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Conserved domains on  [gi|808351875|gb|AKD43013|]
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Cyp4d1-RB [Drosophila melanogaster]

Protein Classification

cytochrome P450( domain architecture ID 15334963)

cytochrome P450 catalyzes 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
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
63-495 0e+00

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: 612.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  63 GDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIF 142
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 143 DRQSLRLVEELALRIsrGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFDLT 222
Cdd:cd20628   81 NENSKILVEKLKKKA--GGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 223 YMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGssqESSNDDADVGAKRKMAFLDILLQSTVDERPLSNLDIREEVD 302
Cdd:cd20628  159 FRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEK---RNSEEDDEFGKKKRKAFLDLLLEAHEDGGPLTDEDIREEVD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 303 TFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPvSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVL 382
Cdd:cd20628  236 TFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRRP-TLEDLNKMKYLERVIKETLRLYPSVPFIGRRLT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 383 EDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAeKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVA 462
Cdd:cd20628  315 EDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSA-KRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLA 393
                        410       420       430
                 ....*....|....*....|....*....|...
gi 808351875 463 NVLRHYEVDFVgDSSEPPVLIAELILRTKEPLM 495
Cdd:cd20628  394 KILRNFRVLPV-PPGEDLKLIAEIVLRSKNGIR 425
 
Name Accession Description Interval E-value
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
63-495 0e+00

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: 612.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  63 GDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIF 142
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 143 DRQSLRLVEELALRIsrGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFDLT 222
Cdd:cd20628   81 NENSKILVEKLKKKA--GGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 223 YMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGssqESSNDDADVGAKRKMAFLDILLQSTVDERPLSNLDIREEVD 302
Cdd:cd20628  159 FRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEK---RNSEEDDEFGKKKRKAFLDLLLEAHEDGGPLTDEDIREEVD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 303 TFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPvSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVL 382
Cdd:cd20628  236 TFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRRP-TLEDLNKMKYLERVIKETLRLYPSVPFIGRRLT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 383 EDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAeKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVA 462
Cdd:cd20628  315 EDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSA-KRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLA 393
                        410       420       430
                 ....*....|....*....|....*....|...
gi 808351875 463 NVLRHYEVDFVgDSSEPPVLIAELILRTKEPLM 495
Cdd:cd20628  394 KILRNFRVLPV-PPGEDLKLIAEIVLRSKNGIR 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
57-498 5.49e-129

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: 382.78  E-value: 5.49e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875   57 ELAERHGDTFGLFLGPSYSVMLFNPRDVERVLG-----SSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFH 131
Cdd:pfam00067  28 KLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIkkgeeFSGRPDEPWFATSRGPFLGKGIVFANGPRWRQLRRFLTPTFT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  132 FRILEPYVEIFDRQSLRLVEELALRISRGQeRINLGEAIHLCALDAICETAMGVSIN-AQSNADSEYVQAVKTISMVLHK 210
Cdd:pfam00067 108 SFGKLSFEPRVEEEARDLVEKLRKTAGEPG-VIDITDLLFRAALNVICSILFGERFGsLEDPKFLELVKAVQELSSLLSS 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  211 RMFNILYRF-DLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELiregssqessnddaDVGAKRKMAFLDILLQSTVDE 289
Cdd:pfam00067 187 PSPQLLDLFpILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL--------------DSAKKSPRDFLDALLLAKEEE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  290 RP--LSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLHYVDLCVKET 367
Cdd:pfam00067 253 DGskLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKR--SPTYDDLQNMPYLDAVIKET 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  368 LRMYPSVP-LLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvVTTAEKLNPYAYIPFSAGPRN 446
Cdd:pfam00067 331 LRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFL-DENGKFRKSFAFLPFGAGPRN 409
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808351875  447 CIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPLMFKV 498
Cdd:pfam00067 410 CLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-501 2.39e-58

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: 198.19  E-value: 2.39e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFL---GRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEP 137
Cdd:COG2124   30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVlrpLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 138 YVEIFDRQSLRLVEELAlrisrGQERINLGEAIHLCALDAICETAMGVsinaqsnaDSEYVQAVKTISMVLhkrmfnily 217
Cdd:COG2124  110 LRPRIREIADELLDRLA-----ARGPVDLVEEFARPLPVIVICELLGV--------PEEDRDRLRRWSDAL--------- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 218 rFDLTYMLTPLARAE-KKALNVLHQFTEKIIVQRReeliregssQESSNDdadvgakrkmaFLDILLQSTVDERPLSNLD 296
Cdd:COG2124  168 -LDALGPLPPERRRRaRRARAELDAYLRELIAERR---------AEPGDD-----------LLSALLAARDDGERLSDEE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 297 IREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKcfeeirsvvgndkstpvsyeLLNQLHYVDLCVKETLRMYPSVPL 376
Cdd:COG2124  227 LRDELLLLLLAGHETTANALAWALYALLRHPEQLAR--------------------LRAEPELLPAAVEETLRLYPPVPL 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 377 LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERfdvvttaeklNPYAYIPFSAGPRNCIGQKFAMLE 456
Cdd:COG2124  287 LPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLE 356
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 808351875 457 IKAIVANVLRHYEvDFVGDSSEPPVLIAELILRTKEPLMFKVRER 501
Cdd:COG2124  357 ARIALATLLRRFP-DLRLAPPEELRWRPSLTLRGPKSLPVRLRPR 400
PLN02936 PLN02936
epsilon-ring hydroxylase
110-501 2.39e-42

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 157.26  E-value: 2.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 110 GLLVSNGRKWHRRRKIITPAFHFRILEPYVE-IFDRQSLRLVEELALRISRGqERINLGEAIHLCALDAIcetamGVSI- 187
Cdd:PLN02936  98 GFAIAEGELWTARRRAVVPSLHRRYLSVMVDrVFCKCAERLVEKLEPVALSG-EAVNMEAKFSQLTLDVI-----GLSVf 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 188 --NAQS-NADSEYVQAVKTISMVLHKRMFNIL--YRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQE 262
Cdd:PLN02936 172 nyNFDSlTTDSPVIQAVYTALKEAETRSTDLLpyWKVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 263 SSN--DDADVgakrkmAFLDILLQStvdERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSV 340
Cdd:PLN02936 252 GEEyvNDSDP------SVLRFLLAS---REEVSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRV 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 341 VGNdksTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRK-VLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFK 419
Cdd:PLN02936 323 LQG---RPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRaQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFV 399
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 420 PERFDVVTTA--EKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDssEPPVLIAELILRTKEPLMFK 497
Cdd:PLN02936 400 PERFDLDGPVpnETNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPD--QDIVMTTGATIHTTNGLYMT 477

                 ....
gi 808351875 498 VRER 501
Cdd:PLN02936 478 VSRR 481
 
Name Accession Description Interval E-value
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
63-495 0e+00

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: 612.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  63 GDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIF 142
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 143 DRQSLRLVEELALRIsrGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFDLT 222
Cdd:cd20628   81 NENSKILVEKLKKKA--GGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 223 YMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGssqESSNDDADVGAKRKMAFLDILLQSTVDERPLSNLDIREEVD 302
Cdd:cd20628  159 FRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEK---RNSEEDDEFGKKKRKAFLDLLLEAHEDGGPLTDEDIREEVD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 303 TFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPvSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVL 382
Cdd:cd20628  236 TFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRRP-TLEDLNKMKYLERVIKETLRLYPSVPFIGRRLT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 383 EDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAeKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVA 462
Cdd:cd20628  315 EDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSA-KRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLA 393
                        410       420       430
                 ....*....|....*....|....*....|...
gi 808351875 463 NVLRHYEVDFVgDSSEPPVLIAELILRTKEPLM 495
Cdd:cd20628  394 KILRNFRVLPV-PPGEDLKLIAEIVLRSKNGIR 425
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
66-494 5.21e-176

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: 501.41  E-value: 5.21e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  66 FGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQ 145
Cdd:cd20660    4 FRIWLGPKPIVVLYSAETVEVILSSSKHIDKSFEYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 146 SLRLVEELALRIsrGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFDLTYML 225
Cdd:cd20660   84 SEILVKKLKKEV--GKEEFDIFPYITLCALDIICETAMGKSVNAQQNSDSEYVKAVYRMSELVQKRQKNPWLWPDFIYSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 226 TPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNDDADVGAKRKMAFLDILLQSTVDERPLSNLDIREEVDTFM 305
Cdd:cd20660  162 TPDGREHKKCLKILHGFTNKVIQERKAELQKSLEEEEEDDEDADIGKRKRLAFLDLLLEASEEGTKLSDEDIREEVDTFM 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 306 FEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDC 385
Cdd:cd20660  242 FEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSDR-PATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 386 EINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVL 465
Cdd:cd20660  321 EIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRF-LPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSIL 399
                        410       420
                 ....*....|....*....|....*....
gi 808351875 466 RHYEVDFVgDSSEPPVLIAELILRTKEPL 494
Cdd:cd20660  400 RNFRIESV-QKREDLKPAGELILRPVDGI 427
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
66-497 3.19e-144

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: 420.42  E-value: 3.19e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  66 FGLFLGPSY-SVMLFNPRDVERVLGSSQllTKS-QEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFD 143
Cdd:cd20659    4 YVFWLGPFRpILVLNHPDTIKAVLKTSE--PKDrDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVYN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 144 RQSLRLVEELaLRISRGQERINLGEAIHLCALDAICETAMGVSINAQ-SNADSEYVQAVKTISMVLHKRMFNILYRFDLT 222
Cdd:cd20659   82 ECTDILLEKW-SKLAETGESVEVFEDISLLTLDIILRCAFSYKSNCQqTGKNHPYVAAVHELSRLVMERFLNPLLHFDWI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 223 YMLTPLARAEKKALNVLHQFTEKIIVQRREELiregssqeSSNDDADVGAKRKMAFLDILLQSTvDE--RPLSNLDIREE 300
Cdd:cd20659  161 YYLTPEGRRFKKACDYVHKFAEEIIKKRRKEL--------EDNKDEALSKRKYLDFLDILLTAR-DEdgKGLTDEEIRDE 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 301 VDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDksTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRK 380
Cdd:cd20659  232 VDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDR--DDIEWDDLSKLPYLTMCIKESLRLYPPVPFIART 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 381 VLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAI 460
Cdd:cd20659  310 LTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL-PENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVV 388
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 808351875 461 VANVLRHYEVDFvgDSSEPPVLIAELILRTKEPLMFK 497
Cdd:cd20659  389 LARILRRFELSV--DPNHPVEPKPGLVLRSKNGIKLK 423
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
61-489 2.15e-143

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: 419.17  E-value: 2.15e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVE 140
Cdd:cd20680   10 RHEPLLKLWIGPVPFVILYHAENVEVILSSSKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 141 IFDRQSLRLVEELALRIsrGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFD 220
Cdd:cd20680   90 VMNEQSNILVEKLEKHV--DGEAFNCFFDITLCALDIICETAMGKKIGAQSNKDSEYVQAVYRMSDIIQRRQKMPWLWLD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 221 LTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNDDADVGAKRKmAFLDILLQSTVDE-RPLSNLDIRE 299
Cdd:cd20680  168 LWYLMFKEGKEHNKNLKILHTFTDNVIAERAEEMKAEEDKTGDSDGESPSKKKRK-AFLDMLLSVTDEEgNKLSHEDIRE 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 300 EVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStPVSYELLNQLHYVDLCVKETLRMYPSVPLLGR 379
Cdd:cd20680  247 EVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDR-PVTMEDLKKLRYLECVIKESLRLFPSVPLFAR 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 380 KVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKA 459
Cdd:cd20680  326 SLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERF-FPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKV 404
                        410       420       430
                 ....*....|....*....|....*....|
gi 808351875 460 IVANVLRHYEVDfVGDSSEPPVLIAELILR 489
Cdd:cd20680  405 VLSCILRHFWVE-ANQKREELGLVGELILR 433
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
57-498 5.49e-129

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: 382.78  E-value: 5.49e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875   57 ELAERHGDTFGLFLGPSYSVMLFNPRDVERVLG-----SSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFH 131
Cdd:pfam00067  28 KLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIkkgeeFSGRPDEPWFATSRGPFLGKGIVFANGPRWRQLRRFLTPTFT 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  132 FRILEPYVEIFDRQSLRLVEELALRISRGQeRINLGEAIHLCALDAICETAMGVSIN-AQSNADSEYVQAVKTISMVLHK 210
Cdd:pfam00067 108 SFGKLSFEPRVEEEARDLVEKLRKTAGEPG-VIDITDLLFRAALNVICSILFGERFGsLEDPKFLELVKAVQELSSLLSS 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  211 RMFNILYRF-DLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELiregssqessnddaDVGAKRKMAFLDILLQSTVDE 289
Cdd:pfam00067 187 PSPQLLDLFpILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL--------------DSAKKSPRDFLDALLLAKEEE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  290 RP--LSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLHYVDLCVKET 367
Cdd:pfam00067 253 DGskLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKR--SPTYDDLQNMPYLDAVIKET 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  368 LRMYPSVP-LLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvVTTAEKLNPYAYIPFSAGPRN 446
Cdd:pfam00067 331 LRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFL-DENGKFRKSFAFLPFGAGPRN 409
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 808351875  447 CIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPLMFKV 498
Cdd:pfam00067 410 CLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
54-491 7.42e-117

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: 351.19  E-value: 7.42e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  54 KIGELAERHGDTFGLFLGPSYSVM-LFNPRDVERVLGSSQllTKSQE-YSFLGRWLNEGLLVSNGRKWHRRRKIITPAFH 131
Cdd:cd20678    3 KILKWVEKYPYAFPLWFGGFKAFLnIYDPDYAKVVLSRSD--PKAQGvYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFH 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 132 FRILEPYVEIFDrQSLRLVEELALRISRGQERINLGEAIHLCALDAICETAMGVSINAQSNADSE-YVQAVKTISMVLHK 210
Cdd:cd20678   81 YDILKPYVKLMA-DSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNsYIQAVSDLSNLIFQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 211 RMFNILYRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNddadvgaKRKMAFLDILLQSTV-DE 289
Cdd:cd20678  160 RLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKK-------KRHLDFLDILLFAKDeNG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 290 RPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGnDKSTpVSYELLNQLHYVDLCVKETLR 369
Cdd:cd20678  233 KSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILG-DGDS-ITWEHLDQMPYTTMCIKEALR 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 370 MYPSVPLLGRKV-----LEDceinGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGP 444
Cdd:cd20678  311 LYPPVPGISRELskpvtFPD----GRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRF-SPENSSKRHSHAFLPFSAGP 385
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 808351875 445 RNCIGQKFAMLEIKAIVANVLRHYEvdFVGDSSEPPVLIAELILRTK 491
Cdd:cd20678  386 RNCIGQQFAMNEMKVAVALTLLRFE--LLPDPTRIPIPIPQLVLKSK 430
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
55-490 1.03e-106

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: 325.11  E-value: 1.03e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  55 IGELAERHGDTFGLFLGPSYSVM-LFNPRDVERVLGSSQLLTKSQE--YSFLGRWLNEGLLVSNGRKWHRRRKIITPAFH 131
Cdd:cd20679    4 VTQLVATYPQGCLWWLGPFYPIIrLFHPDYIRPVLLASAAVAPKDElfYGFLKPWLGDGLLLSSGDKWSRHRRLLTPAFH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 132 FRILEPYVEIFDRQSLRLVEELALRISRGQERINLGEAIHLCALDAICETAMGVSINAQSNAdSEYVQAVKTISMVLHKR 211
Cdd:cd20679   84 FNILKPYVKIFNQSTNIMHAKWRRLASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKP-SEYIAAILELSALVVKR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 212 MFNILYRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNddadvGAKRK-MAFLDILLQSTvDE- 289
Cdd:cd20679  163 QQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKA-----KAKSKtLDFIDVLLLSK-DEd 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 290 -RPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYELLNQLHYVDLCVKETL 368
Cdd:cd20679  237 gKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 369 RMYPSVPLLGRKVLEDCEI-NGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvVTTAEKLNPYAYIPFSAGPRNC 447
Cdd:cd20679  317 RLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFD-PENSQGRSPLAFIPFSAGPRNC 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 808351875 448 IGQKFAMLEIKAIVANVLRHYEVDfvgDSSEPPVLIAELILRT 490
Cdd:cd20679  396 IGQTFAMAEMKVVLALTLLRFRVL---PDDKEPRRKPELILRA 435
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
65-469 1.27e-104

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: 319.16  E-value: 1.27e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  65 TFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLgrWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDR 144
Cdd:cd11057    3 PFRAWLGPRPFVITSDPEIVQVVLNSPHCLNKSFFYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 145 QSLRLVEELALRIsrGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILYRFDLTYM 224
Cdd:cd11057   81 EAQKLVQRLDTYV--GGGEFDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFELIAKRVLNPWLHPEFIYR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 225 LTPLARAEKKALNVLHQFTEKIIVQRREElIREGSSQESSNDDADVgaKRKMAFLDILLQSTVDERPLSNLDIREEVDTF 304
Cdd:cd11057  159 LTGDYKEEQKARKILRAFSEKIIEKKLQE-VELESNLDSEEDEENG--RKPQIFIDQLLELARNGEEFTDEEIMDEIDTM 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 305 MFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLED 384
Cdd:cd11057  236 IFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQ-FITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTAD 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 385 CEI-NGKLIPAGTNIGISPLYLGRREELF-SEPNIFKPERFDVVTTAEKlNPYAYIPFSAGPRNCIGQKFAMLEIKAIVA 462
Cdd:cd11057  315 IQLsNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQR-HPYAFIPFSAGPRNCIGWRYAMISMKIMLA 393

                 ....*..
gi 808351875 463 NVLRHYE 469
Cdd:cd11057  394 KILRNYR 400
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
62-494 2.35e-89

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: 279.85  E-value: 2.35e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLG--PSYSVMlfnprDVERVlgsSQLLTKsqEYS-FLGRW--------LNEGLLVSNGRKWHRRRKIITPAF 130
Cdd:cd11055    2 YGKVFGLYFGtiPVIVVS-----DPEMI---KEILVK--EFSnFTNRPlfilldepFDSSLLFLKGERWKRLRTTLSPTF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 131 HFRILEPYVEIFDRQSLRLVEELaLRISRGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTI--SMVL 208
Cdd:cd11055   72 SSGKLKLMVPIINDCCDELVEKL-EKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIfrNSII 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 209 HKRMFNILYRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELiregssQESSNDdadvgakrkmaFLDILL----- 283
Cdd:cd11055  151 RLFLLLLLFPLRLFLFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNK------SSRRKD-----------LLQLMLdaqds 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 284 QSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDksTPVSYELLNQLHYVDLC 363
Cdd:cd11055  214 DEDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDD--GSPTYDTVSKLKYLDMV 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 364 VKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAeKLNPYAYIPFSAG 443
Cdd:cd11055  292 INETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKA-KRHPYAYLPFGAG 370
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808351875 444 PRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPL 494
Cdd:cd11055  371 PRNCIGMRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSPKNGI 421
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
63-495 1.30e-87

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: 274.84  E-value: 1.30e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  63 GDTFGLFLGPSYSVMLFNPRDVERVLGS-SQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEI 141
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTnARNYVKGGVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 142 FDRQSLRLVEELALRISRGqeRINLGEAIHLCALDAICETAMGVSINAQSNADSEyvqAVKTISMVLHKRMFNilYRFDL 221
Cdd:cd20620   81 MVEATAALLDRWEAGARRG--PVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGD---ALDVALEYAARRMLS--PFLLP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 222 TYMLTPLARAEKKALNVLHQFTEKIIVQRReeliregSSQESSNDdadvgakrkmaFLDILLQSTVDE--RPLSNLDIRE 299
Cdd:cd20620  154 LWLPTPANRRFRRARRRLDEVIYRLIAERR-------AAPADGGD-----------LLSMLLAARDEEtgEPMSDQQLRD 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 300 EVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPvsyELLNQLHYVDLCVKETLRMYPSVPLLGR 379
Cdd:cd20620  216 EVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTA---EDLPQLPYTEMVLQESLRLYPPAWIIGR 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 380 KVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvvTTAEKLNP-YAYIPFSAGPRNCIGQKFAMLEIK 458
Cdd:cd20620  293 EAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFT--PEREAARPrYAYFPFGGGPRICIGNHFAMMEAV 370
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 808351875 459 AIVANVLRHYEVDFVGDSsePPVLIAELILRTKEPLM 495
Cdd:cd20620  371 LLLATIAQRFRLRLVPGQ--PVEPEPLITLRPKNGVR 405
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
57-473 1.05e-80

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: 257.45  E-value: 1.05e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  57 ELAERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLG-----RWLNEGLLV-SNGRKWHRRRKIITPAF 130
Cdd:cd20613    6 EWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLITLNLPKPPRVYSRLAflfgeRFLGNGLVTeVDHEKWKKRRAILNPAF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 131 HFRILEPYVEIFDRQSLRLVEELALRiSRGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHK 210
Cdd:cd20613   86 HRKYLKNLMDEFNESADLLVEKLSKK-ADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDSPFPKAISLVLEGIQE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 211 RMFNILYRFDltymltPLARAE----KKALNVLHQFTEKIIVQRREELIREgssQESSNDdadvgakrkmaFLDILLQST 286
Cdd:cd20613  165 SFRNPLLKYN------PSKRKYrrevREAIKFLRETGRECIEERLEALKRG---EEVPND-----------ILTHILKAS 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 287 VDErplSNLDIREEVD---TFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGnDKSTpVSYELLNQLHYVDLC 363
Cdd:cd20613  225 EEE---PDFDMEELLDdfvTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLG-SKQY-VEYEDLGKLEYLSQV 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 364 VKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvVTTAEKLNPYAYIPFSAG 443
Cdd:cd20613  300 LKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFS-PEAPEKIPSYAYFPFSLG 378
                        410       420       430
                 ....*....|....*....|....*....|
gi 808351875 444 PRNCIGQKFAMLEIKAIVANVLRHYEVDFV 473
Cdd:cd20613  379 PRSCIGQQFAQIEAKVILAKLLQNFKFELV 408
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
63-489 4.59e-80

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: 254.75  E-value: 4.59e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  63 GDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSF--LGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVE 140
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLpaLGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 141 IFDRQSLRLVEELAlriSRGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQavktismvlhkRMFNILYRFD 220
Cdd:cd00302   81 VIREIARELLDRLA---AGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLE-----------ALLKLLGPRL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 221 LTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSqessnddadvgakrkmafldILLQSTVDERPLSNLDIREE 300
Cdd:cd00302  147 LRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDL--------------------LLLADADDGGGLSDEEIVAE 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 301 VDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDkstpvSYELLNQLHYVDLCVKETLRMYPSVPLLGRK 380
Cdd:cd00302  207 LLTLLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG-----TPEDLSKLPYLEAVVEETLRLYPPVPLLPRV 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 381 VLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvvtTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAI 460
Cdd:cd00302  282 ATEDVELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFL---PEREEPRYAHLPFGAGPHRCLGARLARLELKLA 358
                        410       420
                 ....*....|....*....|....*....
gi 808351875 461 VANVLRHYevDFVGDSSEPPVLIAELILR 489
Cdd:cd00302  359 LATLLRRF--DFELVPDEELEWRPSLGTL 385
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
68-494 1.31e-78

