilon-ring hydroxylase
 221-415 7.79e-26

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 109.11  E-value: 7.79e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 221 LIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPaPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDc 300
Cdd:PLN02936 287 LVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRP-PTYEDIKE-LKYLTRCINESMRLYPHPPVLIRRAQVE- 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 301 EVL--GQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRP---FTYLPFGAGPRSCLGVRLGLLVVKLTI 375
Cdd:PLN02936 364 DVLpgGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETntdFRYIPFSGGPRKCVGDQFALLEAIVAL 443

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568941360 376 LQVLHKFRFEASPETQVplQLESKSALGPKNGVYIKIVSR 415
Cdd:PLN02936 444 AVLLQRLDLELVPDQDI--VMTTGATIHTTNGLYMTVSRR 481
PLN02655 PLN02655
ent-kaurene oxidase
 237-382 1.22e-25

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 108.29  E-value: 1.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 237 YLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQegLPYLDMVISETLRMYPPA----FRFTREaaqDCEVLGQRIPAGTV 312
Cdd:PLN02655 287 YELAKNPDKQERLYREIREVCGDERVTEEDLPN--LPYLNAVFHETLRKYSPVpllpPRFVHE---DTTLGGYDIPAGTQ 361

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 313 LEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKF 382
Cdd:PLN02655 362 IAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEF 431
PLN02738 PLN02738
carotene beta-ring hydroxylase
 221-415 3.50e-25

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 108.08  E-value: 3.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 221 LIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHpAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDc 300
Cdd:PLN02738 400 LIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDR-FPTIEDMKK-LKYTTRVINESLRLYPQPPVLIRRSLEN- 476

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 301 EVLGQ-RIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEA---RLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTIL 376
Cdd:PLN02738 477 DMLGGyPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPLDGpnpNETNQNFSYLPFGGGPRKCVGDMFASFENVVATA 556

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568941360 377 QVLHKFRFEASPETQvPLQLESKSALGPKNGVYIKIVSR 415
Cdd:PLN02738 557 MLVRRFDFQLAPGAP-PVKMTTGATIHTTEGLKMTVTRR 594
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 208-408 9.11e-25

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


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 105.14  E-value: 9.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHeviTNTLS----FITYLLAtHPDCQERLLKEVDLFMGKHPAPEYH----SLQEGLPYLDMVI 279
Cdd:cd11040  219 LSEEDIARAELALLWAIN---ANTIPaafwLLAHILS-DPELLERIREEIEPAVTPDSGTNAIldltDLLTSCPLLDSTY 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 280 SETLRMYPPAFRfTREAAQDCEVLGQ-RIPAGTVLEIAVGALHHDPEHW-PNPETFDPERF---TAEARLQRRPFTYLPF 354
Cdd:cd11040  295 LETLRLHSSSTS-VRLVTEDTVLGGGyLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkDGDKKGRGLPGAFRPF 373

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568941360 355 GAGPRSCLGVRLGLLVVKLTILQVLHKFRFE--ASPETQVPlQLESKSALG---PKNGV 408
Cdd:cd11040  374 GGGASLCPGRHFAKNEILAFVALLLSRFDVEpvGGGDWKVP-GMDESPGLGilpPKRDV 431
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 223-394 4.51e-24

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


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 103.26  E-value: 4.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 223 AGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRM---YPPAFrfTREAAQD 299
Cdd:cd20652  245 AGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSS-LPYLQACISESQRIrsvVPLGI--PHGCTED 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 300 CEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVL 379
Cdd:cd20652  322 AVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARIL 401

                        170
                 ....*....|....*
gi 568941360 380 HKFRFEASPETQVPL 394
Cdd:cd20652  402 RKFRIALPDGQPVDS 416
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 207-369 4.78e-24

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 102.91  E-value: 4.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 207 PFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVdlfMGKHPAPEYHSLQEGLPYLDMVISETLRMY 286
Cdd:cd20614  203 GLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEA---AAAGDVPRTPAELRRFPLAEALFRETLRLH 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 287 PPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTaEARLQRRPFTYLPFGAGPRSCLGVRL 366
Cdd:cd20614  280 PPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWL-GRDRAPNPVELLQFGGGPHFCLGYHV 358


                 ...
gi 568941360 367 GLL 369
Cdd:cd20614  359 ACV 361
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 208-383 7.81e-24

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 101.91  E-value: 7.81e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGkhpapeyhslqeglpyldmVISETLRMYP 287
Cdd:cd11032  194 LTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLIPG-------------------AIEEVLRYRP 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 288 PAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPErftaearlqRRPFTYLPFGAGPRSCLGVRLG 367
Cdd:cd11032  255 PVQRTARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDID---------RNPNPHLSFGHGIHFCLGAPLA 325

                        170
                 ....*....|....*.
gi 568941360 368 LLVVKLTILQVLHKFR 383
Cdd:cd11032  326 RLEARIALEALLDRFP 341
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 209-393 1.31e-23

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


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 101.99  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPP 288
Cdd:cd11041  224 TPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNK-LKKLDSFMKESQRLNPL 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 289 AFR-FTREAAQDcEVL--GQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF----TAEARLQRRPFT-----YLPFGA 356
Cdd:cd11041  303 SLVsLRRKVLKD-VTLsdGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFyrlrEQPGQEKKHQFVstspdFLGFGH 381

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568941360 357 GPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVP 393
Cdd:cd11041  382 GRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERP 418
PLN02183 PLN02183
ferulate 5-hydroxylase
 128-403 1.63e-23

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 102.24  E-value: 1.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 128 KNRDELNGFFNTLIRNVIALRDQQAAEERRRDflqmvldaqhsmnsvgVEgFDMVPESLS--SSECTKEPPQRchpTSTS 205
Cdd:PLN02183 238 KARKSLDGFIDDIIDDHIQKRKNQNADNDSEE----------------AE-TDMVDDLLAfySEEAKVNESDD---LQNS 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 206 KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLqEGLPYLDMVISETLRM 285
Cdd:PLN02183 298 IKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDL-EKLTYLKCTLKETLRL 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 286 YPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEA--RLQRRPFTYLPFGAGPRSCLG 363
Cdd:PLN02183 377 HPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGvpDFKGSHFEFIPFGSGRRSCPG 456

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 568941360 364 VRLGLLVVKLTILQVLHKFRFEAsPETQVPLQLESKSALG 403
Cdd:PLN02183 457 MQLGLYALDLAVAHLLHCFTWEL-PDGMKPSELDMNDVFG 495
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 209-390 1.89e-23

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: 101.66  E-value: 1.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVdlfMGKHPAPEYHSLQE--GLPYLDMVISETLRMY 286
Cdd:cd20646  230 SPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEV---ISVCPGDRIPTAEDiaKMPLLKAVIKETLRLY 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 287 P--PA-FRFTREaaQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLG 363
Cdd:cd20646  307 PvvPGnARVIVE--KEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVG 384

                        170       180
                 ....*....|....*....|....*..
gi 568941360 364 VRLGLLVVKLTILQVLHKFRFEASPET 390
Cdd:cd20646  385 RRIAELEMYLALSRLIKRFEVRPDPSG 411
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 213-389 2.73e-23

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: 100.98  E-value: 2.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 213 IVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRF 292
Cdd:cd20648  235 IYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVAR-MPLLKAVVKEVLRLYPVIPGN 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 293 TREAA-QDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEaRLQRRPFTYLPFGAGPRSCLGVRLGLLVV 371
Cdd:cd20648  314 ARVIPdRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGK-GDTHHPYASLPFGFGKRSCIGRRIAELEV 392

                        170
                 ....*....|....*...
gi 568941360 372 KLTILQVLhkFRFEASPE 389
Cdd:cd20648  393 YLALARIL--THFEVRPE 408
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 231-392 3.60e-23

