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Conserved domains on  [gi|983173864|ref|NP_001306091|]
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cytochrome P450 4B1 isoform d [Homo sapiens]

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 ...
 1-339 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 cd20678:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 436  Bit Score: 686.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPH 80
Cdd:cd20678   98 MLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPH 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 GRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTS 160
Cdd:cd20678  178 GRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTAS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 161 GISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAG 240
Cdd:cd20678  258 GISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAG 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 241 SLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSR 320
Cdd:cd20678  338 ITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLPDPTR 417

                        330
                 ....*....|....*....
gi 983173864 321 LPIKMPQLVLRSKNGFHLH 339
Cdd:cd20678  418 IPIPIPQLVLKSKNGIHLY 436
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 1-339 0e+00

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: 686.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPH 80
Cdd:cd20678   98 MLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPH 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 GRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTS 160
Cdd:cd20678  178 GRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTAS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 161 GISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAG 240
Cdd:cd20678  258 GISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAG 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 241 SLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSR 320
Cdd:cd20678  338 ITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLPDPTR 417

                        330
                 ....*....|....*....
gi 983173864 321 LPIKMPQLVLRSKNGFHLH 339
Cdd:cd20678  418 IPIPIPQLVLKSKNGIHLY 436
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 1-338 1.63e-123

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


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 363.14  E-value: 1.63e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864    1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDL-TLLMQQRLVSFQYHNDFIYWLTP 79
Cdd:pfam00067 125 LVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFGSLEDPKFLELVKAVQELsSLLSSPSPQLLDLFPILKYFPGP 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   80 HGRRFLRACQVAHDHTDQVIRERKAALQDekvrkkiQNRRHLDFLDILLGARDEDDI-KLSDADLRAEVDTFMFEGHDTT 158
Cdd:pfam00067 205 HGRKLKRARKKIKDLLDKLIEERRETLDS-------AKKSPRDFLDALLLAKEEEDGsKLTDEELRATVLELFFAGTDTT 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  159 TSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFvDGRSL 237
Cdd:pfam00067 278 SSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVI-PGYLI 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  238 PAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLD 317
Cdd:pfam00067 357 PKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELP 436

                         330       340
                  ....*....|....*....|....
gi 983173864  318 P-SRLPIKM--PQLVLRSKNGFHL 338
Cdd:pfam00067 437 PgTDPPDIDetPGLLLPPKPYKLK 460
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 78-342 1.81e-50

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: 173.16  E-value: 1.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  78 TPHGRRFLRACQVAHDHTDQVIRERKAALQDekvrkkiqnrrhlDFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDT 157
Cdd:COG2124  176 PERRRRARRARAELDAYLRELIAERRAEPGD-------------DLLSALLAARDDGE-RLSDEELRDELLLLLLAGHET 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 158 TTSGISWFLYCMALYPEHQHRCREEVreilgdqdffqwddlgkmTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSL 237
Cdd:COG2124  242 TANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVE-LGGVTI 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 238 PAGSLISMHIYALHRNSAVWPDPEVFDsLRfstenaskRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE-FSL 316
Cdd:COG2124  303 PAGDRVLLSLAAANRDPRVFPDPDRFD-PD--------RPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRL 373

                        250       260
                 ....*....|....*....|....*.
gi 983173864 317 DPSRLPIKMPQLVLRSKNGFHLHLKP 342
Cdd:COG2124  374 APPEELRWRPSLTLRGPKSLPVRLRP 399
PLN02290 PLN02290
cytokinin trans-hydroxylase
 122-345 1.60e-40

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 148.81  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 122 DFLDILLGARDEDDIKLSDADLRAEVD---TFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDqDFFQWDDL 198
Cdd:PLN02290 293 DLLGMLLNEMEKKRSNGFNLNLQLIMDeckTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGG-ETPSVDHL 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 199 GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRsLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTEN-ASKR 276
Cdd:PLN02290 372 SKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH-IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPfAPGR 450

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 277 HpfaFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQLVLRSKNGFHLHLKPLGP 345
Cdd:PLN02290 451 H---FIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNYRHAPVVVLTIKPKYGVQVCLKPLNP 516
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 1-339 0e+00

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: 686.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPH 80
Cdd:cd20678   98 MLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPH 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 GRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTS 160
Cdd:cd20678  178 GRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTAS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 161 GISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAG 240
Cdd:cd20678  258 GISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAG 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 241 SLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSR 320
Cdd:cd20678  338 ITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLPDPTR 417

                        330
                 ....*....|....*....
gi 983173864 321 LPIKMPQLVLRSKNGFHLH 339
Cdd:cd20678  418 IPIPIPQLVLKSKNGIHLY 436
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 1-338 0e+00

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: 551.01  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPH 80
Cdd:cd20659   87 LLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNCQQTGKNHPYVAAVHELSRLVMERFLNPLLHFDWIYYLTPE 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 GRRFLRACQVAHDHTDQVIRERKAALQDEKvRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTS 160
Cdd:cd20659  167 GRRFKKACDYVHKFAEEIIKKRRKELEDNK-DEALSKRKYLDFLDILLTARDEDGKGLTDEEIRDEVDTFLFAGHDTTAS 245

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 161 GISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLPAG 240
Cdd:cd20659  246 GISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITI-DGVTLPAG 324

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 241 SLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSR 320
Cdd:cd20659  325 TLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNH 404

                        330
                 ....*....|....*...
gi 983173864 321 LPIKMPQLVLRSKNGFHL 338
Cdd:cd20659  405 PVEPKPGLVLRSKNGIKL 422
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 1-338 4.34e-148

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: 424.24  E-value: 4.34e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKArEGKSFDIFCDVGHMALNTLMKCTFGRgDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPH 80
Cdd:cd20628   87 LVEKLKKKA-GGGEFDIFPYISLCTLDIICETAMGV-KLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFIFRLTSL 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 GRRFLRACQVAHDHTDQVIRERKAALQDEKVRKK----IQNRRHLDFLDILLGARdEDDIKLSDADLRAEVDTFMFEGHD 156
Cdd:cd20628  165 GKEQRKALKVLHDFTNKVIKERREELKAEKRNSEeddeFGKKKRKAFLDLLLEAH-EDGGPLTDEDIREEVDTFMFAGHD 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 157 TTTSGISWFLYCMALYPEHQHRCREEVREILGDQDF-FQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGR 235
Cdd:cd20628  244 TTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRrPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIK-LDGY 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 236 SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFS 315
Cdd:cd20628  323 TIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVL 402

                        330       340
                 ....*....|....*....|....
gi 983173864 316 LDPSRLPIK-MPQLVLRSKNGFHL 338
Cdd:cd20628  403 PVPPGEDLKlIAEIVLRSKNGIRV 426
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 1-339 3.18e-139

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: 402.15  E-value: 3.18e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGK-SFDIFCDVGHMALNTLMKCTFGRgDTGLgHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTP 79
Cdd:cd20679  101 MHAKWRRLASEGSaRLDMFEHISLMTLDSLQKCVFSF-DSNC-QEKPSEYIAAILELSALVVKRQQQLLLHLDFLYYLTA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  80 HGRRFLRACQVAHDHTDQVIRERKAALQDEKVR---KKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHD 156
Cdd:cd20679  179 DGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDdflKAKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHD 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 157 TTTSGISWFLYCMALYPEHQHRCREEVREILGDQDF--FQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDG 234
Cdd:cd20679  259 TTASGLSWILYNLARHPEYQERCRQEVQELLKDREPeeIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLPDG 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 235 RSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEF 314
Cdd:cd20679  339 RVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRV 418

                        330       340
                 ....*....|....*....|....*
gi 983173864 315 sLDPSRLPIKMPQLVLRSKNGFHLH 339
Cdd:cd20679  419 -LPDDKEPRRKPELILRAEGGLWLR 442
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 1-338 1.63e-123

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


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 363.14  E-value: 1.63e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864    1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDL-TLLMQQRLVSFQYHNDFIYWLTP 79
Cdd:pfam00067 125 LVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFGSLEDPKFLELVKAVQELsSLLSSPSPQLLDLFPILKYFPGP 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   80 HGRRFLRACQVAHDHTDQVIRERKAALQDekvrkkiQNRRHLDFLDILLGARDEDDI-KLSDADLRAEVDTFMFEGHDTT 158
Cdd:pfam00067 205 HGRKLKRARKKIKDLLDKLIEERRETLDS-------AKKSPRDFLDALLLAKEEEDGsKLTDEELRATVLELFFAGTDTT 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  159 TSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFvDGRSL 237
Cdd:pfam00067 278 SSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVI-PGYLI 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  238 PAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLD 317
Cdd:pfam00067 357 PKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELP 436

                         330       340
                  ....*....|....*....|....
gi 983173864  318 P-SRLPIKM--PQLVLRSKNGFHL 338
Cdd:pfam00067 437 PgTDPPDIDetPGLLLPPKPYKLK 460
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 1-338 2.01e-107

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: 320.75  E-value: 2.01e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKArEGKSFDIFCDVGHMALN----TLMKCTFGRGDTGlghsrDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYW 76
Cdd:cd20660   87 LVKKLKKEV-GKEEFDIFPYITLCALDiiceTAMGKSVNAQQNS-----DSEYVKAVYRMSELVQKRQKNPWLWPDFIYS 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 LTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKK-------IQNRRHLDFLDILLGARDEDDiKLSDADLRAEVDT 149
Cdd:cd20660  161 LTPDGREHKKCLKILHGFTNKVIQERKAELQKSLEEEEeddedadIGKRKRLAFLDLLLEASEEGT-KLSDEDIREEVDT 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 150 FMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQD-FFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKP 228
Cdd:cd20660  240 FMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSDrPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSED 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 229 VTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMC 308
Cdd:cd20660  320 IE-IGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSI 398

                        330       340       350
                 ....*....|....*....|....*....|.
gi 983173864 309 LLRFEF-SLDPSRLPIKMPQLVLRSKNGFHL 338
Cdd:cd20660  399 LRNFRIeSVQKREDLKPAGELILRPVDGIRV 429
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 1-338 3.34e-81

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: 252.88  E-value: 3.34e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGkSFDIFCDVGHMALNTLMKCTFG---RGDTG-LGHsrdssyylAVSDLTLLMQQRLVSFQYHNDfiYW 76
Cdd:cd20620   88 LLDRWEAGARRG-PVDVHAEMMRLTLRIVAKTLFGtdvEGEADeIGD--------ALDVALEYAARRMLSPFLLPL--WL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 LTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKvrkkiqnrrhlDFLDILLGARDEDD-IKLSDADLRAEVDTFMFEGH 155
Cdd:cd20620  157 PTPANRRFRRARRRLDEVIYRLIAERRAAPADGG-----------DLLSMLLAARDEETgEPMSDQQLRDEVMTLFLAGH 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 156 DTTTSGISWFLYCMALYPEHQHRCREEVREILGDqDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGR 235
Cdd:cd20620  226 ETTANALSWTWYLLAQHPEVAARLRAEVDRVLGG-RPPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDE-IGGY 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 236 SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFS 315
Cdd:cd20620  304 RIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLR 383

                        330       340
                 ....*....|....*....|....
gi 983173864 316 LDPSRlPIKM-PQLVLRSKNGFHL 338
Cdd:cd20620  384 LVPGQ-PVEPePLITLRPKNGVRM 406
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 12-345 2.98e-76

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: 240.97  E-value: 2.98e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  12 GKSFDIFCDVGHMALNTLMKCTFGRgDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPHGRRFLRACQVA 91
Cdd:cd11057   95 GGEFDILPDLSRCTLEMICQTTLGS-DVNDESDGNEEYLESYERLFELIAKRVLNPWLHPEFIYRLTGDYKEEQKARKIL 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  92 HDHTDQVIRERKAALQDEKV----RKKIQNRRHLDFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDTTTSGISWFLY 167
Cdd:cd11057  174 RAFSEKIIEKKLQEVELESNldseEDEENGRKPQIFIDQLLELARNGE-EFTDEEIMDEIDTMIFAGNDTSATTVAYTLL 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 168 CMALYPEHQHRCREEVREILGD-QDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMH 246
Cdd:cd11057  253 LLAMHPEVQEKVYEEIMEVFPDdGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNGVVIPKGTTIVID 332

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 247 IYALHRNSAVW-PDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDpsrlpIKM 325
Cdd:cd11057  333 IFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTS-----LRL 407

                        330       340
                 ....*....|....*....|
gi 983173864 326 PQLVLRskngFHLHLKPLGP 345
Cdd:cd11057  408 EDLRFK----FNITLKLANG 423
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 1-336 8.03e-75

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: 237.10  E-value: 8.03e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFG--------RGDTGLGHSRD--SSYYLAVSDLTLLMQQRLVSFqyh 70
Cdd:cd11055   90 LVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGidvdsqnnPDDPFLKAAKKifRNSIIRLFLLLLLFPLRLFLF--- 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  71 ndFIYWLTPHGRRFLRACQVAHdhtdQVIRERKAAlqdekvrkkiQNRRHLDFLDILLGARDEDDI----KLSDADLRAE 146
Cdd:cd11055  167 --LLFPFVFGFKSFSFLEDVVK----KIIEQRRKN----------KSSRRKDLLQLMLDAQDSDEDvskkKLTDDEIVAQ 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 147 VDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLS 226
Cdd:cd11055  231 SFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECK 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 227 KPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTA 306
Cdd:cd11055  311 EDCT-INGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALV 389

                        330       340       350
                 ....*....|....*....|....*....|..
gi 983173864 307 MCLLRFEFSLDPS-RLPIKM-PQLVLRSKNGF 336
Cdd:cd11055  390 KILQKFRFVPCKEtEIPLKLvGGATLSPKNGI 421
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 7-335 1.16e-74

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: 236.97  E-value: 1.16e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   7 EKAREGKSFDIFCDVGHMALNTLMKCTFGRgDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPHGRRFLR 86
Cdd:cd20680  103 EKHVDGEAFNCFFDITLCALDIICETAMGK-KIGAQSNKDSEYVQAVYRMSDIIQRRQKMPWLWLDLWYLMFKEGKEHNK 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  87 ACQVAHDHTDQVIRERKAALQDEKVRK-------KIQNRRHLdFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTT 159
Cdd:cd20680  182 NLKILHTFTDNVIAERAEEMKAEEDKTgdsdgesPSKKKRKA-FLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTA 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 160 SGISWFLYCMALYPEHQHRCREEVREILGDQDF-FQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLP 238
Cdd:cd20680  261 AAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRpVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCE-IRGFKVP 339

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 239 AGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd20680  340 KGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQ 419

                        330
                 ....*....|....*...
gi 983173864 319 SRLPIK-MPQLVLRSKNG 335
Cdd:cd20680  420 KREELGlVGELILRPQNG 437
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 1-335 1.80e-74

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: 236.40  E-value: 1.80e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHM----ALNTLMKCTFGRgDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYW 76
Cdd:cd11069   91 LVDKLEEEIEESGDESISIDVLEWlsraTLDIIGLAGFGY-DFDSLENPDNELAEAYRRLFEPTLLGSLLFILLLFLPRW 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 L-----TPHGRRFLRACQVAHDHTDQVIRERKAALQDEKvrkkiqNRRHLDFLDILLGARDE-DDIKLSDADLRAEVDTF 150
Cdd:cd11069  170 LvrilpWKANREIRRAKDVLRRLAREIIREKKAALLEGK------DDSGKDILSILLRANDFaDDERLSDEELIDQILTF 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 151 MFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGD--QDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKP 228
Cdd:cd11069  244 LAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDppDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKD 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 229 vTFVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRF-----STENASKRHPFAFMPFSAGPRNCIGQQFAMSEMK 302
Cdd:cd11069  324 -TVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlepdgAASPGGAGSNYALLTFLHGPRSCIGKKFALAEMK 402

                        330       340       350
                 ....*....|....*....|....*....|....
gi 983173864 303 VVTAMCLLRFEFSLDPSR-LPIKMPQLVLRSKNG 335
Cdd:cd11069  403 VLLAALVSRFEFELDPDAeVERPIGIITRPPVDG 436
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 1-319 1.05e-70

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: 226.63  E-value: 1.05e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKArEGKS----FDIFCdvgHMALNTLMKCTFGRgDTGLGHSRDSSYYLAVSDLtllmqqrLVSFQ-YHNDFIY 75
Cdd:cd20613  104 LVEKLSKKA-DGKTevnmLDEFN---RVTLDVIAKVAFGM-DLNSIEDPDSPFPKAISLV-------LEGIQeSFRNPLL 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  76 WLTPHGRRFLR----ACQVAHDHTDQVIRERKAALQD-EKVRKkiqnrrhlDFLDILLGARDEDDiKLSDADLRAEVDTF 150
Cdd:cd20613  172 KYNPSKRKYRRevreAIKFLRETGRECIEERLEALKRgEEVPN--------DILTHILKASEEEP-DFDMEELLDDFVTF 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 151 MFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVT 230
Cdd:cd20613  243 FIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIE 322