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: 252.58  E-value: 1.31e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  68 LFLGPSYSVMLFNPRDVERVLGSSQL-LTKSQEY-SFLGRWLNEGLLVSNGRKwHRR-RKIITPAFHFRILEPYVEIFDR 144
Cdd:cd11069    8 RGLFGSERLLVTDPKALKHILVTNSYdFEKPPAFrRLLRRILGDGLLAAEGEE-HKRqRKILNPAFSYRHVKELYPIFWS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 145 QSLRLVEELALRISRGQERINLGEAIH---LCALDAICETAMGVSINAQSNADSEYVQAVKTI-SMVLHK---RMFNILY 217
Cdd:cd11069   87 KAEELVDKLEEEIEESGDESISIDVLEwlsRATLDIIGLAGFGYDFDSLENPDNELAEAYRRLfEPTLLGsllFILLLFL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 218 RFDLTYML-TPLARAEKKALNVLHQFTEKIIVQRREELirEGSSQESSNDdadvgakrkmaFLDILLQSTV--DERPLSN 294
Cdd:cd11069  167 PRWLVRILpWKANREIRRAKDVLRRLAREIIREKKAAL--LEGKDDSGKD-----------ILSILLRANDfaDDERLSD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 295 LDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYELLNQLHYVDLCVKETLRMYPSV 374
Cdd:cd11069  234 EELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPV 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 375 PLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELF-SEPNIFKPERFDVVTTAEKLN----PYAYIPFSAGPRNCIG 449
Cdd:cd11069  314 PLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASPGgagsNYALLTFLHGPRSCIG 393
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 808351875 450 QKFAMLEIKAIVANVLRHYEVDFvGDSSEPPVLIAELILRTKEPL 494
Cdd:cd11069  394 KKFALAEMKVLLAALVSRFEFEL-DPDAEVERPIGIITRPPVDGL 437
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
60-494 1.40e-77

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: 249.37  E-value: 1.40e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  60 ERHGDTFGLFLGPSYSVMLFNPRDVERVL---------GSSQLLTKSQEYsflgRWLNEGLLVSNGRKWHRRRKIITPAF 130
Cdd:cd11054    2 KKYGPIVREKLGGRDIVHLFDPDDIEKVFrnegkypirPSLEPLEKYRKK----RGKPLGLLNSNGEEWHRLRSAVQKPL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 131 -HFRILEPYVEIFDRQSLRLVEEL-ALRISRGQERINLGEAIHLCALDAICETAMGVSINA-QSNADSE---YVQAVKTI 204
Cdd:cd11054   78 lRPKSVASYLPAINEVADDFVERIrRLRDEDGEEVPDLEDELYKWSLESIGTVLFGKRLGClDDNPDSDaqkLIEAVKDI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 205 SMVLHKRMFNI-LYRfdltYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNDdadvgakrkmaFLDILL 283
Cdd:cd11054  158 FESSAKLMFGPpLWK----YFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDEEEDS-----------LLEYLL 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 284 QStvderplSNLDIREEVDT---FMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLHYV 360
Cdd:cd11054  223 SK-------PGLSKKEIVTMaldLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGE--PITAEDLKKMPYL 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 361 DLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVV-TTAEKLNPYAYIP 439
Cdd:cd11054  294 KACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDdSENKNIHPFASLP 373
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 440 FSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDfvgDSSEPPVLIAELILRTKEPL 494
Cdd:cd11054  374 FGFGPRMCIGRRFAELEMYLLLAKLLQNFKVE---YHHEELKVKTRLILVPDKPL 425
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
61-475 1.39e-69

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: 229.17  E-value: 1.39e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFGLFLGPSYSVMLFNPRDVERVLgssqlLTKSQEYSFLGRW-------LNEGLLVSNGRKWHRRRKIITPAFHFR 133
Cdd:cd11046    9 EYGPIYKLAFGPKSFLVISDPAIAKHVL-----RSNAFSYDKKGLLaeilepiMGKGLIPADGEIWKKRRRALVPALHKD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 134 ILEPYVEIFDRQSLRLVEELaLRISRGQERINLGEAIHLCALDAICETAMGVSINAQSNaDSEYVQAVKT-ISMVLHKRM 212
Cdd:cd11046   84 YLEMMVRVFGRCSERLMEKL-DAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTE-ESPVIKAVYLpLVEAEHRSV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 213 FNILY-RFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREelIREGSSQESSNDDADVgaKRKMAFLDILLQSTVDErp 291
Cdd:cd11046  162 WEPPYwDIPAALFIVPRQRKFLRDLKLLNDTLDDLIRKRKE--MRQEEDIELQQEDYLN--EDDPSLLRFLVDMRDED-- 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 292 LSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDksTPVSYELLNQLHYVDLCVKETLRMY 371
Cdd:cd11046  236 VDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDR--LPPTYEDLKKLKYTRRVLNESLRLY 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 372 PSVPLLGRKVLEDCEI--NGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVV---TTAEKLNPYAYIPFSAGPRN 446
Cdd:cd11046  314 PQPPVLIRRAVEDDKLpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPfinPPNEVIDDFAFLPFGGGPRK 393
                        410       420
                 ....*....|....*....|....*....
gi 808351875 447 CIGQKFAMLEIKAIVANVLRHYEVDFVGD 475
Cdd:cd11046  394 CLGDQFALLEATVALAMLLRRFDFELDVG 422
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
57-481 2.03e-68

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: 225.16  E-value: 2.03e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  57 ELAERHGDTFGL-FLGPSYSVMLFNPRDVERVL-GSSQLLTKSQEYSFLGRWLNE-GLLVSNGRKWHRRRKIITPAFHFR 133
Cdd:cd11053    6 RLRARYGDVFTLrVPGLGPVVVLSDPEAIKQIFtADPDVLHPGEGNSLLEPLLGPnSLLLLDGDRHRRRRKLLMPAFHGE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 134 ILEPYVEIFDRQSLRLVEELAlrisRGQeRINLGEAIHLCALDAICETAMGVSINAQSNADSEYV-QAVKTISMVLhkRM 212
Cdd:cd11053   86 RLRAYGELIAEITEREIDRWP----PGQ-PFDLRELMQEITLEVILRVVFGVDDGERLQELRRLLpRLLDLLSSPL--AS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 213 FNILYRFDLTymLTPLARAekkaLNVLHQFTEKI---IVQRREELIREGSsqessnddaDVgakrkmafLDILLQST-VD 288
Cdd:cd11053  159 FPALQRDLGP--WSPWGRF----LRARRRIDALIyaeIAERRAEPDAERD---------DI--------LSLLLSARdED 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 289 ERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStpvsyELLNQLHYVDLCVKETL 368
Cdd:cd11053  216 GQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP-----EDIAKLPYLDAVIKETL 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 369 RMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvvttAEKLNPYAYIPFSAGPRNCI 448
Cdd:cd11053  291 RLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFL----GRKPSPYEYLPFGGGVRRCI 366
                        410       420       430
                 ....*....|....*....|....*....|...
gi 808351875 449 GQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPV 481
Cdd:cd11053  367 GAAFALLEMKVVLATLLRRFRLELTDPRPERPV 399
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
91-469 5.03e-67

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: 221.83  E-value: 5.03e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  91 SQLLTKSQEYS-----------FLGRwlneGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELALRISR 159
Cdd:cd11052   34 KELLSKKEGYFgksplqpglkkLLGR----GLVMSNGEKWAKHRRIANPAFHGEKLKGMVPAMVESVSDMLERWKKQMGE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 160 GQERINLGEAIHLCALDAICETAMGVSinaqsnadseYVQAVKTISM--VLHKRMFNILYRFDLTYMLTPLARAEKKALN 237
Cdd:cd11052  110 EGEEVDVFEEFKALTADIISRTAFGSS----------YEEGKEVFKLlrELQKICAQANRDVGIPGSRFLPTKGNKKIKK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 238 VLHQFTEKI--IVQRREELIREGSSQESSNDdadvgakrkmaFLDILL---QSTVDERPLSNLDIREEVDTFMFEGHDTT 312
Cdd:cd11052  180 LDKEIEDSLleIIKKREDSLKMGRGDDYGDD-----------LLGLLLeanQSDDQNKNMTVQEIVDECKTFFFAGHETT 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 313 SSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstpVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLI 392
Cdd:cd11052  249 ALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDK---PPSDSLSKLKTVSMVINESLRLYPPAVFLTRKAKEDIKLGGLVI 325
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808351875 393 PAGTNIGISPLYLGRREELFSE-PNIFKPERF-DVVTTAEKlNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:cd11052  326 PKGTSIWIPVLALHHDEEIWGEdANEFNPERFaDGVAKAAK-HPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFS 403
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
62-486 3.56e-63

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: 211.35  E-value: 3.56e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQE-YSFLGRWLNEGLLVSNGRKwHRR-RKIITPAFHFRILEPYV 139
Cdd:cd11049   12 HGDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKGGPlFDRARPLLGNGLATCPGED-HRRqRRLMQPAFHRSRIPAYA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 140 EIFDRQslrlVEELALRISRGQeRINLGEAIHLCALDAICETAMGVSINAQSNAdsEYVQAVKTISMVLHKRM--FNILY 217
Cdd:cd11049   91 EVMREE----AEALAGSWRPGR-VVDVDAEMHRLTLRVVARTLFSTDLGPEAAA--ELRQALPVVLAGMLRRAvpPKFLE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 218 RFDltymlTPLARAEKKALNVLHQFTEKIIVQRReeliregssqeSSNDDADvgakrkmAFLDILLQSTVDE-RPLSNLD 296
Cdd:cd11049  164 RLP-----TPGNRRFDRALARLRELVDEIIAEYR-----------ASGTDRD-------DLLSLLLAARDEEgRPLSDEE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 297 IREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNdksTPVSYELLNQLHYVDLCVKETLRMYPSVPL 376
Cdd:cd11049  221 LRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGG---RPATFEDLPRLTYTRRVVTEALRLYPPVWL 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 377 LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEkLNPYAYIPFSAGPRNCIGQKFAMLE 456
Cdd:cd11049  298 LTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAA-VPRGAFIPFGAGARKCIGDTFALTE 376
                        410       420       430
                 ....*....|....*....|....*....|
gi 808351875 457 IKAIVANVLRHYEVDFVGDSSEPPVLIAEL 486
Cdd:cd11049  377 LTLALATIASRWRLRPVPGRPVRPRPLATL 406
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
67-473 3.53e-62

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: 209.37  E-value: 3.53e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  67 GLFLGPSYSVMLFNPRDVERVLgSSQLLT--KSQEYS-----FLGrwlnEGLLVSNGRKWHRRRKIITPAFHFRILEPYV 139
Cdd:cd11064    5 GPWPGGPDGIVTADPANVEHIL-KTNFDNypKGPEFRdlffdLLG----DGIFNVDGELWKFQRKTASHEFSSRALREFM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 140 E-IFDRQSLRLVEELALRISRGQERINLGEAIHLCALDAICETAMGVSIN--AQSNADSEYVQAVKTISMVLHKR--MFN 214
Cdd:cd11064   80 EsVVREKVEKLLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGslSPSLPEVPFAKAFDDASEAVAKRfiVPP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 215 ILYRfdltymltpLARA-----EKK---ALNVLHQFTEKIIVQRREELireGSSQESSNDDADVGAKrkmaFLDIllqST 286
Cdd:cd11064  160 WLWK---------LKRWlnigsEKKlreAIRVIDDFVYEVISRRREEL---NSREEENNVREDLLSR----FLAS---EE 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 287 VDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVV---GNDKSTPVSYELLNQLHYVDLC 363
Cdd:cd11064  221 EEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLpklTTDESRVPTYEELKKLVYLHAA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 364 VKETLRMYPSVPLLGRKVLEDCEI-NGKLIPAGTNIGISPLYLGRREELFSE-PNIFKPERF---DVVTTAEklNPYAYI 438
Cdd:cd11064  301 LSESLRLYPPVPFDSKEAVNDDVLpDGTFVKKGTRIVYSIYAMGRMESIWGEdALEFKPERWldeDGGLRPE--SPYKFP 378
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 808351875 439 PFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFV 473
Cdd:cd11064  379 AFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVV 413
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
111-482 3.98e-62

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: 208.93  E-value: 3.98e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 111 LLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELALRISRGQErinlGEAIHLCA---LDAICETAMGVSI 187
Cdd:cd11056   53 LFSLDGEKWKELRQKLTPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGKE----LEIKDLMArytTDVIASCAFGLDA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 188 NAQSNADSEYVQAVKtismvlhkRMFNILYRFDLTYMLTPLARAEKKALNVlhQFTEKIIVQRREELIREGSSQESSNdd 267
Cdd:cd11056  129 NSLNDPENEFREMGR--------RLFEPSRLRGLKFMLLFFFPKLARLLRL--KFFPKEVEDFFRKLVRDTIEYREKN-- 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 268 advGAKRKmAFLDILLQ--------STVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRS 339
Cdd:cd11056  197 ---NIVRN-DFIDLLLElkkkgkieDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDE 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 340 VVGNDKStPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGK--LIPAGTNIGISPLYLGRREELFSEPNI 417
Cdd:cd11056  273 VLEKHGG-ELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTdvVIEKGTPVIIPVYALHHDPKYYPEPEK 351
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 418 FKPERFDVvTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVL 482
Cdd:cd11056  352 FDPERFSP-ENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKL 415
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
63-470 5.24e-61

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: 205.91  E-value: 5.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  63 GDTFGLFLGPSYSVMLFNPRDVERVLgssqlltKSQEYSFLGRWLNE---------GLLVSNGRKWHRRRKIITPAF-HF 132
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAF-------VKNGDNFSDRPLLPsfeiisggkGILFSNGDYWKELRRFALSSLtKT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 133 RILEPYVEIFDRQSLRLVEELALRISRGQErINLGEAIHLCALDAICETAMGVSINAQSnaDSEYVQAVKTISMVLHKRM 212
Cdd:cd20617   74 KLKKKMEELIEEEVNKLIESLKKHSKSGEP-FDPRPYFKKFVLNIINQFLFGKRFPDED--DGEFLKLVKPIEEIFKELG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 213 -FNILYRFDLTYMLTPLARAE-KKALNVLHQFTEKIIVQRREELiregssqessndDADVGAKRKMAFLDILLQStVDER 290
Cdd:cd20617  151 sGNPSDFIPILLPFYFLYLKKlKKSYDKIKDFIEKIIEEHLKTI------------DPNNPRDLIDDELLLLLKE-GDSG 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 291 PLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYelLNQLHYVDLCVKETLRM 370
Cdd:cd20617  218 LFDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSD--RSKLPYLNAVIKEVLRL 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 371 YPSVPL-LGRKVLEDCEINGKLIPAGTNIgISPLY-LGRREELFSEPNIFKPERFdvVTTAEKLNPYAYIPFSAGPRNCI 448
Cdd:cd20617  296 RPILPLgLPRVTTEDTEIGGYFIPKGTQI-IINIYsLHRDEKYFEDPEEFNPERF--LENDGNKLSEQFIPFGIGKRNCV 372
                        410       420
                 ....*....|....*....|..
gi 808351875 449 GQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20617  373 GENLARDELFLFFANLLLNFKF 394
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
60-483 4.06e-59

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: 200.97  E-value: 4.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  60 ERHGDTFGLFLGPSYSVMLFNPRDVERVL-GSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPY 138
Cdd:cd11044   19 QKYGPVFKTHLLGRPTVFVIGAEAVRFILsGEGKLVRYGWPRSVRRLLGENSLSLQDGEEHRRRRKLLAPAFSREALESY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 139 VEIFDRQSLRLVEELAlrisrGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAvktismvLHKRMFNILYR 218
Cdd:cd11044   99 VPTIQAIVQSYLRKWL-----KAGEVALYPELRRLTFDVAARLLLGLDPEVEAEALSQDFET-------WTDGLFSLPVP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 219 FDLTymltPLARAeKKALNVLHQFTEKIIVQRREELIREGssqessnDDAdvgakrkmafLDILLQStVDER--PLSNLD 296
Cdd:cd11044  167 LPFT----PFGRA-IRARNKLLARLEQAIRERQEEENAEA-------KDA----------LGLLLEA-KDEDgePLSMDE 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 297 IREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVvgnDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPL 376
Cdd:cd11044  224 LKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDAL---GLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGG 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 377 LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLE 456
Cdd:cd11044  301 GFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPRECLGKEFAQLE 380
                        410       420
                 ....*....|....*....|....*..
gi 808351875 457 IKAIVANVLRHYEVDFVGDSSEPPVLI 483
Cdd:cd11044  381 MKILASELLRNYDWELLPNQDLEPVVV 407
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
61-469 2.18e-58

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: 199.48  E-value: 2.18e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFgLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEP-YV 139
Cdd:cd11070    1 KLGAVK-ILFVSRWNILVTKPEYLTQIFRRRDDFPKPGNQYKIPAFYGPNVISSEGEDWKRYRKIVAPAFNERNNALvWE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 140 EIFdRQSLRLVEELALRISRGQERIN-LGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTIsmvlhKRMF--NIL 216
Cdd:cd11070   80 ESI-RQAQRLIRYLLEEQPSAKGGGVdVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNAI-----KLAIfpPLF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 217 YRF-DLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREgsSQESSNDDADVGAKRKMAFLDILLQstvDERPLSNL 295
Cdd:cd11070  154 LNFpFLDRLPWVLFPSRKRAFKDVDEFLSELLDEVEAELSAD--SKGKQGTESVVASRLKRARRSGGLT---EKELLGNL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 296 DIreevdtFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYELLNQLHYVDLCVKETLRMYPSVP 375
Cdd:cd11070  229 FI------FFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDFPKLPYLLAVIYETLRLYPPVQ 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 376 LLGRKVLEDCEINGKL-----IPAGTNIGISPLYLGRREEL-FSEPNIFKPERF----DVVTTAEKLNPY--AYIPFSAG 443
Cdd:cd11070  303 LLNRKTTEPVVVITGLgqeivIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWgstsGEIGAATRFTPArgAFIPFSAG 382
                        410       420
                 ....*....|....*....|....*.
gi 808351875 444 PRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:cd11070  383 PRACLGRKFALVEFVAALAELFRQYE 408
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-501 2.39e-58

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: 198.19  E-value: 2.39e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFL---GRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEP 137
Cdd:COG2124   30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVlrpLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAA 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 138 YVEIFDRQSLRLVEELAlrisrGQERINLGEAIHLCALDAICETAMGVsinaqsnaDSEYVQAVKTISMVLhkrmfnily 217
Cdd:COG2124  110 LRPRIREIADELLDRLA-----ARGPVDLVEEFARPLPVIVICELLGV--------PEEDRDRLRRWSDAL--------- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 218 rFDLTYMLTPLARAE-KKALNVLHQFTEKIIVQRReeliregssQESSNDdadvgakrkmaFLDILLQSTVDERPLSNLD 296
Cdd:COG2124  168 -LDALGPLPPERRRRaRRARAELDAYLRELIAERR---------AEPGDD-----------LLSALLAARDDGERLSDEE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 297 IREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKcfeeirsvvgndkstpvsyeLLNQLHYVDLCVKETLRMYPSVPL 376
Cdd:COG2124  227 LRDELLLLLLAGHETTANALAWALYALLRHPEQLAR--------------------LRAEPELLPAAVEETLRLYPPVPL 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 377 LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERfdvvttaeklNPYAYIPFSAGPRNCIGQKFAMLE 456
Cdd:COG2124  287 LPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLE 356
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 808351875 457 IKAIVANVLRHYEvDFVGDSSEPPVLIAELILRTKEPLMFKVRER 501
Cdd:COG2124  357 ARIALATLLRRFP-DLRLAPPEELRWRPSLTLRGPKSLPVRLRPR 400
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
61-497 1.59e-57

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: 196.87  E-value: 1.59e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFGLFLGPSYSVMLFNPRDVERVLGSS--QLLTKSQEYSFLGrWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPY 138
Cdd:cd20650    1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKEcySVFTNRRPFGPVG-FMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 139 VEIFDRQSLRLVEELALRISRGqERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTIsmvLHKRMFNILYR 218
Cdd:cd20650   80 FPIIAQYGDVLVKNLRKEAEKG-KPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKL---LKFDFLDPLFL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 219 FDLTY-MLTPLARA------EKKALNVLHQFTEKIivqrREEliREGSSQessnddadvgaKRKMAFLDILLQSTVDE-- 289
Cdd:cd20650  156 SITVFpFLTPILEKlnisvfPKDVTNFFYKSVKKI----KES--RLDSTQ-----------KHRVDFLQLMIDSQNSKet 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 290 ---RPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDksTPVSYELLNQLHYVDLCVKE 366
Cdd:cd20650  219 eshKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNK--APPTYDTVMQMEYLDMVVNE 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 367 TLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvVTTAEKLNPYAYIPFSAGPRN 446
Cdd:cd20650  297 TLRLFPIAGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFS-KKNKDNIDPYIYLPFGSGPRN 375
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808351875 447 CIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPLMFK 497
Cdd:cd20650  376 CIGMRFALMNMKLALVRVLQNFSFKPCKETQIPLKLSLQGLLQPEKPIVLK 426
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
121-472 2.91e-56

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: 193.21  E-value: 2.91e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 121 RRRKIITPAF---HFRILEPYVEIFDRQslrLVEELALRISRGQER-INLGEAIHLCALDAICETAMGVSINAQSNADSE 196
Cdd:cd11061   56 RRRRVWSHAFsdkALRGYEPRILSHVEQ---LCEQLDDRAGKPVSWpVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKDR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 197 YVQAVKTISMVLHKRMFNI--LYRFDLTYMLTPLARaekKALNVLHQFTEKIIVQRREeliregsSQESSNDDadvgakr 274
Cdd:cd11061  133 YILDLLEKSMVRLGVLGHApwLRPLLLDLPLFPGAT---KARKRFLDFVRAQLKERLK-------AEEEKRPD------- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 275 kmaFLDILLQSTVDE--RPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDkSTPVSYE 352
Cdd:cd11061  196 ---IFSYLLEAKDPEtgEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSD-DEIRLGP 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 353 LLNQLHYVDLCVKETLRMYPSVP-LLGRKVL-EDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAE 430
Cdd:cd11061  272 KLKSLPYLRACIDEALRLSPPVPsGLPRETPpGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEEL 351
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 808351875 431 KLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDF 472
Cdd:cd11061  352 VRARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRL 393
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
109-470 6.25e-56

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: 192.47  E-value: 6.25e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 109 EGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEelalrisrgQERINLGEAIHLCAL---DAI-----CE 180
Cdd:cd20621   49 KGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEITKEKIK---------KLDNQNVNIIQFLQKitgEVVirsffGE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 181 TAMGVSINAQSNAdseyVQAVKTISMVLHKRMFNILY-----RFDLTYMLTPLARAEKKAL---NVLHQFTEKIIVQRRE 252
Cdd:cd20621  120 EAKDLKINGKEIQ----VELVEILIESFLYRFSSPYFqlkrlIFGRKSWKLFPTKKEKKLQkrvKELRQFIEKIIQNRIK 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 253 ELirEGSSQESSNDDADvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKK 332
Cdd:cd20621  196 QI--KKNKDEIKDIIID--------LDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEK 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 333 CFEEIRSVVGNDksTPVSYELLNQLHYVDLCVKETLRMYPSVP-LLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREEL 411
Cdd:cd20621  266 LRQEIKSVVGND--DDITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKY 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 808351875 412 FSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20621  344 FENPDEFNPERW-LNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEI 401
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
62-481 2.29e-52