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: 100.56  E-value: 3.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 231 TLSFITYLLATHPDCQERLLKEVdlfMGKHPAPEYHSLQ--EGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIP 308
Cdd:cd20643  253 TLQWTLYELARNPNVQEMLRAEV---LAARQEAQGDMVKmlKSVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIP 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 309 AGTVLEIAVGALHHDPEHWPNPETFDPERFTaeaRLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:cd20643  330 AGTLVQVGLYAMGRDPTVFPKPEKYDPERWL---SKDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIETQR 406


                 ....
gi 568941360 389 ETQV 392
Cdd:cd20643  407 LVEV 410
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 209-389 3.64e-23

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


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 100.44  E-value: 3.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIvgqaflfLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDlfmgKHPAPEYHSLQEGL----PYLDMVISETLR 284
Cdd:cd20615  219 TLDEM-------LFANLDVTTGVLSWNLVFLAANPAVQEKLREEIS----AAREQSGYPMEDYIlstdTLLAYCVLESLR 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 285 MYP-PAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHW-PNPETFDPERFTAEARLQRRpFTYLPFGAGPRSCL 362
Cdd:cd20615  288 LRPlLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWgPDGEAYRPERFLGISPTDLR-YNFWRFGFGPRKCL 366

                        170       180
                 ....*....|....*....|....*..
gi 568941360 363 GVRLGLLVVKLTILQVLHKFRFEASPE 389
Cdd:cd20615  367 GQHVADVILKALLAHLLEQYELKLPDQ 393
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 209-369 1.26e-22

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


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 98.39  E-value: 1.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDcQERLLKEvdlfmgkHPApeyhslqeglpYLDMVISETLRMYPP 288
Cdd:cd20625  198 SEDELVANCILLLVAGHETTVNLIGNGLLALLRHPE-QLALLRA-------DPE-----------LIPAAVEELLRYDSP 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 289 AFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPerftaearlQRRPFTYLPFGAGPRSCLGVRLGL 368
Cdd:cd20625  259 VQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDI---------TRAPNRHLAFGAGIHFCLGAPLAR 329


                 .
gi 568941360 369 L 369
Cdd:cd20625  330 L 330
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 209-363 2.15e-22

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


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 97.37  E-value: 2.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMVISETLRMYPP 288
Cdd:cd20629  189 DDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRRDRSL-------------------IPAAIEEGLRWEPP 249

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568941360 289 AFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDperftaearLQRRPFTYLPFGAGPRSCLG 363
Cdd:cd20629  250 VASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFD---------IDRKPKPHLVFGGGAHRCLG 315
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 222-392 2.39e-22

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 98.34  E-value: 2.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 222 IAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMyPPAFRFTREAAQDCE 301
Cdd:cd20645  236 IGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKN-MPYLKACLKESMRL-TPSVPFTSRTLDKDT 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 302 VLGQR-IPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARlQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLH 380
Cdd:cd20645  314 VLGDYlLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKH-SINPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQ 392

                        170
                 ....*....|..
gi 568941360 381 KFRFEASPETQV 392
Cdd:cd20645  393 KYQIVATDNEPV 404
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 211-398 3.71e-22

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


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 97.25  E-value: 3.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 211 DEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMVISETLRMYPP-- 288
Cdd:cd11031  205 EELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRADPEL-------------------VPAAVEELLRYIPLga 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 289 AFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPErftaearlqRRPFTYLPFGAGPRSCLGVRLGL 368
Cdd:cd11031  266 GGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLD---------REPNPHLAFGHGPHHCLGAPLAR 336

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568941360 369 LVVKLTILQVLHKF---RFeASPETQVPLQLES 398
Cdd:cd11031  337 LELQVALGALLRRLpglRL-AVPEEELRWREGL 368
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 211-393 6.71e-22

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


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 97.17  E-value: 6.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 211 DEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA- 289
Cdd:cd20656  229 DTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQ-LPYLQCVVKEALRLHPPTp 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 290 FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAE-ARLQRRPFTYLPFGAGPRSCLGVRLGL 368
Cdd:cd20656  308 LMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEdVDIKGHDFRLLPFGAGRRVCPGAQLGI 387

                        170       180
                 ....*....|....*....|....*
gi 568941360 369 LVVKLTILQVLHKFRFeASPETQVP 393
Cdd:cd20656  388 NLVTLMLGHLLHHFSW-TPPEGTPP 411
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 212-383 1.09e-21

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


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 96.27  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 212 EIVGQAFL-FLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHpAPEYHSLQeGLPYLDMVISETLRmYPPAF 290
Cdd:cd20616  223 ENVNQCVLeMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGER-DIQNDDLQ-KLKVLENFINESMR-YQPVV 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 291 RFT-REAAQDCEVLGQRIPAGTVLEIAVGALHHDpEHWPNPETFDPERFTAEArlqrrPFTYL-PFGAGPRSCLGVRLGL 368
Cdd:cd20616  300 DFVmRKALEDDVIDGYPVKKGTNIILNIGRMHRL-EFFPKPNEFTLENFEKNV-----PSRYFqPFGFGPRSCVGKYIAM 373

                        170
                 ....*....|....*
gi 568941360 369 LVVKLTILQVLHKFR 383
Cdd:cd20616  374 VMMKAILVTLLRRFQ 388
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 219-382 1.13e-21

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 96.85  E-value: 1.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 219 LFlIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAA 297
Cdd:PLN00110 297 LF-TAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPK-LPYLQAICKESFRKHPSTpLNLPRVST 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 298 QDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRP----FTYLPFGAGPRSCLGVRLGLLVVKL 373
Cdd:PLN00110 375 QACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDPrgndFELIPFGAGRRICAGTRMGIVLVEY 454


                 ....*....
gi 568941360 374 TILQVLHKF 382
Cdd:PLN00110 455 ILGTLVHSF 463
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 70-394 1.53e-21

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


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 96.00  E-value: 1.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  70 DVVASVAFGTQVDSQNSPEDPFVQHCRRASTFCIPRPLlvlILSFPSIMVPLARILPNKNRDELNGFFNTLIRNVIALRD 149
Cdd:cd20666  117 NVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAA---ILVNICPWLYYLPFGPFRELRQIEKDITAFLKKIIADHR 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 150 QQAAEERRRDFLQMVLdaqhsmnsvgvegFDMVPESLSSSECTkeppqrchptstskpFTVD---EIVGQAFlflIAGHE 226
Cdd:cd20666  194 ETLDPANPRDFIDMYL-------------LHIEEEQKNNAESS---------------FNEDylfYIIGDLF---IAGTD 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 227 VITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVISETLRMYP-PAFRFTREAAQDCEVLGQ 305
Cdd:cd20666  243 TTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTD-KAQMPFTEATIMEVQRMTVvVPLSIPHMASENTVLQGY 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 306 RIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAE-ARLQRRPfTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRF 384
Cdd:cd20666  322 TIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDEnGQLIKKE-AFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTF 400

                        330
                 ....*....|
gi 568941360 385 EASPETQVPL 394
Cdd:cd20666  401 LLPPNAPKPS 410
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 207-393 2.43e-21

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 94.59  E-value: 2.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 207 PFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMVISETLRMY 286
Cdd:cd11078  204 RLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSL-------------------IPNAVEETLRYD 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 287 PPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEArlqrrpftYLPFGAGPRSCLGV-- 364
Cdd:cd11078  265 SPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDRPNARK--------HLTFGHGIHFCLGAal 336

                        170       180       190
                 ....*....|....*....|....*....|
gi 568941360 365 -RLGLLVVKLTILQVLHKFRFEASPETQVP 393
Cdd:cd11078  337 aRMEARIALEELLRRLPGMRVPGQEVVYSP 366
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 206-388 8.61e-21