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 231 fVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLL 310
Cdd:cd20613  323 -LGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQ 401


                 ....*....
gi 983173864 311 RFEFSLDPS 319
Cdd:cd20613  402 NFKFELVPG 410
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 1-336 7.59e-70

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


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 223.16  E-value: 7.59e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGksFDIFCDVGHMALNTLMKCTFGRGDtglgHSRDSSYYLAVSDLTLLMQQRLVSFqyhndfiyWLTPH 80
Cdd:cd00302   89 LLDRLAAGGEVG--DDVADLAQPLALDVIARLLGGPDL----GEDLEELAELLEALLKLLGPRLLRP--------LPSPR 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 GRRFLRACQVAHDHTDQVIRERKAALQDEkvrkkiqnrrhldfLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTS 160
Cdd:cd00302  155 LRRLRRARARLRDYLEELIARRRAEPADD--------------LDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTAS 220

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 161 GISWFLYCMALYPEHQHRCREEVREILGDQDFfqwDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAG 240
Cdd:cd00302  221 LLAWALYLLARHPEVQERLRAEIDAVLGDGTP---EDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVE-LGGYTIPAG 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 241 SLISMHIYALHRNSAVWPDPEVFDSLRFSteNASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPS- 319
Cdd:cd00302  297 TLVLLSLYAAHRDPEVFPDPDEFDPERFL--PEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDe 374

                        330
                 ....*....|....*..
gi 983173864 320 RLPIKMPQLVLRSKNGF 336
Cdd:cd00302  375 ELEWRPSLGTLGPASLP 391
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 72-320 4.98e-67

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: 216.68  E-value: 4.98e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  72 DFIYWlTPhGRRFLRACQVAHDHTDQVIRERKAALQDEKVrkkiqnrrhlDFLDILLGARDEDDIKLSDADLRAEVDTFM 151
Cdd:cd11053  165 DLGPW-SP-WGRFLRARRRIDALIYAEIAERRAEPDAERD----------DILSLLLSARDEDGQPLSDEELRDELMTLL 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 152 FEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFfqwDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTF 231
Cdd:cd11053  233 FAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP---EDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVEL 309

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 vDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASkrhPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLR 311
Cdd:cd11053  310 -GGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPS---PYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRR 385


                 ....*....
gi 983173864 312 FEFSLDPSR 320
Cdd:cd11053  386 FRLELTDPR 394
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 60-337 3.40e-65

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: 212.40  E-value: 3.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  60 MQQRLVSFQYHNDFIYWLT---PHGRRFLRACQVAHDHTD-------QVIRERKaalqDEKVRKKiqnrrhlDFLDILLG 129
Cdd:cd11056  141 MGRRLFEPSRLRGLKFMLLfffPKLARLLRLKFFPKEVEDffrklvrDTIEYRE----KNNIVRN-------DFIDLLLE 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 130 AR-------DEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQD-FFQWDDLGKM 201
Cdd:cd11056  210 LKkkgkiedDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGgELTYEALQEM 289

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 202 TYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGR-SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFA 280
Cdd:cd11056  290 KYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYT 369

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 281 FMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL---DPSRLPIKMPQLVLRSKNGFH 337
Cdd:cd11056  370 YLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPsskTKIPLKLSPKSFVLSPKGGIW 429
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 1-335 7.75e-64

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: 209.14  E-value: 7.75e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDI---FCdvgHMALNTLMKCTFGRGDTGLghSRDSSYYLAVsdLTLLMQ--QRLVSFQYHND--F 73
Cdd:cd11046   99 LMEKLDAAAETGESVDMeeeFS---SLTLDIIGLAVFNYDFGSV--TEESPVIKAV--YLPLVEaeHRSVWEPPYWDipA 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  74 IYWLTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQ---NRRHLDFLDILLGARDEDdikLSDADLRAEVDTF 150
Cdd:cd11046  172 ALFIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEdylNEDDPSLLRFLVDMRDED---VDSKQLRDDLMTM 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 151 MFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVT 230
Cdd:cd11046  249 LIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDK 328

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 231 FVDGR-SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRH----PFAFMPFSAGPRNCIGQQFAMSEMKVVT 305
Cdd:cd11046  329 LPGGGvKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNevidDFAFLPFGGGPRKCLGDQFALLEATVAL 408

                        330       340       350
                 ....*....|....*....|....*....|.
gi 983173864 306 AMCLLRFEFSLDPSRLPIKM-PQLVLRSKNG 335
Cdd:cd11046  409 AMLLRRFDFELDVGPRHVGMtTGATIHTKNG 439
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 1-342 2.73e-60

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: 199.33  E-value: 2.73e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGkSFDIFCDVGHMALNTLMKCTFGRgdtglghsRDSSYYLA---------VSDLTLLMQQ-RLVSFQyh 70
Cdd:cd11068  102 LVLKWERLGPDE-PIDVPDDMTRLTLDTIALCGFGY--------RFNSFYRDephpfveamVRALTEAGRRaNRPPIL-- 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  71 nDFIYWLTphGRRFLRACQVAHDHTDQVIRERKAALQDEKVrkkiqnrrhlDFLDILLGARD-EDDIKLSDADLRAEVDT 149
Cdd:cd11068  171 -NKLRRRA--KRQFREDIALMRDLVDEIIAERRANPDGSPD----------DLLNLMLNGKDpETGEKLSDENIRYQMIT 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 150 FMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDqDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPV 229
Cdd:cd11068  238 FLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGD-DPPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDT 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 230 TFVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMC 308
Cdd:cd11068  317 VLGGKYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAML 396

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 983173864 309 LLRFEFSLDPS-RLPIKMpQLVLRSKnGFHLHLKP 342
Cdd:cd11068  397 LQRFDFEDDPDyELDIKE-TLTLKPD-GFRLKARP 429
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 74-335 7.87e-58

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: 192.77  E-value: 7.87e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  74 IYWLTPHgRRFLRACQVAHDHTDQVIRErkaALQDEKVRKKIQNRRHLDFLDILlgARDEDDIKLsdadLRAEVDTFMFE 153
Cdd:cd11063  158 LLWLLRD-KKFREACKVVHRFVDPYVDK---ALARKEESKDEESSDRYVFLDEL--AKETRDPKE----LRDQLLNILLA 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 154 GHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTF-- 231
Cdd:cd11063  228 GRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLpr 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 ---VDGRS---LPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTEnasKRHPFAFMPFSAGPRNCIGQQFAMSEMKVV 304
Cdd:cd11063  308 gggPDGKSpifVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDL---KRPGWEYLPFNGGPRICLGQQFALTEASYV 384

                        250       260       270
                 ....*....|....*....|....*....|..
gi 983173864 305 TAMCLLRFE-FSLDPSRLPIKMPQLVLRSKNG 335
Cdd:cd11063  385 LVRLLQTFDrIESRDVRPPEERLTLTLSNANG 416
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 82-336 1.27e-56

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: 190.11  E-value: 1.27e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVAHDHTDQVIRERKAalqdEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSG 161
Cdd:cd11064  174 KKLREAIRVIDDFVYEVISRRRE----ELNSREEENNVREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAA 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 162 ISWFLYCMALYPEHQHRCREEVREIL-----GDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRS 236
Cdd:cd11064  250 LTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTF 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 237 LPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTENASKRH--PFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:cd11064  330 VKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLRPesPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFD 409

                        250       260
                 ....*....|....*....|...
gi 983173864 314 FSLDPSRLPIKMPQLVLRSKNGF 336
Cdd:cd11064  410 FKVVPGHKVEPKMSLTLHMKGGL 432
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 1-337 3.26e-55

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: 186.01  E-value: 3.26e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEK-AREGKSFDIFCDVGHMALNTLMKCTFGrgdtglghsrdSSYYLAVSDLTLLMQQRLVSFQyhnDFIYWLTP 79
Cdd:cd11052   99 MLERWKKQmGEEGEEVDVFEEFKALTADIISRTAFG-----------SSYEEGKEVFKLLRELQKICAQ---ANRDVGIP 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  80 hGRRFLRACQ-VAHDHTDQVIRE--RKAALQDEKVRKKIQNRRH-LDFLDILLGA--RDEDDIKLSDADLRAEVDTFMFE 153
Cdd:cd11052  165 -GSRFLPTKGnKKIKKLDKEIEDslLEIIKKREDSLKMGRGDDYgDDLLGLLLEAnqSDDQNKNMTVQEIVDECKTFFFA 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 154 GHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDfFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFvD 233
Cdd:cd11052  244 GHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDK-PPSDSLSKLKTVSMVINESLRLYPPAVFLTRKAKEDIKL-G 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 234 GRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFStENASK--RHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLL 310
Cdd:cd11052  322 GLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFA-DGVAKaaKHPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQ 400

                        330       340
                 ....*....|....*....|....*....
gi 983173864 311 RFEFSLDPS--RLPIKMpqLVLRSKNGFH 337
Cdd:cd11052  401 RFSFTLSPTyrHAPTVV--LTLRPQYGLQ 427
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 1-320 1.06e-54

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: 184.38  E-value: 1.06e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWeekaREGKSFDIFCDVGHMALNTLMKCTFGrgdTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQyhndfiyWL--- 77
Cdd:cd11049  100 LAGSW----RPGRVVDVDAEMHRLTLRVVARTLFS---TDLGPEAAAELRQALPVVLAGMLRRAVPPK-------FLerl 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  78 -TPHGRRFLRACQVAHDHTDQVIRERKAALQDekvrkkiqnrrHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHD 156
Cdd:cd11049  166 pTPGNRRFDRALARLRELVDEIIAEYRASGTD-----------RDDLLSLLLAARDEEGRPLSDEELRDQVITLLTAGTE 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 157 TTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFfQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRS 236
Cdd:cd11049  235 TTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPA-TFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVE-LGGHR 312

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 237 LPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:cd11049  313 LPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRP 392


                 ....
gi 983173864 317 DPSR 320
Cdd:cd11049  393 VPGR 396
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 82-318 1.56e-53

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: 181.71  E-value: 1.56e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVAHDHTDQVIRERKAALQDEKvrkkiqnrrhLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSG 161
Cdd:cd11044  173 GRAIRARNKLLARLEQAIRERQEEENAEA----------KDALGLLLEAKDEDGEPLSMDELKDQALLLLFAGHETTASA 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 162 ISWFLYCMALYPEHQHRCREEVREILGDQDfFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLPAGS 241
Cdd:cd11044  243 LTSLCFELAQHPDVLEKLRQEQDALGLEEP-LTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFEL-GGYQIPKGW 320

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983173864 242 LISMHIYALHRNSAVWPDPEVFDSLRFS-TENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd11044  321 LVYYSIRDTHRDPELYPDPERFDPERFSpARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLP 398
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 52-331 1.00e-51

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: 176.95  E-value: 1.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  52 AVSDLTLLMQQRLVSFQYHNdfiYWLTPHGRRFLRAC----QVAHDHTDQVIRERKAALQDEKvrkkiqnrRHLDFLDIL 127
Cdd:cd11054  153 AVKDIFESSAKLMFGPPLWK---YFPTPAWKKFVKAWdtifDIASKYVDEALEELKKKDEEDE--------EEDSLLEYL 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 128 L--GARDEDDIKLSDADLraevdtfMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLT 205
Cdd:cd11054  222 LskPGLSKKEIVTMALDL-------LLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLK 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 206 MCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRF--STENASKRHPFAFMP 283
Cdd:cd11054  295 ACIKESLRLYPVAPGNGRILPKDIV-LSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrDDSENKNIHPFASLP 373

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 983173864 284 FSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMpQLVLR 331
Cdd:cd11054  374 FGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEELKVKT-RLILV 420
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 78-342 1.81e-50

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: 173.16  E-value: 1.81e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  78 TPHGRRFLRACQVAHDHTDQVIRERKAALQDekvrkkiqnrrhlDFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDT 157
Cdd:COG2124  176 PERRRRARRARAELDAYLRELIAERRAEPGD-------------DLLSALLAARDDGE-RLSDEELRDELLLLLLAGHET 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 158 TTSGISWFLYCMALYPEHQHRCREEVreilgdqdffqwddlgkmTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSL 237
Cdd:COG2124  242 TANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVE-LGGVTI 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 238 PAGSLISMHIYALHRNSAVWPDPEVFDsLRfstenaskRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE-FSL 316
Cdd:COG2124  303 PAGDRVLLSLAAANRDPRVFPDPDRFD-PD--------RPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRL 373

                        250       260
                 ....*....|....*....|....*.
gi 983173864 317 DPSRLPIKMPQLVLRSKNGFHLHLKP 342
Cdd:COG2124  374 APPEELRWRPSLTLRGPKSLPVRLRP 399
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 1-315 6.05e-49

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: 169.40  E-value: 6.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGR--GDTGLGHsRDSSYYLAVSDLTLLMQQRLVSFQYHNDFiywlt 78
Cdd:cd11059   87 LIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGEsfGTLLLGD-KDSRERELLRRLLASLAPWLRWLPRYLPL----- 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  79 PHGRRFLRACQVAHDHTDQVIRER-KAALQDEKVRKKIQNRRHLDFLDILLgardEDDIKLSDADLRAEVDTFMFEGHDT 157
Cdd:cd11059  161 ATSRLIIGIYFRAFDEIEEWALDLcARAESSLAESSDSESLTVLLLEKLKG----LKKQGLDDLEIASEALDHIVAGHDT 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 158 TTSGISWFLYCMALYPEHQHRCREEVREILGDQDFF-QWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFVDGR 235
Cdd:cd11059  237 TAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPpDLEDLDKLPYLNAVIRETLRLYPPIPgSLPRVVPEGGATIGGY 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 236 SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRF-----STENASKRhpfAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLL 310
Cdd:cd11059  317 YIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWldpsgETAREMKR---AFWPFGSGSRMCIGMNLALMEMKLALAAIYR 393


                 ....*
gi 983173864 311 RFEFS 315
Cdd:cd11059  394 NYRTS 398
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 76-318 1.07e-48

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: 168.94  E-value: 1.07e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  76 WLTPHGRRFLRACQvahdhtdQVIRERKAAlQDEKVRkkiqnrrhlDFLDILLGARD-EDDIKLSDADLRAEVDTFMFEG 154
Cdd:cd11061  166 GATKARKRFLDFVR-------AQLKERLKA-EEEKRP---------DIFSYLLEAKDpETGEGLDLEELVGEARLLIVAG 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 155 HDTTTSGISWFLYCMALYPEHQHRCREEVREIL-GDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQV-YRQLSKPVTFV 232
Cdd:cd11061  229 SDTTATALSAIFYYLARNPEAYEKLRAELDSTFpSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGlPRETPPGGLTI 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 233 DGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLR-FSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLR 311
Cdd:cd11061  309 DGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERwLSRPEELVRARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHR 388


                 ....*..
gi 983173864 312 FEFSLDP 318
Cdd:cd11061  389 YDFRLAP 395
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 72-323 2.17e-48

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: 168.16  E-value: 2.17e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  72 DFIYWLTPHG----RRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLraev 147
Cdd:cd20617  156 DFIPILLPFYflylKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDL---- 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 148 dtfMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLS 226
Cdd:cd20617  232 ---FLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPlGLPRVTT 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 227 KPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENaSKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTA 306
Cdd:cd20617  309 EDTE-IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLEND-GNKLSEQFIPFGIGKRNCVGENLARDELFLFFA 386

                        250
                 ....*....|....*..
gi 983173864 307 MCLLRFEFSLDPSrLPI 323
Cdd:cd20617  387 NLLLNFKFKSSDG-LPI 402
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 122-326 3.11e-47

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: 164.80  E-value: 3.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 122 DFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVrEILGDQDFfQWDDLGKM 201
Cdd:cd11045  191 DLFSALCRAEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREES-LALGKGTL-DYEDLGQL 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 202 TYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTE-NASKRHPFA 280
Cdd:cd11045  269 EVTDWVFKEALRLVPPVPTLPRRAVKDTE-VLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPErAEDKVHRYA 347

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 983173864 281 FMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPS------RLPIKMP 326
Cdd:cd11045  348 WAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGyyppwwQSPLPAP 399
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 112-325 1.74e-46

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: 163.35  E-value: 1.74e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 112 RKKIQNRRHLDFLDILLGARDEDDIK----LSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREIL 187
Cdd:cd20650  194 RLDSTQKHRVDFLQLMIDSQNSKETEshkaLSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVL 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 188 GDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLR 267
Cdd:cd20650  274 PNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVE-INGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPER 352

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 268 FSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL-DPSRLPIKM 325
Cdd:cd20650  353 FSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPcKETQIPLKL 411
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 1-337 2.22e-46