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: 182.76  E-value: 2.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGPSYSVMLFNPRDVERVLGssqllTKSQEYS-----------FLGRwlneGLLVSNGRKWHRRRKIITPAF 130
Cdd:cd11063    1 YGNTFEVNLLGTRVIFTIEPENIKAVLA-----TQFKDFGlgerrrdafkpLLGD----GIFTSDGEEWKHSRALLRPQF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 131 ---HFRILEpyveIFDRqslrLVEELALRISRGQERINLGEAIHLCALDAICETAMGVSINAQSNADS-----EYVQAVK 202
Cdd:cd11063   72 srdQISDLE----LFER----HVQNLIKLLPRDGSTVDLQDLFFRLTLDSATEFLFGESVDSLKPGGDsppaaRFAEAFD 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 203 TISMVLHKRM----FNILYRfDLTYmltplaraeKKALNVLHQFTEKIIvqrREELIREGSSQESSNDDADVgakrkmaF 278
Cdd:cd11063  144 YAQKYLAKRLrlgkLLWLLR-DKKF---------REACKVVHRFVDPYV---DKALARKEESKDEESSDRYV-------F 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 279 LDILLQSTVDERplsnlDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDksTPVSYELLNQLH 358
Cdd:cd11063  204 LDELAKETRDPK-----ELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPE--PTPTYEDLKNMK 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVPLLGRKVLEDCEI------NGK---LIPAGTNIGISPLYLGRREELFSE-PNIFKPERFDVVTT 428
Cdd:cd11063  277 YLRAVINETLRLYPPVPLNSRVAVRDTTLprgggpDGKspiFVPKGTRVLYSVYAMHRRKDIWGPdAEEFRPERWEDLKR 356
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 808351875 429 aeklNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVdFVGDSSEPPV 481
Cdd:cd11063  357 ----PGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFDR-IESRDVRPPE 404
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
80-478 2.98e-52

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: 182.78  E-value: 2.98e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  80 NPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGR--KWH-RRRKIITPAFHFR---ILEPYVeifDRQSLRLVEEL 153
Cdd:cd11060   15 DPEAIKTIYGTRSPYTKSDWYKAFRPKDPRKDNLFSERdeKRHaALRRKVASGYSMSsllSLEPFV---DECIDLLVDLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 154 ALRISRGQErINLGEAIHLCALDAICETAMGVS------------INAQSNADSEYVQAVKTISMvLHKRMFNILYRFDL 221
Cdd:cd11060   92 DEKAVSGKE-VDLGKWLQYFAFDVIGEITFGKPfgfleagtdvdgYIASIDKLLPYFAVVGQIPW-LDRLLLKNPLGPKR 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 222 TYmltplaraeKKALNVLHQFTEKIIVQRREEliregsSQESSNDDADvgakrkmaFLDILLQS-TVDERPLSNLDIREE 300
Cdd:cd11060  170 KD---------KTGFGPLMRFALEAVAERLAE------DAESAKGRKD--------MLDSFLEAgLKDPEKVTDREVVAE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 301 VDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDK-STPVSYELLNQLHYVDLCVKETLRMYPSVPL-LG 378
Cdd:cd11060  227 ALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKlSSPITFAEAQKLPYLQAVIKEALRLHPPVGLpLE 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 379 RKVLED-CEINGKLIPAGTNIGISPLYLGRREELFSE-PNIFKPERFdVVTTAEKLNP--YAYIPFSAGPRNCIGQKFAM 454
Cdd:cd11060  307 RVVPPGgATICGRFIPGGTIVGVNPWVIHRDKEVFGEdADVFRPERW-LEADEEQRRMmdRADLTFGAGSRTCLGKNIAL 385
                        410       420
                 ....*....|....*....|....
gi 808351875 455 LEIKAIVANVLRHYEVDFVGDSSE 478
Cdd:cd11060  386 LELYKVIPELLRRFDFELVDPEKE 409
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
60-499 3.09e-50

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: 177.02  E-value: 3.09e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  60 ERHGD--TFGLF-------LGPSYSVMLFNPRDvervlgsSQLltkSQE--YSFLGRWLNEGLLVSN---GRKWHRrrKI 125
Cdd:cd11042    3 KKYGDvfTFNLLgkkvtvlLGPEANEFFFNGKD-------EDL---SAEevYGFLTPPFGGGVVYYApfaEQKEQL--KF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 126 ITPAFHFRILEPYVEIFDRQSLRLVEELalrisrGQERI-----NLGEAIHLCAldaiCETAMGVSINaqSNADSEYVQa 200
Cdd:cd11042   71 GLNILRRGKLRGYVPLIVEEVEKYFAKW------GESGEvdlfeEMSELTILTA----SRCLLGKEVR--ELLDDEFAQ- 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 201 vktismvLHKRM---FNILYRFDLtYMLTPLARAEKKALNVLHQFTEKIIVQRREeliregsSQESSNDDadvgakrkma 277
Cdd:cd11042  138 -------LYHDLdggFTPIAFFFP-PLPLPSFRRRDRARAKLKEIFSEIIQKRRK-------SPDKDEDD---------- 192
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 278 FLDILLQSTV-DERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStPVSYELLNQ 356
Cdd:cd11042  193 MLQTLMDAKYkDGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDD-PLTYDVLKE 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 357 LHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGK--LIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAE-KLN 433
Cdd:cd11042  272 MPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGgyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDsKGG 351
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808351875 434 PYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDfVGDSSEPPVLIAELILRTKEPLMFKVR 499
Cdd:cd11042  352 KFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFE-LVDSPFPEPDYTTMVVWPKGPARVRYK 416
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
57-472 5.00e-48

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: 171.69  E-value: 5.00e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  57 ELAERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQeYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILE 136
Cdd:cd20642    6 HTVKTYGKNSFTWFGPIPRVIIMDPELIKEVLNKVYDFQKPK-TNPLTKLLATGLASYEGDKWAKHRKIINPAFHLEKLK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 137 PYVEIFDRQSLRLVEELALRIS-RGQERINLGEAIHLCALDAICETAMGvsinaqsnadSEYVQAvKTISMVLHKRMFNI 215
Cdd:cd20642   85 NMLPAFYLSCSEMISKWEKLVSsKGSCELDVWPELQNLTSDVISRTAFG----------SSYEEG-KKIFELQKEQGELI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 216 LYRFDLTYM----LTPLARAEK-KALNVLHQFTEKIIVQRREELIREGssqESSNDDadvgakrkmaFLDILLQSTVDER 290
Cdd:cd20642  154 IQALRKVYIpgwrFLPTKRNRRmKEIEKEIRSSLRGIINKREKAMKAG---EATNDD----------LLGILLESNHKEI 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 291 P--------LSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTpvsYELLNQLHYVDL 362
Cdd:cd20642  221 KeqgnknggMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPD---FEGLNHLKVVTM 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 363 CVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSE-PNIFKPERF-DVVTTAEKlNPYAYIPF 440
Cdd:cd20642  298 ILYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERFaEGISKATK-GQVSYFPF 376
                        410       420       430
                 ....*....|....*....|....*....|..
gi 808351875 441 SAGPRNCIGQKFAMLEIKAIVANVLRHYEVDF 472
Cdd:cd20642  377 GWGPRICIGQNFALLEAKMALALILQRFSFEL 408
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
79-477 2.87e-47

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: 2.87e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  79 FN-PRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHR-RRKIITPAFH-----FRILEPYVeifdRQSLRLVE 151
Cdd:cd11059   13 VNdLDAVREIYGGGFGKTKSYWYFTLRGGGGPNLFSTLDPKEHSaRRRLLSGVYSkssllRAAMEPII----RERVLPLI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 152 ELALRISRGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVktismvlhkrmFNILYRFDLTYMLTPLARA 231
Cdd:cd11059   89 DRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSRERE-----------LLRRLLASLAPWLRWLPRY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 232 ekkaLNVLHQFTEKIIVQRREELIRE---GSSQESSNDDADVGAKRKMAFLDILLQSTVDERPLSNLDIREEVDTFMFEG 308
Cdd:cd11059  158 ----LPLATSRLIIGIYFRAFDEIEEwalDLCARAESSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAG 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 309 HDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPvSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLED--CE 386
Cdd:cd11059  234 HDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPP-DLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEggAT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 387 INGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPY-AYIPFSAGPRNCIGQKFAMLEIKAIVANVL 465
Cdd:cd11059  313 IGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMKrAFWPFGSGSRMCIGMNLALMEMKLALAAIY 392
                        410
                 ....*....|..
gi 808351875 466 RHYEVDFVGDSS 477
Cdd:cd11059  393 RNYRTSTTTDDD 404
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
57-470 3.47e-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: 168.65  E-value: 3.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  57 ELAERHGD-TFGLFLGPSYsVMLFNPRDVERVLGS-SQLLTKSQEYS-FLGRWLNEGLLVSNGRKwHR-RRKIITPAFHF 132
Cdd:cd11045    5 QRYRRYGPvSWTGMLGLRV-VALLGPDANQLVLRNrDKAFSSKQGWDpVIGPFFHRGLMLLDFDE-HRaHRRIMQQAFTR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 133 RILEPYVEIFDRQSLRLVEELalrisRGQERINLGEAIHLCALDAICETAMGVSINAQSN----ADSEYVQAvkTISMVl 208
Cdd:cd11045   83 SALAGYLDRMTPGIERALARW-----PTGAGFQFYPAIKELTLDLATRVFLGVDLGPEADkvnkAFIDTVRA--STAII- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 209 hkrmfnilyRFDLTYmlTPLARAeKKALNVLHQFTEKIIVQRREeliregssqeSSNDDadvgakrkmaFLDILLQSTV- 287
Cdd:cd11045  155 ---------RTPIPG--TRWWRG-LRGRRYLEEYFRRRIPERRA----------GGGDD----------LFSALCRAEDe 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 288 DERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVvGNDkstPVSYELLNQLHYVDLCVKET 367
Cdd:cd11045  203 DGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL-GKG---TLDYEDLGQLEVTDWVFKEA 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 368 LRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNC 447
Cdd:cd11045  279 LRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYAWAPFGGGAHKC 358
                        410       420
                 ....*....|....*....|...
gi 808351875 448 IGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd11045  359 IGLHFAGMEVKAILHQMLRRFRW 381
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
110-499 1.79e-46

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: 167.11  E-value: 1.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 110 GLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELALRISRGqERINLGEAIHLCALDAICETAMGVSINA 189
Cdd:cd11083   50 GVFSAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWERAAAEG-EAVDVHKDLMRYTVDVTTSLAFGYDLNT 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 190 QSNADSEYVQAVKTISMVLHKRMfniLYRFDL-TYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNDda 268
Cdd:cd11083  129 LERGGDPLQEHLERVFPMLNRRV---NAPFPYwRYLRLPADRALDRALVEVRALVLDIIAAARARLAANPALAEAPET-- 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 269 dvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKsTP 348
Cdd:cd11083  204 ---------LLAMMLAEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGAR-VP 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 349 VSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-DVVT 427
Cdd:cd11083  274 PLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWlDGAR 353
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808351875 428 TAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPpvliAELILRTKEPLMFKVR 499
Cdd:cd11083  354 AAEPHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPAPAV----GEEFAFTMSPEGLRVR 421
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
120-495 3.14e-45

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 163.52  E-value: 3.14e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 120 HRR-RKIITPAFHFRIL---EPyveIFDRQSLRLVEELALRISRGQErINLGEAIHLCALDAICETAMGVSINA-QSNAD 194
Cdd:cd11058   58 HARlRRLLAHAFSEKALreqEP---IIQRYVDLLVSRLRERAGSGTP-VDMVKWFNFTTFDIIGDLAFGESFGClENGEY 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 195 SEYVQAV-KTISMVLHKRMFNILYRFDLTYMLTPLARAEKKALNVLHQFTEKiiVQRReeliregssQESSNDDADvgak 273
Cdd:cd11058  134 HPWVALIfDSIKALTIIQALRRYPWLLRLLRLLIPKSLRKKRKEHFQYTREK--VDRR---------LAKGTDRPD---- 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 274 rkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKS-TPVSye 352
Cdd:cd11058  199 ----FMSYILRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDiTLDS-- 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 353 lLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCE-INGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvvttae 430
Cdd:cd11058  273 -LAQLPYLNAVIQEALRLYPPVPAgLPRVVPAGGAtIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERW------- 344
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 431 kLNPY----------AYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPLM 495
Cdd:cd11058  345 -LGDPrfefdndkkeAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESEDWLDQQKVYILWEKPPLM 418
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
110-470 4.77e-44

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: 160.81  E-value: 4.77e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 110 GLLVSNG--RKWHRRRKIITPAFHFRILEPYveiFDRQsLRLVEELALRISR--GQERINLGEAIHLCALDAICETAMGV 185
Cdd:cd11068   61 GLFTAYThePNWGKAHRILMPAFGPLAMRGY---FPMM-LDIAEQLVLKWERlgPDEPIDVPDDMTRLTLDTIALCGFGY 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 186 SINAQSNADS-----EYVQAVKTISMVLHKRMFnilyrfdLTYMLTPLARAEKKALNVLHQFTEKIIVQRReeliregSS 260
Cdd:cd11068  137 RFNSFYRDEPhpfveAMVRALTEAGRRANRPPI-------LNKLRRRAKRQFREDIALMRDLVDEIIAERR-------AN 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 261 QESSNDDadvgakrkmaFLDILLqSTVDE---RPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEI 337
Cdd:cd11068  203 PDGSPDD----------LLNLML-NGKDPetgEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEV 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 338 RSVVGNDkstPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGK-LIPAGTNIGISPLYLGRREELFSE-P 415
Cdd:cd11068  272 DEVLGDD---PPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGKyPLKKGDPVLVLLPALHRDPSVWGEdA 348
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 416 NIFKPERFDVVtTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd11068  349 EEFRPERFLPE-EFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDF 402
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
107-495 1.06e-43

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: 160.39  E-value: 1.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 107 LNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELalrisrgQERINLGEA--IHLC----ALDAICE 180
Cdd:cd20649   48 MSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNL-------KSYAESGNAfnIQRCygcfTMDVVAS 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 181 TAMGVSINAQSNADSEYVQAVKT-ISMVLHKRMFNILYRFdlTYMLTPLAR----AEKKALN-VLHQFTEKIIV------ 248
Cdd:cd20649  121 VAFGTQVDSQKNPDDPFVKNCKRfFEFSFFRPILILFLAF--PFIMIPLARilpnKSRDELNsFFTQCIRNMIAfrdqqs 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 249 --QRREELIREGSSQESSND-----------DADVGAKRKMAFLDILLQ--STVDERPLSNLDIREEVDTFMFEGHDTTS 313
Cdd:cd20649  199 peERRRDFLQLMLDARTSAKflsvehfdivnDADESAYDGHPNSPANEQtkPSKQKRMLTEDEIVGQAFIFLIAGYETTT 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 314 SALMFFFYNIATHPEAQKKCFEEIRsvVGNDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIP 393
Cdd:cd20649  279 NTLSFATYLLATHPECQKKLLREVD--EFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIP 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 394 AGTNIGISPLYLGRREELFSEPNIFKPERFdvvtTAE---KLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20649  357 AGAVLEIPVGFLHHDPEHWPEPEKFIPERF----TAEakqRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRF 432
                        410       420
                 ....*....|....*....|....*
gi 808351875 471 DFVGDSSEPPVLIAELILRTKEPLM 495
Cdd:cd20649  433 QACPETEIPLQLKSKSTLGPKNGVY 457
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
61-469 4.62e-43

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: 158.00  E-value: 4.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWL-NEGLLVSNGRKWHRRRKIITPAFHFRILEPYV 139
Cdd:cd20639   10 IYGKTFLYWFGPTPRLTVADPELIREILLTRADHFDRYEAHPLVRQLeGDGLVSLRGEKWAHHRRVITPAFHMENLKRLV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 140 EIFDRQSLRLVEEL-ALRISRGQERINLGEAIHLCALDAICETAMGvsinaQSNADSEYVQAVKTISMVL----HKRMFN 214
Cdd:cd20639   90 PHVVKSVADMLDKWeAMAEAGGEGEVDVAEWFQNLTEDVISRTAFG-----SSYEDGKAVFRLQAQQMLLaaeaFRKVYI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 215 ILYRFDLTYMLTPLARAEKKALNVLHQFTEkiivqRREELIREGSSQESSNDdadvgakrkmaFLDILLQSTVD--ERPL 292
Cdd:cd20639  165 PGYRFLPTKKNRKSWRLDKEIRKSLLKLIE-----RRQTAADDEKDDEDSKD-----------LLGLMISAKNArnGEKM 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 293 SNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDkSTPvSYELLNQLHYVDLCVKETLRMYP 372
Cdd:cd20639  229 TVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKG-DVP-TKDHLPKLKTLGMILNETLRLYP 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 373 SVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFS-EPNIFKPERF-DVVTTAEKlNPYAYIPFSAGPRNCIGQ 450
Cdd:cd20639  307 PAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWGnDAAEFNPARFaDGVARAAK-HPLAFIPFGLGPRTCVGQ 385
                        410
                 ....*....|....*....
gi 808351875 451 KFAMLEIKAIVANVLRHYE 469
Cdd:cd20639  386 NLAILEAKLTLAVILQRFE 404
PLN02936 PLN02936
epsilon-ring hydroxylase
110-501 2.39e-42

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 157.26  E-value: 2.39e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 110 GLLVSNGRKWHRRRKIITPAFHFRILEPYVE-IFDRQSLRLVEELALRISRGqERINLGEAIHLCALDAIcetamGVSI- 187
Cdd:PLN02936  98 GFAIAEGELWTARRRAVVPSLHRRYLSVMVDrVFCKCAERLVEKLEPVALSG-EAVNMEAKFSQLTLDVI-----GLSVf 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 188 --NAQS-NADSEYVQAVKTISMVLHKRMFNIL--YRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQE 262
Cdd:PLN02936 172 nyNFDSlTTDSPVIQAVYTALKEAETRSTDLLpyWKVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIE 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 263 SSN--DDADVgakrkmAFLDILLQStvdERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSV 340
Cdd:PLN02936 252 GEEyvNDSDP------SVLRFLLAS---REEVSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRV 322
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 341 VGNdksTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRK-VLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFK 419
Cdd:PLN02936 323 LQG---RPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRaQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFV 399
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 420 PERFDVVTTA--EKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDssEPPVLIAELILRTKEPLMFK 497
Cdd:PLN02936 400 PERFDLDGPVpnETNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPD--QDIVMTTGATIHTTNGLYMT 477

                 ....
gi 808351875 498 VRER 501
Cdd:PLN02936 478 VSRR 481
PLN02290 PLN02290
cytokinin trans-hydroxylase
102-491 3.00e-42

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 157.67  E-value: 3.00e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 102 FLGRwlneGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELALRISRGQERINLGEAIHLCALDAICET 181
Cdd:PLN02290 139 FIGR----GLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQTEVEIGEYMTRLTADIISRT 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 182 AMGVSINAQsnadseyvqavktismvlhKRMFNILYRFD-LTYMLT-----PLAR-------AEKKALNVLHQFTEKIIV 248
Cdd:PLN02290 215 EFDSSYEKG-------------------KQIFHLLTVLQrLCAQATrhlcfPGSRffpskynREIKSLKGEVERLLMEII 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 249 QRREELIREGSSQESSNDdadvgakrkmaFLDILLQSTVDERPLS-NLD---IREEVDTFMFEGHDTTSSALMFFFYNIA 324
Cdd:PLN02290 276 QSRRDCVEIGRSSSYGDD-----------LLGMLLNEMEKKRSNGfNLNlqlIMDECKTFFFAGHETTALLLTWTLMLLA 344
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 325 THPEAQKKCFEEIRSVVGNDkstPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLY 404
Cdd:PLN02290 345 SNPTWQDKVRAEVAEVCGGE---TPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPKGLSIWIPVLA 421
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 405 LGRREELFSE-PNIFKPERFdvvttAEKLNPYA--YIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPV 481
Cdd:PLN02290 422 IHHSEELWGKdANEFNPDRF-----AGRPFAPGrhFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNYRHAPV 496
                        410
                 ....*....|
gi 808351875 482 LIaeLILRTK 491
Cdd:PLN02290 497 VV--LTIKPK 504
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
120-478 2.66e-41

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: 153.18  E-value: 2.66e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 120 HR-RRKIITPAF---HFRILEPYVeifdrqsLRLVEELALRI---SRGQERINLGEAIHLCALDAICETAMGVSINAQSN 192
Cdd:cd11062   55 HRlRRKALSPFFskrSILRLEPLI-------QEKVDKLVSRLreaKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDE 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 193 AD--SEYVQAVKTISMVLH-KRMFNILyrFDLTYMLtPLARAEKKALNVLHQFTekiIVQRREELIREGSSQESSNDDAD 269
Cdd:cd11062  128 PDfgPEFLDALRALAEMIHlLRHFPWL--LKLLRSL-PESLLKRLNPGLAVFLD---FQESIAKQVDEVLRQVSAGDPPS 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 270 vgakRKMAFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGnDKSTPV 349
Cdd:cd11062  202 ----IVTSLFHALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMP-DPDSPP 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 350 SYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVL-EDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVT 427
Cdd:cd11062  277 SLAELEKLPYLTAVIKEGLRLSYGVPTrLPRVVPdEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAA 356
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808351875 428 TAEKLNPYaYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSE 478
Cdd:cd11062  357 EKGKLDRY-LVPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYETTEE 406
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
69-471 1.10e-40

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: 150.87  E-value: 1.10e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  69 FLGPSysVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNEGLLVS-NGRKWHRRRKIITPAF---HFRILEPY----VE 140
Cdd:cd11051    8 FAPPL--LVVTDPELAEQITQVTNLPKPPPLRKFLTPLTGGSSLISmEGEEWKRLRKRFNPGFspqHLMTLVPTildeVE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 141 IFdrqsLRLVEELALRisrgqerinlGEAIHLCAL------DAICETAMGVSINAQSNADSEYVQAVKTISMVLHkrMFN 214
Cdd:cd11051   86 IF----AAILRELAES----------GEVFSLEELttnltfDVIGRVTLDIDLHAQTGDNSLLTALRLLLALYRS--LLN 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 215 ILYRFdltymltplaraekkalnvlhqFTEKIIVQRREEliregssqessnddadvgakRKMaflDILLQSTVDERPLSN 294
Cdd:cd11051  150 PFKRL----------------------NPLRPLRRWRNG--------------------RRL---DRYLKPEVRKRFELE 184
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 295 LDIREeVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKST-----PVSYELLNQLHYVDLCVKETLR 369
Cdd:cd11051  185 RAIDQ-IKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPSAaaellREGPELLNQLPYTTAVIKETLR 263
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 370 MYP----------SVPLLGRkvledceiNGKLIP-AGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNP--YA 436
Cdd:cd11051  264 LFPpagtarrgppGVGLTDR--------DGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERW-LVDEGHELYPpkSA 334
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 808351875 437 YIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVD 471
Cdd:cd11051  335 WRPFERGPRNCIGQELAMLELKIILAMTVRRFDFE 369
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
60-468 4.09e-40