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


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 93.75  E-value: 8.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 206 KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVD---LFMGKHPAPEYHSLQE--GLPYLDMVIS 280
Cdd:cd20636  221 KELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVshgLIDQCQCCPGALSLEKlsRLRYLDCVVK 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 281 ETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTA---EARLQRrpFTYLPFGAG 357
Cdd:cd20636  301 EVLRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVereESKSGR--FNYIPFGGG 378

                        170       180       190
                 ....*....|....*....|....*....|..
gi 568941360 358 PRSCLGVRLGLLVVKLTILQVLHKFRFE-ASP 388
Cdd:cd20636  379 VRSCIGKELAQVILKTLAVELVTTARWElATP 410
PTZ00404 PTZ00404
cytochrome P450; Provisional
 213-392 1.09e-20

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 93.63  E-value: 1.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 213 IVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FR 291
Cdd:PTZ00404 284 ILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQS-TPYTVAIIKETLRYKPVSpFG 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 292 FTREAAQDCEVL-GQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAearlQRRPFTYLPFGAGPRSCLGVRLGLLV 370
Cdd:PTZ00404 363 LPRSTSNDIIIGgGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLN----PDSNDAFMPFSIGPRNCVGQQFAQDE 438

                        170       180
                 ....*....|....*....|..
gi 568941360 371 VKLTILQVLHKFRFEASPETQV 392
Cdd:PTZ00404 439 LYLAFSNIILNFKLKSIDGKKI 460
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 208-390 4.68e-20

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 91.41  E-value: 4.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIvgqaflfLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYP 287
Cdd:cd20661  241 FSVGEL-------IIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCK-MPYTEAVLHEVLRFCN 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 288 PA----FRFTreaAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLG 363
Cdd:cd20661  313 IVplgiFHAT---SKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLG 389

                        170       180
                 ....*....|....*....|....*..
gi 568941360 364 VRLGLLVVKLTILQVLHKFRFEASPET 390
Cdd:cd20661  390 EQLARMEMFLFFTALLQRFHLHFPHGL 416
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 206-363 4.68e-20

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 90.73  E-value: 4.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 206 KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMgkhpapeyhslqeglpyldMVISETLRM 285
Cdd:cd11035  184 RPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLREDPELIP-------------------AAVEELLRR 244

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568941360 286 YPPAFRFtREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPErftaearlqRRPFTYLPFGAGPRSCLG 363
Cdd:cd11035  245 YPLVNVA-RIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFD---------RKPNRHLAFGAGPHRCLG 312
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 239-388 6.02e-20

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 91.38  E-value: 6.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLR--MYPPAFrFTREAAQDCEVLGQRIPAGTvlEIA 316
Cdd:cd11074  260 LVNHPEIQKKLRDELDTVLGPGVQITEPDLHK-LPYLQAVVKETLRlrMAIPLL-VPHMNLHDAKLGGYDIPAES--KIL 335

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941360 317 VGA--LHHDPEHWPNPETFDPERFTAE---ARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:cd11074  336 VNAwwLANNPAHWKKPEEFRPERFLEEeskVEANGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPPP 412
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 209-366 8.88e-20

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-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: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 90.28  E-value: 8.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDcQERLLKEvdlfmgkHPAPeyhslqeglpyLDMVISETLRMYPP 288
Cdd:cd11029  208 SEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPD-QLALLRA-------DPEL-----------WPAAVEELLRYDGP 268

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568941360 289 AFRFT-REAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEarlqrrpftYLPFGAGPRSCLGVRL 366
Cdd:cd11029  269 VALATlRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITRDANG---------HLAFGHGIHYCLGAPL 338
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 207-405 1.08e-19

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


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 90.45  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 207 PFTVDEIVGqaflfliAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVISETLRmy 286
Cdd:cd20675  237 PSTVTDIFG-------ASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIED-QPNLPYVMAFLYEAMR-- 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 287 ppafrFT--------REAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEA-RLQR-RPFTYLPFGA 356
Cdd:cd20675  307 -----FSsfvpvtipHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENgFLNKdLASSVMIFSV 381

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568941360 357 GPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSALGPK 405
Cdd:cd20675  382 GKRRCIGEELSKMQLFLFTSILAHQCNFTANPNEPLTMDFSYGLTLKPK 430
PLN00168 PLN00168
Cytochrome P450; Provisional
 82-392 2.84e-19

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 89.62  E-value: 2.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  82 DSQNSPEDPFVQHCRRASTFCiprpLLVLILSFPSIMVPLARILPNKNRDEL---------NGFFNTLIRNVIALRDQQA 152
Cdd:PLN00168 168 REAEDAAAPRVVETFQYAMFC----LLVLMCFGERLDEPAVRAIAAAQRDWLlyvskkmsvFAFFPAVTKHLFRGRLQKA 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 153 AEERRRD---FLQMVLDAQHSMNSVGVEGFDMVPESLSSSECTKEPPQRCHPTSTSKPFTVDEIVGQAFLFLIAGHEVIT 229
Cdd:PLN00168 244 LALRRRQkelFVPLIDARREYKNHLGQGGEPPKKETTFEHSYVDTLLDIRLPEDGDRALTDDEIVNLCSEFLNAGTDTTS 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 230 NTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIP 308
Cdd:PLN00168 324 TALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEVSEEDVHKMPYLKAVVLEGLRKHPPAhFVLPHKAAEDMEVGGYLIP 403

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 309 AGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQ------RRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKF 382
Cdd:PLN00168 404 KGATVNFMVAEMGRDEREWERPMEFVPERFLAGGDGEgvdvtgSREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREF 483

                        330
                 ....*....|
gi 568941360 383 RFEASPETQV 392
Cdd:PLN00168 484 EWKEVPGDEV 493
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 208-389 4.12e-19

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


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 88.46  E-value: 4.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAP-EYHSLQEgLPYLDMVISETLRMY 286
Cdd:cd11082  216 SSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPlTLDLLEE-MKYTRQVVKEVLRYR 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 287 PPA----------FRFTREAAqdcevlgqrIPAGTVLEIAVGALHHDPehWPNPETFDPERFTAEaRLQRRPFT--YLPF 354
Cdd:cd11082  295 PPApmvphiakkdFPLTEDYT---------VPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPE-RQEDRKYKknFLVF 362

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568941360 355 GAGPRSCLGVRLGL--LVVKLTILQVLHKFRFEASPE 389
Cdd:cd11082  363 GAGPHQCVGQEYAInhLMLFLALFSTLVDWKRHRTPG 399
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 232-387 5.38e-19

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: 88.36  E-value: 5.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 232 LSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGT 311
Cdd:cd20644  252 LLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTE-LPLLKAALKETLRLYPVGITVQRVPSSDLVLQNYHIPAGT 330

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568941360 312 VLEIAVGALHHDPEHWPNPETFDPERFTAEaRLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEAS 387
Cdd:cd20644  331 LVQVFLYSLGRSAALFPRPERYDPQRWLDI-RGSGRNFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVETL 405
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 151-374 1.07e-18

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


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 87.56  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 151 QAAEERRRDFLQMVLDAQHSMNSVGVEGFDMV----PESLSSSECTKEPPQRC---------HPTSTSKPFTVDEIVGQA 217
Cdd:cd20638  156 EAFEEMIRNLFSLPIDVPFSGLYRGLRARNLIhakiEENIRAKIQREDTEQQCkdalqllieHSRRNGEPLNLQALKESA 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 218 FLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDL--FMGKHPAPEYH---SLQEGLPYLDMVISETLRMYPPAFRF 292
Cdd:cd20638  236 TELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEkgLLSTKPNENKElsmEVLEQLKYTGCVIKETLRLSPPVPGG 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 293 TREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLG-----VRLG 367
Cdd:cd20638  316 FRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGkefakVLLK 395


                 ....*..
gi 568941360 368 LLVVKLT 374
Cdd:cd20638  396 IFTVELA 402
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 239-388 2.01e-18