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: 163.00  E-value: 2.22e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIfcDVgHMALNTLMKCTFGRgdTGLGHSRDSSYYLavsdltLLMQQRLVSFQYHNdFIYWLTPh 80
Cdd:cd20639   99 MLDKWEAMAEAGGEGEV--DV-AEWFQNLTEDVISR--TAFGSSYEDGKAV------FRLQAQQMLLAAEA-FRKVYIP- 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 GRRFL---------RACQVAHDHTDQVIRERKAALQDEKVRKKIQnrrhlDFLDILLGAR-DEDDIKLSDADLRAEVDTF 150
Cdd:cd20639  166 GYRFLptkknrkswRLDKEIRKSLLKLIERRQTAADDEKDDEDSK-----DLLGLMISAKnARNGEKMTVEEIIEECKTF 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 151 MFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVT 230
Cdd:cd20639  241 FFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVK 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 231 fVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTENA-SKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMC 308
Cdd:cd20639  321 -LGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVArAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVI 399

                        330       340
                 ....*....|....*....|....*....
gi 983173864 309 LLRFEFSLDPSRLPIKMPQLVLRSKNGFH 337
Cdd:cd20639  400 LQRFEFRLSPSYAHAPTVLMLLQPQHGAP 428
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 73-322 4.30e-45

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: 159.30  E-value: 4.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  73 FIYWLTPHGRRFLRACQVAHDHTDQVIRERKAAlqdekvrkkiQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMF 152
Cdd:cd11042  153 FPPLPLPSFRRRDRARAKLKEIFSEIIQKRRKS----------PDKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLF 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 153 EGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDF-FQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTF 231
Cdd:cd11042  223 AGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDpLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEV 302

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 -VDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENA--SKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMC 308
Cdd:cd11042  303 eGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAedSKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTL 382

                        250
                 ....*....|....
gi 983173864 309 LLRFEFSLDPSRLP 322
Cdd:cd11042  383 LRNFDFELVDSPFP 396
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 1-341 8.11e-45

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: 159.03  E-value: 8.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKARE--GKSFDIFCDVGHMALNTLmkctfgrGDTGLGHSRDSSYYLAVSDLTLLMQ--QRLVSFQYHNDFIYW 76
Cdd:cd11070   88 LIRYLLEEQPSakGGGVDVRDLLQRLALNVI-------GEVGFGFDLPALDEEESSLHDTLNAikLAIFPPLFLNFPFLD 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 LTPHgrRFLRACQVAHdhtdQVIRERKAALQDEKVRKKIQNRRHLDFLDILLG---ARDEDDIKLSDADLRAEVDTFMFE 153
Cdd:cd11070  161 RLPW--VLFPSRKRAF----KDVDEFLSELLDEVEAELSADSKGKQGTESVVAsrlKRARRSGGLTEKELLGNLFIFFIA 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 154 GHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWD--DLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTF 231
Cdd:cd11070  235 GHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYeeDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVV 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 VDGRS----LPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTENASKRHPF-------AFMPFSAGPRNCIGQQFAMS 299
Cdd:cd11070  315 ITGLGqeivIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGEIGAATrftpargAFIPFSAGPRACLGRKFALV 394

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 983173864 300 EMKVVTAMCLLRFEFSLDPSRLPIKMPQLVLRSKNgFHLHLK 341
Cdd:cd11070  395 EFVAALAELFRQYEWRVDPEWEEGETPAGATRDSP-AKLRLR 435
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 1-318 1.78e-44

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: 157.96  E-value: 1.78e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEE--KAREGKSFDIFCDvGHM---ALNTLMKCTFGrgdtglghsrdSSY------YLAVSDLTLLMQQRLVSFQY 69
Cdd:cd20640  100 LLSSWEEriDRAGGMAADIVVD-EDLrafSADVISRACFG-----------SSYskgkeiFSKLRELQKAVSKQSVLFSI 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  70 HNDFiYWLTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKvrkkiqnrrhlDFLD-ILLGARDEDDIKLSDADLRaeVD 148
Cdd:cd20640  168 PGLR-HLPTKSNRKIWELEGEIRSLILEIVKEREEECDHEK-----------DLLQaILEGARSSCDKKAEAEDFI--VD 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 149 ---TFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQ--DFfqwDDLGKMTYLTMCIKESFRLYPPVPQVYR 223
Cdd:cd20640  234 nckNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGppDA---DSLSRMKTVTMVIQETLRLYPPAAFVSR 310

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 224 QLSKPVTFvDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFST-ENASKRHPFAFMPFSAGPRNCIGQQFAMSEM 301
Cdd:cd20640  311 EALRDMKL-GGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNgVAAACKPPHSYMPFGAGARTCLGQNFAMAEL 389

                        330
                 ....*....|....*..
gi 983173864 302 KVVTAMCLLRFEFSLDP 318
Cdd:cd20640  390 KVLVSLILSKFSFTLSP 406
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 98-342 3.10e-43

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: 154.26  E-value: 3.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  98 VIRERKAALQDEKVRKkiqnrrhlDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQH 177
Cdd:cd11043  174 IIEERRAELEKASPKG--------DLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQ 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 178 RCREEVREIL---GDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNS 254
Cdd:cd11043  246 ELLEEHEEIAkrkEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVE-YKGYTIPKGWKVLWSARATHLDP 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 255 AVWPDPEVFDSLRFstENASKRHPFAFMPFSAGPRNCIGQQFAmsemKVVTAMCL----LRFEFSLDP----SRLPIKMP 326
Cdd:cd11043  325 EYFPDPLKFNPWRW--EGKGKGVPYTFLPFGGGPRLCPGAELA----KLEILVFLhhlvTRFRWEVVPdekiSRFPLPRP 398

                        250
                 ....*....|....*.
gi 983173864 327 qlvlrsKNGFHLHLKP 342
Cdd:cd11043  399 ------PKGLPIRLSP 408
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 96-318 3.57e-43

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: 154.34  E-value: 3.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  96 DQVIRERKAALQDEKvrKKIQNRRHLDFLDILLGARDEDDIklSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEH 175
Cdd:cd20621  187 EKIIQNRIKQIKKNK--DEIKDIIIDLDLYLLQKKKLEQEI--TKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEI 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 176 QHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSA 255
Cdd:cd20621  263 QEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPK 342

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983173864 256 VWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd20621  343 YFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIP 405
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 8-325 5.29e-43

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: 153.90  E-value: 5.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   8 KAREGKSFDIFCDVGHMALNTLMKCTFGrgdtglghsrdSSYYLAVSDLTLLMQQRLVSFQY-----HNDFIYWL----T 78
Cdd:cd11027   99 ASQEGQPFDPKDELFLAVLNVICSITFG-----------KRYKLDDPEFLRLLDLNDKFFELlgagsLLDIFPFLkyfpN 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  79 PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRkkiqnrrhlDFLDILLGAR-------DEDDIKLSDADLRAEVDTFM 151
Cdd:cd11027  168 KALRELKELMKERDEILRKKLEEHKETFDPGNIR---------DLTDALIKAKkeaedegDEDSGLLTDDHLVMTISDIF 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 152 FEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPqvyrqLSKP--- 228
Cdd:cd11027  239 GAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVP-----LALPhkt 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 229 --VTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKR-HPFAFMPFSAGPRNCIGQQFAMSEMKVVT 305
Cdd:cd11027  314 tcDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVpKPESFLPFSAGRRVCLGESLAKAELFLFL 393

                        330       340
                 ....*....|....*....|
gi 983173864 306 AMCLLRFEFSLDPSRLPIKM 325
Cdd:cd11027  394 ARLLQKFRFSPPEGEPPPEL 413
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 100-338 9.04e-43

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: 153.20  E-value: 9.04e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 100 RERKAALQDEKVR-KKIQNRR----------HLDFLDILLGARDED-------DIKLSDADLRAEVDTFMFEGHDTTTSG 161
Cdd:cd20642  174 RRMKEIEKEIRSSlRGIINKRekamkageatNDDLLGILLESNHKEikeqgnkNGGMSTEDVIEECKLFYFAGQETTSVL 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 162 ISWFLYCMALYPEHQHRCREEVREILGDQ--DFfqwDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDgRSLPA 239
Cdd:cd20642  254 LVWTMVLLSQHPDWQERAREEVLQVFGNNkpDF---EGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGD-LTLPA 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 240 GSLISMHIYALHRNSAVW-PDPEVFDSLRFS--TENASKRHpFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:cd20642  330 GVQVSLPILLVHRDPELWgDDAKEFNPERFAegISKATKGQ-VSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFEL 408

                        250       260
                 ....*....|....*....|..
gi 983173864 317 DPSRLPIKMPQLVLRSKNGFHL 338
Cdd:cd20642  409 SPSYVHAPYTVLTLQPQFGAHL 430
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 122-318 3.96e-41

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: 149.14  E-value: 3.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 122 DFLDILLGA------RDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQW 195
Cdd:cd20641  209 DLLGLMLEAassnegGRRTERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDA 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 196 DDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSteNAS 274
Cdd:cd20641  289 DTLSKLKLMNMVLMETLRLYGPVINIARRASEDMK-LGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFA--NGV 365

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 983173864 275 KR---HPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd20641  366 SRaatHPNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSP 412
PLN02290 PLN02290
cytokinin trans-hydroxylase
 122-345 1.60e-40

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 148.81  E-value: 1.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 122 DFLDILLGARDEDDIKLSDADLRAEVD---TFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDqDFFQWDDL 198
Cdd:PLN02290 293 DLLGMLLNEMEKKRSNGFNLNLQLIMDeckTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGG-ETPSVDHL 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 199 GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRsLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTEN-ASKR 276
Cdd:PLN02290 372 SKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH-IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPfAPGR 450

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 277 HpfaFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQLVLRSKNGFHLHLKPLGP 345
Cdd:PLN02290 451 H---FIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNYRHAPVVVLTIKPKYGVQVCLKPLNP 516
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 97-318 1.81e-40

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: 146.96  E-value: 1.81e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  97 QVIRERKAALQ--DEKVRKKIQNRR-HLDFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYP 173
Cdd:cd11058  170 SLRKKRKEHFQytREKVDRRLAKGTdRPDFMSYILRNKDEKK-GLTREELEANASLLIIAGSETTATALSGLTYYLLKNP 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 174 EHQHRCREEVR-------EILGDQdffqwddLGKMTYLTMCIKESFRLYPPVPQVY-RQLSKPVTFVDGRSLPAGSLISM 245
Cdd:cd11058  249 EVLRKLVDEIRsafssedDITLDS-------LAQLPYLNAVIQEALRLYPPVPAGLpRVVPAGGATIDGQFVPGGTSVSV 321

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 246 HIYALHRNSAVWPDPEVF------DSLRFSTENASKRhpfAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd11058  322 SQWAAYRSPRNFHDPDEFiperwlGDPRFEFDNDKKE---AFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDP 397
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 1-320 6.60e-39

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: 142.72  E-value: 6.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGR--GDtgLGHSRDSSYYLAVSDlTLLMQQRLVSfQYHNdFIYWLT 78
Cdd:cd11060   87 LVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKpfGF--LEAGTDVDGYIASID-KLLPYFAVVG-QIPW-LDRLLL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  79 PHGRRFLRACQVAHDH----TDQVIRERKAALQDEKVRKKiqnrrhlDFLDILLGARDEDDIKLSDADLRAEVDTFMFEG 154
Cdd:cd11060  162 KNPLGPKRKDKTGFGPlmrfALEAVAERLAEDAESAKGRK-------DMLDSFLEAGLKDPEKVTDREVVAEALSNILAG 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 155 HDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQ---DFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVT 230
Cdd:cd11060  235 SDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGklsSPITFAEAQKLPYLQAVIKEALRLHPPVGlPLERVVPPGGA 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 231 FVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRF--STENASKRHPFAFMPFSAGPRNCIGQQFAMSEM-KVVTA 306
Cdd:cd11060  315 TICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleADEEQRRMMDRADLTFGAGSRTCLGKNIALLELyKVIPE 394

                        330
                 ....*....|....*
gi 983173864 307 McLLRFEFSL-DPSR 320
Cdd:cd11060  395 L-LRRFDFELvDPEK 408
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 4-324 1.13e-38

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: 142.08  E-value: 1.13e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   4 KWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDssyylAVSD-LTLLM---QQRLVSfqyhnDFIYW--- 76
Cdd:cd11083   92 RWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGD-----PLQEhLERVFpmlNRRVNA-----PFPYWryl 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 LTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKiqnrRHLDfLDILLGARDEDDIKLSDADLRAEVDTFMFEGHD 156
Cdd:cd11083  162 RLPADRALDRALVEVRALVLDIIAAARARLAANPALAE----APET-LLAMMLAEDDPDARLTDDEIYANVLTLLLAGED 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 157 TTTSGISWFLYCMALYPEHQHRCREEVREILGDQDF-FQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGR 235
Cdd:cd11083  237 TTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVpPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTV-VGDI 315

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 236 SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTEN--ASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:cd11083  316 ALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGAraAEPHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFD 395

                        330       340
                 ....*....|....*....|....*.
gi 983173864 314 ---------------FSLDPSRLPIK 324
Cdd:cd11083  396 ielpepapavgeefaFTMSPEGLRVR 421
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 140-315 1.86e-38

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: 141.24  E-value: 1.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 140 DADLRAEVD-------------TFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILG-----DQDFFQWDD--LG 199
Cdd:cd11051  170 DRYLKPEVRkrfeleraidqikTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGpdpsaAAELLREGPelLN 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 200 KMTYLTMCIKESFRLYPPVPQVyRQLSKPVTFVD--GRSLP-AGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKR 276
Cdd:cd11051  250 QLPYTTAVIKETLRLFPPAGTA-RRGPPGVGLTDrdGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHEL 328

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 983173864 277 HP--FAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFS 315
Cdd:cd11051  329 YPpkSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFE 369
PLN02936 PLN02936
epsilon-ring hydroxylase
 72-318 1.04e-36

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 138.00  E-value: 1.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  72 DFIYWLTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKvrKKIQNRRHLD-----FLDILLGARDEddikLSDADLRAE 146
Cdd:PLN02936 209 DFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEG--EVIEGEEYVNdsdpsVLRFLLASREE----VSSVQLRDD 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 147 VDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFfQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLS 226
Cdd:PLN02936 283 LLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPP-TYEDIKELKYLTRCINESMRLYPHPPVLIRRAQ 361

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 227 KPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHP---FAFMPFSAGPRNCIGQQFAMSEMKV 303
Cdd:PLN02936 362 VEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETntdFRYIPFSGGPRKCVGDQFALLEAIV 441

                        250
                 ....*....|....*
gi 983173864 304 VTAMCLLRFEFSLDP 318
Cdd:PLN02936 442 ALAVLLQRLDLELVP 456
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 150-335 3.29e-36

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: 136.12  E-value: 3.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 150 FMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPV 229
Cdd:cd20649  269 FLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDC 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 230 TfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCL 309
Cdd:cd20649  349 V-VLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHIL 427

                        170       180
                 ....*....|....*....|....*...
gi 983173864 310 LRFEF-SLDPSRLPIKMPQL-VLRSKNG 335
Cdd:cd20649  428 RRFRFqACPETEIPLQLKSKsTLGPKNG 455
PTZ00404 PTZ00404
cytochrome P450; Provisional
 114-315 4.38e-35

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 133.69  E-value: 4.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 114 KIQNRRhlDFLDILL---GARDEDDIkLSdadLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQ 190
Cdd:PTZ00404 258 DPEVPR--DLLDLLIkeyGTNTDDDI-LS---ILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGR 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 191 DFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFS 269
Cdd:PTZ00404 332 NKVLLSDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDIIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFL 411

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 983173864 270 TENAskrhPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFS 315
Cdd:PTZ00404 412 NPDS----NDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLK 453
PLN02738 PLN02738
carotene beta-ring hydroxylase
 77-325 2.86e-34

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 132.73  E-value: 2.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 LTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVR--KKIQNRRHLDFLDILLGARDEddikLSDADLRAEVDTFMFEG 154
Cdd:PLN02738 328 ISPRQRKVAEALKLINDTLDDLIAICKRMVEEEELQfhEEYMNERDPSILHFLLASGDD----VSSKQLRDDLMTMLIAG 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 155 HDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQdFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQlSKPVTFVDG 234
Cdd:PLN02738 404 HETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDR-FPTIEDMKKLKYTTRVINESLRLYPQPPVLIRR-SLENDMLGG 481

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 235 RSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTE----NASKRHpFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLL 310
Cdd:PLN02738 482 YPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPLDgpnpNETNQN-FSYLPFGGGPRKCVGDMFASFENVVATAMLVR 560

                        250
                 ....*....|....*
gi 983173864 311 RFEFSLDPSRLPIKM 325
Cdd:PLN02738 561 RFDFQLAPGAPPVKM 575
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 1-318 3.62e-34