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 149.91  E-value: 4.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  60 ERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLT-KSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILE-- 136
Cdd:cd20641    9 SQYGETFLYWQGTTPRICISDHELAKQVLSDKFGFFgKSKARPEILKLSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKsm 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 137 --PYVEIFDRQSLRLVEELALRISRGQErINLGEAIHLCALDAICETAMGvsinaqsnadSEYVQAVKTI-SMVLHKRMF 213
Cdd:cd20641   89 tqVMADCTERMFQEWRKQRNNSETERIE-VEVSREFQDLTADIIATTAFG----------SSYAEGIEVFlSQLELQKCA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 214 ----NILYRFDLTYMLTP----LARAEKKALNVLhqfteKIIVQRReeLIREGSSQessNDDadvgakrkmaFLDILL-- 283
Cdd:cd20641  158 aaslTNLYIPGTQYLPTPrnlrVWKLEKKVRNSI-----KRIIDSR--LTSEGKGY---GDD----------LLGLMLea 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 284 -----QSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLH 358
Cdd:cd20641  218 assneGGRRTERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDK--IPDADTLSKLK 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELF-SEPNIFKPERF-DVVTTAEKlNPYA 436
Cdd:cd20641  296 LMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFaNGVSRAAT-HPNA 374
                        410       420       430
                 ....*....|....*....|....*....|..
gi 808351875 437 YIPFSAGPRNCIGQKFAMLEIKAIVANVLRHY 468
Cdd:cd20641  375 LLSFSLGPRACIGQNFAMIEAKTVLAMILQRF 406
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
88-470 1.01e-39

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: 148.71  E-value: 1.01e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  88 LGSSQLLTKSQEySFLGRwlneGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELALRISRGQER---I 164
Cdd:cd20640   44 LGKPSYLKKTLK-PLFGG----GILTSNGPHWAHQRKIIAPEFFLDKVKGMVDLMVDSAQPLLSSWEERIDRAGGMaadI 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 165 NLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVKTISmvlhKRmfNILYRFDltyMLTPLARAEKKALNVLHQFTE 244
Cdd:cd20640  119 VVDEDLRAFSADVISRACFGSSYSKGKEIFSKLRELQKAVS----KQ--SVLFSIP---GLRHLPTKSNRKIWELEGEIR 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 245 KIIVqrreELIREGSSQESSNDDadvgakrkmaFLDILLQSTVDERplsnlDIREEVDTFM--------FEGHDTTSSAL 316
Cdd:cd20640  190 SLIL----EIVKEREEECDHEKD----------LLQAILEGARSSC-----DKKAEAEDFIvdnckniyFAGHETTAVTA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 317 MFFFYNIATHPEAQKKCFEEIRSVVGNDkstPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGT 396
Cdd:cd20640  251 AWCLMLLALHPEWQDRVRAEVLEVCKGG---PPDADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGV 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 397 NIGISPLYLGRREELF-SEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20640  328 NIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSF 402
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
81-475 1.46e-37

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: 142.32  E-value: 1.46e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  81 PRDVERVLGSSQLLTKSQEYsflgrwlnegllvsngrkwHR--RRKIITPAFHFRILEPYVEIFDRQSLRLVEELAlris 158
Cdd:cd11043   43 PKSVRKLLGKSSLLTVSGEE-------------------HKrlRGLLLSFLGPEALKDRLLGDIDELVRQHLDSWW---- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 159 rGQERINLGEAIHLCALDAICETAMGVSinaqsnaDSEYVQAVKTISMVLHKRMFnilyRFDLTYMLTPLARAeKKALNV 238
Cdd:cd11043  100 -RGKSVVVLELAKKMTFELICKLLLGID-------PEEVVEELRKEFQAFLEGLL----SFPLNLPGTTFHRA-LKARKR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 239 LHQFTEKIIVQRREELiregsSQESSNDDadvgakrkmaFLDILLQST-VDERPLSNLDIREEVDTFMFEGHDTTSSALM 317
Cdd:cd11043  167 IRKELKKIIEERRAEL-----EKASPKGD----------LLDVLLEEKdEDGDSLTDEEILDNILTLLFAGHETTSTTLT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 318 FFFYNIATHPEAQKKCFEE---IRSvvGNDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPA 394
Cdd:cd11043  232 LAVKFLAENPKVLQELLEEheeIAK--RKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPK 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 395 GTNIGISPLYLGRREELFSEPNIFKPERFDVvttAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVG 474
Cdd:cd11043  310 GWKVLWSARATHLDPEYFPDPLKFNPWRWEG---KGKGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVP 386

                 .
gi 808351875 475 D 475
Cdd:cd11043  387 D 387
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
111-465 9.10e-36

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: 137.71  E-value: 9.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 111 LLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELALRISrgqeriNLGEAIHLCALDAICETAMGVSInaq 190
Cdd:cd11065   54 LLMPYGPRWRLHRRLFHQLLNPSAVRKYRPLQELESKQLLRDLLESPD------DFLDHIRRYAASIILRLAYGYRV--- 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 191 SNADSEYVQAVKTISMVLHKRMFNILYRFD----LTYMLTPLARAEKKALNVLHQFTEKIIVQRRE---ELIREGSSQES 263
Cdd:cd11065  125 PSYDDPLLRDAEEAMEGFSEAGSPGAYLVDffpfLRYLPSWLGAPWKRKARELRELTRRLYEGPFEaakERMASGTATPS 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 264 snddadvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGN 343
Cdd:cd11065  205 --------------FVKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGP 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 344 DKSTpvSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIgISPLY-LGRREELFSEPNIFKPE 421
Cdd:cd11065  271 DRLP--TFEDRPNLPYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKGTTV-IPNAWaIHHDPEVYPDPEEFDPE 347
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 808351875 422 RF----DVVTTAEKLNPYAyipFSAGPRNCIGQKFAMLEIKAIVANVL 465
Cdd:cd11065  348 RYlddpKGTPDPPDPPHFA---FGFGRRICPGRHLAENSLFIAIARLL 392
PLN02738 PLN02738
carotene beta-ring hydroxylase
57-502 1.76e-35

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 140.05  E-value: 1.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  57 ELAERHGDTFGLFLGPSYSVMLFNPRDVERVL-GSSQLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRIL 135
Cdd:PLN02738 159 ELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILrDNSKAYSKGILAEILEFVMGKGLIPADGEIWRVRRRAIVPALHQKYV 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 136 EPYVEIFDRQSLRLVEELALRISRGQErINLGEAIHLCALDAICETAMGVSINAQSNaDSEYVQAVKTISMVLHKRMFNI 215
Cdd:PLN02738 239 AAMISLFGQASDRLCQKLDAAASDGED-VEMESLFSRLTLDIIGKAVFNYDFDSLSN-DTGIVEAVYTVLREAEDRSVSP 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 216 LYRFDLTYM--LTPLARAEKKALNVLHQFTEKII-VQRReeLIREGSSQ---ESSNDdadvgakRKMAFLDILLQSTVDe 289
Cdd:PLN02738 317 IPVWEIPIWkdISPRQRKVAEALKLINDTLDDLIaICKR--MVEEEELQfheEYMNE-------RDPSILHFLLASGDD- 386
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 290 rpLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTpvsYELLNQLHYVDLCVKETLR 369
Cdd:PLN02738 387 --VSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPT---IEDMKKLKYTTRVINESLR 461
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 370 MYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF--DVVTTAEKLNPYAYIPFSAGPRNC 447
Cdd:PLN02738 462 LYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWplDGPNPNETNQNFSYLPFGGGPRKC 541
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808351875 448 IGQKFAMLEIKAIVANVLRHYevDFVGDSSEPPV-LIAELILRTKEPLMFKVRERV 502
Cdd:PLN02738 542 VGDMFASFENVVATAMLVRRF--DFQLAPGAPPVkMTTGATIHTTEGLKMTVTRRT 595
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
80-473 4.48e-34

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 134.52  E-value: 4.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  80 NPRDVERVLGSS-QLLTKSQEY-SFLGRWLNEGLLVSNGRKWHRRRKiiTPAFHF--RILEPY-VEIFDRQSLRLVEELA 154
Cdd:PLN03195  82 DPVNVEHVLKTNfANYPKGEVYhSYMEVLLGDGIFNVDGELWRKQRK--TASFEFasKNLRDFsTVVFREYSLKLSSILS 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 155 lRISRGQERINLGEAIHLCALDAICETAMGVSIN--AQSNADSEYVQAVKTISMVLHKRMFNILYRFDLTYMLTPLARAE 232
Cdd:PLN03195 160 -QASFANQVVDMQDLFMRMTLDSICKVGFGVEIGtlSPSLPENPFAQAFDTANIIVTLRFIDPLWKLKKFLNIGSEALLS 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 233 KkALNVLHQFTEKIIVQRREELiregssQESSNDDADVGAKRKMAFLDIllqstvDERPLSNLD---IREEVDTFMFEGH 309
Cdd:PLN03195 239 K-SIKVVDDFTYSVIRRRKAEM------DEARKSGKKVKHDILSRFIEL------GEDPDSNFTdksLRDIVLNFVIAGR 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 310 DTTSSALMFFFYNIATHPEAQKKCFEEIRSV---------VGNDKS---------TPVSYELLNQLHYVDLCVKETLRMY 371
Cdd:PLN03195 306 DTTATTLSWFVYMIMMNPHVAEKLYSELKALekerakeedPEDSQSfnqrvtqfaGLLTYDSLGKLQYLHAVITETLRLY 385
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 372 PSVPLLGRKVLEDCEI-NGKLIPAGTNIGISPLYLGRREELF-SEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIG 449
Cdd:PLN03195 386 PAVPQDPKGILEDDVLpDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLG 465
                        410       420
                 ....*....|....*....|....
gi 808351875 450 QKFAMLEIKAIVANVLRHYEVDFV 473
Cdd:PLN03195 466 KDSAYLQMKMALALLCRFFKFQLV 489
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
114-469 4.60e-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: 133.06  E-value: 4.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 114 SNGRKWHRRRKIITpafhfrilepyVEIFDRQSLRL-----VEELA------LRISRGQERINLGEAIHLCALDAICETA 182
Cdd:cd20618   56 PYGPHWRHLRKICT-----------LELFSAKRLESfqgvrKEELShlvkslLEESESGKPVNLREHLSDLTLNNITRML 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 183 MGVSINAQSNADSEYVQAVKTI---SMVLHKRmFNI------LYRFDLTymltPLARAEKKALNVLHQFTEKIIVQRREE 253
Cdd:cd20618  125 FGKRYFGESEKESEEAREFKELideAFELAGA-FNIgdyipwLRWLDLQ----GYEKRMKKLHAKLDRFLQKIIEEHREK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 254 liREGSSQESSNDDadvgakrkmaFLDILLQSTvDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKC 333
Cdd:cd20618  200 --RGESKKGGDDDD----------DLLLLLDLD-GEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKA 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 334 FEEIRSVVGNDKstPVSYELLNQLHYVDLCVKETLRMYPSVPLLG-RKVLEDCEINGKLIPAGTNIGISpLY-LGRREEL 411
Cdd:cd20618  267 QEELDSVVGRER--LVEESDLPKLPYLQAVVKETLRLHPPGPLLLpHESTEDCKVAGYDIPAGTRVLVN-VWaIGRDPKV 343
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808351875 412 FSEPNIFKPERF-----DVVttaeKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:cd20618  344 WEDPLEFKPERFlesdiDDV----KGQDFELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFD 402
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
71-478 2.57e-33

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: 130.48  E-value: 2.57e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  71 GPSYSVMLFNPRDVERVLGSSQLLTKSQEYS---FLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSL 147
Cdd:cd20615    9 GPTPEIVLTTPEHVKEFYRDSNKHHKAPNNNsgwLFGQLLGQCVGLLSGTDWKRVRKVFDPAFSHSAAVYYIPQFSREAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 148 RLVEELALRISRGQE-RINLGEAIHLCALDAICETAMGvsinaqsNADSEYVQAVKTISM----VLHKRMFNILYRFDLT 222
Cdd:cd20615   89 KWVQNLPTNSGDGRRfVIDPAQALKFLPFRVIAEILYG-------ELSPEEKEELWDLAPlreeLFKYVIKGGLYRFKIS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 223 YMLTplaRAEKKALNVLHQ----FTEKIIVQRREeliregSSQESSNDDADVGAKRKMAFLDILLQsTVDERPLSNLDIr 298
Cdd:cd20615  162 RYLP---TAANRRLREFQTrwraFNLKIYNRARQ------RGQSTPIVKLYEAVEKGDITFEELLQ-TLDEMLFANLDV- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 299 eevdtfmfeghdtTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYELLNQ--LHYvdlCVKETLRMYP---- 372
Cdd:cd20615  231 -------------TTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILSTDtlLAY---CVLESLRLRPllaf 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 373 SVPllgRKVLEDCEINGKLIPAGTNIGISPLYLGRREELF-SEPNIFKPERFDVVTTAEKLnpYAYIPFSAGPRNCIGQK 451
Cdd:cd20615  295 SVP---ESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWgPDGEAYRPERFLGISPTDLR--YNFWRFGFGPRKCLGQH 369
                        410       420
                 ....*....|....*....|....*....
gi 808351875 452 FAMLEIKAIVANVLRHYEVDFV--GDSSE 478
Cdd:cd20615  370 VADVILKALLAHLLEQYELKLPdqGENEE 398
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
145-468 1.33e-32

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: 129.12  E-value: 1.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 145 QSLRLV--EELALRI------SRGQERINLGEAIHLCALDAICETAMGVSINAQSNadSEYVQAVKTISMVLHKrmFNIL 216
Cdd:cd11072   81 QSFRSIreEEVSLLVkkiresASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQ--DKFKELVKEALELLGG--FSVG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 217 YRF---DLTYMLTPLARAEKKALNVLHQFTEKIIVQRREElireGSSQESSNDDADVgakrkmaFLDILLQSTVDERPLS 293
Cdd:cd11072  157 DYFpslGWIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDK----KRSKDEDDDDDDL-------LDLRLQKEGDLEFPLT 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 294 NLDIREEV-DtfMFE-GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMY 371
Cdd:cd11072  226 RDNIKAIIlD--MFLaGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGK--VTEEDLEKLKYLKAVIKETLRLH 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 372 PSVPLLG-RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQ 450
Cdd:cd11072  302 PPAPLLLpRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDFKGQDFELIPFGAGRRICPGI 381
                        330
                 ....*....|....*...
gi 808351875 451 KFAMLEIKAIVANVLRHY 468
Cdd:cd11072  382 TFGLANVELALANLLYHF 399
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
144-462 4.21e-32

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: 127.71  E-value: 4.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 144 RQSLRLVEELALRISRGQERINLG-EAIHLcALDAICETAMGVSINaQSNADSEYVQAVKTISMVLHKrMFNI------L 216
Cdd:cd20655   86 AQELERFLRRLLDKAEKGESVDIGkELMKL-TNNIICRMIMGRSCS-EENGEAEEVRKLVKESAELAG-KFNAsdfiwpL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 217 YRFDLTYMltplaraEKKALNVLHQF---TEKIIVQRREEliREGSSQESSNDdadvgakrkmaFLDILLQSTVDErpls 293
Cdd:cd20655  163 KKLDLQGF-------GKRIMDVSNRFdelLERIIKEHEEK--RKKRKEGGSKD-----------LLDILLDAYEDE---- 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 294 NLDI---REEVDTFMFE----GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSyELLNqLHYVDLCVKE 366
Cdd:cd20655  219 NAEYkitRNHIKAFILDlfiaGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQES-DLPN-LPYLQAVVKE 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 367 TLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-DVVTTAEKLNP----YAYIPFS 441
Cdd:cd20655  297 TLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFlASSRSGQELDVrgqhFKLLPFG 376
                        330       340
                 ....*....|....*....|.
gi 808351875 442 AGPRNCIGQKFAMLEIKAIVA 462
Cdd:cd20655  377 SGRRGCPGASLAYQVVGTAIA 397
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
71-480 4.77e-32

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: 127.33  E-value: 4.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  71 GPSYSVMLFNPRDVerVLGSSQ-----LLTKSQEYSflGR-WLNEGLLVSNGRK----------WHRRRKIITPAFHFri 134
Cdd:cd11027    2 GDVFSLYLGSRLVV--VLNSGAaikeaLVKKSADFA--GRpKLFTFDLFSRGGKdiafgdysptWKLHRKLAHSALRL-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 135 lepYVEIFDRQSLRLVEELALRISR-----GQErINLGEAIHLCALDAICETAMGVSInaqSNADSEY---VQAVKTISM 206
Cdd:cd11027   76 ---YASGGPRLEEKIAEEAEKLLKRlasqeGQP-FDPKDELFLAVLNVICSITFGKRY---KLDDPEFlrlLDLNDKFFE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 207 VLHkrMFNILYRFD-LTYMLTPLARAEKKALNVLHQFTEKIIVQRREELiregssQESSNDD-ADvgakrkmAFLDILLQ 284
Cdd:cd11027  149 LLG--AGSLLDIFPfLKYFPNKALRELKELMKERDEILRKKLEEHKETF------DPGNIRDlTD-------ALIKAKKE 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 285 STV----DERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLHYV 360
Cdd:cd11027  214 AEDegdeDSGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDR--LPTLSDRKRLPYL 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 361 DLCVKETLRMYPSVPLLG-RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-----DVVTTaeklnP 434
Cdd:cd11027  292 EATIAEVLRLSSVVPLALpHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFldengKLVPK-----P 366
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 808351875 435 YAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEvdFVGDSSEPP 480
Cdd:cd11027  367 ESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFR--FSPPEGEPP 410
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
59-469 1.92e-30

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


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 123.03  E-value: 1.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  59 AERHGDTFGLFLGPSYSVMLFNPRDVERVLgssqlltKSQEYSFLGRWLNE-----------GLLVSNGRKWHRRRKIIT 127
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVL-------KTHDRVLSGRDVPDavralghhkssIVWPPYGPRWRMLRKICT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 128 pafhfrilepyVEIFDRQSL--------RLVEELALRI---SRGQERINLGEAIHLCALDAICETAMGVSI-NAQSNADS 195
Cdd:cd11073   74 -----------TELFSPKRLdatqplrrRKVRELVRYVrekAGSGEAVDIGRAAFLTSLNLISNTLFSVDLvDPDSESGS 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 196 EYVQAVKTISMVLHK----RMFNILYRFDLTymltPLARAEKKALNVLHQFTEKIIVQRREElireGSSQESSNDDADvg 271
Cdd:cd11073  143 EFKELVREIMELAGKpnvaDFFPFLKFLDLQ----GLRRRMAEHFGKLFDIFDGFIDERLAE----REAGGDKKKDDD-- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 272 akrkmaFLDILLQSTVDERPLSnldiREEVDTFMFE----GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGndKST 347
Cdd:cd11073  213 ------LLLLLDLELDSESELT----RNHIKALLLDlfvaGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIG--KDK 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 348 PVSYELLNQLHYVDLCVKETLRMYPSVPLL-GRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVV 426
Cdd:cd11073  281 IVEESDISKLPYLQAVVKETLRLHPPAPLLlPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGS 360
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 808351875 427 TTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:cd11073  361 EIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLASLLHSFD 403
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
233-502 2.61e-30

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 123.65  E-value: 2.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 233 KKALNVLHQFTEKIIVQRReeliREGSSqeSSNDdadvgakrkmaFLDILLQSTVDERPLsnldiREEVDTFMFEGHDTT 312
Cdd:PLN02426 252 KEAIKLVDELAAEVIRQRR----KLGFS--ASKD-----------LLSRFMASINDDKYL-----RDIVVSFLLAGRDTV 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 313 SSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPvSYELLNQLHYVDLCVKETLRMYPSVPL-----LGRKVLEDcei 387
Cdd:PLN02426 310 ASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAA-SFEEMKEMHYLHAALYESMRLFPPVQFdskfaAEDDVLPD--- 385
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 388 nGKLIPAGTNIGISPLYLGRREELFSePNI--FKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVL 465
Cdd:PLN02426 386 -GTFVAKGTRVTYHPYAMGRMERIWG-PDCleFKPERWLKNGVFVPENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVV 463
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 808351875 466 RHYEVDFVGDSSEPPVLIAELILRTKEPLMFKVRERV 502
Cdd:PLN02426 464 RRFDIEVVGRSNRAPRFAPGLTATVRGGLPVRVRERV 500
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
59-470 2.62e-30

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


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 122.72  E-value: 2.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  59 AERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQL------LTKSQEYSFLgRWLNEGLLVSNGRKWHRRRKIITPafhf 132
Cdd:cd20647    1 TREYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAapqranMESWQEYRDL-RGRSTGLISAEGEQWLKMRSVLRQ---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 133 RILEPY-VEIFDRQSLRLVEELALRI-------SRGQERINLGEAIHLCALDAIC----ETAMGVSINAQSNADSEYVQA 200
Cdd:cd20647   76 KILRPRdVAVYSGGVNEVVADLIKRIktlrsqeDDGETVTNVNDLFFKYSMEGVAtilyECRLGCLENEIPKQTVEYIEA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 201 VKtismvLHKRMFNI-LYRFDLTYMLTPLA----RAEKKALNVLHQFTEkIIVQRReelIREGSSQessnddADVGAKRK 275
Cdd:cd20647  156 LE-----LMFSMFKTtMYAGAIPKWLRPFIpkpwEEFCRSWDGLFKFSQ-IHVDNR---LREIQKQ------MDRGEEVK 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 276 MAFLDILLQStvdeRPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDksTPVSYELLN 355
Cdd:cd20647  221 GGLLTYLLVS----KELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKR--VVPTAEDVP 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 356 QLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPY 435
Cdd:cd20647  295 KLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNF 374
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 808351875 436 AYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20647  375 GSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEI 409
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
215-470 3.68e-30

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: 121.70  E-value: 3.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 215 ILYRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELiregSSQESSNDDADVGAKRkmafldILLQSTVDerpLSN 294
Cdd:cd20616  156 LLIKPDIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRI----STAEKLEDHMDFATEL------IFAQKRGE---LTA 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 295 LDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstpVSYELLNQLHYVDLCVKETLRMYPSV 374
Cdd:cd20616  223 ENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGERD---IQNDDLQKLKVLENFINESMRYQPVV 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 375 PLLGRKVLEDCEINGKLIPAGTNIgisPLYLGR--REELFSEPNIFKPERFdvvttaEKLNPYAYI-PFSAGPRNCIGQK 451
Cdd:cd20616  300 DFVMRKALEDDVIDGYPVKKGTNI---ILNIGRmhRLEFFPKPNEFTLENF------EKNVPSRYFqPFGFGPRSCVGKY 370
                        250
                 ....*....|....*....
gi 808351875 452 FAMLEIKAIVANVLRHYEV 470
Cdd:cd20616  371 IAMVMMKAILVTLLRRFQV 389
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
304-469 9.25e-30

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: 120.81  E-value: 9.25e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 304 FMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLHYVDLCVKETLRMYPSVP-LLGRKVL 382
Cdd:cd11075  239 FLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEA--VVTEEDLPKMPYLKAVVLETLRRHPPGHfLLPHAVT 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 383 EDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF------DVVTTAEKLnpYAYIPFSAGPRNCIGQKFAMLE 456
Cdd:cd11075  317 EDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFlaggeaADIDTGSKE--IKMMPFGAGRRICPGLGLATLH 394
                        170
                 ....*....|...
gi 808351875 457 IKAIVANVLRHYE 469
Cdd:cd11075  395 LELFVARLVQEFE 407
PTZ00404 PTZ00404
cytochrome P450; Provisional
279-468 2.19e-29

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 120.60  E-value: 2.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 279 LDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVG-------NDK-STPvs 350
Cdd:PTZ00404 266 LDLLIKEYGTNTDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNgrnkvllSDRqSTP-- 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 351 yellnqlhYVDLCVKETLRMYPSVPL-LGRKVLEDCEI-NGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvvtt 428
Cdd:PTZ00404 344 --------YTVAIIKETLRYKPVSPFgLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRF----- 410
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 808351875 429 AEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHY 468
Cdd:PTZ00404 411 LNPDSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNF 450
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
116-501 1.48e-28