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 87.10  E-value: 2.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 239 LATHPDCQERLLKEVDLFMGK-HPAPEyhSLQEGLPYLDMVISETLRMYPP-AFRFTREAAQDCEVLGQRIPAGTvlEIA 316
Cdd:PLN02394 320 LVNHPEIQKKLRDELDTVLGPgNQVTE--PDTHKLPYLQAVVKETLRLHMAiPLLVPHMNLEDAKLGGYDIPAES--KIL 395

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941360 317 VGA--LHHDPEHWPNPETFDPERFTAE---ARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASP 388
Cdd:PLN02394 396 VNAwwLANNPELWKNPEEFRPERFLEEeakVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPP 472
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 208-389 2.44e-18

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


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 86.39  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVISETLR--- 284
Cdd:cd20668  222 FYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFED-RAKMPYTEAVIHEIQRfgd 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 285 MYPpaFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLG- 363
Cdd:cd20668  301 VIP--MGLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGe 378

                        170       180
                 ....*....|....*....|....*...
gi 568941360 364 --VRLGLLVVKLTILQVLHkFRFEASPE 389
Cdd:cd20668  379 glARMELFLFFTTIMQNFR-FKSPQSPE 405
PLN02966 PLN02966
cytochrome P450 83A1
 14-385 4.07e-18

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 86.34  E-value: 4.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  14 WEEVRGALMSS-FSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPFV 92
Cdd:PLN02966 123 YREIRKMGMNHlFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFI 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  93 QHCRRASTfciprpllVLILSFPSIMVPLARILpnknrDELNGFFNTLirnvialrdqQAAEERRRDFLQMVLDAQHSMN 172
Cdd:PLN02966 203 KILYGTQS--------VLGKIFFSDFFPYCGFL-----DDLSGLTAYM----------KECFERQDTYIQEVVNETLDPK 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 173 SVGVEGFDMVPESLsssECTKEPPqrchptsTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKE 252
Cdd:PLN02966 260 RVKPETESMIDLLM---EIYKEQP-------FASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAE 329

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 253 VDLFMgKHPAPEYHSLQE--GLPYLDMVISETLRMYPP-AFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHW-P 328
Cdd:PLN02966 330 VREYM-KEKGSTFVTEDDvkNLPYFRALVKETLRIEPViPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgP 408

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568941360 329 NPETFDPERF-TAEARLQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE 385
Cdd:PLN02966 409 NPDEFRPERFlEKEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFK 466
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 208-388 4.58e-18

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


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 85.62  E-value: 4.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVISETLRMYP 287
Cdd:cd20671  219 FHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYED-RKALPYTSAVIHEVQRFIT 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 288 PAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-TAEARLQRRPfTYLPFGAGPRSCLGVRL 366
Cdd:cd20671  298 LLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFlDAEGKFVKKE-AFLPFSAGRRVCVGESL 376

                        170       180
                 ....*....|....*....|..
gi 568941360 367 GLLVVKLTILQVLHKFRFEASP 388
Cdd:cd20671  377 ARTELFIFFTGLLQKFTFLPPP 398
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 200-366 6.00e-18

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. 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: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 84.89  E-value: 6.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 200 HPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMVI 279
Cdd:cd11033  197 NAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRADPSL-------------------LPTAV 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 280 SETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPErftaearlqRRPFTYLPFGAGPR 359
Cdd:cd11033  258 EEILRWASPVIHFRRTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDIT---------RSPNPHLAFGGGPH 328


                 ....*..
gi 568941360 360 SCLGVRL 366
Cdd:cd11033  329 FCLGAHL 335
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 208-376 1.09e-17

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


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 83.95  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDcQERLLKEvdlfmgkhpapeyhslQEGLPylDMVISETLRMYP 287
Cdd:cd11038  210 LSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALRE----------------DPELA--PAAVEEVLRWCP 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 288 PAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDpehwpnPETFDPERFTAEARLQrRPFTylpFGAGPRSCLGVRLG 367
Cdd:cd11038  271 TTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRD------PRVFDADRFDITAKRA-PHLG---FGGGVHHCLGAFLA 340

                        170
                 ....*....|.
gi 568941360 368 L--LVVKLTIL 376
Cdd:cd11038  341 RaeLAEALTVL 351
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 208-377 1.13e-17

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 84.24  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPeyhSLQE--GLPYLDMVISETLR- 284
Cdd:cd20665  222 FTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSP---CMQDrsHMPYTDAVIHEIQRy 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 285 --MYP---PafrftREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPR 359
Cdd:cd20665  299 idLVPnnlP-----HAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKR 373

                        170       180
                 ....*....|....*....|.
gi 568941360 360 SCLG---VRLGLLVVKLTILQ 377
Cdd:cd20665  374 ICAGeglARMELFLFLTTILQ 394
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 211-412 1.26e-17

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 84.60  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 211 DEIVGQAFlfliAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEG--LPYLDMVISETLRMyPP 288
Cdd:PLN02196 267 DNIIGVIF----AARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGESLTWEDTkkMPLTSRVIQETLRV-AS 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 289 AFRFT-REAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFtaeaRLQRRPFTYLPFGAGPRSCLGVRLG 367
Cdd:PLN02196 342 ILSFTfREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF----EVAPKPNTFMPFGNGTHSCPGNELA 417

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568941360 368 llvvKLTILQVLH----KFRFEASpETQVPLQLeSKSALgPKNGVYIKI 412
Cdd:PLN02196 418 ----KLEISVLIHhlttKYRWSIV-GTSNGIQY-GPFAL-PQNGLPIAL 459
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 242-403 1.62e-17

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 84.49  E-value: 1.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 242 HPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGAL 320
Cdd:PLN03112 326 NPRVLRKIQEELDSVVGRNRMVQESDLVH-LNYLRCVVRETFRMHPAGpFLIPHESLRATTINGYYIPAKTRVFINTHGL 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 321 HHDPEHWPNPETFDPERFTA--EARL---QRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFeASPETQVPLQ 395
Cdd:PLN03112 405 GRNTKIWDDVEEFRPERHWPaeGSRVeisHGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDW-SPPDGLRPED 483


                 ....*...
gi 568941360 396 LESKSALG 403
Cdd:PLN03112 484 IDTQEVYG 491
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 212-385 1.97e-17

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


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 83.29  E-value: 1.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 212 EIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMVISETLRMYPPAFR 291
Cdd:cd11080  193 DIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRADRSL-------------------VPRAIAETLRYHPPVQL 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 292 FTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPER--------FTAEARlqrrpftYLPFGAGPRSCLG 363
Cdd:cd11080  254 IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHRedlgirsaFSGAAD-------HLAFGSGRHFCVG 326

                        170       180
                 ....*....|....*....|....*
gi 568941360 364 VRLG---LLVVKLTILQVLHKFRFE 385
Cdd:cd11080  327 AALAkreIEIVANQVLDALPNIRLE 351
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 223-393 3.32e-17

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: 83.13  E-value: 3.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 223 AGHEVITNTLSFITYLLATHP--DCQERLLKEVDLFMGKHPAPEYHSLQEG-LPYLDMVISETLRMYPP-AFRFTREAAQ 298
Cdd:cd11066  239 AGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAEEkCPYVVALVKETLRYFTVlPLGLPRKTTK 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 299 DCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPER-FTAEARLQRRPFTYlPFGAGPRSCLGVRLGLLVVKLTILQ 377
Cdd:cd11066  319 DIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERwLDASGDLIPGPPHF-SFGAGSRMCAGSHLANRELYTAICR 397

                        170
                 ....*....|....*.
gi 568941360 378 VLHKFRFEASPETQVP 393
Cdd:cd11066  398 LILLFRIGPKDEEEPM 413
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 220-415 4.13e-17