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: 129.98  E-value: 3.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGR---GDTGLGHSRDSSYYLAVSDLTLLMQQRLVSfqyhnDFIYWL 77
Cdd:cd20618   92 LVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKryfGESEKESEEAREFKELIDEAFELAGAFNIG-----DYIPWL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  78 TP---HG-RRFLRACQVAHDH-TDQVIRERKAALQDEKvrkkiQNRRHLDFLDILLGarDEDDIKLSDADLRAEVDTFMF 152
Cdd:cd20618  167 RWldlQGyEKRMKKLHAKLDRfLQKIIEEHREKRGESK-----KGGDDDDDLLLLLD--LDGEGKLSDDNIKALLLDMLA 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 153 EGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTf 231
Cdd:cd20618  240 AGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPlLLPHESTEDCK- 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 VDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRF--STENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCL 309
Cdd:cd20618  319 VAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFleSDIDDVKGQDFELLPFGSGRRMCPGMPLGLRMVQLTLANLL 398


                 ....*....
gi 983173864 310 LRFEFSLDP 318
Cdd:cd20618  399 HGFDWSLPG 407
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 73-318 5.69e-34

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: 129.72  E-value: 5.69e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  73 FIYWLTPHGRRfLRACQVAHDHT-DQVIRERKAALQDEKVRKkiqnrrHLDFLDILL-GARDEDDikLSDADLRAEVDTF 150
Cdd:cd11041  165 LVAPFLPEPRR-LRRLLRRARPLiIPEIERRRKLKKGPKEDK------PNDLLQWLIeAAKGEGE--RTPYDLADRQLAL 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 151 MFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVY-RQLSKPV 229
Cdd:cd11041  236 SFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLrRKVLKDV 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 230 TFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFS----TENASKRHPFA-----FMPFSAGPRNCIGQQFAMSE 300
Cdd:cd11041  316 TLSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYrlreQPGQEKKHQFVstspdFLGFGHGRHACPGRFFASNE 395

                        250
                 ....*....|....*...
gi 983173864 301 MKVVTAMCLLRFEFSLDP 318
Cdd:cd11041  396 IKLILAHLLLNYDFKLPE 413
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 92-329 6.32e-34

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: 129.45  E-value: 6.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  92 HDHTDQVIRERKAALQDEKVRKKIQNRRH-LDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMA 170
Cdd:cd20652  183 HAIYQKIIDEHKRRLKPENPRDAEDFELCeLEKAKKEGEDRDLFDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMA 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 171 LYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYAL 250
Cdd:cd20652  263 LFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAV 342

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 251 HRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLdPSRLPIKMPQLV 329
Cdd:cd20652  343 HMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIAL-PDGQPVDSEGGN 420
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 96-318 8.35e-34

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: 128.91  E-value: 8.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  96 DQVIRERKAALQDEKVRKKIQNRRHLDFLDILLGARDEDDikLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEH 175
Cdd:cd11062  180 QESIAKQVDEVLRQVSAGDPPSIVTSLFHALLNSDLPPSE--KTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEI 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 176 QHRCREEVREILGD-QDFFQWDDLGKMTYLTMCIKESFRLYPPV----PQVYRQlsKPVTFvDGRSLPAGSLISMHIYAL 250
Cdd:cd11062  258 LERLREELKTAMPDpDSPPSLAELEKLPYLTAVIKEGLRLSYGVptrlPRVVPD--EGLYY-KGWVIPPGTPVSMSSYFV 334

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 251 HRNSAVWPDPEVFDSLR-FSTENASKRHPFaFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd11062  335 HHDEEIFPDPHEFRPERwLGAAEKGKLDRY-LVPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYE 402
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 96-316 1.17e-33

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: 128.73  E-value: 1.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  96 DQVIRERKaalqdEKVRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEV-DtfMFE-GHDTTTSGISWflyCMA-L- 171
Cdd:cd11072  187 EKIIDEHL-----DKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNIKAIIlD--MFLaGTDTSATTLEW---AMTeLi 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 172 -YPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQ-VYRQLSKPVTfVDGRSLPAGSLISMHIYA 249
Cdd:cd11072  257 rNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLlLPRECREDCK-INGYDIPAKTRVIVNAWA 335

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 250 LHRNSAVWPDPEVFDSLRFstENAS---KRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:cd11072  336 IGRDPKYWEDPEEFRPERF--LDSSidfKGQDFELIPFGAGRRICPGITFGLANVELALANLLYHFDWKL 403
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 76-323 3.26e-33

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: 127.31  E-value: 3.26e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  76 WLtphGRRFLRACQVAHDHTDQVIRERKAAlqdekVRKKIQNRRHLD-FLDILLGARDEDDiKLSDADLRAEVDTFMFEG 154
Cdd:cd11065  165 WL---GAPWKRKARELRELTRRLYEGPFEA-----AKERMASGTATPsFVKDLLEELDKEG-GLSEEEIKYLAGSLYEAG 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 155 HDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFvD 233
Cdd:cd11065  236 SDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPlGIPHALTEDDEY-E 314

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 234 GRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRF-----STENASKRHPFAfmpFSAGPRNCIGQQFAMSEMKVVTAMC 308
Cdd:cd11065  315 GYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYlddpkGTPDPPDPPHFA---FGFGRRICPGRHLAENSLFIAIARL 391

                        250
                 ....*....|....*..
gi 983173864 309 LLRFEFS--LDPSRLPI 323
Cdd:cd11065  392 LWAFDIKkpKDEGGKEI 408
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 85-335 6.79e-33

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 127.97  E-value: 6.79e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  85 LRACQVAHDHTDQVIRERKAALQDekVRKKIQNRRHlDFLD--ILLGarDEDDIKLSDADLRAEVDTFMFEGHDTTTSGI 162
Cdd:PLN03195 238 SKSIKVVDDFTYSVIRRRKAEMDE--ARKSGKKVKH-DILSrfIELG--EDPDSNFTDKSLRDIVLNFVIAGRDTTATTL 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 163 SWFLYCMALYPEHQHRCREEVRE----------ILGDQDFFQ----------WDDLGKMTYLTMCIKESFRLYPPVPQVY 222
Cdd:PLN03195 313 SWFVYMIMMNPHVAEKLYSELKAlekerakeedPEDSQSFNQrvtqfaglltYDSLGKLQYLHAVITETLRLYPAVPQDP 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 223 RQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTE----NASkrhPFAFMPFSAGPRNCIGQQFA 297
Cdd:PLN03195 393 KGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDgvfqNAS---PFKFTAFQAGPRICLGKDSA 469

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 983173864 298 MSEMKVVTAMCLLRFEFSLDPSRlPIKMPQL-VLRSKNG 335
Cdd:PLN03195 470 YLQMKMALALLCRFFKFQLVPGH-PVKYRMMtILSMANG 507
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 1-325 1.58e-32

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: 125.72  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDLTLLMQQRLVSfqyhnDF---IYWL 77
Cdd:cd11073   96 LVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESGSEFKELVREIMELAGKPNVA-----DFfpfLKFL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  78 TPHG--RRFLRACQVAHDHTDQVIRERKAAlqdekvRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAevdtFMFE-- 153
Cdd:cd11073  171 DLQGlrRRMAEHFGKLFDIFDGFIDERLAE------REAGGDKKKDDDLLLLLDLELDSESELTRNHIKA----LLLDlf 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 154 --GHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVT 230
Cdd:cd11073  241 vaGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPlLLPRKAEEDVE 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 231 fVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRF-STENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCL 309
Cdd:cd11073  321 -VMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFlGSEIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLASLL 399

                        330
                 ....*....|....*.
gi 983173864 310 LRFEFSLDPSRLPIKM 325
Cdd:cd11073  400 HSFDWKLPDGMKPEDL 415
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 99-318 3.29e-32

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: 124.66  E-value: 3.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  99 IRERKAALQDekvRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHR 178
Cdd:cd11075  191 IRARRKRRAS---GEADKDYTDFLLLDLLDLKEEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEK 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 179 CREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQ-VYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVW 257
Cdd:cd11075  268 LYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHFlLPHAVTEDTV-LGGYDIPAGAEVNFNVAAIGRDPKVW 346

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983173864 258 PDPEVFDSLRFSTEN-------ASKRhpFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd11075  347 EDPEEFKPERFLAGGeaadidtGSKE--IKMMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVE 412
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 72-325 9.09e-31

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 120.99  E-value: 9.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  72 DFI---YWLTPHG---------RRFlracqvaHDHTDQVIRERKAALQDEKVRKkiqnrrhlDFLDILLGARDED--DIK 137
Cdd:cd20657  159 DFIpslAWMDLQGvekkmkrlhKRF-------DALLTKILEEHKATAQERKGKP--------DFLDFVLLENDDNgeGER 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 138 LSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPP 217
Cdd:cd20657  224 LTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPS 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 218 VPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHP----FAFMPFSAGPRNCIG 293
Cdd:cd20657  304 TPLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKVDVrgndFELIPFGAGRRICAG 383

                        250       260       270
                 ....*....|....*....|....*....|..
gi 983173864 294 QQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKM 325
Cdd:cd20657  384 TRMGIRMVEYILATLVHSFDWKLPAGQTPEEL 415
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 79-324 1.12e-29

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: 117.84  E-value: 1.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  79 PHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKIQNRRHLDFLdiLLGArdeddiKLSDADLRAEVDTFMFEGHDTT 158
Cdd:cd20646  178 PFWKRYVDAWDTIFSFGKKLIDKKMEEIEERVDRGEPVEGEYLTYL--LSSG------KLSPKEVYGSLTELLLAGVDTT 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 159 TSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLP 238
Cdd:cd20646  250 SNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLFP 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 239 AGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd20646  330 KNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVRPDP 409


                 ....*.
gi 983173864 319 SRLPIK 324
Cdd:cd20646  410 SGGEVK 415
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 96-319 1.62e-28

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: 114.73  E-value: 1.62e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  96 DQVIRERKAAL------------QDEKVRKKIQNRRHLDFLDILLGARDEDdiKLSDADLRAEVDTFMFEGHDTTTSGIS 163
Cdd:cd11076  168 LQGIRRRCSALvprvntfvgkiiEEHRAKRSNRARDDEDDVDVLLSLQGEE--KLSDSDMIAVLWEMIFRGTDTVAILTE 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 164 WFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQV-YRQLSKPVTFVDGRSLPAGSL 242
Cdd:cd11076  246 WIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLLsWARLAIHDVTVGGHVVPAGTT 325

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 243 ISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRhpFAFM-------PFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFS 315
Cdd:cd11076  326 AMVNMWAITHDPHVWEDPLEFKPERFVAAEGGAD--VSVLgsdlrlaPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWL 403


                 ....
gi 983173864 316 LDPS 319
Cdd:cd11076  404 PDDA 407
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 91-330 2.61e-27

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: 111.38  E-value: 2.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  91 AHDHTDQviRERKAALQDEkvRKKIQNRRHL-DFLdillgARDeddiKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCM 169
Cdd:cd20648  195 AKGHIDR--RMAEVAAKLP--RGEAIEGKYLtYFL-----ARE----KLPMKSIYGNVTELLLAGVDTISSTLSWSLYEL 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 170 ALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYA 249
Cdd:cd20648  262 SRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDIQVGEYIIPKKTLITLCHYA 341

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 250 LHRNSAVWPDPEVFDSLRFSTENASKrHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIK-MPQL 328
Cdd:cd20648  342 TSRDENQFPDPNSFRPERWLGKGDTH-HPYASLPFGFGKRSCIGRRIAELEVYLALARILTHFEVRPEPGGSPVKpMTRT 420


                 ..
gi 983173864 329 VL 330
Cdd:cd20648  421 LL 422
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 72-325 4.22e-27

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 111.44  E-value: 4.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  72 DFI---YWLTPHG---------RRFlracqvaHDHTDQVIRERKAALQDEKvrkkiqnRRHLDFLDILLGARDE-----D 134
Cdd:PLN02687 224 DFVpalRWLDLQGvvgkmkrlhRRF-------DAMMNGIIEEHKAAGQTGS-------EEHKDLLSTLLALKREqqadgE 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 135 DIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRL 214
Cdd:PLN02687 290 GGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRL 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 215 YPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRF-----STENASKRHPFAFMPFSAGPR 289
Cdd:PLN02687 370 HPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFlpggeHAGVDVKGSDFELIPFGAGRR 449

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 983173864 290 NCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKM 325
Cdd:PLN02687 450 ICAGLSWGLRMVTLLTATLVHAFDWELADGQTPDKL 485
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 72-343 4.28e-27

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: 110.92  E-value: 4.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  72 DFIYWLT-----PHGRRFLRACQVAHDHTDQVIRERkAALQDEKVRKKIQnrrhlDFLDILLGARDEDDIKLSDAD-LRA 145
Cdd:cd20658  167 DYLPFLRgldldGHEKIVREAMRIIRKYHDPIIDER-IKQWREGKKKEEE-----DWLDVFITLKDENGNPLLTPDeIKA 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 146 EVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQL 225
Cdd:cd20658  241 QIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHV 320

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 226 SKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENAS---KRHPFAFMPFSAGPRNCIGQQFAMSEMK 302
Cdd:cd20658  321 AMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtlTEPDLRFISFSTGRRGCPGVKLGTAMTV 400

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 983173864 303 VVTAMCLLRFEFSLDPSRLPIKMpqlvLRSKNGFHLhLKPL 343
Cdd:cd20658  401 MLLARLLQGFTWTLPPNVSSVDL----SESKDDLFM-AKPL 436
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 109-322 1.75e-26

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


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 108.84  E-value: 1.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 109 EKVRKKIQNRRHLDFLDILL---GARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVRE 185
Cdd:cd20651  189 KEHKKTYDEDNPRDLIDAYLremKKKEPPSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDE 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 186 ILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFvDGRSLPAGSLISMHIYALHRNSAVWPDPEVFD 264
Cdd:cd20651  269 VVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPiGIPHRALKDTTL-GGYRIPKDTTILASLYSVHMDPEYWGDPEEFR 347

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 983173864 265 SLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLP 322
Cdd:cd20651  348 PERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLP 405
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 96-314 1.91e-26

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: 108.84  E-value: 1.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  96 DQVIRERkaalqdEKVRKKIQNRRHLDFLDILLGA-RDED-DIKLSDADLRA-EVDTFMfEGHDTTTSGISWFLYCMALY 172
Cdd:cd20655  186 ERIIKEH------EEKRKKRKEGGSKDLLDILLDAyEDENaEYKITRNHIKAfILDLFI-AGTDTSAATTEWAMAELINN 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 173 PEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHR 252
Cdd:cd20655  259 PEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCK-INGYDIPEKTTLFVNVYAIMR 337

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983173864 253 NSAVWPDPEVFDSLRF------STENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEF 314
Cdd:cd20655  338 DPNYWEDPLEFKPERFlassrsGQELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDW 405
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 139-336 7.28e-26

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 107.79  E-value: 7.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 139 SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREIlgdqdfFQWDDLGKMTYLTMCIKESFRLYPPV 218
Cdd:PLN02169 298 KDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTK------FDNEDLEKLVYLHAALSESMRLYPPL 371

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 219 PQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTENASKRH--PFAFMPFSAGPRNCIGQQ 295
Cdd:PLN02169 372 PFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRHepSYKFMAFNSGPRTCLGKH 451

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 983173864 296 FAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQLVLRSKNGF 336
Cdd:PLN02169 452 LALLQMKIVALEIIKNYDFKVIEGHKIEAIPSILLRMKHGL 492
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 139-314 7.32e-26

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: 106.95  E-value: 7.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 139 SDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQD-FFQWDDLGKMTYLTMCIKESFRLYPP 217
Cdd:cd11082  217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEpPLTLDLLEEMKYTRQVVKEVLRYRPP 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 218 VPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSavWPDPEVFDSLRFSTENASKR-HPFAFMPFSAGPRNCIGQQF 296
Cdd:cd11082  297 APMVPHIAKKDFPLTEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRkYKKNFLVFGAGPHQCVGQEY 374

                        170
                 ....*....|....*...
gi 983173864 297 AMSEMKVVTAMCLLRFEF 314
Cdd:cd11082  375 AINHLMLFLALFSTLVDW 392
PLN02183 PLN02183
ferulate 5-hydroxylase
 72-316 9.44e-26

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 107.63  E-value: 9.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  72 DFIYWL---TPHG--RRFLRACQVAHDHTDQVIrerkaalqDEKVRKKIQNRRH-------LDFLDILLGARDED----- 134
Cdd:PLN02183 219 DFIPWLgwiDPQGlnKRLVKARKSLDGFIDDII--------DDHIQKRKNQNADndseeaeTDMVDDLLAFYSEEakvne 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 135 ------DIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCI 208
Cdd:PLN02183 291 sddlqnSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTL 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 209 KESFRLYPPVPQVYRQLSKPvTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENAS--KRHPFAFMPFSA 286
Cdd:PLN02183 371 KETLRLHPPIPLLLHETAED-AEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPdfKGSHFEFIPFGS 449