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: 117.52  E-value: 1.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 116 GRKWHRRRKIItpAFHF---RILEPYVEIFDRQSLRLVEELAlRISRGQERINLGEAIHLCALDAICETAMG-----VSI 187
Cdd:cd20657   58 GPRWRLLRKLC--NLHLfggKALEDWAHVRENEVGHMLKSMA-EASRKGEPVVLGEMLNVCMANMLGRVMLSkrvfaAKA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 188 NAQSNADSEYVQAVKTISMVlhkrmFNI------LYRFDLTYMLTPLARAEKKALNVLHQFTEKiivqrreeliREGSSQ 261
Cdd:cd20657  135 GAKANEFKEMVVELMTVAGV-----FNIgdfipsLAWMDLQGVEKKMKRLHKRFDALLTKILEE----------HKATAQ 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 262 ESsnddadvgaKRKMAFLDILLQSTVD----ERpLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEI 337
Cdd:cd20657  200 ER---------KGKPDFLDFVLLENDDngegER-LTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEM 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 338 RSVVGNDKstPVSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPN 416
Cdd:cd20657  270 DQVIGRDR--RLLESDIPNLPYLQAICKETFRLHPSTPLnLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPL 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 417 IFKPERF--------DVvttaeKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAE--- 485
Cdd:cd20657  348 EFKPERFlpgrnakvDV-----RGNDFELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPAGQTPEELNMEEafg 422
                        410
                 ....*....|....*.
gi 808351875 486 LILRTKEPLMFKVRER 501
Cdd:cd20657  423 LALQKAVPLVAHPTPR 438
PLN02687 PLN02687
flavonoid 3'-monooxygenase
116-502 1.73e-28

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 118.38  E-value: 1.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 116 GRKWHRRRKIIT-PAFHFRILEPYVEIFDRQSLRLVEELALriSRGQERINLGEAIHLCALDAICETAMG---VSINAQS 191
Cdd:PLN02687 124 GPRWRALRKICAvHLFSAKALDDFRHVREEEVALLVRELAR--QHGTAPVNLGQLVNVCTTNALGRAMVGrrvFAGDGDE 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 192 NADsEYVQAVKTIsMVLhKRMFNI------LYRFDLTYMLTPLARAEKKALNVLHQFTEKiivqrreeliREGSSQESSN 265
Cdd:PLN02687 202 KAR-EFKEMVVEL-MQL-AGVFNVgdfvpaLRWLDLQGVVGKMKRLHRRFDAMMNGIIEE----------HKAAGQTGSE 268
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 266 DDADVgakrkmafLDILL------QSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRS 339
Cdd:PLN02687 269 EHKDL--------LSTLLalkreqQADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDA 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 340 VVGNDKstPVSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIF 418
Cdd:PLN02687 341 VVGRDR--LVSESDLPQLTYLQAVIKETFRLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEF 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 419 KPERF---------DVvttaeKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAE---L 486
Cdd:PLN02687 419 RPDRFlpggehagvDV-----KGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTPDKLNMEEaygL 493
                        410
                 ....*....|....*.
gi 808351875 487 ILRTKEPLMFKVRERV 502
Cdd:PLN02687 494 TLQRAVPLMVHPRPRL 509
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
110-470 1.89e-28

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: 117.07  E-value: 1.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 110 GLLVSNGRKWHRRRKIITPafhfRILEP-----YVEIFDRqslrLVEELALRISRGQER-------INLGEAIHLCALDA 177
Cdd:cd20646   57 GPFTEEGEKWYRLRSVLNQ----RMLKPkevslYADAINE----VVSDLMKRIEYLRERsgsgvmvSDLANELYKFAFEG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 178 IC----ETAMGVsinAQSNADSEYVQAVKTISMVLHKRMFNILY-RFDLTYMltPLARAEKKALNVLHQFTEKIIVQRRE 252
Cdd:cd20646  129 ISsilfETRIGC---LEKEIPEETQKFIDSIGEMFKLSEIVTLLpKWTRPYL--PFWKRYVDAWDTIFSFGKKLIDKKME 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 253 EL---IREGSSQESSnddadvgakrkmaFLDILLQSTvderPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEA 329
Cdd:cd20646  204 EIeerVDRGEPVEGE-------------YLTYLLSSG----KLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEI 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 330 QKKCFEEIRSVVGNDKsTPVSyELLNQLHYVDLCVKETLRMYPSVPLLGRKVLE-DCEINGKLIPAGTNIGISPLYLGRR 408
Cdd:cd20646  267 QERLYQEVISVCPGDR-IPTA-EDIAKMPLLKAVIKETLRLYPVVPGNARVIVEkEVVVGDYLFPKNTLFHLCHYAVSHD 344
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808351875 409 EELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20646  345 ETNFPEPERFKPERW-LRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEV 405
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
194-501 2.15e-28

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


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 117.01  E-value: 2.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 194 DSEYVQAVK--TISMVLHKRMFNILYRFD--LTYMLTPLARAEKKALNVLhqftEKIIVQRREELIREGSSQESSNDDaD 269
Cdd:cd11041  134 NEEWLDLTInyTIDVFAAAAALRLFPPFLrpLVAPFLPEPRRLRRLLRRA----RPLIIPEIERRRKLKKGPKEDKPN-D 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 270 vgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStpV 349
Cdd:cd11041  209 --------LLQWLIEAAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGG--W 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 350 SYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEI-NGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF---- 423
Cdd:cd11041  279 TKAALNKLKKLDSFMKESQRLNPLSLVsLRRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFyrlr 358
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 424 ---------DVVTTAEKlnpyaYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVLIAELILRTKEPL 494
Cdd:cd11041  359 eqpgqekkhQFVSTSPD-----FLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERPKNIWFGEFIMPDPNA 433

                 ....*..
gi 808351875 495 MFKVRER 501
Cdd:cd11041  434 KVLVRRR 440
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
63-480 2.61e-27

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: 113.85  E-value: 2.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  63 GDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEYSFLGRWLNE--GLLVSNGRKWHRRRKIITPafHFRIL----E 136
Cdd:cd20651    1 GDVVGLKLGKDKVVVVSGYEAVREVLSREEFDGRPDGFFFRLRTFGKrlGITFTDGPFWKEQRRFVLR--HLRDFgfgrR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 137 PYVEIFDRQSLRLVEELAlriSRGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAV----KTISMV--LHK 210
Cdd:cd20651   79 SMEEVIQEEAEELIDLLK---KGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVhllfRNFDMSggLLN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 211 RMFNILYRFDLTYMLTPLARAEKKalnvLHQFTEKIIVQRREELiregssQESSNDDadvgakrkmaFLDILLQSTVDER 290
Cdd:cd20651  156 QFPWLRFIAPEFSGYNLLVELNQK----LIEFLKEEIKEHKKTY------DEDNPRD----------LIDAYLREMKKKE 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 291 PLSN-----------LDireevdtFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTpvSYELLNQLHY 359
Cdd:cd20651  216 PPSSsftddqlvmicLD-------LFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLP--TLDDRSKLPY 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 360 VDLCVKETLRMYPSVPLLG-RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-DVvtTAEKLNPYAY 437
Cdd:cd20651  287 TEAVILEVLRIFTLVPIGIpHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFlDE--DGKLLKDEWF 364
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 808351875 438 IPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPP 480
Cdd:cd20651  365 LPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDL 407
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
308-471 2.85e-27

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: 113.75  E-value: 2.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 308 GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVgNDKSTPVSyELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEI 387
Cdd:cd20645  238 GVETTANSLLWILYNLSRNPQAQQKLLQEIQSVL-PANQTPRA-EDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVL 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 388 NGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRH 467
Cdd:cd20645  316 GDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERW--LQEKHSINPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQK 393

                 ....
gi 808351875 468 YEVD 471
Cdd:cd20645  394 YQIV 397
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
110-470 6.62e-26

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: 109.84  E-value: 6.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 110 GLLVSNGRKWHRRRKIITPafhfRILEP-----YVEIFDRQSLRLVEELALRISRGQERI--NLGEAIHLCALDAICETA 182
Cdd:cd20648   58 GLLTAEGEEWQRLRSLLAK----HMLKPkaveaYAGVLNAVVTDLIRRLRRQRSRSSPGVvkDIAGEFYKFGLEGISSVL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 183 MGVSI---NAQSNADSE-YVQAVKTI--SMVLHKRMFNILYRFdltyMLTPLARAeKKALNVLHQFTEKIIVQRREELir 256
Cdd:cd20648  134 FESRIgclEANVPEETEtFIQSINTMfvMTLLTMAMPKWLHRL----FPKPWQRF-CRSWDQMFAFAKGHIDRRMAEV-- 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 257 egsSQESSNDDADVGAkrkmaFLDILLQStvDERPLSNldIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEE 336
Cdd:cd20648  207 ---AAKLPRGEAIEGK-----YLTYFLAR--EKLPMKS--IYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHRE 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 337 IRSVVGnDKSTPvSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLE-DCEINGKLIPAGTNIGISPLYLGRREELFSEP 415
Cdd:cd20648  275 ITAALK-DNSVP-SAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDrDIQVGEYIIPKKTLITLCHYATSRDENQFPDP 352
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 416 NIFKPERFdvVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20648  353 NSFRPERW--LGKGDTHHPYASLPFGFGKRSCIGRRIAELEVYLALARILTHFEV 405
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
111-469 1.36e-25

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: 109.70  E-value: 1.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 111 LLVSNGRKWHRRRKII----TPAFHFRILEPyvEIFDRqSLRLVE--ELALRISRGQErINLGEAIHLCALDAICETAMG 184
Cdd:cd20622   54 LVKSTGPAFRKHRSLVqdlmTPSFLHNVAAP--AIHSK-FLDLIDlwEAKARLAKGRP-FSAKEDIHHAALDAIWAFAFG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 185 ---------VSINAQSNADS-------------------EYVQAVKTISMVLHKRM---FNILYRFDLTYMLTPlaraeK 233
Cdd:cd20622  130 infdasqtrPQLELLEAEDStilpagldepvefpeaplpDELEAVLDLADSVEKSIkspFPKLSHWFYRNQPSY-----R 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 234 KALNVLHQFTEKIIVQRREELIREGSSQESSN------DDADVGAKRKMAFLDilLQSTVderplsnldIREEVDTFMFE 307
Cdd:cd20622  205 RAAKIKDDFLQREIQAIARSLERKGDEGEVRSavdhmvRRELAAAEKEGRKPD--YYSQV---------IHDELFGYLIA 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 308 GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSV---VGNDKSTPVSYELLN-QLHYVDLCVKETLRMYPSVPLLGRKVLE 383
Cdd:cd20622  274 GHDTTSTALSWGLKYLTANQDVQSKLRKALYSAhpeAVAEGRLPTAQEIAQaRIPYLDAVIEEILRCANTAPILSREATV 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 384 DCEINGKLIPAGTNIGI---SPLYL------------------GRREELFSEPNI--FKPERF---DVVTTAEKLNPYAY 437
Cdd:cd20622  354 DTQVLGYSIPKGTNVFLlnnGPSYLsppieidesrrssssaakGKKAGVWDSKDIadFDPERWlvtDEETGETVFDPSAG 433
                        410       420       430
                 ....*....|....*....|....*....|....
gi 808351875 438 --IPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:cd20622  434 ptLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFE 467
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
291-457 5.11e-25

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: 106.76  E-value: 5.11e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 291 PLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVvgndKSTPVSYELLNQLHYVDLCVKETLRM 370
Cdd:cd20614  203 GLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA----GDVPRTPAELRRFPLAEALFRETLRL 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 371 YPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvVTTAEKLNPYAYIPFSAGPRNCIGQ 450
Cdd:cd20614  279 HPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERW--LGRDRAPNPVELLQFGGGPHFCLGY 356

                 ....*..
gi 808351875 451 KFAMLEI 457
Cdd:cd20614  357 HVACVEL 363
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
252-470 1.01e-24

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: 106.55  E-value: 1.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 252 EELIREGSSQESSNDDADvgakrkmaFLDILLQSTVDERPLSNLD----IREEVDTFMFEGHDTTSSALMFFFYNIATHP 327
Cdd:cd20654  201 EEHRQKRSSSGKSKNDED--------DDDVMMLSILEDSQISGYDadtvIKATCLELILGGSDTTAVTLTWALSLLLNNP 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 328 EAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSVPLLG-RKVLEDCEINGKLIPAGTNIGISPLYLG 406
Cdd:cd20654  273 HVLKKAQEELDTHVGKDRW--VEESDIKNLVYLQAIVKETLRLYPPGPLLGpREATEDCTVGGYHVPKGTRLLVNVWKIQ 350
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808351875 407 RREELFSEPNIFKPERFdvVTTAEKLN----PYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20654  351 RDPNVWSDPLEFKPERF--LTTHKDIDvrgqNFELIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDI 416
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
61-479 4.23e-24

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: 104.37  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  61 RHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTksqEYSFLGRwLNEGLLVSNGRKWHRRRKIITPAFHFRI------ 134
Cdd:cd11040   10 SGGPIFTIRLGGQKIYVITDPELISAVFRNPKTLS---FDPIVIV-VVGRVFGSPESAKKKEGEPGGKGLIRLLhdlhkk 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 135 -------LEPYVEIFDRQSLRLVEELALRISRGQERINLGEAI--HLCAldAICETAMGVSINAQsnaDSEYVQAVktis 205
Cdd:cd11040   86 alsggegLDRLNEAMLENLSKLLDELSLSGGTSTVEVDLYEWLrdVLTR--ATTEALFGPKLPEL---DPDLVEDF---- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 206 MVLHKRMFNILYRFdltymLTPLARAEKKALNVLHQFTEKIIVQRREELIregssqessnDDADVGAKRkmafLDILLQS 285
Cdd:cd11040  157 WTFDRGLPKLLLGL-----PRLLARKAYAARDRLLKALEKYYQAAREERD----------DGSELIRAR----AKVLREA 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 286 TVDERPLSNLDIreevdTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSY---ELLNQLHYVDL 362
Cdd:cd11040  218 GLSEEDIARAEL-----ALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILdltDLLTSCPLLDS 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 363 CVKETLRMYpSVPLLGRKVLEDC-EINGKLIPAGTNIGISPLYLGRREELF-SEPNIFKPERFDVVTTAEKLN--PYAYI 438
Cdd:cd11040  293 TYLETLRLH-SSSTSVRLVTEDTvLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKKGRglPGAFR 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 808351875 439 PFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEP 479
Cdd:cd11040  372 PFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWK 412
PLN02183 PLN02183
ferulate 5-hydroxylase
116-465 4.28e-24

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 105.32  E-value: 4.28e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 116 GRKWHRRRKI-ITPAFHFRILEPYVEIFDRqslrlVEELALRIS-RGQERINLGEAIHLCALDAICETAMGVSINaqsNA 193
Cdd:PLN02183 126 GPFWRQMRKLcVMKLFSRKRAESWASVRDE-----VDSMVRSVSsNIGKPVNIGELIFTLTRNITYRAAFGSSSN---EG 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 194 DSEYVQAVKTISMVLHKrmFNILYRFDLTYMLTP--LARAEKKALNVLHQFTEKII---VQRREELIREGSSQESSNDDA 268
Cdd:PLN02183 198 QDEFIKILQEFSKLFGA--FNVADFIPWLGWIDPqgLNKRLVKARKSLDGFIDDIIddhIQKRKNQNADNDSEEAETDMV 275
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 269 DvgakRKMAFL--DILLQSTVDER---PLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGN 343
Cdd:PLN02183 276 D----DLLAFYseEAKVNESDDLQnsiKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGL 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 344 DKStpVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF 423
Cdd:PLN02183 352 NRR--VEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRF 429
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 808351875 424 -DVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVL 465
Cdd:PLN02183 430 lKPGVPDFKGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLL 472
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
57-502 4.35e-24

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 105.09  E-value: 4.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  57 ELAERHGDTFgLFLGP--SYSVMLF--NPRDVERVLGSS-QLLTKSQEYSFLGRWLNEGLLVSNGRKWHRRRKIITPAFH 131
Cdd:PLN02169  61 EVLEASNLTF-YFKGPwlSGTDMLFtaDPKNIHHILSSNfGNYPKGPEFKKIFDVLGEGILTVDFELWEDLRKSNHALFH 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 132 FrilEPYVEI-FDRQSLRLVEELALRISRGQER---INLGEAIHLCALD--AICETA---MGVSINAqsnADSEYVQAVK 202
Cdd:PLN02169 140 N---QDFIELsLSSNKSKLKEGLVPFLDNAAHEniiIDLQDVFMRFMFDtsSILMTGydpMSLSIEM---LEVEFGEAAD 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 203 TISMVLHKRMFN--ILYRFDlTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSNDDADVGAKRKMAFLD 280
Cdd:PLN02169 214 IGEEAIYYRHFKpvILWRLQ-NWIGIGLERKMRTALATVNRMFAKIISSRRKEEISRAETEPYSKDALTYYMNVDTSKYK 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 281 ILlqstvdeRPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIrsvvgNDKSTPvsyELLNQLHYV 360
Cdd:PLN02169 293 LL-------KPKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI-----NTKFDN---EDLEKLVYL 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 361 DLCVKETLRMYPSVPLLGRKVLE-DCEINGKLIPAGTNIGISPLYLGRREELFSEPNI-FKPERFDVVTTAEKLNP-YAY 437
Cdd:PLN02169 358 HAALSESMRLYPPLPFNHKAPAKpDVLPSGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWISDNGGLRHEPsYKF 437
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808351875 438 IPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFV-GDSSEPpvlIAELILRTKEPLMFKVRERV 502
Cdd:PLN02169 438 MAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKVIeGHKIEA---IPSILLRMKHGLKVTVTKKI 500
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
123-469 8.19e-24

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: 103.48  E-value: 8.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 123 RKIITPAFHFRILEPYVEIFDRqSLRlvEELALRISRGQERINLGEAIHLCAlDAICETAMGVSInaqsnadSEYVQAvk 202
Cdd:cd11082   62 RKSLLPLFTRKALGLYLPIQER-VIR--KHLAKWLENSKSGDKPIEMRPLIR-DLNLETSQTVFV-------GPYLDD-- 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 203 tismvlHKRMFNILYR-FDLTYMLTPLA----------RAEKKALNVLHQFTEKiivqrreeliregssqessnddadvg 271
Cdd:cd11082  129 ------EARRFRIDYNyFNVGFLALPVDfpgtalwkaiQARKRIVKTLEKCAAK-------------------------- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 272 AKRKMA-------FLDILLQSTVDE------------RPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKK 332
Cdd:cd11082  177 SKKRMAageeptcLLDFWTHEILEEikeaeeegepppPHSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAK 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 333 CFEEIRSVVGNDkSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEIN-GKLIPAGTnIGISPLYLGRREEl 411
Cdd:cd11082  257 VREEQARLRPND-EPPLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTeDYTVPKGT-IVIPSIYDSCFQG- 333
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808351875 412 FSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:cd11082  334 FPEPDKFDPDRFSPERQEDRKYKKNFLVFGAGPHQCVGQEYAINHLMLFLALFSTLVD 391
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
234-467 9.33e-24

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: 103.36  E-value: 9.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 234 KALNVLHqftEKIivqrrEELIREgssqESSNDDADVGAKRKMAFLdiLLQSTVDERPLSNLDIREEVDTFMFEGHDTTS 313
Cdd:cd20638  182 RARNLIH---AKI-----EENIRA----KIQREDTEQQCKDALQLL--IEHSRRNGEPLNLQALKESATELLFGGHETTA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 314 SALMFFFYNIATHPEAQKKCFEEIRSVV----GNDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEING 389
Cdd:cd20638  248 SAATSLIMFLGLHPEVLQKVRKELQEKGllstKPNENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNG 327
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808351875 390 KLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRH 467
Cdd:cd20638  328 YQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRF-MSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARH 404
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
62-482 1.26e-23

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: 103.17  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGPSYSVMLFNPRDVERVLgssqlLTKSQEYSFLGRWLNEGLLVSNGR---------KWHRRRKIITPAFH- 131
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVL-----LKKGKEFSGRPRMVTTDLLSRNGKdiafadysaTWQLHRKLVHSAFAl 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 132 FRILEPYVE-IFDRQSLRLVEELAlriSRGQERINLGEAIHLCALDAICETAMGVSInaqSNADSEYvQAVKTISmvlhK 210
Cdd:cd20673   76 FGEGSQKLEkIICQEASSLCDTLA---THNGESIDLSPPLFRAVTNVICLLCFNSSY---KNGDPEL-ETILNYN----E 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 211 RMFNILYRFDLTYMLTPLARAEKKALNVLHQFtekiiVQRREELI-------REGSSQESSNDdadvgakrkmaFLDILL 283
Cdd:cd20673  145 GIVDTVAKDSLVDIFPWLQIFPNKDLEKLKQC-----VKIRDKLLqkkleehKEKFSSDSIRD-----------LLDALL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 284 Q-----------STVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYE 352
Cdd:cd20673  209 QakmnaennnagPDQDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDR 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 353 llNQLHYVDLCVKETLRMYPSVPLL-GRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-DVVTTAE 430
Cdd:cd20673  289 --NHLPLLEATIREVLRIRPVAPLLiPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFlDPTGSQL 366
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 808351875 431 KLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDfVGDSSEPPVL 482
Cdd:cd20673  367 ISPSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLE-VPDGGQLPSL 417
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
234-466 5.32e-23

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


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 101.45  E-value: 5.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 234 KALNVLHQFTEKIIvqrREELIREGSSQESsndDAdvgakrkmafLDILLQSTVD-ERPLSNLDIREEVDTFMFEGHDTT 312
Cdd:cd20636  180 KARDILHEYMEKAI---EEKLQRQQAAEYC---DA----------LDYMIHSAREnGKELTMQELKESAVELIFAAFSTT 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 313 SSALMFFFYNIATHPEAQKKCFEEIRS--VVGNDKSTP--VSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEIN 388
Cdd:cd20636  244 ASASTSLVLLLLQHPSAIEKIRQELVShgLIDQCQCCPgaLSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELD 323
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808351875 389 GKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLR 466
Cdd:cd20636  324 GYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELVT 401
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
212-451 2.24e-22

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: 99.36  E-value: 2.24e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 212 MFNIL---YRFDLTYMLtPLAR------AEKKALNVLHQFTE--KIIVQRREELIREGSSQESSNddadvgakrkmaFLD 280
Cdd:cd20658  153 IFTALkclYAFSISDYL-PFLRgldldgHEKIVREAMRIIRKyhDPIIDERIKQWREGKKKEEED------------WLD 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 281 ILLQ-STVDERPLSNLD-IREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLH 358
Cdd:cd20658  220 VFITlKDENGNPLLTPDeIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERL--VQESDIPNLN 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVP-LLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-----DVVTTAEKL 432
Cdd:cd20658  298 YVKACAREAFRLHPVAPfNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHlnedsEVTLTEPDL 377
                        250
                 ....*....|....*....
gi 808351875 433 NpyaYIPFSAGPRNCIGQK 451
Cdd:cd20658  378 R---FISFSTGRRGCPGVK 393
PLN00168 PLN00168
Cytochrome P450; Provisional
42-469 3.30e-22