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 83.29  E-value: 4.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 220 FLIAGHEVITNTLSFITYLLATHPDCQERL---LKEVDLFMGKHPAPE-----------------YHSLQEgLPYLDMVI 279
Cdd:PLN03195 300 FVIAGRDTTATTLSWFVYMIMMNPHVAEKLyseLKALEKERAKEEDPEdsqsfnqrvtqfaglltYDSLGK-LQYLHAVI 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 280 SETLRMYPPAFRFTREAAQDcEVL--GQRIPAGTVLEIAVGALHHDPEHW-PNPETFDPERFTAEARLQR-RPFTYLPFG 355
Cdd:PLN03195 379 TETLRLYPAVPQDPKGILED-DVLpdGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVFQNaSPFKFTAFQ 457

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 356 AGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVplQLESKSALGPKNGVYIKIVSR 415
Cdd:PLN03195 458 AGPRICLGKDSAYLQMKMALALLCRFFKFQLVPGHPV--KYRMMTILSMANGLKVTVSRR 515
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 209-394 1.15e-16

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


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 81.30  E-value: 1.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGqaflfliAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLR--MY 286
Cdd:cd20677  240 TVNDIFG-------AGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKS-LHYTEAFINEVFRhsSF 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 287 PPaFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFT--YLPFGAGPRSCLG- 363
Cdd:cd20677  312 VP-FTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVekVLIFGMGVRKCLGe 390

                        170       180       190
                 ....*....|....*....|....*....|...
gi 568941360 364 --VRLGLLVVKLTILQVLHkfrFEASPETQVPL 394
Cdd:cd20677  391 dvARNEIFVFLTTILQQLK---LEKPPGQKLDL 420
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 206-393 1.22e-16

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


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 80.84  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 206 KPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMVISETLRM 285
Cdd:cd11034  184 KPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLIADPSL-------------------IPNAVEEFLRF 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 286 YPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDperftaearLQRRPFTYLPFGAGPRSCLGVR 365
Cdd:cd11034  245 YSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRID---------IDRTPNRHLAFGSGVHRCLGSH 315

                        170       180
                 ....*....|....*....|....*....
gi 568941360 366 LGLLVVKLTILQVLHKFR-FEASPETQVP 393
Cdd:cd11034  316 LARVEARVALTEVLKRIPdFELDPGATCE 344
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 223-403 4.34e-16

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


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 79.46  E-value: 4.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 223 AGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQegLPYLDMVISETLRMYPPA-FRFTREAAQDCE 301
Cdd:cd20664  236 AGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKN--MPYTDAVIHEIQRFANIVpMNLPHATTRDVT 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 302 VLGQRIPAGT-VLEIAVGALHhDPEHWPNPETFDPERF-TAEARLQRRPfTYLPFGAGPRSCLGVRLGLLVVKLTILQVL 379
Cdd:cd20664  314 FRGYFIPKGTyVIPLLTSVLQ-DKTEWEKPEEFNPEHFlDSQGKFVKRD-AFMPFSAGRRVCIGETLAKMELFLFFTSLL 391

                        170       180
                 ....*....|....*....|....
gi 568941360 380 HKFRFEASPETQVPlQLESKSALG 403
Cdd:cd20664  392 QRFRFQPPPGVSED-DLDLTPGLG 414
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 220-366 4.82e-16

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 79.16  E-value: 4.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 220 FLIAGHEVITNTLSFITYLLATHPDcQERLLKEvDlfmgkhpapeyHSLQEGlpyldmVISETLRMYPPAFRFTREAAQD 299
Cdd:cd11037  210 YLSAGLDTTISAIGNALWLLARHPD-QWERLRA-D-----------PSLAPN------AFEEAVRLESPVQTFSRTTTRD 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941360 300 CEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDperftaearLQRRPFTYLPFGAGPRSCLGVRL 366
Cdd:cd11037  271 TELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFD---------ITRNPSGHVGFGHGVHACVGQHL 328
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 271-411 5.15e-16

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 79.51  E-value: 5.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 271 GLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFtAEARLQRRP-- 348
Cdd:cd20637  290 SLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRF-GQERSEDKDgr 368

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941360 349 FTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASpeTQVPLQLESKSALGPKNGVYIK 411
Cdd:cd20637  369 FHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFELA--TRTFPRMTTVPVVHPVDGLRVK 429
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 208-363 6.14e-16

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 78.72  E-value: 6.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMVISETLRMYP 287
Cdd:cd11030  204 LTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALRADPSL-------------------VPGAVEELLRYLS 264

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568941360 288 PA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDperftaearLQRRPFTYLPFGAGPRSCLG 363
Cdd:cd11030  265 IVqDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLD---------ITRPARRHLAFGHGVHQCLG 332
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 223-388 6.30e-16

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 79.29  E-value: 6.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 223 AGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYhSLQEGLPYLDMVISETLR--MYPPaFRFTREAAQDC 300
Cdd:cd20676  248 AGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRL-SDRPQLPYLEAFILETFRhsSFVP-FTIPHCTTRDT 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 301 EVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-TAEARLQRRPFT--YLPFGAGPRSCLGVRLGLLVVKLTILQ 377
Cdd:cd20676  326 SLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFlTADGTEINKTESekVMLFGLGKRRCIGESIARWEVFLFLAI 405

                        170
                 ....*....|.
gi 568941360 378 VLHKFRFEASP 388
Cdd:cd20676  406 LLQQLEFSVPP 416
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 14-382 7.48e-16

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 79.35  E-value: 7.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  14 WEEVRGALMSS-FSPEKLDEMTPLISQACELLVAHLKRYAASRDAFNIQRCYCCYTIDVVASVAFGTQVDSQNSPEDPFV 92
Cdd:PLN03234 122 YREMRKMCMVNlFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFI 201

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360  93 QHCRRASTfciprpllVLILSFPSIMVPLARILpnknrDELNGffntlirnvIALRDQQAAEERRrDFLQMVLDAQHSMN 172
Cdd:PLN03234 202 DILYETQA--------LLGTLFFSDLFPYFGFL-----DNLTG---------LSARLKKAFKELD-TYLQELLDETLDPN 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 173 SVGVEGFDMVPESLsssECTKEPPqrchptsTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKE 252
Cdd:PLN03234 259 RPKQETESFIDLLM---QIYKDQP-------FSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDE 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 253 VDLFMGKHpapEYHSLQE--GLPYLDMVISETLRMYPP-AFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHW-P 328
Cdd:PLN03234 329 VRNVIGDK---GYVSEEDipNLPYLKAVIKESLRLEPViPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgD 405

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568941360 329 NPETFDPERFTAEAR---LQRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKF 382
Cdd:PLN03234 406 NPNEFIPERFMKEHKgvdFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKF 462
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 201-397 7.85e-16

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


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 78.73  E-value: 7.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 201 PTSTskpFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMG-KHPApeYHSLQEGLPYLDMVI 279
Cdd:cd20667  217 PVST---FSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGaSQLI--CYEDRKRLPYTNAVI 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 280 SETLRMYP-PAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGP 358
Cdd:cd20667  292 HEVQRLSNvVSVGAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGH 371

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568941360 359 RSCLGVRLGLLVVKLTILQVLHKFRFEAsPETQVPLQLE 397
Cdd:cd20667  372 RVCLGEQLARMELFIFFTTLLRTFNFQL-PEGVQELNLE 409
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 231-396 1.04e-15

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


Pssm-ID: 410728  Cd Length: 410  Bit Score: 78.51  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 231 TLSFITyllaTHPDCQERLLKEVD---LFMGKHPAPEYHSLQEGLPYLDMVISETLRMYPPAFrFTREAAQDCEVLGQRI 307
Cdd:cd20635  233 TLAFIL----SHPSVYKKVMEEISsvlGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGA-ITRKVVKPIKIKNYTI 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 308 PAGTVLEIAVGALHHDPEHWPNPETFDPERFTaEARLQRRPF--TYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE 385
Cdd:cd20635  308 PAGDMLMLSPYWAHRNPKYFPDPELFKPERWK-KADLEKNVFleGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFT 386