                        250       260       270
                 ....*....|....*....|....*....|
gi 983173864 287 GPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:PLN02183 450 GRRSCPGMQLGLYALDLAVAHLLHCFTWEL 479
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 103-318 1.82e-25

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: 106.01  E-value: 1.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 103 KAALQDEKVRKKIQNRRhlDFLDILLGARDEDDIKLSDADLRAE-----VDTFMFEGHDTTTSGISWFLYCMALYPEHQH 177
Cdd:cd20666  186 KKIIADHRETLDPANPR--DFIDMYLLHIEEEQKNNAESSFNEDylfyiIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQE 263

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 178 RCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVW 257
Cdd:cd20666  264 KVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIW 343

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983173864 258 PDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd20666  344 EKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPP 404
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 80-328 2.92e-25

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: 105.67  E-value: 2.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  80 HGRRFLRACQVaHDHTDQVIRERKaalqdekVRKKIQNRRHL--DFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDT 157
Cdd:cd20661  182 HQQLFRNAAEV-YDFLLRLIERFS-------ENRKPQSPRHFidAYLDEMDQNKNDPESTFSMENLIFSVGELIIAGTET 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 158 TTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPvTFVDGRS 236
Cdd:cd20661  254 TTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPlGIFHATSKD-AVVRGYS 332

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 237 LPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:cd20661  333 IPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHF 412

                        250
                 ....*....|..
gi 983173864 317 DPSRLPIKMPQL 328
Cdd:cd20661  413 PHGLIPDLKPKL 424
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 108-325 5.91e-25

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: 104.62  E-value: 5.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 108 DEKVRKKIQNRR----HLDFLDILLGARDEDDIKLSDAD--LRAEVDTFMFEGHDTTTSGISWflyCMALYPEHQH---R 178
Cdd:cd20654  201 EEHRQKRSSSGKskndEDDDDVMMLSILEDSQISGYDADtvIKATCLELILGGSDTTAVTLTW---ALSLLLNNPHvlkK 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 179 CREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVW 257
Cdd:cd20654  278 AQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPlLGPREATEDCT-VGGYHVPKGTRLLVNVWKIQRDPNVW 356

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983173864 258 PDPEVFDSLRFSTENAS---KRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSlDPSRLPIKM 325
Cdd:cd20654  357 SDPLEFKPERFLTTHKDidvRGQNFELIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIK-TPSNEPVDM 426
PLN02655 PLN02655
ent-kaurene oxidase
 97-345 7.66e-25

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 104.82  E-value: 7.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  97 QVIRERKAALQDEKVRKKIQNRRHLD---FLDILLgardEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYP 173
Cdd:PLN02655 218 TTEFRRTAVMKALIKQQKKRIARGEErdcYLDFLL----SEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNP 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 174 EHQHRCREEVREILGDQDFFQwDDLGKMTYLTMCIKESFRLYPPVPQVyrqlskPVTFVD------GRSLPAGSLISMHI 247
Cdd:PLN02655 294 DKQERLYREIREVCGDERVTE-EDLPNLPYLNAVFHETLRKYSPVPLL------PPRFVHedttlgGYDIPAGTQIAINI 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 248 YALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLP-IKMP 326
Cdd:PLN02655 367 YGCNMDKKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREGDEEkEDTV 446

                        250
                 ....*....|....*....
gi 983173864 327 QLVLRSKNGFHLHLKPLGP 345
Cdd:PLN02655 447 QLTTQKLHPLHAHLKPRGS 465
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 122-325 1.85e-24

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 103.78  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 122 DFLDILLGAR-DEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGK 200
Cdd:PLN00110 268 DFLDVVMANQeNSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPK 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 201 MTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHP-- 278
Cdd:PLN00110 348 LPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDPrg 427

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 983173864 279 --FAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLdPSRLPIKM 325
Cdd:PLN00110 428 ndFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKL-PDGVELNM 475
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 130-338 4.95e-24

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: 101.99  E-value: 4.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 130 ARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIK 209
Cdd:cd11028  219 EEEKPEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFIL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 210 ESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENAS--KRHPFAFMPFSAG 287
Cdd:cd11028  299 ETMRHSSFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLldKTKVDKFLPFGAG 378

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 983173864 288 PRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQ--LVLRSKNgFHL 338
Cdd:cd11028  379 RRRCLGEELARMELFLFFATLLQQCEFSVKPGEKLDLTPIygLTMKPKP-FKV 430
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 106-342 1.64e-23

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 100.92  E-value: 1.64e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 106 LQDEKVRKKIQNRRHLDFLDILLGARDED--DIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEV 183
Cdd:PLN03234 250 LLDETLDPNRPKQETESFIDLLMQIYKDQpfSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEV 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 184 REILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPD-PEV 262
Cdd:PLN03234 330 RNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNE 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 263 FDSLRFSTENAS---KRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLP--IKMPQLV-LRSKNGF 336
Cdd:PLN03234 410 FIPERFMKEHKGvdfKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPedIKMDVMTgLAMHKKE 489


                 ....*.
gi 983173864 337 HLHLKP 342
Cdd:PLN03234 490 HLVLAP 495
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 74-339 5.68e-23

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: 98.59  E-value: 5.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  74 IYWLTphgRRFLRACQVAHDHTDQVIRERKAAL-QDEKVRKkiqnrrHLDFLDILLGARDEDDikLSDADLRAEVDTFMF 152
Cdd:cd20616  166 ISWLY---KKYEKAVKDLKDAIEILIEQKRRRIsTAEKLED------HMDFATELIFAQKRGE--LTAENVNQCVLEMLI 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 153 EGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFfQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQ-LSKPVtf 231
Cdd:cd20616  235 AAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDI-QNDDLQKLKVLENFINESMRYQPVVDFVMRKaLEDDV-- 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 VDGRSLPAGSLISMHIYALHRnSAVWPDPEvfdslRFSTENASKRHPFA-FMPFSAGPRNCIGQQFAMSEMKVVTAMCLL 310
Cdd:cd20616  312 IDGYPVKKGTNIILNIGRMHR-LEFFPKPN-----EFTLENFEKNVPSRyFQPFGFGPRSCVGKYIAMVMMKAILVTLLR 385

                        250       260
                 ....*....|....*....|....*....
gi 983173864 311 RFEFSLDPSRLPIKMPQlvlrsKNGFHLH 339
Cdd:cd20616  386 RFQVCTLQGRCVENIQK-----TNDLSLH 409
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 94-322 6.86e-23

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: 98.71  E-value: 6.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  94 HTDQVIRERKAALQDEKVRKKIQNRRHlDFLDILLGARDEDDikLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYP 173
Cdd:cd20656  185 HGARRDRLTKAIMEEHTLARQKSGGGQ-QHFVALLTLKEQYD--LSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNP 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 174 EHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRN 253
Cdd:cd20656  262 RVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARD 341

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 254 SAVWPDPEVFDSLRFSTENAS-KRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLP 322
Cdd:cd20656  342 PAVWKNPLEFRPERFLEEDVDiKGHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPEGTPP 411
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 66-340 1.42e-22

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 98.27  E-value: 1.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  66 SFQY-HNDFIYWLTPHGRRFLRACQVahdhtdqvIRERKAALQDEKV---RKKIQNRRHLD------FLDILLGARDEDD 135
Cdd:PLN02394 217 SFEYnYGDFIPILRPFLRGYLKICQD--------VKERRLALFKDYFvdeRKKLMSAKGMDkeglkcAIDHILEAQKKGE 288

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 136 IklSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLY 215
Cdd:PLN02394 289 I--NEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLH 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 216 PPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENAS---KRHPFAFMPFSAGPRNCI 292
Cdd:PLN02394 367 MAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKveaNGNDFRFLPFGVGRRSCP 446

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 983173864 293 GQQFAMSEMKVVTAMCLLRFEfsLDPsrlPIKMPQLVLRSKNG-FHLHL 340
Cdd:PLN02394 447 GIILALPILGIVLGRLVQNFE--LLP---PPGQSKIDVSEKGGqFSLHI 490
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 93-325 1.81e-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: 97.57  E-value: 1.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  93 DHT---DQVIRERKAALqDEKVRKKIQNRRHlDFL-DILLGARdeddikLSDADLRAEVDTFMFEGHDTTTSGISWFLYC 168
Cdd:cd20645  181 DHTeawDNIFKTAKHCI-DKRLQRYSQGPAN-DFLcDIYHDNE------LSKKELYAAITELQIGGVETTANSLLWILYN 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 169 MALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDgRSLPAGSLISMHIY 248
Cdd:cd20645  253 LSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGD-YLLPKGTVLMINSQ 331

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 983173864 249 ALHRNSAVWPDPEVFDSLRFsTENASKRHPFAFMPFSAGPRNCIGQQFAmsEMKVVTAMCLLRFEFSLDPSRL-PIKM 325
Cdd:cd20645  332 ALGSSEEYFEDGRQFKPERW-LQEKHSINPFAHVPFGIGKRMCIGRRLA--ELQLQLALCWIIQKYQIVATDNePVEM 406
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 164-328 1.86e-22

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: 97.44  E-value: 1.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 164 WFLYCMALYPEHQHRCREEVREILGDQDFFQW-----DDLGKMTYLTMCIKESFRLYPPVPQVyRQLSKPVTFVDGRSLP 238
Cdd:cd11040  245 WLLAHILSDPELLERIREEIEPAVTPDSGTNAildltDLLTSCPLLDSTYLETLRLHSSSTSV-RLVTEDTVLGGGYLLR 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 239 AGSLISMHIYALHRNSAVW-PDPEVFDSLRFSTEN---ASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEF 314
Cdd:cd11040  324 KGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDgdkKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDV 403

                        170
                 ....*....|....
gi 983173864 315 SLDPSRlPIKMPQL 328
Cdd:cd11040  404 EPVGGG-DWKVPGM 416
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 100-322 2.45e-22

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 97.45  E-value: 2.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 100 RERKAALQ--DEKVRKKIQNRR------HLDFLDILLGARDEDDIklsdadLRAEVDTFMFEGHDTTTSGISWFLYCMAL 171
Cdd:PLN02426 249 RKLKEAIKlvDELAAEVIRQRRklgfsaSKDLLSRFMASINDDKY------LRDIVVSFLLAGRDTVASALTSFFWLLSK 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 172 YPEHQHRCREEVREILG-DQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYAL 250
Cdd:PLN02426 323 HPEVASAIREEADRVMGpNQEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAM 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 251 HRNSAVW-PDPEVFDSLR------FSTENaskrhPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL--DPSRL 321
Cdd:PLN02426 403 GRMERIWgPDCLEFKPERwlkngvFVPEN-----PFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVvgRSNRA 477


                 .
gi 983173864 322 P 322
Cdd:PLN02426 478 P 478
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 79-319 5.18e-22

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


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 96.09  E-value: 5.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  79 PHgRRFLRACQVAHDHTDQVIRERKAALQDEKVRkkiqnrrhlDFLDILL----GARDEDDIKLSDADLRAEVDTFMFEG 154
Cdd:cd11026  169 PH-QKLFRNVEEIKSFIRELVEEHRETLDPSSPR---------DFIDCFLlkmeKEKDNPNSEFHEENLVMTVLDLFFAG 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 155 HDTTTSGISW-FLYcMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFv 232
Cdd:cd11026  239 TETTSTTLRWaLLL-LMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPlGVPHAVTRDTKF- 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 233 DGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF 312
Cdd:cd11026  317 RGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRF 396


                 ....*..
gi 983173864 313 EFSLDPS 319
Cdd:cd11026  397 SLSSPVG 403
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 83-305 6.68e-22

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: 96.04  E-value: 6.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  83 RFLRACQVAHDHTDQVIRERKAALQDEKvrkkiqnrRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGI 162
Cdd:cd20638  179 RGLRARNLIHAKIEENIRAKIQREDTEQ--------QCKDALQLLIEHSRRNGEPLNLQALKESATELLFGGHETTASAA 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 163 SWFLYCMALYPEHQHRCREEVRE--ILG----DQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKpvTFV-DGR 235
Cdd:cd20638  251 TSLIMFLGLHPEVLQKVRKELQEkgLLStkpnENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALK--TFElNGY 328

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 236 SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVT 305
Cdd:cd20638  329 QIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFT 398
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 152-322 7.85e-22

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: 95.63  E-value: 7.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 152 FEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPvT 230
Cdd:cd20662  235 FAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPlNVPREVAVD-T 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 231 FVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFsTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLL 310
Cdd:cd20662  314 KLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHF-LENGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQ 392

                        170
                 ....*....|..
gi 983173864 311 RFEFSLDPSRLP 322
Cdd:cd20662  393 KFTFKPPPNEKL 404
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 82-311 1.31e-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: 94.90  E-value: 1.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVAHDHTDQVIRErkaalqdekvrkKIQNRR---HLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTT 158
Cdd:cd20636  176 RKGIKARDILHEYMEKAIEE------------KLQRQQaaeYCDALDYMIHSARENGKELTMQELKESAVELIFAAFSTT 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 159 TSGISWFLYCMALYPEHQHRCREE-VREILGDQ-----DFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKpvTF- 231
Cdd:cd20636  244 ASASTSLVLLLLQHPSAIEKIRQElVSHGLIDQcqccpGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQ--TFe 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 VDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTE-NASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVtAMCLL 310
Cdd:cd20636  322 LDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVErEESKSGRFNYIPFGGGVRSCIGKELAQVILKTL-AVELV 400


                 .
gi 983173864 311 R 311
Cdd:cd20636  401 T 401
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 82-319 2.53e-21

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: 94.02  E-value: 2.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVAHDHTDQVIRERKAALQDEKVRkkiqnrrhlDFLD-ILLGAR----DEDDIKLSDADLR-AEVDTFMfEGH 155
Cdd:cd20674  170 RRLKQAVENRDHIVESQLRQHKESLVAGQWR---------DMTDyMLQGLGqprgEKGMGQLLEGHVHmAVVDLFI-GGT 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 156 DTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGR 235
Cdd:cd20674  240 ETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRDSSIAGY 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 236 SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRhpfAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFs 315
Cdd:cd20674  320 DIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANR---ALLPFGCGARVCLGEPLARLELFVFLARLLQAFTL- 395


                 ....
gi 983173864 316 LDPS 319
Cdd:cd20674  396 LPPS 399
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 7-322 3.57e-21

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 94.12  E-value: 3.57e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   7 EKAREGKSFDIFCDVGHMALNTLMKCTFGR---GDTGLGHSRDSSYYLAVSDLTllmqqRLVSFQYHNDFI---YWLTPH 80
Cdd:PLN03112 162 EAAQTGKPVNLREVLGAFSMNNVTRMLLGKqyfGAESAGPKEAMEFMHITHELF-----RLLGVIYLGDYLpawRWLDPY 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 G-RRFLRACQVAHDHT-DQVIRE-RKAALQDEKVRKKIqnrrhlDFLDILLGARDEDDIK-LSDADLRAEVDTFMFEGHD 156
Cdd:PLN03112 237 GcEKKMREVEKRVDEFhDKIIDEhRRARSGKLPGGKDM------DFVDVLLSLPGENGKEhMDDVEIKALMQDMIAAATD 310

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 157 TTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRS 236
Cdd:PLN03112 311 TSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYY 390

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 237 LPAGSLISMHIYALHRNSAVWPDPEVFDSLRF---STENASKRH--PFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLR 311
Cdd:PLN03112 391 IPAKTRVFINTHGLGRNTKIWDDVEEFRPERHwpaEGSRVEISHgpDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHC 470

                        330
                 ....*....|.
gi 983173864 312 FEFSLDPSRLP 322
Cdd:PLN03112 471 FDWSPPDGLRP 481
PLN02971 PLN02971
tryptophan N-hydroxylase
 77-325 3.95e-21

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 94.33  E-value: 3.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 LTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKvRKKIQnrrhlDFLDILLGARDEDDIKLSDAD-LRAEVDTFMFEGH 155
Cdd:PLN02971 267 LNGHEKIMRESSAIMDKYHDPIIDERIKMWREGK-RTQIE-----DFLDIFISIKDEAGQPLLTADeIKPTIKELVMAAP 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 156 DTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGR 235
Cdd:PLN02971 341 DNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGY 420

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 236 SLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENAS---KRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF 312
Cdd:PLN02971 421 HIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGF 500

                        250
                 ....*....|...
gi 983173864 313 EFSLDPSRLPIKM 325
Cdd:PLN02971 501 KWKLAGSETRVEL 513
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 98-313 5.59e-21