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 99.64  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  42 IFLGLTPAEACLKIGELAERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLT----KSQEYSFLGRWLNEGLLVSNGR 117
Cdd:PLN00168  50 VWLTNSSADVEPLLRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALadrpAVASSRLLGESDNTITRSSYGP 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 118 KWHR-RRKIITPAFHfrilEPYVEIFDRQSLRLVEELALRISRGQERINLGEAIH------LCALDAICetaMGVSINAQ 190
Cdd:PLN00168 130 VWRLlRRNLVAETLH----PSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVEtfqyamFCLLVLMC---FGERLDEP 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 191 SNADSEYVQAVKTISMVLHKRMFN-------ILYRFDLTYMLTplARAEKKALNVlhqfteKIIVQRREELIREGSSQES 263
Cdd:PLN00168 203 AVRAIAAAQRDWLLYVSKKMSVFAffpavtkHLFRGRLQKALA--LRRRQKELFV------PLIDARREYKNHLGQGGEP 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 264 SNDDADVGAKRKMAFLDILLQSTVDeRPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGN 343
Cdd:PLN00168 275 PKKETTFEHSYVDTLLDIRLPEDGD-RALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGD 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 344 DKSTpVSYELLNQLHYVDLCVKETLRMYPsvP---LLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKP 420
Cdd:PLN00168 354 DQEE-VSEEDVHKMPYLKAVVLEGLRKHP--PahfVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVP 430
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 808351875 421 ERF---------DVVTTAEklnpYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:PLN00168 431 ERFlaggdgegvDVTGSRE----IRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFE 484
PLN02655 PLN02655
ent-kaurene oxidase
278-469 3.48e-22

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 99.05  E-value: 3.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 278 FLDILLQstvDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstpVSYELLNQL 357
Cdd:PLN02655 247 YLDFLLS---EATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDER---VTEEDLPNL 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 358 HYVDLCVKETLRMYPSVPLL-GRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYA 436
Cdd:PLN02655 321 PYLNAVFHETLRKYSPVPLLpPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERF-LGEKYESADMYK 399
                        170       180       190
                 ....*....|....*....|....*....|...
gi 808351875 437 YIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:PLN02655 400 TMAFGAGKRVCAGSLQAMLIACMAIARLVQEFE 432
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
240-471 1.88e-21

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: 96.71  E-value: 1.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 240 HQFTEKIIVQRREELIREGSSQ-ESSNDDADVGAKRKMAFLDILLQSTVDERpLSNLDIreevDTFMfEGHDTTSSALMF 318
Cdd:cd20652  183 HAIYQKIIDEHKRRLKPENPRDaEDFELCELEKAKKEGEDRDLFDGFYTDEQ-LHHLLA----DLFG-AGVDTTITTLRW 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 319 FFYNIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTN 397
Cdd:cd20652  257 FLLYMALFPKEQRRIQRELDEVVGRPDL--VTLEDLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVLAGYRIPKGSM 334
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808351875 398 IGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVD 471
Cdd:cd20652  335 IIPLLWAVHMDPNLWEEPEEFRPERF-LDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIA 407
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
62-481 3.14e-21

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


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 96.00  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGpSYSVMLFNprDVERVlgSSQLLTKSQEYSflGR---------WLNEGLLVSN-GRKWHRRRKIITPAF- 130
Cdd:cd20666    1 YGNIFSLFIG-SQLVVVLN--DFESV--REALVQKAEVFS--DRpsvplvtilTKGKGIVFAPyGPVWRQQRKFSHSTLr 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 131 HFRI----LEPYVEifdrQSLRLVEELALRisRGQERINLGEAIHLCALDAICETAMGVSINAQsnaDSEYVQAVKTISM 206
Cdd:cd20666   74 HFGLgklsLEPKII----EEFRYVKAEMLK--HGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQ---DVEFKTMLGLMSR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 207 VL----HKRMFNILYRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREgssqessnddadvgakRKMAFLDI- 281
Cdd:cd20666  145 GLeisvNSAAILVNICPWLYYLPFGPFRELRQIEKDITAFLKKIIADHRETLDPA----------------NPRDFIDMy 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 282 LLQSTVDERPLSNLDIREE-----VDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQ 356
Cdd:cd20666  209 LLHIEEEQKNNAESSFNEDylfyiIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDR--APSLTDKAQ 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 357 LHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPY 435
Cdd:cd20666  287 MPFTEATIMEVQRMTVVVPLsIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRF-LDENGQLIKKE 365
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 808351875 436 AYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPV 481
Cdd:cd20666  366 AFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAPKPSM 411
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
60-493 3.91e-21

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: 95.68  E-value: 3.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  60 ERHGDTFGLFLGPSYSVMLFNPRDVERVLGSSQLLTKSQEysfLGRWL--------NEGLLVSNGRKWHRRR-----KII 126
Cdd:cd20644    2 QELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMT---LEPWVahrqhrghKCGVFLLNGPEWRFDRlrlnpEVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 127 TPAFHFRILePYVEIFDRQSLRLVEELALRISRGQERINLGEAIHLCALDAICETAMGVSI---NAQSNADSE-YVQAVK 202
Cdd:cd20644   79 SPAAVQRFL-PMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLglvGHSPSSASLrFISAVE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 203 TISMVLHKRMFniLYRFDLTYMLTPLARAEKKALNVLHQFTEKIIVQRREELIREGSSQESSnddadvgakrKMAflDIL 282
Cdd:cd20644  158 VMLKTTVPLLF--MPRSLSRWISPKLWKEHFEAWDCIFQYADNCIQKIYQELAFGRPQHYTG----------IVA--ELL 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 283 LQStvdERPLSNldIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVsyELLNQLHYVDL 362
Cdd:cd20644  224 LQA---ELSLEA--IKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQ--KALTELPLLKA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 363 CVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvVTTAEKLNPYAYIPFSA 442
Cdd:cd20644  297 ALKETLRLYPVGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRW--LDIRGSGRNFKHLAFGF 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 808351875 443 GPRNCIGQKFAMLEIKAIVANVLRHYEVDFVgdSSEPPVLIAELILRTKEP 493
Cdd:cd20644  375 GMRQCLGRRLAEAEMLLLLMHVLKNFLVETL--SQEDIKTVYSFILRPEKP 423
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
323-471 2.91e-20

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: 92.76  E-value: 2.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 323 IATHPEAQKKCFEEIRSVVGN--DKSTPVSYELLNQLHYVDLCVKETLRMYpSVPLLGRKVLEDCEINGKLIPAGTNIGI 400
Cdd:cd20635  237 ILSHPSVYKKVMEEISSVLGKagKDKIKISEDDLKKMPYIKRCVLEAIRLR-SPGAITRKVVKPIKIKNYTIPAGDMLML 315
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808351875 401 SPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVD 471
Cdd:cd20635  316 SPYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFT 386
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
242-494 3.07e-20

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: 92.78  E-value: 3.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 242 FTEKIIVQRREEliregsSQESSNDDADVgakrkmafLDILLQSTVDERpLSNLDIREEVDTFMFEGHDTTSSALMFFFY 321
Cdd:cd11076  185 FVGKIIEEHRAK------RSNRARDDEDD--------VDVLLSLQGEEK-LSDSDMIAVLWEMIFRGTDTVAILTEWIMA 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 322 NIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSVPLL--GRKVLEDCEINGKLIPAGTNIG 399
Cdd:cd11076  250 RMVLHPDIQSKAQAEIDAAVGGSRR--VADSDVAKLPYLQAVVKETLRLHPPGPLLswARLAIHDVTVGGHVVPAGTTAM 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 400 ISPLYLGRREELFSEPNIFKPERF---------DVVTTAEKLnpyayIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEv 470
Cdd:cd11076  328 VNMWAITHDPHVWEDPLEFKPERFvaaeggadvSVLGSDLRL-----APFGAGRRVCPGKALGLATVHLWVAQLLHEFE- 401
                        250       260
                 ....*....|....*....|....*..
gi 808351875 471 dfVGDSSEPPVLIAE---LILRTKEPL 494
Cdd:cd11076  402 --WLPDDAKPVDLSEvlkLSCEMKNPL 426
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
62-479 5.93e-20

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: 91.85  E-value: 5.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGPSYSVMLFNPRDVERVLGssqllTKSQEYSflGR-------WLNE--GLLVSNGRKW--HRRRKIIT--- 127
Cdd:cd11026    1 YGPVFTVYLGSKPVVVLCGYEAVKEALV-----DQAEEFS--GRppvplfdRVTKgyGVVFSNGERWkqLRRFSLTTlrn 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 128 -----PAFHFRILEpyveifdrQSLRLVEELalRISRGQErINLGEAIHLCALDAICETAMGVSINAQsnaDSEYVQAVK 202
Cdd:cd11026   74 fgmgkRSIEERIQE--------EAKFLVEAF--RKTKGKP-FDPTFLLSNAVSNVICSIVFGSRFDYE---DKEFLKLLD 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 203 TISMVLH------KRMFNILYRFdltyMLTPLARAEK--KALNVLHQFTEKIIVQRREELiregssqessnddaDVGAKR 274
Cdd:cd11026  140 LINENLRllsspwGQLYNMFPPL----LKHLPGPHQKlfRNVEEIKSFIRELVEEHRETL--------------DPSSPR 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 275 KmaFLDILLQSTVDERPLSNLDIREE------VDTFmFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstP 348
Cdd:cd11026  202 D--FIDCFLLKMEKEKDNPNSEFHEEnlvmtvLDLF-FAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNR--T 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 349 VSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNigISPLyLG---RREELFSEPNIFKPERFd 424
Cdd:cd11026  277 PSLEDRAKMPYTDAVIHEVQRFGDIVPLgVPHAVTRDTKFRGYTIPKGTT--VIPN-LTsvlRDPKQWETPEEFNPGHF- 352
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808351875 425 vvttaekLN-------PYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEP 479
Cdd:cd11026  353 -------LDeqgkfkkNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKDP 407
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
273-469 6.17e-20

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 92.61  E-value: 6.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 273 KRKMAFLDILL--QSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVS 350
Cdd:PLN00110 264 KGNPDFLDVVManQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVES 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 351 YelLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTA 429
Cdd:PLN00110 344 D--LPKLPYLQAICKESFRKHPSTPLnLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERF-LSEKN 420
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 808351875 430 EKLNP----YAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:PLN00110 421 AKIDPrgndFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFD 464
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
305-454 2.54e-19

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: 89.97  E-value: 2.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 305 MFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLHYVDLCVKETLRMYPSVPLL-GRKVLE 383
Cdd:cd20653  236 LLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDR--LIEESDLPKLPYLQNIISETLRLYPAAPLLvPHESSE 313
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808351875 384 DCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvvttAEKLNPYAYIPFSAGPRNCIGQKFAM 454
Cdd:cd20653  314 DCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFE----GEEREGYKLIPFGLGRRACPGAGLAQ 380
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
62-471 4.31e-19

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: 89.66  E-value: 4.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGpSYSVMLFNPRDVERvlgssQLLTKSQE--------YSFlgRWLNEGLLVS---NGRKWHRRRKIITPAF 130
Cdd:cd11028    1 YGDVFQIRMG-SRPVVVLNGLETIK-----QALVRQGEdfagrpdfYSF--QFISNGKSMAfsdYGPRWKLHRKLAQNAL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 131 H-FRILEP--YVEIFDRQSLR-LVEELaLRISRGQERINLGEAIHLCALDAICETAMGvsiNAQSNADSEYVQAVKtism 206
Cdd:cd11028   73 RtFSNARThnPLEEHVTEEAEeLVTEL-TENNGKPGPFDPRNEIYLSVGNVICAICFG---KRYSRDDPEFLELVK---- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 207 vlHKRMF-------NILyrfD-LTYMLTPLARAEKKALNVLHQFTEKIIVQRREELiregssqessnDDADVGAKRKMaf 278
Cdd:cd11028  145 --SNDDFgafvgagNPV---DvMPWLRYLTRRKLQKFKELLNRLNSFILKKVKEHL-----------DTYDKGHIRDI-- 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 279 LDILLQST----VDERPLSNLDiREEVDTFMFE----GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVS 350
Cdd:cd11028  207 TDALIKASeekpEEEKPEVGLT-DEHIISTVQDlfgaGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRER--LPR 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 351 YELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-DVVTT 428
Cdd:cd11028  284 LSDRPNLPYTEAFILETMRHSSFVPFtIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFlDDNGL 363
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 808351875 429 AEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVD 471
Cdd:cd11028  364 LDKTKVDKFLPFGAGRRRCLGEELARMELFLFFATLLQQCEFS 406
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
93-469 4.62e-19

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 89.75  E-value: 4.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  93 LLTKSQEYSFLGRWLNEGLLVSNGRKwhRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELaLRISRGQERINLGEAIHL 172
Cdd:PLN03234  99 LLKGQQTMSYQGRELGFGQYTAYYRE--MRKMCMVNLFSPNRVASFRPVREEECQRMMDKI-YKAADQSGTVDLSELLLS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 173 CALDAICETAMGVSINAQSNADSEYVQAVKTISMVLHKRMFNILY-RFDLTYMLTPLARAEKKALNVLHQFTEKIIvqrR 251
Cdd:PLN03234 176 FTNCVVCRQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSDLFpYFGFLDNLTGLSARLKKAFKELDTYLQELL---D 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 252 EELIREGSSQESSnddadvgakrkmAFLDILLQSTVDErPLSNLDIREEVDTFMFE----GHDTTSSALMFFFYNIATHP 327
Cdd:PLN03234 253 ETLDPNRPKQETE------------SFIDLLMQIYKDQ-PFSIKFTHENVKAMILDivvpGTDTAAAVVVWAMTYLIKYP 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 328 EAQKKCFEEIRSVVGnDKSTpVSYELLNQLHYVDLCVKETLRMYPSVP-LLGRKVLEDCEINGKLIPAGTNIGISPLYLG 406
Cdd:PLN03234 320 EAMKKAQDEVRNVIG-DKGY-VSEEDIPNLPYLKAVIKESLRLEPVIPiLLHRETIADAKIGGYDIPAKTIIQVNAWAVS 397
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808351875 407 RREELFSE-PNIFKPERF--DVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:PLN03234 398 RDTAAWGDnPNEFIPERFmkEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFD 463
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
71-471 6.20e-19

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: 89.00  E-value: 6.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  71 GPSY--------SVMLFNPRDVervlgssQLLTKSqEYSFLGR-----WL--------NEGLLVSNGRKWHRRRKII-TP 128
Cdd:cd20643    5 GPIYrekigyyeSVNIINPEDA-------AILFKS-EGMFPERlsvppWVayrdyrkrKYGVLLKNGEAWRKDRLILnKE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 129 AFHFRILEPYVEIFDRQSLRLVEELALRI---SRGQERINLGEAIHLCALDAICETAMGVSINA-QSNADSEYVQAVKTI 204
Cdd:cd20643   77 VLAPKVIDNFVPLLNEVSQDFVSRLHKRIkksGSGKWTADLSNDLFRFALESICNVLYGERLGLlQDYVNPEAQRFIDAI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 205 SMVLHKR--MFNI---LYRfdltYMLTPLARAEKKALNVLHQFTEKIIvqrreELIREGSSQESSNDDADVGakrkmaFL 279
Cdd:cd20643  157 TLMFHTTspMLYIppdLLR----LINTKIWRDHVEAWDVIFNHADKCI-----QNIYRDLRQKGKNEHEYPG------IL 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 280 DILLQStvDERPLSnlDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVsyELLNQLHY 359
Cdd:cd20643  222 ANLLLQ--DKLPIE--DIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMV--KMLKSVPL 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 360 VDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvvtTAEKLNPYAYIP 439
Cdd:cd20643  296 LKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERW----LSKDITHFRNLG 371
                        410       420       430
                 ....*....|....*....|....*....|..
gi 808351875 440 FSAGPRNCIGQKFAMLEIKAIVANVLRHYEVD 471
Cdd:cd20643  372 FGFGPRQCLGRRIAETEMQLFLIHMLENFKIE 403
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
232-449 2.43e-18

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 87.57  E-value: 2.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 232 EKKALNVLHQFTE---KIIVQRReeliREGSSQESSNDDADvgakrkmaFLDILLQSTVD--ERPLSNLDIREEVDTFMF 306
Cdd:PLN03112 239 EKKMREVEKRVDEfhdKIIDEHR----RARSGKLPGGKDMD--------FVDVLLSLPGEngKEHMDDVEIKALMQDMIA 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 307 EGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSVP-LLGRKVLEDC 385
Cdd:PLN03112 307 AATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRM--VQESDLVHLNYLRCVVRETFRMHPAGPfLIPHESLRAT 384
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808351875 386 EINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF---DVVTTAEKLNP-YAYIPFSAGPRNCIG 449
Cdd:PLN03112 385 TINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHwpaEGSRVEISHGPdFKILPFSAGKRKCPG 452
PLN02966 PLN02966
cytochrome P450 83A1
286-457 2.81e-18

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 87.50  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 286 TVDERPLSNLDIreevdtfMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYELLNQLHYVDLCVK 365
Cdd:PLN02966 286 TVDNVKAVILDI-------VVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTFVTEDDVKNLPYFRALVK 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 366 ETLRMYPSVPLL-GRKVLEDCEINGKLIPAGTNIGISPLYLGRRE-ELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAG 443
Cdd:PLN02966 359 ETLRIEPVIPLLiPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEkEWGPNPDEFRPERFLEKEVDFKGTDYEFIPFGSG 438
                        170
                 ....*....|....*.
gi 808351875 444 PRNCIGQKF--AMLEI 457
Cdd:PLN02966 439 RRMCPGMRLgaAMLEV 454
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
308-469 3.50e-18

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: 86.77  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 308 GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCE 386
Cdd:cd20656  242 GMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRV--MTEADFPQLPYLQCVVKEALRLHPPTPLmLPHKASENVK 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 387 INGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLR 466
Cdd:cd20656  320 IGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLH 399

                 ...
gi 808351875 467 HYE 469
Cdd:cd20656  400 HFS 402
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
245-468 5.08e-18

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: 86.31  E-value: 5.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 245 KIIVQRREELIRegSSQESSNDDADVGAKRKMafLDILLQS---TVDERPLSNLdiREE------VDTFMfEGHDTTSSA 315
Cdd:cd20674  173 KQAVENRDHIVE--SQLRQHKESLVAGQWRDM--TDYMLQGlgqPRGEKGMGQL--LEGhvhmavVDLFI-GGTETTAST 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 316 LMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTpvSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPA 394
Cdd:cd20674  246 LSWAVAFLLHHPEIQDRLQEELDRVLGPGASP--SYKDRARLPLLNATIAEVLRLRPVVPLaLPHRTTRDSSIAGYDIPK 323
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 395 GTNIgISPLYLGRREE-LFSEPNIFKPERFDVVTTAeklNPyAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHY 468
Cdd:cd20674  324 GTVV-IPNLQGAHLDEtVWEQPHEFRPERFLEPGAA---NR-ALLPFGCGARVCLGEPLARLELFVFLARLLQAF 393
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
76-467 7.34e-18

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: 85.04  E-value: 7.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  76 VMLFNPRDVERVLGSSQLLTKSQEY-SFLGRWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQ-SLRLVEEL 153
Cdd:cd20629   12 YVLLRHDDVMAVLRDPRTFSSETYDaTLGGPFLGHSILAMDGEEHRRRRRLLQPAFAPRAVARWEEPIVRPiAEELVDDL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 154 AlrisrGQERINLGE--AIHLCALdAICETaMGVSinaqsNADSEYVQAvKTISMVLhkrmfnilyrfdltYMLTPLARA 231
Cdd:cd20629   92 A-----DLGRADLVEdfALELPAR-VIYAL-LGLP-----EEDLPEFTR-LALAMLR--------------GLSDPPDPD 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 232 EKKALNVLHQFTE---KIIVQRReeliregssQESSNDdadvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEG 308
Cdd:cd20629  145 VPAAEAAAAELYDyvlPLIAERR---------RAPGDD-----------LISRLLRAEVEGEKLDDEEIISFLRLLLPAG 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 309 HDTTSSALMFFFYNIATHPEAqkkcFEEIRsvvgNDKStpvsyeLLNQLhyvdlcVKETLRMYPSVPLLGRKVLEDCEIN 388
Cdd:cd20629  205 SDTTYRALANLLTLLLQHPEQ----LERVR----RDRS------LIPAA------IEEGLRWEPPVASVPRMALRDVELD 264
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808351875 389 GKLIPAGTNIGISPLYLGRREELFSepnifKPERFDVVTTaeklnPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRH 467
Cdd:cd20629  265 GVTIPAGSLLDLSVGSANRDEDVYP-----DPDVFDIDRK-----PKPHLVFGGGAHRCLGEHLARVELREALNALLDR 333
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
326-469 4.48e-17

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 83.63  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 326 HPEAQKKCFEEIRSVVGNDksTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKV-LEDCEINGKLIPAGTNIGISPLY 404
Cdd:PLN02394 323 HPEIQKKLRDELDTVLGPG--NQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMnLEDAKLGGYDIPAESKILVNAWW 400
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808351875 405 LGRREELFSEPNIFKPERF--DVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:PLN02394 401 LANNPELWKNPEEFRPERFleEEAKVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFE 467
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
278-458 6.81e-17

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: 82.25  E-value: 6.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 278 FLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQkkcfEEIRsvvgNDKSTpvsyellnql 357
Cdd:cd11035  172 LISAILNAEIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDR----RRLR----EDPEL---------- 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 358 hyVDLCVKETLRMYPsVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERfdvvttaeklNPYAY 437
Cdd:cd11035  234 --IPAAVEELLRRYP-LVNVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR----------KPNRH 300
                        170       180
                 ....*....|....*....|.
gi 808351875 438 IPFSAGPRNCIGQKFAMLEIK 458
Cdd:cd11035  301 LAFGAGPHRCLGSHLARLELR 321
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
289-482 7.77e-17

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


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 82.75  E-value: 7.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 289 ERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHP--EAQKKCFEEIRSVVGNDKSTPVSYELLNQLHYVDLCVKE 366
Cdd:cd11066  221 ESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAEEKCPYVVALVKE 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 367 TLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYiPFSAGPR 445
Cdd:cd11066  301 TLRYFTVLPLgLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHF-SFGAGSR 379
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 808351875 446 NCIGQKFAMLEIKAIVANVLRHYEVdFVGDSSEPPVL 482
Cdd:cd11066  380 MCAGSHLANRELYTAICRLILLFRI-GPKDEEEPMEL 415
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
278-468 2.88e-16

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: 80.74  E-value: 2.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 278 FLDILLQSTVDER--PLSNLDIREEVDT---FMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYE 352
Cdd:cd20670  203 FIDCFLIKMHQDKnnPHTEFNLKNLVLTtlnLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDR 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 353 LlnQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNigISPLyLG---RREELFSEPNIFKPERFDVVTT 428
Cdd:cd20670  283 V--KMPYTDAVIHEIQRLTDIVPLgVPHNVIRDTQFRGYLLPKGTD--VFPL-LGsvlKDPKYFRYPEAFYPQHFLDEQG 357
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 808351875 429 AEKLNPyAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHY 468
Cdd:cd20670  358 RFKKNE-AFVPFSSGKRVCLGEAMARMELFLYFTSILQNF 396
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
252-460 3.87e-16

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 80.28  E-value: 3.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 252 EELIREGSSQESSNDDADVgakrkmafLDILLQSTVDE-RPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQ 330
Cdd:cd20637  189 EKAIREKLQGTQGKDYADA--------LDILIESAKEHgKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVL 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 331 KKCFEEIRSV----VGNDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLG 406
Cdd:cd20637  261 EKLREELRSNgilhNGCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDTH 340
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 808351875 407 RREELFSEPNIFKPERFDVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAI 460
Cdd:cd20637  341 DTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVL 394
PLN02302 PLN02302
ent-kaurenoic acid oxidase
230-470 1.50e-15