                        170
                 ....*....|...
gi 568941360 386 ASPE--TQVPLQL 396
Cdd:cd20635  387 LLDPvpKPSPLHL 399
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 208-389 1.04e-15

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


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 78.26  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLR--- 284
Cdd:cd20669  222 FNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRAR-MPYTDAVIHEIQRfad 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 285 MYPpaFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGV 364
Cdd:cd20669  301 IIP--MSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGE 378

                        170       180
                 ....*....|....*....|....*..
gi 568941360 365 RLGLLVVKLTILQVLHKFRFE--ASPE 389
Cdd:cd20669  379 SLARMELFLYLTAILQNFSLQplGAPE 405
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 220-393 1.63e-15

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 78.19  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 220 FLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMG-KHPAPEYHSLQEgLPYLDMVISETLRMYPPAfRFTREAAQ 298
Cdd:PLN02426 301 FLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGpNQEAASFEEMKE-MHYLHAALYESMRLFPPV-QFDSKFAA 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 299 DCEVL--GQRIPAGTVLEIAVGALHHDPEHW-PNPETFDPERFTAEAR-LQRRPFTYLPFGAGPRSCLGVRLGLLVVKLT 374
Cdd:PLN02426 379 EDDVLpdGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVfVPENPFKYPVFQAGLRVCLGKEMALMEMKSV 458

                        170       180
                 ....*....|....*....|
gi 568941360 375 ILQVLHKFRFEASPE-TQVP 393
Cdd:PLN02426 459 AVAVVRRFDIEVVGRsNRAP 478
PLN03018 PLN03018
homomethionine N-hydroxylase
 209-401 4.54e-15

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 76.97  E-value: 4.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 209 TVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYPP 288
Cdd:PLN03018 311 TPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPN-LNYLKACCRETFRIHPS 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 289 AFRFTREAA-QDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPER------FTAEARLQRRPFTYLPFGAGPRSC 361
Cdd:PLN03018 390 AHYVPPHVArQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERhlqgdgITKEVTLVETEMRFVSFSTGRRGC 469

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568941360 362 LGVRLGLLVVKLTILQVLHKFRFEASPETQvPLQLESKSA 401
Cdd:PLN03018 470 VGVKVGTIMMVMMLARFLQGFNWKLHQDFG-PLSLEEDDA 508
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 208-393 7.59e-15

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


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 75.73  E-value: 7.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVISETLRMYP 287
Cdd:cd20670  222 FNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDD-RVKMPYTDAVIHEIQRLTD 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 288 PA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLGVRL 366
Cdd:cd20670  301 IVpLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAM 380

                        170       180
                 ....*....|....*....|....*..
gi 568941360 367 GLLVVKLTILQVLHKFrfeaSPETQVP 393
Cdd:cd20670  381 ARMELFLYFTSILQNF----SLRSLVP 403
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 219-391 1.17e-14

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


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 75.12  E-value: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 219 LFlIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVISETLRMYPPA-FRFTREAA 297
Cdd:cd20663  238 LF-SAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMAD-QARMPYTNAVIHEVQRFGDIVpLGVPHMTS 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 298 QDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-TAEARLQrRPFTYLPFGAGPRSCLG---VRLGLLVVKL 373
Cdd:cd20663  316 RDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFlDAQGHFV-KPEAFMPFSAGRRACLGeplARMELFLFFT 394

                        170
                 ....*....|....*...
gi 568941360 374 TILQvlhKFRFEAsPETQ 391
Cdd:cd20663  395 CLLQ---RFSFSV-PAGQ 408
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 212-383 4.25e-14

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 73.31  E-value: 4.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 212 EIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPApeyhSLQ--EGLPYLDMVISETLRmyppA 289
Cdd:cd20627  202 QVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGKGPI----TLEkiEQLRYCQQVLCETVR----T 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 290 FRFTREAAQDCEVLGQ----RIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRrpFTYLPFgAGPRSCLGVR 365
Cdd:cd20627  274 AKLTPVSARLQELEGKvdqhIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDESVMKS--FSLLGF-SGSQECPELR 350

                        170
                 ....*....|....*...
gi 568941360 366 LGLLVVKLTILQVLHKFR 383
Cdd:cd20627  351 FAYMVATVLLSVLVRKLR 368
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 208-391 7.29e-14

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 73.09  E-value: 7.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPeyHSLQ----EGLPYLDMVISETL 283
Cdd:PLN02987 263 FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDS--YSLEwsdyKSMPFTQCVVNETL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 284 RMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLG 363
Cdd:PLN02987 341 RVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPG 420

                        170       180       190
                 ....*....|....*....|....*....|
gi 568941360 364 VRLGLLVVKLtilqVLHKF--RFEASPETQ 391
Cdd:PLN02987 421 YELARVALSV----FLHRLvtRFSWVPAEQ 446
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 218-377 8.91e-14

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 72.50  E-value: 8.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 218 FLFLiAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSlQEGLPYLDMVISETLRMYPPA-FRFTREA 296
Cdd:cd20672  233 SLFF-AGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDD-RAKMPYTDAVIHEIQRFSDLIpIGVPHRV 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 297 AQDCEVLGQRIPAGT-VLEIAVGALhHDPEHWPNPETFDPERFTAEARLQRRPFTYLPFGAGPRSCLG---VRLGLLVVK 372
Cdd:cd20672  311 TKDTLFRGYLLPKNTeVYPILSSAL-HDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGegiARNELFLFF 389


                 ....*
gi 568941360 373 LTILQ 377
Cdd:cd20672  390 TTILQ 394
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 140-382 1.20e-13

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 71.69  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 140 LIRNVIALRDQQAAEErrrDFLQMVLDAQHsmnsvgvEGfdmvpESLSSsectkeppqrchptstskpftvDEIVGQAFL 219
Cdd:cd20630  168 LIEEVIAERRQAPVED---DLLTTLLRAEE-------DG-----ERLSE----------------------DELMALVAA 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 220 FLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGkhpapeyhslqeglpyldmVISETLRmYPPAFR--FTREAA 297
Cdd:cd20630  211 LIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPELLRN-------------------ALEEVLR-WDNFGKmgTARYAT 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 298 QDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPErftaearlqRRPFTYLPFGAGPRSCLGVRLGLLVVKLTILQ 377
Cdd:cd20630  271 EDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVR---------RDPNANIAFGYGPHFCIGAALARLELELAVST 341


                 ....*
gi 568941360 378 VLHKF 382
Cdd:cd20630  342 LLRRF 346
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 218-385 1.27e-13

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 72.35  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 218 FLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPApeyhslqEGLPYLDMVISETLRMYPP-AFRFTREA 296
Cdd:PLN02169 307 FSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDNEDL-------EKLVYLHAALSESMRLYPPlPFNHKAPA 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 297 AQDCEVLGQRIPAGTVLEIAVGALHHDPEHW-PNPETFDPERFTAE-ARLQRRP-FTYLPFGAGPRSCLGVRLGLLVVKL 373
Cdd:PLN02169 380 KPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDnGGLRHEPsYKFMAFNSGPRTCLGKHLALLQMKI 459

                        170
                 ....*....|..
gi 568941360 374 TILQVLHKFRFE 385
Cdd:PLN02169 460 VALEIIKNYDFK 471
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 196-366 1.49e-13

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 71.37  E-value: 1.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 196 PQRCHPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLlkevdlfmgkHPAPEYhslqeglpyL 275
Cdd:cd11036  161 LTRSAAADALALSAPGDLVANAILLAVQGAEAAAGLVGNAVLALLRRPAQWARL----------RPDPEL---------A 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 276 DMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARlqrrpftylPFG 355
Cdd:cd11036  222 AAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTARSA---------HFG 292