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 93.62  E-value: 5.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  98 VIRERKAAlqdekvRKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQH 177
Cdd:PLN02302 249 IVDERRNS------RKQNISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQ 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 178 RCREE----VREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVtFVDGRSLPAGSLISMHIYALHRN 253
Cdd:PLN02302 323 KAKAEqeeiAKKRPPGQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDV-EVNGYTIPKGWKVLAWFRQVHMD 401

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 254 SAVWPDPEVFDSLRFSTENASkrhPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:PLN02302 402 PEVYPNPKEFDPSRWDNYTPK---AGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYR 458
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 112-325 5.15e-20

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: 90.45  E-value: 5.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 112 RKKIQNRRHLDFLDILLGARDEDD-----------------IKLSDADLRAEVDTFMFEGHDTTTSGISWflyCMAL--- 171
Cdd:cd11066  181 ADEYRNRRDKYLKKLLAKLKEEIEdgtdkpcivgnilkdkeSKLTDAELQSICLTMVSAGLDTVPLNLNH---LIGHlsh 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 172 --YPEHQHRCREEVREILGDQDFFQWDDL--GKMTYLTMCIKESFRLYPPVPQVY-RQLSKPVTFvDGRSLPAGSLISMH 246
Cdd:cd11066  258 ppGQEIQEKAYEEILEAYGNDEDAWEDCAaeEKCPYVVALVKETLRYFTVLPLGLpRKTTKDIVY-NGAVIPAGTILFMN 336

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 247 IYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMkvVTAMCLLRFEFSLDPSRLPIKM 325
Cdd:cd11066  337 AWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANREL--YTAICRLILLFRIGPKDEEEPM 413
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 1-321 6.39e-20

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: 90.44  E-value: 6.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAR--EGKSFDIFCDVGHMALNTLMKCTFG-----------------RGDTGLGHSRDSSYYL---------- 51
Cdd:cd20622   93 LIDLWEAKARlaKGRPFSAKEDIHHAALDAIWAFAFGinfdasqtrpqlelleaEDSTILPAGLDEPVEFpeaplpdele 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  52 AVSDLTLLMQQRLVS-FQYHNDFIYWLTPHGRRFLRAcqvahdHTDQVIRERKAAL-------QDEKVRKKIQN--RRHL 121
Cdd:cd20622  173 AVLDLADSVEKSIKSpFPKLSHWFYRNQPSYRRAAKI------KDDFLQREIQAIArslerkgDEGEVRSAVDHmvRREL 246

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 122 dfldilLGARDED-DIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREIL------GDQDFFQ 194
Cdd:cd20622  247 ------AAAEKEGrKPDYYSQVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHpeavaeGRLPTAQ 320

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 195 WDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVdGRSLPAGSLISMhiyALHRNSAVWPDPEVFDSLRFSTENAS 274
Cdd:cd20622  321 EIAQARIPYLDAVIEEILRCANTAPILSREATVDTQVL-GYSIPKGTNVFL---LNNGPSYLSPPIEIDESRRSSSSAAK 396

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 275 KR-------------HP-------------------FAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRL 321
Cdd:cd20622  397 GKkagvwdskdiadfDPerwlvtdeetgetvfdpsaGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPEAL 475
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 137-301 7.35e-20

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: 89.77  E-value: 7.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 137 KLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEV----REILGdqdffqwdDLGKM----TYLTMCI 208
Cdd:cd20643  229 KLPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVlaarQEAQG--------DMVKMlksvPLLKAAI 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 209 KESFRLYPPVPQVYRQLSKPVTFVDGRsLPAGSLISMHIYALHRNSAVWPDPEVFDSLRF-STENASKRHpfafMPFSAG 287
Cdd:cd20643  301 KETLRLHPVAVSLQRYITEDLVLQNYH-IPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWlSKDITHFRN----LGFGFG 375

                        170
                 ....*....|....
gi 983173864 288 PRNCIGQQFAMSEM 301
Cdd:cd20643  376 PRQCLGRRIAETEM 389
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 97-322 8.62e-20

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


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 89.69  E-value: 8.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  97 QVIRERKAALQD--EKVRKKIQNRRHLDFLDILLGAR----------DEDDIKLSDADLRAEVDTFMFEGHDTTTSGISW 164
Cdd:cd20673  175 QCVKIRDKLLQKklEEHKEKFSSDSIRDLLDALLQAKmnaennnagpDQDSVGLSDDHILMTVGDIFGAGVETTTTVLKW 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 165 FLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLIS 244
Cdd:cd20673  255 IIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPLLIPHVALQDSSIGEFTIPKGTRVV 334

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 245 MHIYALHRNSAVWPDPEVFDSLRFSTENASKRH--PFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPS-RL 321
Cdd:cd20673  335 INLWALHHDEKEWDQPDQFMPERFLDPTGSQLIspSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGgQL 414


                 .
gi 983173864 322 P 322
Cdd:cd20673  415 P 415
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 66-340 3.37e-19

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: 87.91  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  66 SFQYH-NDFIYWLTPHGRRFLRACQVahdhtdqvIRERKAAL-----QDEkvRKKIQNRRHLD------FLDILLGARDE 133
Cdd:cd11074  157 SFEYNyGDFIPILRPFLRGYLKICKE--------VKERRLQLfkdyfVDE--RKKLGSTKSTKneglkcAIDHILDAQKK 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 134 DDIklSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFR 213
Cdd:cd11074  227 GEI--NEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLR 304

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 214 LYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENA---SKRHPFAFMPFSAGPRN 290
Cdd:cd11074  305 LRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESkveANGNDFRYLPFGVGRRS 384

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 983173864 291 CIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQlvlrsKNG-FHLHL 340
Cdd:cd11074  385 CPGIILALPILGITIGRLVQNFELLPPPGQSKIDTSE-----KGGqFSLHI 430
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 82-336 6.37e-19

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: 87.21  E-value: 6.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVAHDHTDQVIRERKAALQDekvrkkiqnRRHLDFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSG 161
Cdd:cd20637  175 RRGIRARDSLQKSLEKAIREKLQGTQG---------KDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFATTASA 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 162 ISWFLYCMALYPEHQHRCREEVRE--ILGD----QDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKpvTF-VDG 234
Cdd:cd20637  246 STSLIMQLLKHPGVLEKLREELRSngILHNgclcEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQ--TFeLDG 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 235 RSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRH-PFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:cd20637  324 FQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDgRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSR 403

                        250       260
                 ....*....|....*....|...
gi 983173864 314 FSLDPSRLPIKMPQLVLRSKNGF 336
Cdd:cd20637  404 FELATRTFPRMTTVPVVHPVDGL 426
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 111-342 1.06e-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: 86.39  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 111 VRKKIQNRR-HLD------FLDILLGARDEDDIK---LSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCR 180
Cdd:cd20671  182 LRTLIEARRpTIDgnplhsYIEALIQKQEEDDPKetlFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQ 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 181 EEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLPAGSLISMHIYALHRNSAVWPDP 260
Cdd:cd20671  262 EEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQF-KGYLIPKGTPVIPLLSSVLLDKTQWETP 340

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 261 EVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIkmpQLVLRSKNGFHLHL 340
Cdd:cd20671  341 YQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPGVSPA---DLDATPAAAFTMRP 417


                 ..
gi 983173864 341 KP 342
Cdd:cd20671  418 QP 419
PLN03018 PLN03018
homomethionine N-hydroxylase
 88-327 2.49e-18

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 85.83  E-value: 2.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  88 CQVAHDHTDQVIRERKAALQDEKVRKKIQnrrhlDFLDILLGARDEDDIKLSDAD-LRAEVDTFMFEGHDTTTSGISWFL 166
Cdd:PLN03018 264 VNLVRSYNNPIIDERVELWREKGGKAAVE-----DWLDTFITLKDQNGKYLVTPDeIKAQCVEFCIAAIDNPANNMEWTL 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 167 YCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMH 246
Cdd:PLN03018 339 GEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVC 418

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 247 IYALHRNSAVWPDPEVFDSLR------FSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSR 320
Cdd:PLN03018 419 RPGLGRNPKIWKDPLVYEPERhlqgdgITKEVTLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDF 498


                 ....*..
gi 983173864 321 LPIKMPQ 327
Cdd:PLN03018 499 GPLSLEE 505
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 180-321 2.55e-18

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: 85.44  E-value: 2.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 180 REEVREILGDQDFFQW----DDLGKMTYLTMCIKESFRLYPPvPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSA 255
Cdd:cd20635  248 MEEISSVLGKAGKDKIkiseDDLKKMPYIKRCVLEAIRLRSP-GAITRKVVKPIK-IKNYTIPAGDMLMLSPYWAHRNPK 325

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983173864 256 VWPDPEVFDSLRFSTENASKR-HPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL-----DPSRL 321
Cdd:cd20635  326 YFPDPELFKPERWKKADLEKNvFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLldpvpKPSPL 397
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 151-298 2.64e-18

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


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 85.35  E-value: 2.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 151 MFEGHDTTTSGISWflyCMAL---YPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQ-VYRQLS 226
Cdd:cd20653  236 LLAGTDTSAVTLEW---AMSNllnHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLlVPHESS 312

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983173864 227 KPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFsteNASKRHPFAFMPFSAGPRNCIGQQFAM 298
Cdd:cd20653  313 EDCK-IGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF---EGEEREGYKLIPFGLGRRACPGAGLAQ 380
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 109-342 6.26e-18

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: 84.09  E-value: 6.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 109 EKVRKKIQNRRHLDFLDILLGARDED----DIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVR 184
Cdd:cd20664  188 MKHLDVLEPNDQRGFIDAFLVKQQEEeessDSFFHDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEID 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 185 EILGDQDFfQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFvDGRSLPAGSLISMHIYALHRNSAVWPDPEVF 263
Cdd:cd20664  268 RVIGSRQP-QVEHRKNMPYTDAVIHEIQRFANIVPmNLPHATTRDVTF-RGYFIPKGTYVIPLLTSVLQDKTEWEKPEEF 345

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 264 DSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPsrlPIKMPQLVLRSKNGFHLHLKP 342
Cdd:cd20664  346 NPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPP---GVSEDDLDLTPGLGFTLNPLP 421
PLN02966 PLN02966
cytochrome P450 83A1
 124-316 6.48e-18

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 84.41  E-value: 6.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 124 LDILLGARDEDDI--KLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQ--DFFQWDDLG 199
Cdd:PLN02966 269 IDLLMEIYKEQPFasEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKgsTFVTEDDVK 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 200 KMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRF-STENASKRH 277
Cdd:PLN02966 349 NLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFlEKEVDFKGT 428

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 983173864 278 PFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:PLN02966 429 DYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKL 467
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 100-327 1.10e-17

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: 83.26  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 100 RERKA-ALQDEKVRKKIQN-RRHLD---FLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPE 174
Cdd:cd20614  161 RSRRArAWIDARLSQLVATaRANGArtgLVAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPA 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 175 HQHRCREEVREiLGDQDFFQwDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNS 254
Cdd:cd20614  241 VWDALCDEAAA-AGDVPRTP-AELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIE-LGGRRIPAGTHLGIPLLLFSRDP 317

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983173864 255 AVWPDPEVFDSLRFsTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQ 327
Cdd:cd20614  318 ELYPDPDRFRPERW-LGRDRAPNPVELLQFGGGPHFCLGYHVACVELVQFIVALARELGAAGIRPLLVGVLPG 389
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 142-323 1.21e-17

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: 83.43  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 142 DLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQV 221
Cdd:cd20647  237 EIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGN 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 222 YRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKR-HPFAFMPFSAGPRNCIGQQFAMSE 300
Cdd:cd20647  317 GRVTQDDLI-VGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRvDNFGSIPFGYGIRSCIGRRIAELE 395

                        170       180
                 ....*....|....*....|...
gi 983173864 301 MKVVTAMCLLRFEFSLDPSRLPI 323
Cdd:cd20647  396 IHLALIQLLQNFEIKVSPQTTEV 418
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 156-316 1.33e-17

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: 83.10  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 156 DTTTSGISWFLYCMALYPEHQHRCREEVrEILGDQDFFQWDD--LGKMTYLTMCIKESFRLYP----PVPQvyrqlSKPV 229
Cdd:cd20615  229 DVTTGVLSWNLVFLAANPAVQEKLREEI-SAAREQSGYPMEDyiLSTDTLLAYCVLESLRLRPllafSVPE-----SSPT 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 230 T-FVDGRSLPAGSLISMHIYAL-HRNSAVWPDPEVFDSLRFSTENASK-RhpFAFMPFSAGPRNCIGQQFAMSEMKVVTA 306
Cdd:cd20615  303 DkIIGGYRIPANTPVVVDTYALnINNPFWGPDGEAYRPERFLGISPTDlR--YNFWRFGFGPRKCLGQHVADVILKALLA 380

                        170
                 ....*....|
gi 983173864 307 MCLLRFEFSL 316
Cdd:cd20615  381 HLLEQYELKL 390
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 127-340 1.63e-17

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 83.06  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 127 LLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGD---QDFFQWDDLGKMTY 203
Cdd:PLN02196 249 LLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDkeeGESLTWEDTKKMPL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 204 LTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFstENASKrhPFAFMP 283
Cdd:PLN02196 329 TSRVIQETLRVASILSFTFREAVEDVEY-EGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF--EVAPK--PNTFMP 403

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983173864 284 FSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQLVLrSKNGFHLHL 340
Cdd:PLN02196 404 FGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTSNGIQYGPFAL-PQNGLPIAL 459
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 76-322 1.66e-17

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: 82.65  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  76 WLTPHGRRFLRACQVA---HDHTDQVIRERKAALQDekvrkkiqnrrhlDFLDILLGARDEDDIKLSDADLRAEVDTFMF 152
Cdd:cd11078  153 WGRPSEEEQVEAAAAVgelWAYFADLVAERRREPRD-------------DLISDLLAAADGDGERLTDEELVAFLFLLLV 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 153 EGHDTTTSGISWFLYCMALYPEHQHRCREEVREIlgdQDFfqwddlgkmtyltmcIKESFRLYPPVPQVYRQLSKPVTfV 232
Cdd:cd11078  220 AGHETTTNLLGNAVKLLLEHPDQWRRLRADPSLI---PNA---------------VEETLRYDSPVQGLRRTATRDVE-I 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 233 DGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRfstENASKrHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF 312
Cdd:cd11078  281 GGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR---PNARK-H----LTFGHGIHFCLGAALARMEARIALEELLRRL 352

                        250
                 ....*....|.
gi 983173864 313 -EFSLDPSRLP 322
Cdd:cd11078  353 pGMRVPGQEVV 363
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 1-301 3.65e-17

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: 81.81  E-value: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   1 MLDKWEEKAREGKSFDIFCDVGHMALNTLMKCTFGRGDTGLGHSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPH 80
Cdd:cd20644  101 LKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVMLKTTVPLLFMPRSLSRWISPK 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  81 -GRRFLRACQVAHDHTDQVIrerkaalqdEKVRKKIQNRRHLDFLDILlgARDEDDIKLSDADLRAEVDTFMFEGHDTTT 159
Cdd:cd20644  181 lWKEHFEAWDCIFQYADNCI---------QKIYQELAFGRPQHYTGIV--AELLLQAELSLEAIKANITELTAGGVDTTA 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 160 SGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRsLPA 239
Cdd:cd20644  250 FPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDLVLQNYH-IPA 328

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983173864 240 GSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHpFAFMPFSAGPRNCIGQQFAMSEM 301
Cdd:cd20644  329 GTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRN-FKHLAFGFGMRQCLGRRLAEAEM 389
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 9-316 8.59e-17

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


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 81.04  E-value: 8.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864   9 AREGKSFDIFCDVGHMALNTLMKCTFGRGDTglghSRDSSYYLAVSDLTLLMQQRLVSFQYHNDFIYWLTPHGRRFLRAC 88
Cdd:cd20667   98 QENGRPFDPQDPIVHATANVIGAVVFGHRFS----SEDPIFLELIRAINLGLAFASTIWGRLYDAFPWLMRYLPGPHQKI 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  89 QVAHDHTDQVIRERkaaLQDEKVRKKIQNRRHLDF-LDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLY 167
Cdd:cd20667  174 FAYHDAVRSFIKKE---VIRHELRTNEAPQDFIDCyLAQITKTKDDPVSTFSEENMIQVVIDLFLGGTETTATTLHWALL 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 168 CMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPvTFVDGRSLPAGSLISMH 246
Cdd:cd20667  251 YMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSvGAVRQCVTS-TTMHGYYVEKGTIILPN 329

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 247 IYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:cd20667  330 LASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQL 399
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 116-315 1.07e-16

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: 80.51  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 116 QNRRHLD--FLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFF 193
Cdd:cd20663  202 QPPRDLTdaFLAEMEKAKGNPESSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRP 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 194 QWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENA 273
Cdd:cd20663  282 EMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQG 361

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 983173864 274 SKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFS 315
Cdd:cd20663  362 HFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFS 403
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 112-325 1.10e-16