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 78.99  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 230 RAEKKALNVLHqfteKIIVQRReeliregssqessNDDADVGAKRKMAFLDILLQSTvDE--RPLSNLDIREEVDTFMFE 307
Cdd:PLN02302 237 KARKKLVALFQ----SIVDERR-------------NSRKQNISPRKKDMLDLLLDAE-DEngRKLDDEEIIDLLLMYLNA 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 308 GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVgndKSTPVSYELLN-----QLHYVDLCVKETLRMYPSVPLLGRKVL 382
Cdd:PLN02302 299 GHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIA---KKRPPGQKGLTlkdvrKMEYLSQVIDETLRLINISLTVFREAK 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 383 EDCEINGKLIPAG-------TNIGISPlylgrreELFSEPNIFKPERFDvvttAEKLNPYAYIPFSAGPRNCIGQKFAML 455
Cdd:PLN02302 376 TDVEVNGYTIPKGwkvlawfRQVHMDP-------EVYPNPKEFDPSRWD----NYTPKAGTFLPFGLGSRLCPGNDLAKL 444
                        250
                 ....*....|....*
gi 808351875 456 EIKAIVANVLRHYEV 470
Cdd:PLN02302 445 EISIFLHHFLLGYRL 459
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
280-477 2.43e-15

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 78.05  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 280 DILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPV-SYELLNQLH 358
Cdd:PLN02196 248 DLLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGESlTWEDTKKMP 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIgiSPLY--LGRREELFSEPNIFKPERFDVvttAEKlnPYA 436
Cdd:PLN02196 328 LTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKV--LPLFrnIHHSADIFSDPGKFDPSRFEV---APK--PNT 400
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 808351875 437 YIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSS 477
Cdd:PLN02196 401 FMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTSN 441
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
278-472 4.94e-15

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: 77.14  E-value: 4.94e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 278 FLDILLQSTVDER--PLSNLDIREEVDT---FMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTpvSYE 352
Cdd:cd20668  203 FIDSFLIRMQEEKknPNTEFYMKNLVMTtlnLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQP--KFE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 353 LLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNigISPLyLG---RREELFSEPNIFKPERFDVVTT 428
Cdd:cd20668  281 DRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKDTKFRDFFLPKGTE--VFPM-LGsvlKDPKFFSNPKDFNPQHFLDDKG 357
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 808351875 429 AEKLNPyAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDF 472
Cdd:cd20668  358 QFKKSD-AFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKS 400
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
277-472 6.05e-15

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: 76.78  E-value: 6.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 277 AFLDILLQSTVD-ERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLN 355
Cdd:cd20661  218 AYLDEMDQNKNDpESTFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNG--MPSFEDKC 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 356 QLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIgISPLY-LGRREELFSEPNIFKPERFdVVTTAEKLN 433
Cdd:cd20661  296 KMPYTEAVLHEVLRFCNIVPLgIFHATSKDAVVRGYSIPKGTTV-ITNLYsVHFDEKYWSDPEVFHPERF-LDSNGQFAK 373
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 808351875 434 PYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDF 472
Cdd:cd20661  374 KEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHF 412
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
278-478 6.18e-15

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


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 76.72  E-value: 6.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 278 FLDILLQSTVDER--PLSNLDIREEVDT---FMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVsyE 352
Cdd:cd20669  203 FIDCFLTKMAEEKqdPLSHFNMETLVMTthnLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTL--E 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 353 LLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIgISPLYLGRRE-ELFSEPNIFKPERFDVVTTAE 430
Cdd:cd20669  281 DRARMPYTDAVIHEIQRFADIIPMsLPHAVTRDTNFRGFLIPKGTDV-IPLLNSVHYDpTQFKDPQEFNPEHFLDDNGSF 359
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 808351875 431 KLNPyAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSE 478
Cdd:cd20669  360 KKND-AFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQPLGAPED 406
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
308-496 7.07e-15

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


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 76.38  E-value: 7.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 308 GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGndkSTPVSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCE 386
Cdd:cd20664  237 GTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIG---SRQPQVEHRKNMPYTDAVIHEIQRFANIVPMnLPHATTRDVT 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 387 INGKLIPAGTNIgiSPLYLG--RREELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANV 464
Cdd:cd20664  314 FRGYFIPKGTYV--IPLLTSvlQDKTEWEKPEEFNPEHF-LDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSL 390
                        170       180       190
                 ....*....|....*....|....*....|..
gi 808351875 465 LRHYevdfvgdSSEPPVLIAELILRTKEPLMF 496
Cdd:cd20664  391 LQRF-------RFQPPPGVSEDDLDLTPGLGF 415
PLN02971 PLN02971
tryptophan N-hydroxylase
252-488 8.03e-15

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 77.00  E-value: 8.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 252 EELIREGSSQESSNDDADVGAKRKM----------AFLDILLqSTVDE--RPLSNLD-IREEVDTFMFEGHDTTSSALMF 318
Cdd:PLN02971 271 EKIMRESSAIMDKYHDPIIDERIKMwregkrtqieDFLDIFI-SIKDEagQPLLTADeIKPTIKELVMAAPDNPSNAVEW 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 319 FFYNIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTN 397
Cdd:PLN02971 350 AMAEMINKPEILHKAMEEIDRVVGKERF--VQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQ 427
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 398 IGISPLYLGRREELFSEPNIFKPERF----DVVTTAEklNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFV 473
Cdd:PLN02971 428 VLLSRYGLGRNPKVWSDPLSFKPERHlnecSEVTLTE--NDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 505
                        250       260
                 ....*....|....*....|....*....
gi 808351875 474 GDS--------------SEPPVLIAELIL 488
Cdd:PLN02971 506 GSEtrvelmesshdmflSKPLVMVGELRL 534
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
323-485 1.62e-14

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: 75.19  E-value: 1.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 323 IATHPEAQKKCFEEIRSVVGndkstPVSyellnqLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISP 402
Cdd:cd20624  218 LAAHPEQAARAREEAAVPPG-----PLA------RPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFA 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 403 LYLGRREELFSEPNIFKPErfdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVgdsSEPPVL 482
Cdd:cd20624  287 PFFHRDDEALPFADRFVPE---IWLDGRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPL---ESPRSG 360

                 ...
gi 808351875 483 IAE 485
Cdd:cd20624  361 PGE 363
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
279-493 4.84e-14

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: 73.66  E-value: 4.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 279 LDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEaqkkCFEEIRSvvgnDKStpvsyellnqlh 358
Cdd:cd11080  176 ISILCTAEYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPE----QLAAVRA----DRS------------ 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLNPYAYI 438
Cdd:cd11080  236 LVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREDLGIRSAFSGAADHL 315
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 808351875 439 PFSAGPRNCIGQKFAMLEIKAIVANVLrhyevDFVGD-SSEPPVLIAELILRTKEP 493
Cdd:cd11080  316 AFGSGRHFCVGAALAKREIEIVANQVL-----DALPNiRLEPGFEYAESGLYTRGP 366
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
323-470 4.93e-14

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: 74.05  E-value: 4.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 323 IATHPEAQKKCFEEIRSVVGndKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKV-LEDCEINGKLIPAGTNIGIS 401
Cdd:cd11074  260 LVNHPEIQKKLRDELDTVLG--PGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMnLHDAKLGGYDIPAESKILVN 337
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 402 PLYLGRREELFSEPNIFKPERFdvvtTAEKL------NPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd11074  338 AWWLANNPAHWKKPEEFRPERF----LEEESkveangNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNFEL 408
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
105-457 5.06e-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: 73.55  E-value: 5.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 105 RWLNEGLLVSNGRKWHRRRKIITPAFHFRILEPYVEIFDRQSLRLVEELAlrisrGQERINLGEAI-HLCALDAICeTAM 183
Cdd:cd11038   65 DWWVDFLLSLEGADHARLRGLVNPAFTPKAVEALRPRFRATANDLIDGFA-----EGGECEFVEAFaEPYPARVIC-TLL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 184 GVSINAQSnadseyvqavktismVLHKRMFNILYRFDLTYmLTPLARAEKkALNVLHQFTEKIIVQRREELiregssqes 263
Cdd:cd11038  139 GLPEEDWP---------------RVHRWSADLGLAFGLEV-KDHLPRIEA-AVEELYDYADALIEARRAEP--------- 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 264 sNDDadvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEaQKKCFEEIRSVVGN 343
Cdd:cd11038  193 -GDD----------LISTLVAAEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALREDPELAPA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 344 dkstpvsyellnqlhyvdlCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRreelfsEPNIFKPERF 423
Cdd:cd11038  261 -------------------AVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANR------DPRVFDADRF 315
                        330       340       350
                 ....*....|....*....|....*....|....
gi 808351875 424 DVvtTAEKLNPYAyipFSAGPRNCIGQKFAMLEI 457
Cdd:cd11038  316 DI--TAKRAPHLG---FGGGVHHCLGAFLARAEL 344
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
280-471 6.11e-14

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: 73.41  E-value: 6.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 280 DILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEiRSVVGNdkstpvsyellnqlhy 359
Cdd:cd11078  193 DLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRAD-PSLIPN---------------- 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 360 vdlCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEpnifkPERFDVvttaEKLNPYAYIP 439
Cdd:cd11078  256 ---AVEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPD-----PDRFDI----DRPNARKHLT 323
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 808351875 440 FSAGPRNCIGQKFAMLEIKAIVANVLR---HYEVD 471
Cdd:cd11078  324 FGHGIHFCLGAALARMEARIALEELLRrlpGMRVP 358
PLN03018 PLN03018
homomethionine N-hydroxylase
233-502 6.80e-14

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 73.89  E-value: 6.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 233 KKALNVLHQFTEKIIvQRREELIREGSSQESSNDdadvgakrkmaFLD--ILLQSTVDERPLSNLDIREEVDTFMFEGHD 310
Cdd:PLN03018 261 KVNVNLVRSYNNPII-DERVELWREKGGKAAVED-----------WLDtfITLKDQNGKYLVTPDEIKAQCVEFCIAAID 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 311 TTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSV----PLLGRkvlEDCE 386
Cdd:PLN03018 329 NPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRL--VQESDIPNLNYLKACCRETFRIHPSAhyvpPHVAR---QDTT 403
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 387 INGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF---DVVTTAEKL--NPYAYIPFSAGPRNCIGQKFAMLEIKAIV 461
Cdd:PLN03018 404 LGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHlqgDGITKEVTLveTEMRFVSFSTGRRGCVGVKVGTIMMVMML 483
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 808351875 462 ANVLRHYEVDFVGDSSEPPVLIAELILRTKEPLMFKVRERV 502
Cdd:PLN03018 484 ARFLQGFNWKLHQDFGPLSLEEDDASLLMAKPLLLSVEPRL 524
PLN02500 PLN02500
cytochrome P450 90B1
226-475 5.15e-13

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 71.05  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 226 TPLARAEKKALNVLhQFTEKIIVQRREELIREGSSQESsnddadvgakrkmaflDILLQSTVDERPLSNLDIREEVDTFM 305
Cdd:PLN02500 226 TAYRKALKSRATIL-KFIERKMEERIEKLKEEDESVEE----------------DDLLGWVLKHSNLSTEQILDLILSLL 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 306 FEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDK---STPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVL 382
Cdd:PLN02500 289 FAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKqsgESELNWEDYKKMEFTQCVINETLRLGNVVRFLHRKAL 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 383 EDCEINGKLIPAGTNI--GISPLYLGrrEELFSEPNIFKPERFD------VVTTAEKLNPYAYIPFSAGPRNCIGQKFAM 454
Cdd:PLN02500 369 KDVRYKGYDIPSGWKVlpVIAAVHLD--SSLYDQPQLFNPWRWQqnnnrgGSSGSSSATTNNFMPFGGGPRLCAGSELAK 446
                        250       260
                 ....*....|....*....|.
gi 808351875 455 LEIKAIVANVLRHYEVDFVGD 475
Cdd:PLN02500 447 LEMAVFIHHLVLNFNWELAEA 467
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
279-474 5.27e-13

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: 70.44  E-value: 5.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 279 LDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKcfeeirsvvgndkstpvsyeLLNQLH 358
Cdd:cd11034  173 ISRLIEGEIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRR--------------------LIADPS 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvvttaeklnPYAYI 438
Cdd:cd11034  233 LIPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRT----------PNRHL 302
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 808351875 439 PFSAGPRNCIGQKFAMLEIKAIVANVLRH---YEVDFVG 474
Cdd:cd11034  303 AFGSGVHRCLGSHLARVEARVALTEVLKRipdFELDPGA 341
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
302-469 6.58e-13

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: 70.37  E-value: 6.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 302 DTFmFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKStPvSYELLNQLHYVDLCVKETLRMYPSVPL-LGRK 380
Cdd:cd20665  233 DLF-GAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRS-P-CMQDRSHMPYTDAVIHEIQRYIDLVPNnLPHA 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 381 VLEDCEINGKLIPAGTNI--GISPLYLGRREelFSEPNIFKPERF-DVVTTAEKLNpyAYIPFSAGPRNCIGQKFAMLEI 457
Cdd:cd20665  310 VTCDTKFRNYLIPKGTTVitSLTSVLHDDKE--FPNPEKFDPGHFlDENGNFKKSD--YFMPFSAGKRICAGEGLARMEL 385
                        170
                 ....*....|..
gi 808351875 458 KAIVANVLRHYE 469
Cdd:cd20665  386 FLFLTTILQNFN 397
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
62-470 1.04e-12

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: 69.87  E-value: 1.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGPSYSVMLFNPRDVErvlgsSQLLTKSQEYS------FLGRWLNE-GLLVSNGRKWHRRRKIITP-----A 129
Cdd:cd20667    1 YGNIYTLWLGSTPIVVLSGFKAVK-----EGLVSHSEEFSgrpltpFFRDLFGEkGIICTNGLTWKQQRRFCMTtlrelG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 130 FHFRILEPYVEifdRQSLRLVEELAlriSRGQERINLGEAIHLCALDAICETAMGVSINAQSNADSEYVQAVK---TISM 206
Cdd:cd20667   76 LGKQALESQIQ---HEAAELVKVFA---QENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINlglAFAS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 207 VLHKRMFNiLYRFDLTYMLTPlaraeKKALNVLHQFTEKIIvqrREELIREGSSQESSNDDadvgakrkmaFLDILLQS- 285
Cdd:cd20667  150 TIWGRLYD-AFPWLMRYLPGP-----HQKIFAYHDAVRSFI---KKEVIRHELRTNEAPQD----------FIDCYLAQi 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 286 --TVDErPLSNLD----IREEVDTFMfEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNdkSTPVSYELLNQLHY 359
Cdd:cd20667  211 tkTKDD-PVSTFSeenmIQVVIDLFL-GGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGA--SQLICYEDRKRLPY 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 360 VDLCVKETLRmYPSVPLLG--RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYAY 437
Cdd:cd20667  287 TNAVIHEVQR-LSNVVSVGavRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHF-LDKDGNFVMNEAF 364
                        410       420       430
                 ....*....|....*....|....*....|...
gi 808351875 438 IPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20667  365 LPFSAGHRVCLGEQLARMELFIFFTTLLRTFNF 397
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
277-501 1.25e-12

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: 69.44  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 277 AFLDILLQSTVDERPLSNLDIREEV-----DTFMfEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSY 351
Cdd:cd20671  200 SYIEALIQKQEEDDPKETLFHDANVlactlDLVM-AGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGC--LPNY 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 352 ELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNI--GISPLYLGRREelFSEPNIFKPERFdVVTTA 429
Cdd:cd20671  277 EDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVipLLSSVLLDKTQ--WETPYQFNPNHF-LDAEG 353
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808351875 430 EKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVdfvgdssEPPVLIAELILRTKEPLMFKVRER 501
Cdd:cd20671  354 KFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTF-------LPPPGVSPADLDATPAAAFTMRPQ 418
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
62-457 1.75e-12

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: 69.06  E-value: 1.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGPSYSVMLFNPRDVERVLgssqlltKSQEYSFLGRW---LNE------GLLVSNGRKW-HRRRKIITPAFH 131
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEAL-------VTQEQNFMNRPetpLRErifnknGLIFSSGQTWkEQRRFALMTLRN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 132 F----RILEpyvEIFDRQSLRLVEelALRISRGQErINLGEAIHLCALDAICETAMGVSINAQsnaDSEYVQAVKTI--S 205
Cdd:cd20662   74 FglgkKSLE---ERIQEECRHLVE--AIREEKGNP-FNPHFKINNAVSNIICSVTFGERFEYH---DEWFQELLRLLdeT 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 206 MVLHKRMFNILYRF---DLTYMLTP---LARAEKKalnvLHQFTEKIIVQRREELiregsSQESSNDdadvgakrkmaFL 279
Cdd:cd20662  145 VYLEGSPMSQLYNAfpwIMKYLPGShqtVFSNWKK----LKLFVSDMIDKHREDW-----NPDEPRD-----------FI 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 280 DILLQStVDERPLSNLDIREE------VDTFmFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGndKSTPVSYEL 353
Cdd:cd20662  205 DAYLKE-MAKYPDPTTSFNEEnlicstLDLF-FAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIG--QKRQPSLAD 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 354 LNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvVTTAEKL 432
Cdd:cd20662  281 RESMPYTNAVIHEVQRMGNIIPLnVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHF--LENGQFK 358
                        410       420
                 ....*....|....*....|....*
gi 808351875 433 NPYAYIPFSAGPRNCIGQKFAMLEI 457
Cdd:cd20662  359 KREAFLPFSMGKRACLGEQLARSEL 383
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
292-465 1.90e-12

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: 68.97  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 292 LSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLHYVDLCVKETLRMY 371
Cdd:cd20677  232 LSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSR--LPRFEDRKSLHYTEAFINEVFRHS 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 372 PSVPL-LGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdvVTTAEKLNPYA---YIPFSAGPRNC 447
Cdd:cd20677  310 SFVPFtIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERF--LDENGQLNKSLvekVLIFGMGVRKC 387
                        170
                 ....*....|....*...
gi 808351875 448 IGQKFAMLEIKAIVANVL 465
Cdd:cd20677  388 LGEDVARNEIFVFLTTIL 405
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
302-457 4.68e-12

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: 67.80  E-value: 4.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 302 DTFMfEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTpvsyELLNQLH--YVDLCVKETLRMYPSVPL-LG 378
Cdd:cd20663  237 DLFS-AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRP----EMADQARmpYTNAVIHEVQRFGDIVPLgVP 311
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808351875 379 RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFdVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEI 457
Cdd:cd20663  312 HMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHF-LDAQGHFVKPEAFMPFSAGRRACLGEPLARMEL 389
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
308-469 6.15e-12

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: 67.35  E-value: 6.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 308 GHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTPVSYEllNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCE 386
Cdd:cd20676  249 GFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDR--PQLPYLEAFILETFRHSSFVPFtIPHCTTRDTS 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 387 INGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF--DVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANV 464
Cdd:cd20676  327 LNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFltADGTEINKTESEKVMLFGLGKRRCIGESIARWEVFLFLAIL 406

                 ....*
gi 808351875 465 LRHYE 469
Cdd:cd20676  407 LQQLE 411
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
312-469 1.26e-11

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: 66.51  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 312 TSSALMFFFYNIATHPEA-QKKCFEEIRSVVGNdkSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEIN-- 388
Cdd:cd11071  241 FSALLPSLLARLGLAGEElHARLAEEIRSALGS--EGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIEsh 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 389 -GKL-IPAGTNI-GISPLYLgRREELFSEPNIFKPERFdvVTTAEKLNPYAYipFSAGP---------RNCIGQKFAMLE 456
Cdd:cd11071  319 dASYkIKKGELLvGYQPLAT-RDPKVFDNPDEFVPDRF--MGEEGKLLKHLI--WSNGPeteeptpdnKQCPGKDLVVLL 393
                        170
                 ....*....|...
gi 808351875 457 IKAIVANVLRHYE 469
Cdd:cd11071  394 ARLFVAELFLRYD 406
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
282-467 3.27e-11

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: 64.86  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 282 LLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEaqkkcfeEIRSVVGNDKSTPVsyellnqlhyvd 361
Cdd:cd11033  195 LANAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPD-------QWERLRADPSLLPT------------ 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 362 lCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIGispLYLG---RREELFSEpnifkPERFDVvttAEKLNPyaYI 438
Cdd:cd11033  256 -AVEEILRWASPVIHFRRTATRDTELGGQRIRAGDKVV---LWYAsanRDEEVFDD-----PDRFDI---TRSPNP--HL 321
                        170       180
                 ....*....|....*....|....*....
gi 808351875 439 PFSAGPRNCIGQKFAMLEIKAIVANVLRH 467
Cdd:cd11033  322 AFGGGPHFCLGAHLARLELRVLFEELLDR 350
PLN02774 PLN02774
brassinosteroid-6-oxidase
245-470 3.42e-11

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 65.18  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 245 KIIVQRREELIREGSSQESSNDDadvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIA 324
Cdd:PLN02774 223 KNIVRMLRQLIQERRASGETHTD----------MLGYLMRKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLH 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 325 THPEAQKKCFEE---IRSvvGNDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIgis 401
Cdd:PLN02774 293 DHPKALQELRKEhlaIRE--RKRPEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRI--- 367
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808351875 402 plYLGRRE-----ELFSEPNIFKPERFdvVTTAEKLNPYAYIpFSAGPRNCIGQKFAMLEIKAIVanvlrHYEV 470
Cdd:PLN02774 368 --YVYTREinydpFLYPDPMTFNPWRW--LDKSLESHNYFFL-FGGGTRLCPGKELGIVEISTFL-----HYFV 431
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
234-498 2.48e-10

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: 62.33  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 234 KALNV-LHQFTEKIIVQRREELiregssqessnddaDVGAKRKM--AFLDILLQ-STVDERPLSNLDIREEVDTFMF-EG 308
Cdd:cd20675  182 KQLNReFYNFVLDKVLQHRETL--------------RGGAPRDMmdAFILALEKgKSGDSGVGLDKEYVPSTVTDIFgAS 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 309 HDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKsTPvSYELLNQLHYVDLCVKETLRMYPSVPL-LGRKVLEDCEI 387
Cdd:cd20675  248 QDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDR-LP-CIEDQPNLPYVMAFLYEAMRFSSFVPVtIPHATTADTSI 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 388 NGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF-DVVTTAEKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVAnVLR 466
Cdd:cd20675  326 LGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFlDENGFLNKDLASSVMIFSVGKRRCIGEELSKMQLFLFTS-ILA 404
                        250       260       270
                 ....*....|....*....|....*....|..
gi 808351875 467 HyEVDFVGDSSEPPVLIAELILRTKePLMFKV 498
Cdd:cd20675  405 H-QCNFTANPNEPLTMDFSYGLTLK-PKPFTI 434
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
62-470 2.58e-10