                        170
                 ....*....|.
gi 568941360 356 AGPRSCLGVRL 366
Cdd:cd11036  293 LGRHACLGAAL 303
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 208-402 9.32e-13

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 69.32  E-value: 9.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGhevITNTLSFITYLLA---THPDCQERLLKEVDLFMGKHpapeyHSLQEG----LPYLDMVIS 280
Cdd:cd20658  233 LTPDEIKAQIKELMIAA---IDNPSNAVEWALAemlNQPEILRKATEELDRVVGKE-----RLVQESdipnLNYVKACAR 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 281 ETLRMYPPA-FRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEAR---LQRRPFTYLPFGA 356
Cdd:cd20658  305 EAFRLHPVApFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSevtLTEPDLRFISFST 384

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568941360 357 GPRSCLGVRLGLLVVKLTILQVLHKFRFEAsPETQVPLQL-ESKSAL 402
Cdd:cd20658  385 GRRGCPGVKLGTAMTVMLLARLLQGFTWTL-PPNVSSVDLsESKDDL 430
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 243-390 1.33e-12

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 68.83  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 243 PDCQERLLKEVDLFMGKHPAPEYHSLqEGLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQ----RIPAGTVLeiaVG 318
Cdd:cd11071  257 EELHARLAEEIRSALGSEGGLTLAAL-EKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIESHdasyKIKKGELL---VG 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 319 AL---HHDPEHWPNPETFDPERFTAEA-RLQRrpftYLPFGAGP---------RSCLGVRLGLLVVKLTILQVLHKF-RF 384
Cdd:cd11071  333 YQplaTRDPKVFDNPDEFVPDRFMGEEgKLLK----HLIWSNGPeteeptpdnKQCPGKDLVVLLARLFVAELFLRYdTF 408


                 ....*.
gi 568941360 385 EASPET 390
Cdd:cd11071  409 TIEPGW 414
PLN02971 PLN02971
tryptophan N-hydroxylase
 208-398 1.66e-12

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 68.91  E-value: 1.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 208 FTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLFMGKHPAPEYHSLQEgLPYLDMVISETLRMYP 287
Cdd:PLN02971 323 LTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPK-LNYVKAIIREAFRLHP 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 288 -PAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF---TAEARLQRRPFTYLPFGAGPRSCLG 363
Cdd:PLN02971 402 vAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHlneCSEVTLTENDLRFISFSTGKRGCAA 481

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 568941360 364 VRLGLLVVKLTILQVLHKFRFE-ASPETQVPLQLES 398
Cdd:PLN02971 482 PALGTAITTMMLARLLQGFKWKlAGSETRVELMESS 517
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 234-388 2.68e-12

cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 67.94  E-value: 2.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 234 FITYL---LATHPDCQERLLKEVDlfmgkhpapeyhslqeglPYLDMVISETLRMYP--PAF--RftreAAQDCEVLGQR 306
Cdd:cd11067  239 FVTFAalaLHEHPEWRERLRSGDE------------------DYAEAFVQEVRRFYPffPFVgaR----ARRDFEWQGYR 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 307 IPAGT--VLEIAvgALHHDPEHWPNPETFDPERFtaeARLQRRPFTYLPFGAGPRS----CLGVRLGLLVVKLTILQVLH 380
Cdd:cd11067  297 FPKGQrvLLDLY--GTNHDPRLWEDPDRFRPERF---LGWEGDPFDFIPQGGGDHAtghrCPGEWITIALMKEALRLLAR 371


                 ....*...
gi 568941360 381 KFRFEASP 388
Cdd:cd11067  372 RDYYDVPP 379
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 199-379 3.96e-12

unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s, predominantly from bacteria. 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: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 67.00  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 199 CHPTSTSKPFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKEVDLfmgkhpapeyhslqeglpyLDMV 278
Cdd:cd11079  170 LRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLRANPAL-------------------LPAA 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 279 ISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERftaEARLQrrpftyLPFGAGP 358
Cdd:cd11079  231 IDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR---HAADN------LVYGRGI 301

                        170       180
                 ....*....|....*....|.
gi 568941360 359 RSCLGVRLGLLVVKLTILQVL 379
Cdd:cd11079  302 HVCPGAPLARLELRILLEELL 322
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 238-390 6.00e-12

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 66.72  E-value: 6.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 238 LLATHPDCQERLLKEVDLFMGkhPAPeyhslqegLPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAV 317
Cdd:cd20624  217 LLAAHPEQAARAREEAAVPPG--PLA--------RPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFA 286

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568941360 318 GALHHDPEHWPNPETFDPERFtAEARLQRRPfTYLPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPET 390
Cdd:cd20624  287 PFFHRDDEALPFADRFVPEIW-LDGRAQPDE-GLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLESP 357
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 210-379 6.17e-12

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 66.59  E-value: 6.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 210 VDEIVGQAFLFLIAGHEVITNTLSFItyllathpdcqerllkeVDLFMG----KHPAPEYH---SLQEGLPYLDMVISET 282
Cdd:cd20612  185 ADEVRDNVLGTAVGGVPTQSQAFAQI-----------------LDFYLRrpgaAHLAEIQAlarENDEADATLRGYVLEA 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 283 LRMYPPAFRFTREAAQDCEVL-----GQRIPAGTVLEIAVGALHHDPEHWPNPETFDPErftaearlqrRPFT-YLPFGA 356
Cdd:cd20612  248 LRLNPIAPGLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLD----------RPLEsYIHFGH 317

                        170       180
                 ....*....|....*....|...
gi 568941360 357 GPRSCLGVRLGLLVVKlTILQVL 379
Cdd:cd20612  318 GPHQCLGEEIARAALT-EMLRVV 339
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 211-382 6.88e-11

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


Pssm-ID: 410716 [Multi-domain]  Cd Length: 367  Bit Score: 63.44  E-value: 6.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 211 DEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDcqerllkevdlFMGkhpapeyhSLQEGLPYLDMVISETLRMYPP-- 288
Cdd:cd20623  195 EEVVHDLVLLLGAGHEPTTNLIGNTLRLMLTDPR-----------FAA--------SLSGGRLSVREALNEVLWRDPPla 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 289 --AFRFtreAAQDCEVLGQRIPAGTVLEIAVGALHHDPehWPNPETFDPErftaearLQRRpfTYLPFGAGPRSCLGVRL 366
Cdd:cd20623  256 nlAGRF---AARDTELGGQWIRAGDLVVLGLAAANADP--RVRPDPGASM-------SGNR--AHLAFGAGPHRCPAQEL 321

                        170
                 ....*....|....*.
gi 568941360 367 GLLVVKLTILQVLHKF 382
Cdd:cd20623  322 AETIARTAVEVLLDRL 337
PLN02774 PLN02774
brassinosteroid-6-oxidase
 207-385 2.77e-10

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 61.72  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 207 PFTVDEIVGQAFLFLIAGHEVITNTLSFITYLLATHPDCQERLLKE-VDLFMGKHPAP-----EYHSLQeglpYLDMVIS 280
Cdd:PLN02774 259 KLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEhLAIRERKRPEDpidwnDYKSMR----FTRAVIF 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 281 ETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTaEARLQRRPFTYLpFGAGPRS 360
Cdd:PLN02774 335 ETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWL-DKSLESHNYFFL-FGGGTRL 412

                        170       180
                 ....*....|....*....|....*
gi 568941360 361 CLGVRLGLLVVKLTILQVLHKFRFE 385
Cdd:PLN02774 413 CPGKELGIVEISTFLHYFVTRYRWE 437
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 272-392 8.13e-10