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: 80.43  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 112 RKKIQNRRHLDFLDILLGARDEDDIKLSDADLRAE-VD---TFMF-EGHDTTTSGISWFLYCMALYPEHQHRCREEVREI 186
Cdd:cd20675  200 RETLRGGAPRDMMDAFILALEKGKSGDSGVGLDKEyVPstvTDIFgASQDTLSTALQWILLLLVRYPDVQARLQEELDRV 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 187 LGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSL 266
Cdd:cd20675  280 VGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPT 359

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983173864 267 RFSTENAS--KRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRlPIKM 325
Cdd:cd20675  360 RFLDENGFlnKDLASSVMIFSVGKRRCIGEELSKMQLFLFTSILAHQCNFTANPNE-PLTM 419
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 82-331 5.79e-16

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: 78.24  E-value: 5.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVAHDhTDQVIRERKAALQD-----EKVRKKIQNRRHL----DFLDILLGARDEDDiKLSDADLRAEVDTFMF 152
Cdd:cd20630  136 RRFGTATIRLLP-PGLDPEELETAAPDvteglALIEEVIAERRQApvedDLLTTLLRAEEDGE-RLSEDELMALVAALIV 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 153 EGHDTTTSGISWFLYCMALYPEHQHRCREEvREILGD--QDFFQWDDLGKM---TYLTmcikESFRLYppvpqvyrqlsk 227
Cdd:cd20630  214 AGTDTTVHLITFAVYNLLKHPEALRKVKAE-PELLRNalEEVLRWDNFGKMgtaRYAT----EDVELC------------ 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 228 pvtfvdGRSLPAGSLISMHIYALHRNSAVWPDPEVFDslrfstenaSKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAM 307
Cdd:cd20630  277 ------GVTIRKGQMVLLLLPSALRDEKVFSDPDRFD---------VRRDPNANIAFGYGPHFCIGAALARLELELAVST 341

                        250       260       270
                 ....*....|....*....|....*....|.
gi 983173864 308 CLLRF-------EFSLDPSRLPIKMPQLVLR 331
Cdd:cd20630  342 LLRRFpemelaePPVFDPHPVLRAIVSLRVR 372
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 131-307 1.08e-15

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: 77.44  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 131 RDEDD--IKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCI 208
Cdd:cd20677  223 RKAEDksAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFI 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 209 KESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENA--SKRHPFAFMPFSA 286
Cdd:cd20677  303 NEVFRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGqlNKSLVEKVLIFGM 382

                        170       180
                 ....*....|....*....|..
gi 983173864 287 GPRNCIGQQFAMSEMKV-VTAM 307
Cdd:cd20677  383 GVRKCLGEDVARNEIFVfLTTI 404
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 82-318 1.37e-15

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: 76.57  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVAHDHTDQVIRERKAALQDeKVRKKIQNRRHL---DFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDTT 158
Cdd:cd20629  131 LAMLRGLSDPPDPDVPAAEAAAAELYD-YVLPLIAERRRApgdDLISRLLRAEVEGE-KLDDEEIISFLRLLLPAGSDTT 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 159 TSGISWFLYcMALypehQHRcrEEVREILGDQDffqwddlgkmtYLTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLP 238
Cdd:cd20629  209 YRALANLLT-LLL----QHP--EQLERVRRDRS-----------LIPAAIEEGLRWEPPVASVPRMALRDVEL-DGVTIP 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 239 AGSLISMHIYALHRNSAVWPDPEVFDSLRfstenasKRHPfaFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF-EFSLD 317
Cdd:cd20629  270 AGSLLDLSVGSANRDEDVYPDPDVFDIDR-------KPKP--HLVFGGGAHRCLGEHLARVELREALNALLDRLpNLRLD 340


                 .
gi 983173864 318 P 318
Cdd:cd20629  341 P 341
PLN02500 PLN02500
cytochrome P450 90B1
 101-316 7.52e-15

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 75.28  E-value: 7.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 101 ERKAALQDEKVRKKIQNRRHLDFLDILLGARDeddikLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCR 180
Cdd:PLN02500 243 ERKMEERIEKLKEEDESVEEDDLLGWVLKHSN-----LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELR 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 181 EEVREI------LGDQDFfQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLPAGSLISMHIYALHRNS 254
Cdd:PLN02500 318 EEHLEIarakkqSGESEL-NWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRY-KGYDIPSGWKVLPVIAAVHLDS 395

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 255 AVWPDPEVFDSLRFSTENA-------SKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL 316
Cdd:PLN02500 396 SLYDQPQLFNPWRWQQNNNrggssgsSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWEL 464
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 79-348 1.51e-14

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: 74.03  E-value: 1.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  79 PHGRRFLRACQVAHDHTDQvIRERKAALQDEKVRkkiqnrrhlDFLDILLGARDEDDIKLS----DADLRAEVDTFMFEG 154
Cdd:cd20669  169 PHQRIFQNFEKLRDFIAES-VREHQESLDPNSPR---------DFIDCFLTKMAEEKQDPLshfnMETLVMTTHNLLFGG 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 155 HDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFvD 233
Cdd:cd20669  239 TETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPmSLPHAVTRDTNF-R 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 234 GRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:cd20669  318 GFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFS 397

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 983173864 314 FsldpsrLPIKMPQLVlrskngfhlHLKPLGPGSG 348
Cdd:cd20669  398 L------QPLGAPEDI---------DLTPLSSGLG 417
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 83-303 4.96e-14

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: 72.40  E-value: 4.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  83 RFLRACQVAHDHTDQVIRERKAALQDekvrkkiqnrrhlDFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDTTTSGI 162
Cdd:cd11038  169 RIEAAVEELYDYADALIEARRAEPGD-------------DLISTLVAAEQDGD-RLSDEELRNLIVALLFAGVDTTRNQL 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 163 SWFLYCMALYPEhqhrcreevreilgdqdffQWDDLGKMTYLTM-CIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGS 241
Cdd:cd11038  235 GLAMLTFAEHPD-------------------QWRALREDPELAPaAVEEVLRWCPTTTWATREAVEDVE-YNGVTIPAGT 294

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 983173864 242 LISMHIYALHRnsavwpDPEVFDSLRFSTENASKRHpfafMPFSAGPRNCIGQQFAMSEMKV 303
Cdd:cd11038  295 VVHLCSHAANR------DPRVFDADRFDITAKRAPH----LGFGGGVHHCLGAFLARAELAE 346
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 97-329 8.06e-14

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: 72.14  E-value: 8.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  97 QVIRERKAaLQDEKVRKKIQNRRHLD------FLD-ILLGARDEDDIKLSDADLRAEVDT---FMFEGHDTTTSGISW-F 165
Cdd:cd20668  172 QAFKELQG-LEDFIAKKVEHNQRTLDpnsprdFIDsFLIRMQEEKKNPNTEFYMKNLVMTtlnLFFAGTETVSTTLRYgF 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 166 LYCMAlYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQ-VYRQLSKPVTFvDGRSLPAGSLIS 244
Cdd:cd20668  251 LLLMK-HPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKDTKF-RDFFLPKGTEVF 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 245 MHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKV--VTAMCLLRFEFSLDPSRLP 322
Cdd:cd20668  329 PMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLffTTIMQNFRFKSPQSPEDID 408


                 ....*..
gi 983173864 323 IKmPQLV 329
Cdd:cd20668  409 VS-PKHV 414
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 82-331 8.09e-14

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: 71.43  E-value: 8.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  82 RRFLRACQVA---HDHTDQVIRERKAALQDekvrkkiqnrrhlDFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDTT 158
Cdd:cd20625  152 EELARANAAAaelAAYFRDLIARRRADPGD-------------DLISALVAAEEDGD-RLSEDELVANCILLLVAGHETT 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 159 TSGISWFLYCMALYPEHqhrcREEVReilgdqdffqwDDLGKMTYLtmcIKESFRLYPPVPQVYRQLSKPVTfVDGRSLP 238
Cdd:cd20625  218 VNLIGNGLLALLRHPEQ----LALLR-----------ADPELIPAA---VEELLRYDSPVQLTARVALEDVE-IGGQTIP 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 239 AGSLISMHIYALHRNSAVWPDPEVFDSLRfstenASKRHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF-EFSLD 317
Cdd:cd20625  279 AGDRVLLLLGAANRDPAVFPDPDRFDITR-----APNRH----LAFGAGIHFCLGAPLARLEAEIALRALLRRFpDLRLL 349

                        250
                 ....*....|....
gi 983173864 318 PSRLPIKmPQLVLR 331
Cdd:cd20625  350 AGEPEWR-PSLVLR 362
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 98-313 1.06e-13

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: 71.35  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  98 VIRERKaalqdekvrkkiQNRRHlDFLDILLgARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEhqh 177
Cdd:cd11080  163 VIEERR------------VNPGS-DLISILC-TAEYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPE--- 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 178 rCREEVREilgDQDFfqwddlgkmtyLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRsLPAGSLISMHIYALHRNSAVW 257
Cdd:cd11080  226 -QLAAVRA---DRSL-----------VPRAIAETLRYHPPVQLIPRQASQDVVVSGME-IKKGTTVFCLIGAANRDPAAF 289

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 258 PDPEVFDSLR--------FStenASKRHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCL-----LRFE 313
Cdd:cd11080  290 EDPDTFNIHRedlgirsaFS---GAADH----LAFGSGRHFCVGAALAKREIEIVANQVLdalpnIRLE 351
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 166-319 2.25e-13

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: 70.18  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 166 LYCMALYPEHQHRCREEVREILGDQDffqwddlgkMTYLTMCIKESFRLYPPVPQVYRQLSKPvTFVDGRSLPAGSLISM 245
Cdd:cd20624  215 LALLAAHPEQAARAREEAAVPPGPLA---------RPYLRACVLDAVRLWPTTPAVLRESTED-TVWGGRTVPAGTGFLI 284

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 983173864 246 HIYALHRnsavwpDPEVFD-SLRFSTE----NASKRHPfAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPS 319
Cdd:cd20624  285 FAPFFHR------DDEALPfADRFVPEiwldGRAQPDE-GLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLES 356
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 83-318 2.51e-13

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: 69.93  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  83 RFLR-ACQVAHDHTDQVIRERKAALQDeKVRKKIQNRRHL---DFLDILLGARDeDDIKLSDADLRAEVDTFMFEGHDTT 158
Cdd:cd11035  129 RFLEwEDAMLRPDDAEERAAAAQAVLD-YLTPLIAERRANpgdDLISAILNAEI-DGRPLTDDELLGLCFLLFLAGLDTV 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 159 TSGISWFLYCMALYPEHQhrcreevREILGDQDFFQwddlgkmtyltMCIKESFRLYPPVpQVYRQLSKPVTFvDGRSLP 238
Cdd:cd11035  207 ASALGFIFRHLARHPEDR-------RRLREDPELIP-----------AAVEELLRRYPLV-NVARIVTRDVEF-HGVQLK 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 239 AGSLISMHIYALHRNSAVWPDPEVFDSLRfstenASKRHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF-EFSLD 317
Cdd:cd11035  267 AGDMVLLPLALANRDPREFPDPDTVDFDR-----KPNRH----LAFGAGPHRCLGSHLARLELRIALEEWLKRIpDFRLA 337


                 .
gi 983173864 318 P 318
Cdd:cd11035  338 P 338
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 77-315 4.16e-13

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 70.01  E-value: 4.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  77 LTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRKKiqnrrhlDFLDILLGARDeddiKLSDADLRAEVDTFMFEGHD 156
Cdd:PLN02987 213 FSTTYRRAIQARTKVAEALTLVVMKRRKEEEEGAEKKK-------DMLAALLASDD----GFSDEEIVDFLVALLVAGYE 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 157 TTTSGISWFLYCMALYPEHQHRCREE---VREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVD 233
Cdd:PLN02987 282 TTSTIMTLAVKFLTETPLALAQLKEEhekIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIE-VK 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 234 GRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:PLN02987 361 GYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFS 440


                 ..
gi 983173864 314 FS 315
Cdd:PLN02987 441 WV 442
PLN02774 PLN02774
brassinosteroid-6-oxidase
 111-342 5.79e-13

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 69.42  E-value: 5.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 111 VRKKIQNRR-----HLDFLDILLgARDEDDIKLSDADLRAEVDTFMFEGHDT--TTSgiswflyCMALYPEHQH-----R 178
Cdd:PLN02774 229 LRQLIQERRasgetHTDMLGYLM-RKEGNRYKLTDEEIIDQIITILYSGYETvsTTS-------MMAVKYLHDHpkalqE 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 179 CREE---VREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSA 255
Cdd:PLN02774 301 LRKEhlaIRERKRPEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDME-LNGYVIPKGWRIYVYTREINYDPF 379

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 256 VWPDPEVFDSLRFsTENASKRHPFaFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDPSRLPIKMPQlvLRSKNG 335
Cdd:PLN02774 380 LYPDPMTFNPWRW-LDKSLESHNY-FFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWEEVGGDKLMKFPR--VEAPNG 455


                 ....*..
gi 983173864 336 FHLHLKP 342
Cdd:PLN02774 456 LHIRVSP 462
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 116-318 6.49e-13

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: 69.18  E-value: 6.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 116 QNRRhlDFLDILL--GARDEDDIKlSDADLRAEVDT---FMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQ 190
Cdd:cd20670  198 QNPR--DFIDCFLikMHQDKNNPH-TEFNLKNLVLTtlnLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPH 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 191 DFFQWDDLGKMTYLTMCIKESFRLYPPVP-----QVYRQlskpvTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDS 265
Cdd:cd20670  275 RLPSVDDRVKMPYTDAVIHEIQRLTDIVPlgvphNVIRD-----TQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYP 349

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 983173864 266 LRFSTENASKRHPFAFMPFSAGPRNCIGQqfAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd20670  350 QHFLDEQGRFKKNEAFVPFSSGKRVCLGE--AMARMELFLYFTSILQNFSLRS 400
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 99-313 6.70e-13

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: 68.78  E-value: 6.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  99 IRERKAALQDekvrkkiqnrrhlDFLDILLGARdEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHR 178
Cdd:cd11032  169 LEERRRNPRD-------------DLISRLVEAE-VDGERLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAAR 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 179 CREEVREILGdqdffqwddlgkmtyltmCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVWP 258
Cdd:cd11032  235 LRADPSLIPG------------------AIEEVLRYRPPVQRTARVTTEDVE-LGGVTIPAGQLVIAWLASANRDERQFE 295

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 983173864 259 DPEVFDSLRfstenASKRHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:cd11032  296 DPDTFDIDR-----NPNPH----LSFGHGIHFCLGAPLARLEARIALEALLDRFP 341
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 93-312 1.45e-12

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: 67.98  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  93 DHTDQVIRERKAALQD---EKVRKKiqnRRHL--DFLDILLGARDEDDiKLSDADLRAEVDTFMFEGHDTTTSGISWFLY 167
Cdd:cd11031  156 ALTPEEAEAARQELRGymaELVAAR---RAEPgdDLLSALVAARDDDD-RLSEEELVTLAVGLLVAGHETTASQIGNGVL 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 168 CMALYPEHQHRCREE-------VREILgdqdffqwddlgkmtyltmcikesfRLYPPVPQV--YRQLSKPVTfVDGRSLP 238
Cdd:cd11031  232 LLLRHPEQLARLRADpelvpaaVEELL-------------------------RYIPLGAGGgfPRYATEDVE-LGGVTIR 285

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983173864 239 AGSLISMHIYALHRNSAVWPDPEVFDSLRfsTENAskrHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF 312
Cdd:cd11031  286 AGEAVLVSLNAANRDPEVFPDPDRLDLDR--EPNP---H----LAFGHGPHHCLGAPLARLELQVALGALLRRL 350
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 208-294 3.92e-12

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: 66.66  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 208 IKESFRLYPPVPQVYRQLSKPvtfvdgrSLPAGSLISMHIYALHRNSAVW-PDPEVFDSLRFST-ENASKRhpfAFMPFS 285
Cdd:cd20626  262 VKEALRLYPPTRRIYRAFQRP-------GSSKPEIIAADIEACHRSESIWgPDALEFNPSRWSKlTPTQKE---AFLPFG 331


                 ....*....
gi 983173864 286 AGPRNCIGQ 294
Cdd:cd20626  332 SGPFRCPAK 340
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 154-307 1.36e-11

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: 64.91  E-value: 1.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 154 GHDTTTSGISWFLYCMALYPEhqhrcreevreilgdqdffQWDDL-GKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfV 232
Cdd:cd11037  214 GLDTTISAIGNALWLLARHPD-------------------QWERLrADPSLAPNAFEEAVRLESPVQTFSRTTTRDTE-L 273

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983173864 233 DGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRfsteNASkRHpfafMPFSAGPRNCIGQQFAMSEMK-VVTAM 307
Cdd:cd11037  274 AGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR----NPS-GH----VGFGHGVHACVGQHLARLEGEaLLTAL 340
PLN00168 PLN00168
Cytochrome P450; Provisional
 100-314 2.26e-11