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: 62.49  E-value: 2.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  62 HGDTFGLFLGPSYSVMLFNPRDVERVLgssqlltKSQEYSFLGR---------WLNEGLLVSNGRKWHR-RRKIITPAFH 131
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLCGTDAIREAL-------VDQAEAFSGRgtiavvdpiFQGYGVIFANGERWKTlRRFSLATMRD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 132 FRILEPYVEIFDRQSLR-LVEELalRISRGQErINLGEAIHLCALDAICETAMGVSINAQsnaDSEYVqavktismvlhk 210
Cdd:cd20672   74 FGMGKRSVEERIQEEAQcLVEEL--RKSKGAL-LDPTFLFQSITANIICSIVFGERFDYK---DPQFL------------ 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 211 RMFNILYRfdlTYMLtpLARAEKKALNVLHQF------TEKIIVQRREELIRE-GSSQESSNDDADVGAKRKmaFLDILL 283
Cdd:cd20672  136 RLLDLFYQ---TFSL--ISSFSSQVFELFSGFlkyfpgAHRQIYKNLQEILDYiGHSVEKHRATLDPSAPRD--FIDTYL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 284 QSTVDERPLSNLDIREE-----VDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKstPVSYELLNQLH 358
Cdd:cd20672  209 LRMEKEKSNHHTEFHHQnlmisVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHR--LPTLDDRAKMP 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVPL-LGRKVLEDCEINGKLIPAGTN---IGISPLYlgrREELFSEPNIFKPERFDVVTTAEKLNP 434
Cdd:cd20672  287 YTDAVIHEIQRFSDLIPIgVPHRVTKDTLFRGYLLPKNTEvypILSSALH---DPQYFEQPDTFNPDHFLDANGALKKSE 363
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 808351875 435 yAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEV 470
Cdd:cd20672  364 -AFMPFSTGKRICLGEGIARNELFLFFTTILQNFSV 398
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
78-483 2.68e-10

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: 61.85  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  78 LFNPRDVERVLG-----SSQLltkSQEYSFLGRWLNEG-LLVSNGRKwHRR-RKIITPAFHFRI---LEPYVEifdrqsl 147
Cdd:cd11032   17 VFRYADVKRVLSdpatfSSDL---GRLLPGEDDALTEGsLLTMDPPR-HRKlRKLVSQAFTPRLiadLEPRIA------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 148 RLVEELALRIsRGQERINLGE--AIHLCALdAICETaMGVSInaqsnADSEYVqavKTISMVlhkrmfnILYRFDLTYML 225
Cdd:cd11032   86 EITDELLDAV-DGRGEFDLVEdlAYPLPVI-VIAEL-LGVPA-----EDRELF---KKWSDA-------LVSGLGDDSFE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 226 TPLARAEKKALNVLHQFTEKIIVQRREELIregssqessnDDadvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFM 305
Cdd:cd11032  148 EEEVEEMAEALRELNAYLLEHLEERRRNPR----------DD----------LISRLVEAEVDGERLTDEEIVGFAILLL 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 306 FEGHDTTSSALMFFFYNIATHPEAQkkcfEEIRSvvgnDKStpvsyeLLNQLhyvdlcVKETLRMYPSVPLLGRKVLEDC 385
Cdd:cd11032  208 IAGHETTTNLLGNAVLCLDEDPEVA----ARLRA----DPS------LIPGA------IEEVLRYRPPVQRTARVTTEDV 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 386 EINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERfdvvttaeklNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVL 465
Cdd:cd11032  268 ELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR----------NPNPHLSFGHGIHFCLGAPLARLEARIALEALL 337
                        410
                 ....*....|....*...
gi 808351875 466 RHYEvDFVGDSSEPPVLI 483
Cdd:cd11032  338 DRFP-RIRVDPDVPLELI 354
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
321-479 3.45e-10

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: 61.93  E-value: 3.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 321 YNIATHPEAQKKCFEEIRSVVGN-------DKSTPVSYELLNQLHYVDLCVKETLRMyPSVPLLGRKVLEDCEIngKLIP 393
Cdd:cd20632  240 YYLLRHPEALAAVRDEIDHVLQStgqelgpDFDIHLTREQLDSLVYLESAINESLRL-SSASMNIRVVQEDFTL--KLES 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 394 AGTN-------IGISPLYLGRREELFSEPNIFKPERF--------DVVTTAEKLnPYAYIPFSAGPRNCIGQKFAMLEIK 458
Cdd:cd20632  317 DGSVnlrkgdiVALYPQSLHMDPEIYEDPEVFKFDRFvedgkkktTFYKRGQKL-KYYLMPFGSGSSKCPGRFFAVNEIK 395
                        170       180
                 ....*....|....*....|.
gi 808351875 459 AIVANVLRHYEVDFVGDSSEP 479
Cdd:cd20632  396 QFLSLLLLYFDLELLEEQKPP 416
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
68-456 1.02e-09

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: 60.26  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875  68 LFLGPSYSVMLFNPRDVERVLGSSQLL--TKSQEYSFLGRWLNEGLLVSNGRKW--------HRR-RKIITPAF---HFR 133
Cdd:cd20625    3 VHRSPLGAWVVTRHADVSAVLRDPRFGsdDPEAAPRRRGGEAALRPLARLLSRSmlfldppdHTRlRRLVSKAFtprAVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 134 ILEPYVEifdrqslRLVEELALRIsRGQERINLGEAihLCA---LDAICETaMGVSInaqsnADSEyvqavktismVLHK 210
Cdd:cd20625   83 RLRPRIE-------RLVDELLDRL-AARGRVDLVAD--FAYplpVRVICEL-LGVPE-----EDRP----------RFRG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 211 RMFNILYRFDLTYMLTPLARAEKkALNVLHQFTEKIIVQRREELiregssqessNDDadvgakrkmaFLDILLQSTVDER 290
Cdd:cd20625  137 WSAALARALDPGPLLEELARANA-AAAELAAYFRDLIARRRADP----------GDD----------LISALVAAEEDGD 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 291 PLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAqkkcFEEIRSvvgndksTPvsyELLNQLhyvdlcVKETLRM 370
Cdd:cd20625  196 RLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQ----LALLRA-------DP---ELIPAA------VEELLRY 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 371 YPSVPLLGRKVLEDCEINGKLIPAGTNIgisPLYLG---RREELFSEpnifkPERFDVvttAEKLNPyaYIPFSAGPRNC 447
Cdd:cd20625  256 DSPVQLTARVALEDVEIGGQTIPAGDRV---LLLLGaanRDPAVFPD-----PDRFDI---TRAPNR--HLAFGAGIHFC 322

                 ....*....
gi 808351875 448 IGQKFAMLE 456
Cdd:cd20625  323 LGAPLARLE 331
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
326-481 1.11e-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: 60.46  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 326 HPEAQKKCFEEIRSVVG------NDKSTPV--SYELLNQLHYVDLCVKETLRMYPSvPLLGRKVLEDCEI---NGK--LI 392
Cdd:cd20633  254 HPEAMKAVREEVEQVLKetgqevKPGGPLInlTRDMLLKTPVLDSAVEETLRLTAA-PVLIRAVVQDMTLkmaNGReyAL 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 393 PAGTNIGISP-LYLGRREELFSEPNIFKPERF---------DVVTTAEKLNpYAYIPFSAGPRNCIGQKFAMLEIKAIVA 462
Cdd:cd20633  333 RKGDRLALFPyLAVQMDPEIHPEPHTFKYDRFlnpdggkkkDFYKNGKKLK-YYNMPWGAGVSICPGRFFAVNEMKQFVF 411
                        170       180
                 ....*....|....*....|
gi 808351875 463 NVLRHYEVDFVGDSSE-PPV 481
Cdd:cd20633  412 LMLTYFDLELVNPDEEiPSI 431
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
120-468 4.60e-09

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: 58.21  E-value: 4.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 120 HRR-RKIITPAFHFRI---LEPYVEifdrqslRLVEELalrisrgqerinLGEAIHLCALDAICETAMGVSINAQSnads 195
Cdd:cd20630   66 HARvRKLVAPAFTPRAidrLRAEIQ-------AIVDQL------------LDELGEPEEFDVIREIAEHIPFRVIS---- 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 196 eyvqAVKTISMVLH---KRMFNILYRFDLTYM----LTPLARAEKKALNVLHQftekIIVQRREELIRegssqessnDDa 268
Cdd:cd20630  123 ----AMLGVPAEWDeqfRRFGTATIRLLPPGLdpeeLETAAPDVTEGLALIEE----VIAERRQAPVE---------DD- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 269 dvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCfeeirsvvgndKSTP 348
Cdd:cd20630  185 ---------LLTTLLRAEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKV-----------KAEP 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 349 vsyELLNQlhyvdlCVKETLRmYPSVPLLG--RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERfdvv 426
Cdd:cd20630  245 ---ELLRN------ALEEVLR-WDNFGKMGtaRYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR---- 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 808351875 427 ttaeklNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHY 468
Cdd:cd20630  311 ------DPNANIAFGYGPHFCIGAALARLELELAVSTLLRRF 346
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
292-482 5.64e-09

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: 58.16  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 292 LSNLDIREEVDT---FMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDKSTP--------VSYELLNQLHYV 360
Cdd:cd20631  220 LSTLDEMEKARThvaMLWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQKVsdggnpivLTREQLDDMPVL 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 361 DLCVKETLRMyPSVPLLGRKVLEDCEI---NGKL--IPAGTNIGISPLYLGRREELFSEPNIFKPERFDVVTTAEKLN-- 433
Cdd:cd20631  300 GSIIKEALRL-SSASLNIRVAKEDFTLhldSGESyaIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTfy 378
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 808351875 434 ------PYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRHYEVDFVGDSSEPPVL 482
Cdd:cd20631  379 kngrklKYYYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYFDMELLDGNAKCPPL 433
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
308-467 1.13e-08

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: 56.82  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 308 GHDTTSSALMFFFYNIATHPEAqkkcFEEIRSvvgnDKSTpvsyellnqlhyVDLCVKETLRMYPSVPLLGRKVLEDCEI 387
Cdd:cd11037  214 GLDTTISAIGNALWLLARHPDQ----WERLRA----DPSL------------APNAFEEAVRLESPVQTFSRTTTRDTEL 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 388 NGKLIPAGTNIGISPLYLGRREELFSEpnifkPERFDVvttaeKLNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLRH 467
Cdd:cd11037  274 AGVTIPAGSRVLVFLGSANRDPRKWDD-----PDRFDI-----TRNPSGHVGFGHGVHACVGQHLARLEGEALLTALARR 343
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
303-466 2.67e-08

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: 55.65  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 303 TFMFEGHDTTSSALMFFFYNIATHPEaqkkCFEEIRSvvgndkstpvSYELlnqlhyVDLCVKETLRMYPSVPLLG--RK 380
Cdd:cd11031  213 GLLVAGHETTASQIGNGVLLLLRHPE----QLARLRA----------DPEL------VPAAVEELLRYIPLGAGGGfpRY 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 381 VLEDCEINGKLIPAGTniGISPLYLG--RREELFSEPnifkpERFDVVTTAeklNPYayIPFSAGPRNCIGQKFAMLEIK 458
Cdd:cd11031  273 ATEDVELGGVTIRAGE--AVLVSLNAanRDPEVFPDP-----DRLDLDREP---NPH--LAFGHGPHHCLGAPLARLELQ 340

                 ....*...
gi 808351875 459 AIVANVLR 466
Cdd:cd11031  341 VALGALLR 348
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
219-468 9.02e-08

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 54.60  E-value: 9.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 219 FDLTYMLTPLARAE-KKALNVlhqftekIIVQRREEliregssqessnddADVGAKRKMAFLDILLQStvdERPLSNLDI 297
Cdd:PLN02987 213 FSTTYRRAIQARTKvAEALTL-------VVMKRRKE--------------EEEGAEKKKDMLAALLAS---DDGFSDEEI 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 298 REEVDTFMFEGHDTTSSALMFFFYNIATHPEAQ---KKCFEEIRSVVGNDKStpVSYELLNQLHYVDLCVKETLRMYPSV 374
Cdd:PLN02987 269 VDFLVALLVAGYETTSTIMTLAVKFLTETPLALaqlKEEHEKIRAMKSDSYS--LEWSDYKSMPFTQCVVNETLRVANII 346
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 375 PLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERF--DVVTTAEKlnpYAYIPFSAGPRNCIGQKF 452
Cdd:PLN02987 347 GGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWqsNSGTTVPS---NVFTPFGGGPRLCPGYEL 423
                        250
                 ....*....|....*.
gi 808351875 453 AMLEIKAIVANVLRHY 468
Cdd:PLN02987 424 ARVALSVFLHRLVTRF 439
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
278-466 1.51e-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: 53.67  E-value: 1.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 278 FLDILLQSTVDERplsnlDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKCFEEIRSVVGNDkstPVSYELLNQL 357
Cdd:cd20627  189 FIDSLLQGNLSEQ-----QVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGKG---PITLEKIEQL 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 358 HYVDLCVKETLRMYPSVPLLGRkvLEDCE--INGKLIPAGTNIgispLY-LG---RREELFSEPNIFKPERFDVVTTAEK 431
Cdd:cd20627  261 RYCQQVLCETVRTAKLTPVSAR--LQELEgkVDQHIIPKETLV----LYaLGvvlQDNTTWPLPYRFDPDRFDDESVMKS 334
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 808351875 432 LnpyAYIPFSaGPRNCIGQKFAMLEIKAIVANVLR 466
Cdd:cd20627  335 F---SLLGFS-GSQECPELRFAYMVATVLLSVLVR 365
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
325-481 1.84e-07

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 53.22  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 325 THPEAQKKCFEEIRSVVGNDKSTPVSYELLNQLHY-----VDLCVKETLRMyPSVPLLGRKVLED---CEINGK------ 390
Cdd:cd20634  250 KHPEAMAAVRGEIQRIKHQRGQPVSQTLTINQELLdntpvFDSVLSETLRL-TAAPFITREVLQDmklRLADGQeynlrr 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 391 -----LIPAgtnigISPlylGRREELFSEPNIFKPERFDVVTTAEKLN--------PYAYIPFSAGPRNCIGQKFAMLEI 457
Cdd:cd20634  329 gdrlcLFPF-----LSP---QMDPEIHQEPEVFKYDRFLNADGTEKKDfykngkrlKYYNMPWGAGDNVCIGRHFAVNSI 400
                        170       180
                 ....*....|....*....|....
gi 808351875 458 KAIVANVLRHYEVDFVGDSSEPPV 481
Cdd:cd20634  401 KQFVFLILTHFDVELKDPEAEIPE 424
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
230-457 2.67e-07

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 52.82  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 230 RAEKKALnvlhQFTEKIIVQRREELIREGSSQESSNDDAdvgakrkmafLDILLQSTVDERPlSNLDIREEVDtFMFEGH 309
Cdd:PLN03141 201 QAKKRMV----KLVKKIIEEKRRAMKNKEEDETGIPKDV----------VDVLLRDGSDELT-DDLISDNMID-MMIPGE 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 310 DTTSSALMFFFYNIATHPEAQKKCFEE---IRSVvGNDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCE 386
Cdd:PLN03141 265 DSVPVLMTLAVKFLSDCPVALQQLTEEnmkLKRL-KADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVE 343
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808351875 387 INGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERFDvvttAEKLNPYAYIPFSAGPRNCIGQKFAMLEI 457
Cdd:PLN03141 344 IKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQ----EKDMNNSSFTPFGGGQRLCPGLDLARLEA 410
PLN02648 PLN02648
allene oxide synthase
327-490 2.73e-07

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 53.01  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 327 PEAQKKCFEEIRSVVGnDKSTPVSYELLNQLHYVDLCVKETLRMYPSVPLLGRKVLEDCEIN----------GKLIpagt 396
Cdd:PLN02648 304 EELQARLAEEVRSAVK-AGGGGVTFAALEKMPLVKSVVYEALRIEPPVPFQYGRAREDFVIEshdaafeikkGEML---- 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 397 nIGISPLYLgRREELFSEPNIFKPERFdVVTTAEKLNPYAYipFSAGP---------RNCIGQKFAMLEIKAIVANVLRH 467
Cdd:PLN02648 379 -FGYQPLVT-RDPKVFDRPEEFVPDRF-MGEEGEKLLKYVF--WSNGRetesptvgnKQCAGKDFVVLVARLFVAELFLR 453
                        170       180
                 ....*....|....*....|....*.
gi 808351875 468 Y---EVDFVGDSSEPPVLIAELILRT 490
Cdd:PLN02648 454 YdsfEIEVDTSGLGSSVTFTSLKKAS 479
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
272-466 5.95e-07

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: 51.57  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 272 AKRKMAFLDILLQSTVDERplsnldIREEVDTFMFEGHDTTSSALM----FFFyniathPEAQKKCFEEIRSvvgNDKST 347
Cdd:cd20612  169 AQAAAARLGALLDAAVADE------VRDNVLGTAVGGVPTQSQAFAqildFYL------RRPGAAHLAEIQA---LAREN 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 348 PVSYELLnqLHYVdlcvKETLRMYPSVPLLGRKVLEDCEI-----NGKLIPAGTNIGISPLYLGRREELFSEPNIFKPER 422
Cdd:cd20612  234 DEADATL--RGYV----LEALRLNPIAPGLYRRATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR 307
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 808351875 423 fdvvttaeklNPYAYIPFSAGPRNCIGQKFAMLEIKAIVANVLR 466
Cdd:cd20612  308 ----------PLESYIHFGHGPHQCLGEEIARAALTEMLRVVLR 341
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
359-439 1.42e-05

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: 47.14  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 359 YVDLCVKETLRMYPSVPLLGRKVLEDCEINGKLIPAG---------TNigisplylgRREELFSEPNIFKPERFdvvtTA 429
Cdd:cd11067  264 YAEAFVQEVRRFYPFFPFVGARARRDFEWQGYRFPKGqrvlldlygTN---------HDPRLWEDPDRFRPERF----LG 330
                         90
                 ....*....|
gi 808351875 430 EKLNPYAYIP 439
Cdd:cd11067  331 WEGDPFDFIP 340
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
282-469 1.71e-05

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: 46.96  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 282 LLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKkcfeeirsvvgndkstpvsyELLNQLHYVD 361
Cdd:cd11079  169 LLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQA--------------------RLRANPALLP 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 362 LCVKETLRMYpsVPLLG--RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEPNIFKPERfdvvttaeklNPYAYIP 439
Cdd:cd11079  229 AAIDEILRLD--DPFVAnrRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR----------HAADNLV 296
                        170       180       190
                 ....*....|....*....|....*....|
gi 808351875 440 FSAGPRNCIGQKFAMLEIKAIVANVLRHYE 469
Cdd:cd11079  297 YGRGIHVCPGAPLARLELRILLEELLAQTE 326
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
121-466 5.90e-05

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: 45.21  E-value: 5.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 121 RRRKIITPAF---HFRILEPYVE-IFDRQ---------SLRLVEELALRI-SRgqerinlgeaihlcaldAICETaMGVS 186
Cdd:cd11030   79 RLRRMLAPEFtvrRVRALRPRIQeIVDELldameaagpPADLVEAFALPVpSL-----------------VICEL-LGVP 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 187 inaqsNADSEYVQavktismvlhkRMFNILYRFDLTymltplARAEKKALNVLHQFTEKIIVQRREE--------LIREG 258
Cdd:cd11030  141 -----YEDREFFQ-----------RRSARLLDLSST------AEEAAAAGAELRAYLDELVARKRREpgddllsrLVAEH 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 259 SSQESSNDDADVGakrkMAFLdiLLqstvderplsnldireevdtfmFEGHDTTSSALMFFFYNIATHPEAqkkcFEEIR 338
Cdd:cd11030  199 GAPGELTDEELVG----IAVL--LL----------------------VAGHETTANMIALGTLALLEHPEQ----LAALR 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 339 svvgNDKStpvsyellnqlhYVDLCVKETLRmYPSVPLLG--RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEpn 416
Cdd:cd11030  247 ----ADPS------------LVPGAVEELLR-YLSIVQDGlpRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPD-- 307
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 808351875 417 ifkPERFDVVTTAEKlnpyaYIPFSAGPRNCIGQKFAMLEIKAIVANVLR 466
Cdd:cd11030  308 ---PDRLDITRPARR-----HLAFGHGVHQCLGQNLARLELEIALPTLFR 349
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
103-456 7.35e-05

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: 44.83  E-value: 7.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 103 LGRWLNEGLLVSNGRKwHRR-RKIITPAF-HFRI--LEPYVEifdrqslRLVEELaLRISRGQERINLGEA-IHLCALDA 177
Cdd:cd11029   65 LPPVLSDNMLTSDPPD-HTRlRRLVAKAFtPRRVeaLRPRIE-------EITDEL-LDALAARGVVDLVADfAYPLPITV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 178 ICETaMGVSinaqsNADSEYVQavktismvlhkRMFNILYRFDltymlTPLARAEKkALNVLHQFTEKIIVQRREELire 257
Cdd:cd11029  136 ICEL-LGVP-----EEDRDRFR-----------RWSDALVDTD-----PPPEEAAA-ALRELVDYLAELVARKRAEP--- 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 258 gssqessNDDadvgakrkmaFLDILLQSTVDERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAqkkcFEEI 337
Cdd:cd11029  190 -------GDD----------LLSALVAARDEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQ----LALL 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 338 RSvvgndksTPvsyELLNQLhyvdlcVKETLRMYPSVPLLG-RKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSEpn 416
Cdd:cd11029  249 RA-------DP---ELWPAA------VEELLRYDGPVALATlRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPD-- 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 808351875 417 ifkPERFDVVTTAEklnpyAYIPFSAGPRNCIGQKFAMLE 456
Cdd:cd11029  311 ---PDRLDITRDAN-----GHLAFGHGIHYCLGAPLARLE 342
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
289-465 4.40e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 42.49  E-value: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 289 ERPLSNLDIREEVDTFMFEGHDTTSSALMFFFYNIATHPEAQKKcfeeirsVVGNDKSTPVSYEllnqlhyvdlcvkETL 368
Cdd:cd11039  195 GMPMSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAE-------VMAGDVHWLRAFE-------------EGL 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 369 RMYPSVPLLGRKVLEDCEINGKLIPAGTNIGISPLYLGRREELFSepnifKPERFDVVTTAEKlnpyaYIPFSAGPRNCI 448
Cdd:cd11039  255 RWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFE-----NPDRFDVFRPKSP-----HVSFGAGPHFCA 324
                        170
                 ....*....|....*..
gi 808351875 449 GQKFAMLEIKAIVANVL 465
Cdd:cd11039  325 GAWASRQMVGEIALPEL 341
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
364-467 6.50e-04

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 42.09  E-value: 6.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 364 VKETLRMYPSVPLLGRKVLEDCEINGKLIPAGTNIgispLYL----GRREELFSEpnifkPERFDVVTTAEklnpyAYIP 439
Cdd:cd11036  225 VAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHV----VVLlaaaNRDPEAFPD-----PDRFDLGRPTA-----RSAH 290
                         90       100
                 ....*....|....*....|....*...
gi 808351875 440 FSAGPRNCIGQKFAMLEIKAIVANVLRH 467
Cdd:cd11036  291 FGLGRHACLGAALARAAAAAALRALAAR 318
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
364-466 7.88e-04

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: 41.62  E-value: 7.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808351875 364 VKETLRMYPSVPLLGRKVLEDCEINGKLIPAgtNIgispLYLGRREELF-SEPNIFKPERFDVVTTAEKLnpyAYIPFSA 442
Cdd:cd20626  262 VKEALRLYPPTRRIYRAFQRPGSSKPEIIAA--DI----EACHRSESIWgPDALEFNPSRWSKLTPTQKE---AFLPFGS 332
                         90       100
                 ....*....|....*....|....*
gi 808351875 443 GPRNCIGQK-FAMLEIKAIVANVLR 466
Cdd:cd20626  333 GPFRCPAKPvFGPRMIALLVGALLD 357
 
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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