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 60.52  E-value: 8.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 272 LPYLDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTaEARLQRRPFTy 351
Cdd:PLN03141 314 LPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQ-EKDMNNSSFT- 391

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 568941360 352 lPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQV 392
Cdd:PLN03141 392 -PFGGGQRLCPGLDLARLEASIFLHHLVTRFRWVAEEDTIV 431
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 218-393 3.37e-09

cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also called 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.18.8) or sterol 12-alpha-hydroxylase. It is involved in the classic (or neutral) pathway of cholesterol catabolism and bile acid synthesis, and is responsible for sterol 12alpha-hydroxylation, which directs the synthesis to cholic acid (CA). It converts 7-alpha-hydroxy-4-cholesten-3-one into 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one, but also displays broad substrate specificity including other 7-alpha-hydroxylated C27 steroids. CYP8B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 58.53  E-value: 3.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 218 FLFLIAGHeviTNT--LSF--ITYLLaTHPDCQERLLKEVDLF---MGKHPAPEYH------SLQEGLPYLDMVISETLR 284
Cdd:cd20633  230 FLLLWASQ---GNTgpASFwlLLYLL-KHPEAMKAVREEVEQVlkeTGQEVKPGGPlinltrDMLLKTPVLDSAVEETLR 305

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 285 MYPPAFrFTREAAQDCEVlgqRIPAGTVLEIAVG---------ALHHDPEHWPNPETFDPERFTAEARLQRRPF------ 349
Cdd:cd20633  306 LTAAPV-LIRAVVQDMTL---KMANGREYALRKGdrlalfpylAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFykngkk 381

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 568941360 350 --TY-LPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFE-ASPETQVP 393
Cdd:cd20633  382 lkYYnMPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLElVNPDEEIP 429
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 236-361 6.92e-09

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. 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: 410719  Cd Length: 381  Bit Score: 57.03  E-value: 6.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 236 TYLLATHPDCQErllkEVDLFMGKHPAPEyhslqeglPYLDMVISETLRMYPPAFRFTReaaqdcevlgQRIPAGT---- 311
Cdd:cd20626  231 TLRDPTHPEWRE----ANADFAKSATKDG--------ISAKNLVKEALRLYPPTRRIYR----------AFQRPGSskpe 288

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568941360 312 VLEIAVGALHHDPEHW-PNPETFDPERFTAEARLQRRPFtyLPFGAGPRSC 361
Cdd:cd20626  289 IIAADIEACHRSESIWgPDALEFNPSRWSKLTPTQKEAF--LPFGSGPFRC 337
PLN02500 PLN02500
cytochrome P450 90B1
 221-385 1.81e-08

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 56.41  E-value: 1.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 221 LIAGHEVITNTLSFITYLLATHPDCQERLLKE-VDLFMGKHPAPEYHSLQEGLPYLDM---VISETLRMYPPAFRFTREA 296
Cdd:PLN02500 288 LFAGHETSSVAIALAIFFLQGCPKAVQELREEhLEIARAKKQSGESELNWEDYKKMEFtqcVINETLRLGNVVRFLHRKA 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 297 AQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERF-------TAEARLQRRPFTYLPFGAGPRSCLGVRLGLL 369
Cdd:PLN02500 368 LKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWqqnnnrgGSSGSSSATTNNFMPFGGGPRLCAGSELAKL 447

                        170
                 ....*....|....*.
gi 568941360 370 VVKLTILQVLHKFRFE 385
Cdd:PLN02500 448 EMAVFIHHLVLNFNWE 463
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 237-394 8.66e-08

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. 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: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 53.99  E-value: 8.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 237 YLLaTHPDCQERLLKEVDLFMGKHPAPEYH---SLQEGL---PYLDMVISETLRMYPPAFrFTREAAQDcevlgqripag 310
Cdd:cd20634  247 FLL-KHPEAMAAVRGEIQRIKHQRGQPVSQtltINQELLdntPVFDSVLSETLRLTAAPF-ITREVLQD----------- 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 311 TVLEIAVGALHH-----------------DPEHWPNPETFDPERFTAEARLQRRPF-------TY--LPFGAGPRSCLGV 364
Cdd:cd20634  314 MKLRLADGQEYNlrrgdrlclfpflspqmDPEIHQEPEVFKYDRFLNADGTEKKDFykngkrlKYynMPWGAGDNVCIGR 393

                        170       180       190
                 ....*....|....*....|....*....|.
gi 568941360 365 RLGLLVVKLTILQVLHKFRFE-ASPETQVPL 394
Cdd:cd20634  394 HFAVNSIKQFVFLILTHFDVElKDPEAEIPE 424
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 235-363 7.23e-07

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 50.96  E-value: 7.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 235 ITYLLATHPDCQERLLKEvdlfmgkhPAPEYHSLQEGLPYLdmvisETLRMYPpafrftREAAQDCEVLGQRIPAGTVLE 314
Cdd:cd11039  225 TCWGLLSNPEQLAEVMAG--------DVHWLRAFEEGLRWI-----SPIGMSP------RRVAEDFEIRGVTLPAGDRVF 285

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568941360 315 IAVGALHHDPEHWPNPETFDPERFTAEArlqrrpftyLPFGAGPRSCLG 363
Cdd:cd11039  286 LMFGSANRDEARFENPDRFDVFRPKSPH---------VSFGAGPHFCAG 325
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
 263-363 1.14e-06

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 50.12  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 263 PEYHSLQEGLPY-LDMVISETLRMYPPAFRFTREAAQDCEVLGQRIPAGTVLEIAVGALHHDPEHWPNPETFDPERfTAE 341
Cdd:cd20619  221 PEVFTAFRNDESaRAAIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTR-PPA 299

                         90       100
                 ....*....|....*....|..
gi 568941360 342 ARLQrrpftyLPFGAGPRSCLG 363
Cdd:cd20619  300 ASRN------LSFGLGPHSCAG 315
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 218-403 7.83e-06

cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also called 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) or oxysterol 7-alpha-hydroxylase. It catalyzes the 7alpha-hydroxylation of both steroids and oxysterols, and is thus implicated in the metabolism of neurosteroids and bile acid synthesis, respectively. It participates in the alternative (or acidic) pathway of cholesterol catabolism and bile acid biosynthesis. It also mediates the formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol; 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor in lymphoid cells. CYP7B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410725  Cd Length: 438  Bit Score: 47.68  E-value: 7.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 218 FLFLIAGhevITNTL--SFIT-YLLATHPDCQERLLKEVDLFM---GKHPAPEY-HSLQ----EGLPYLDMVISETLRM- 285
Cdd:cd20632  221 FAFLWAS---VGNTIpaTFWAmYYLLRHPEALAAVRDEIDHVLqstGQELGPDFdIHLTreqlDSLVYLESAINESLRLs 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 286 -YPPAFR-----FTREAAQDCEVlgqRIPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARL--------QRRPFTY 351
Cdd:cd20632  298 sASMNIRvvqedFTLKLESDGSV---NLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKkttfykrgQKLKYYL 374

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568941360 352 LPFGAGPRSCLGVRLGLLVVKLTILQVLHKFRFEASPETQVPLQLESKSALG 403
Cdd:cd20632  375 MPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDLELLEEQKPPGLDNSRAGLG 426
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 270-363 2.30e-03

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 40.05  E-value: 2.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568941360 270 EGLPYLDMVISETLRMYPPAFRFtREAAQDCEVL---GQR--IPAGTVLEIAVGALHHDPEHWPNPETFDPERFTAEARL 344
Cdd:cd20631  294 DDMPVLGSIIKEALRLSSASLNI-RVAKEDFTLHldsGESyaIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGK 372

                         90       100
                 ....*....|....*....|....*...
gi 568941360 345 QRRPFT---------YLPFGAGPRSCLG 363
Cdd:cd20631  373 EKTTFYkngrklkyyYMPFGSGTSKCPG 400
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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