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 64.59  E-value: 2.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 100 RERKAALQDEKVRKKIQNRRHLDFLDILLGAR--DEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQH 177
Cdd:PLN00168 262 REYKNHLGQGGEPPKKETTFEHSYVDTLLDIRlpEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQS 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 178 RCREEVREILGD-QDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAV 256
Cdd:PLN00168 342 KLHDEIKAKTGDdQEEVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDERE 421

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 983173864 257 WPDPEVFDSLRF------STENASKRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEF 314
Cdd:PLN00168 422 WERPMEFVPERFlaggdgEGVDVTGSREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFEW 485
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 131-318 2.94e-11

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 64.26  E-value: 2.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 131 RDED-DIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIK 209
Cdd:cd20676  225 LDENaNIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFIL 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 210 ESFRLYPPVPQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENA---SKRHPFAFMPFSA 286
Cdd:cd20676  305 ETFRHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGteiNKTESEKVMLFGL 384

                        170       180       190
                 ....*....|....*....|....*....|..
gi 983173864 287 GPRNCIGQQFAMSEMKVVTAMCLLRFEFSLDP 318
Cdd:cd20676  385 GKRRCIGESIARWEVFLFLAILLQQLEFSVPP 416
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 89-322 6.68e-11

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: 62.74  E-value: 6.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  89 QVAHDHTDQVIRERKAALQD--EKVRKKIQNRRHL---DFLDILLGArDEDDIKLSDADLRAEVDTFMFEGHDTTTSGIS 163
Cdd:cd11034  133 WVHAILHDEDPEEGAAAFAElfGHLRDLIAERRANprdDLISRLIEG-EIDGKPLSDGEVIGFLTLLLLGGTDTTSSALS 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 164 WFLYCMALYPEHQHRCREEvreilgdqdffqwDDLgkmtyLTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLPAGSLI 243
Cdd:cd11034  212 GALLWLAQHPEDRRRLIAD-------------PSL-----IPNAVEEFLRFYSPVAGLARTVTQEVEV-GGCRLKPGDRV 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 244 SMHIYALHRNSAVWPDPEVFDSLRFStenasKRHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRF-EFSLDPSRLP 322
Cdd:cd11034  273 LLAFASANRDEEKFEDPDRIDIDRTP-----NRH----LAFGSGVHRCLGSHLARVEARVALTEVLKRIpDFELDPGATC 343
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 164-324 7.37e-11

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: 63.09  E-value: 7.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 164 WFLYCMALYPEHQHRCREEVREILGDQD---FFQWD------DLGKMTYLTMCIKESFRLY-----PPVPQVYRQLSkpv 229
Cdd:cd20632  237 WAMYYLLRHPEALAAVRDEIDHVLQSTGqelGPDFDihltreQLDSLVYLESAINESLRLSsasmnIRVVQEDFTLK--- 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 230 tFVDGRS--LPAGSLISMHIYALHRNSAVWPDPEVFDSLRFsTENASKRHPF---------AFMPFSAGPRNCIGQQFAM 298
Cdd:cd20632  314 -LESDGSvnLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRF-VEDGKKKTTFykrgqklkyYLMPFGSGSSKCPGRFFAV 391

                        170       180
                 ....*....|....*....|....*.
gi 983173864 299 SEMKVVTAMCLLRFEFSLDPSRLPIK 324
Cdd:cd20632  392 NEIKQFLSLLLLYFDLELLEEQKPPG 417
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 173-325 5.44e-10

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: 60.35  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 173 PEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKP--VTFVDGR-SLPAGSLISMHIYA 249
Cdd:cd11071  257 EELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRARKDfvIESHDASyKIKKGELLVGYQPL 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 250 LHRNSAVWPDPEVFDSLRF-STENASKRHPFafmpFSAGP---------RNCIGQQFAMSEMKVVTAMCLLRF-EFSLDP 318
Cdd:cd11071  337 ATRDPKVFDNPDEFVPDRFmGEEGKLLKHLI----WSNGPeteeptpdnKQCPGKDLVVLLARLFVAELFLRYdTFTIEP 412


                 ....*..
gi 983173864 319 SRLPIKM 325
Cdd:cd11071  413 GWTGKKL 419
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 164-327 6.87e-10

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: 60.08  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 164 WFLYCMALYPEHQHRCREEVREIL----------GDQDFFQWDDLGKMTYLTMCIKESFRLyPPVPQVYRQLSKPVTFV- 232
Cdd:cd20631  249 WSLFYLLRCPEAMKAATKEVKRTLektgqkvsdgGNPIVLTREQLDDMPVLGSIIKEALRL-SSASLNIRVAKEDFTLHl 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 233 -DGRSLP--AGSLISMHIYALHRNSAVWPDPEVFDSLRFSTENASKRHPFA---------FMPFSAGPRNCIGQQFAMSE 300
Cdd:cd20631  328 dSGESYAirKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYkngrklkyyYMPFGSGTSKCPGRFFAINE 407

                        170       180
                 ....*....|....*....|....*...
gi 983173864 301 MKVVTAMCLLRFEFSL-DPSRLPIKMPQ 327
Cdd:cd20631  408 IKQFLSLMLCYFDMELlDGNAKCPPLDQ 435
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 164-316 1.71e-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: 58.92  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 164 WFLYCMALYPEHQHRCREEVREILGD--QDFFQWDDLGKMTY--------LTMCIKESFRLyPPVPQVYRQLSKPVTF-- 231
Cdd:cd20633  246 WLLLYLLKHPEAMKAVREEVEQVLKEtgQEVKPGGPLINLTRdmllktpvLDSAVEETLRL-TAAPVLIRAVVQDMTLkm 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 232 VDGR--SLPAGSLISMHIY-ALHRNSAVWPDPEVFDSLRFSTENASKRHPF---------AFMPFSAGPRNCIGQQFAMS 299
Cdd:cd20633  325 ANGReyALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFykngkklkyYNMPWGAGVSICPGRFFAVN 404

                        170
                 ....*....|....*..
gi 983173864 300 EMKVVTAMCLLRFEFSL 316
Cdd:cd20633  405 EMKQFVFLMLTYFDLEL 421
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 67-322 1.75e-09

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: 58.70  E-value: 1.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  67 FQYHNDFIYWLTPHGRRFLRACQVAHDHTDQVIRERKAALQDekvrkkiqnrrhlDFLDILLGARDEDDiKLSDADLRAE 146
Cdd:cd11029  150 FRRWSDALVDTDPPPEEAAAALRELVDYLAELVARKRAEPGD-------------DLLSALVAARDEGD-RLSEEELVST 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 147 VDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEvrEILgdqdffqWDDLgkmtyltmcIKESFRLYPPVPQV-YRQL 225
Cdd:cd11029  216 VFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRAD--PEL-------WPAA---------VEELLRYDGPVALAtLRFA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 226 SKPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRfstenASKRHpfafMPFSAGPRNCIGQQFAMSEMKVVT 305
Cdd:cd11029  278 TEDVE-VGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR-----DANGH----LAFGHGIHYCLGAPLARLEAEIAL 347

                        250       260
                 ....*....|....*....|
gi 983173864 306 AMCLLRF---EFSLDPSRLP 322
Cdd:cd11029  348 GALLTRFpdlRLAVPPDELR 367
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 93-313 1.80e-09

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: 58.31  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  93 DHTDQVIRERKAALQDekvrkkiqnrrhlDFLDILLGArDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALY 172
Cdd:cd11033  174 AYFRELAEERRANPGD-------------DLISVLANA-EVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEH 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 173 PEHQHRCREevreilgdqDFFQWDDlgkmtyltmCIKESFRLYPPVPQVYRQLSKPVTFvDGRSLPAGSLISMHIYALHR 252
Cdd:cd11033  240 PDQWERLRA---------DPSLLPT---------AVEEILRWASPVIHFRRTATRDTEL-GGQRIRAGDKVVLWYASANR 300

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983173864 253 NSAVWPDPEVFDSLRfsTENaskRHpfafMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFE 313
Cdd:cd11033  301 DEEVFDDPDRFDITR--SPN---PH----LAFGGGPHFCLGAHLARLELRVLFEELLDRVP 352
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 108-304 2.31e-09

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: 58.14  E-value: 2.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 108 DEKVRKKIQNRRHL-----DFLDILLGARDEDDIKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREE 182
Cdd:cd11079  144 DGIIRDLLADRRAAprdadDDVTARLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLRAN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 183 VREIlgdqdffqwddlgkmtylTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEV 262
Cdd:cd11079  224 PALL------------------PAAIDEILRLDDPFVANRRITTRDVE-LGGRTIPAGSRVTLNWASANRDERVFGDPDE 284

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 983173864 263 FDSLrfstenaskRHPFAFMPFSAGPRNCIGQQFAMSEMKVV 304
Cdd:cd11079  285 FDPD---------RHAADNLVYGRGIHVCPGAPLARLELRIL 317
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 210-328 4.79e-09

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: 56.96  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 210 ESFRLYPPVPQVYRQLSKPVTFVDG----RSLPAGSLISMHIYALHRNSAVWPDPEVFDslrfstenaSKRHPFAFMPFS 285
Cdd:cd20612  246 EALRLNPIAPGLYRRATTDTTVADGggrtVSIKAGDRVFVSLASAMRDPRAFPDPERFR---------LDRPLESYIHFG 316

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 983173864 286 AGPRNCIGQQFAMSemkVVTAMclLRFEFSLD-PSRLPIKMPQL 328
Cdd:cd20612  317 HGPHQCLGEEIARA---ALTEM--LRVVLRLPnLRRAPGPQGEL 355
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 162-336 6.93e-09

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: 56.77  E-value: 6.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 162 ISWFLYCMAL----YPEHQHRCREEVREilgdqdffqwddlgkmtYLTMCIKESFRLYPPVPQVYRQLSKPVTFvDGRSL 237
Cdd:cd11067  236 VARFVTFAALalheHPEWRERLRSGDED-----------------YAEAFVQEVRRFYPFFPFVGARARRDFEW-QGYRF 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 238 PAGSLISMHIYALHRNSAVWPDPEVFDSLRFSTEnasKRHPFAFMP-----FSAGPRnCIGQQFAMSEMKVVTAMCLLRF 312
Cdd:cd11067  298 PKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGW---EGDPFDFIPqgggdHATGHR-CPGEWITIALMKEALRLLARRD 373

                        170       180
                 ....*....|....*....|....
gi 983173864 313 EFSLDPSRLPIKMPQLVLRSKNGF 336
Cdd:cd11067  374 YYDVPPQDLSIDLNRMPALPRSGF 397
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 67-301 7.04e-09

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: 56.71  E-value: 7.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  67 FQYHNDFIYWLTPHGRRFLRACQVAHDHTDQVIRERKAALQDEKVRkkiqnrrhlDFLDILLGARDED----DIKLSDAD 142
Cdd:cd20672  156 FELFSGFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPR---------DFIDTYLLRMEKEksnhHTEFHHQN 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 143 LRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDDLGKMTYLTMCIKESFRLYPPVP-QV 221
Cdd:cd20672  227 LMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPiGV 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 222 YRQLSKPVTFvDGRSLPAGSlismHIY-----ALHrNSAVWPDPEVFDSLRFSTENASKRHPFAFMPFSAGPRNCIGQQF 296
Cdd:cd20672  307 PHRVTKDTLF-RGYLLPKNT----EVYpilssALH-DPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGI 380


                 ....*
gi 983173864 297 AMSEM 301
Cdd:cd20672  381 ARNEL 385
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 208-298 8.63e-08

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: 53.26  E-value: 8.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 208 IKESFRLYPPVpQVYRQLSKPVTFVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDslrfstenaSKRHPFAFMPFSAG 287
Cdd:cd11036  225 VAETLRYDPPV-RLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFD---------LGRPTARSAHFGLG 294

                         90
                 ....*....|.
gi 983173864 288 PRNCIGQQFAM 298
Cdd:cd11036  295 RHACLGAALAR 305
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 122-301 2.31e-07

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: 52.26  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 122 DFLD-ILLGARDEDDIKLSD---ADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQHRCREEVREILGDQDFFQWDD 197
Cdd:cd20665  202 DFIDcFLIKMEQEKHNQQSEftlENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQD 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 198 LGKMTYLTMCIKESFRLYPPVP-QVYRQLSKPVTFvDGRSLPAG-----SLISMhiyaLHrNSAVWPDPEVFDSLRFSTE 271
Cdd:cd20665  282 RSHMPYTDAVIHEIQRYIDLVPnNLPHAVTCDTKF-RNYLIPKGttvitSLTSV----LH-DDKEFPNPEKFDPGHFLDE 355

                        170       180       190
                 ....*....|....*....|....*....|
gi 983173864 272 NASKRHPFAFMPFSAGPRNCIGQQFAMSEM 301
Cdd:cd20665  356 NGNFKKSDYFMPFSAGKRICAGEGLARMEL 385
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 104-297 3.13e-07

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: 51.74  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 104 AALQDEKVRKKI------QNRRHLDFLDILLGArdeddiKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQH 177
Cdd:cd20627  164 ALMEMESVLKKVikerkgKNFSQHVFIDSLLQG------NLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQK 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 178 RCREEVREILGDQDFfQWDDLGKMTYLTMCIKESFRLYPPVPqVYRQLSKPVTFVDGRSLPAGSLIsmhIYALH---RNS 254
Cdd:cd20627  238 KLYKEVDQVLGKGPI-TLEKIEQLRYCQQVLCETVRTAKLTP-VSARLQELEGKVDQHIIPKETLV---LYALGvvlQDN 312

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 983173864 255 AVWPDPEVFDSLRFSTENASKRhpFAFMPFSaGPRNCIGQQFA 297
Cdd:cd20627  313 TTWPLPYRFDPDRFDDESVMKS--FSLLGFS-GSQECPELRFA 352
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 79-304 1.36e-06

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: 49.44  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  79 PHGRR--FLRACQVAHDHtDQVIRERKAALQ------DEKVRKKiqnRRHL--DFLDILLGARDEDDiKLSDADLRAEVD 148
Cdd:cd11030  140 PYEDRefFQRRSARLLDL-SSTAEEAAAAGAelraylDELVARK---RREPgdDLLSRLVAEHGAPG-ELTDEELVGIAV 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 149 TFMFEGHDTTTSGISWFLYCMALYPEHQHRCREE-------VREILgdqdffqwddlgkmTYLTmcikesfrlyppVPQ- 220
Cdd:cd11030  215 LLLVAGHETTANMIALGTLALLEHPEQLAALRADpslvpgaVEELL--------------RYLS------------IVQd 268

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 221 -VYRQLSKPVTfVDGRSLPAGSLISMHIYALHRNSAVWPDPEVFDSLRfstenaSKRHPFAfmpFSAGPRNCIGQQFAMS 299
Cdd:cd11030  269 gLPRVATEDVE-IGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR------PARRHLA---FGHGVHQCLGQNLARL 338


                 ....*
gi 983173864 300 EMKVV 304
Cdd:cd11030  339 ELEIA 343
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 252-344 1.24e-03

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: 40.51  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 252 RNSAVWPDPEVFDSLRFSTENAS---------KRHPFAFMPFSAGPRNCIGQQFAMSEMKVVTAMCLLRFEFSL-DP-SR 320
Cdd:cd20634  342 MDPEIHQEPEVFKYDRFLNADGTekkdfykngKRLKYYNMPWGAGDNVCIGRHFAVNSIKQFVFLILTHFDVELkDPeAE 421

                         90       100
                 ....*....|....*....|....
gi 983173864 321 LPikmpqLVLRSKNGFHLhLKPLG 344
Cdd:cd20634  422 IP-----EFDPSRYGFGL-LQPEG 439
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 97-303 1.32e-03

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 40.49  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864  97 QVIRERKAALQDEKVRKKIQNRrhlDFLDILLgaRDEDDiKLSDADLRAEVDTFMFEGHDTTTSGISWFLYCMALYPEHQ 176
Cdd:PLN03141 212 KIIEEKRRAMKNKEEDETGIPK---DVVDVLL--RDGSD-ELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVAL 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983173864 177 HRCREE------VREILGDQdfFQWDDLGKMTYLTMCIKESFRLYPPVPQVYRQLSKPVTfVDGRSLPAGSLISMHIYAL 250
Cdd:PLN03141 286 QQLTEEnmklkrLKADTGEP--LYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVE-IKGYLIPKGWCVLAYFRSV 362

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 983173864 251 HRNSAVWPDPEVFDSLRFSTENASKRhpfAFMPFSAGPRNCIGQQFAMSEMKV 303
Cdd:PLN03141 363 HLDEENYDNPYQFNPWRWQEKDMNNS---SFTPFGGGQRLCPGLDLARLEASI 412
 
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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