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Conserved domains on  [gi|1063712834|ref|NP_001327676|]
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cytochrome P450, family 705, subfamily A, polypeptide 33 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
74-504 0e+00

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: 744.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20655     1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKiFFASVLR 233
Cdd:cd20655    81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESAELAGK-FNASDFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 234 RLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKD--TDMMDVLLAAYADENAEYKITRNHIKSFFVELFVG 311
Cdd:cd20655   160 WPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRKEGgsKDLLDILLDAYEDENAEYKITRNHIKAFILDLFIA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 312 GTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKG 391
Cdd:cd20655   240 GTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKING 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 392 FYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQ-VDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVM 470
Cdd:cd20655   320 YDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQeLDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAM 399
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1063712834 471 VQCFDW-GIKGDKINMEETfEGLTLTMVHPIKCTP 504
Cdd:cd20655   400 VQCFDWkVGDGEKVNMEEA-SGLTLPRAHPLKCVP 433
 
Name Accession Description Interval E-value
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
74-504 0e+00

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: 744.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20655     1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKiFFASVLR 233
Cdd:cd20655    81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESAELAGK-FNASDFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 234 RLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKD--TDMMDVLLAAYADENAEYKITRNHIKSFFVELFVG 311
Cdd:cd20655   160 WPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRKEGgsKDLLDILLDAYEDENAEYKITRNHIKAFILDLFIA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 312 GTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKG 391
Cdd:cd20655   240 GTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKING 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 392 FYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQ-VDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVM 470
Cdd:cd20655   320 YDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQeLDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAM 399
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1063712834 471 VQCFDW-GIKGDKINMEETfEGLTLTMVHPIKCTP 504
Cdd:cd20655   400 VQCFDWkVGDGEKVNMEEA-SGLTLPRAHPLKCVP 433
PLN02687 PLN02687
flavonoid 3'-monooxygenase
69-510 1.84e-101

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 314.83  E-value: 1.84e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  69 ISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRP 148
Cdd:PLN02687   62 LAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 149 QVLERSRGLRAEELQrLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRS-FSEENGE-AERVRGLVAESYALAKkI 226
Cdd:PLN02687  142 KALDDFRHVREEEVA-LLVRELARQHGTAPVNLGQLVNVCTTNALGRAMVGRRvFAGDGDEkAREFKEMVVELMQLAG-V 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 227 F----FASVLRRL--------LKKLRiplfkkdimdvsNRFNELLEKILVEHN-EKLDEEHKDTDMMDVLLAAYADENA- 292
Cdd:PLN02687  220 FnvgdFVPALRWLdlqgvvgkMKRLH------------RRFDAMMNGIIEEHKaAGQTGSEEHKDLLSTLLALKREQQAd 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 293 --EYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGL 370
Cdd:PLN02687  288 geGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETF 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 371 RLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFL-GSSRLGqVDEREEAQKYIPFGG 448
Cdd:PLN02687  368 RLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpGGEHAG-VDVKGSDFELIPFGA 446
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712834 449 GRRGCPGANLASIFVGTAIGVMVQCFDW----GIKGDKINMEETFeGLTLTMVHPIKCTPIPRTLP 510
Cdd:PLN02687  447 GRRICAGLSWGLRMVTLLTATLVHAFDWeladGQTPDKLNMEEAY-GLTLQRAVPLMVHPRPRLLP 511
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
72-495 1.02e-68

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: 227.93  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAI--DESLVFGSSGVVYAPYGDYlKFVKKIIATKLLRPQ 149
Cdd:pfam00067  32 KYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfaTSRGPFLGKGIVFANGPRW-RQLRRFLTPTFTSFG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 150 VLE-RSRglRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSF-SEENGEAERVRGLVAESYALAKKIF 227
Cdd:pfam00067 111 KLSfEPR--VEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFgSLEDPKFLELVKAVQELSSLLSSPS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 228 FASVLR-RLLKKLRIPLFKKdIMDVSNRFNELLEKILVEHNEKLD-EEHKDTDMMDVLLAAYADENAEyKITRNHIKSFF 305
Cdd:pfam00067 189 PQLLDLfPILKYFPGPHGRK-LKRARKKIKDLLDKLIEERRETLDsAKKSPRDFLDALLLAKEEEDGS-KLTDEELRATV 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 306 VELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFP-LLTRKFE 384
Cdd:pfam00067 267 LELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVT 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 385 ERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQK---YIPFGGGRRGCPGANLASI 461
Cdd:pfam00067 347 KDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFL--------DENGKFRKsfaFLPFGAGPRNCLGERLARM 418
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1063712834 462 FVGTAIGVMVQCFDW-GIKGDKINMEETFEGLTLT 495
Cdd:pfam00067 419 EMKLFLATLLQNFEVeLPPGTDPPDIDETPGLLLP 453
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
72-459 4.58e-36

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: 138.49  E-value: 4.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYApYGDYLKFVKKIIAtKLLRPQVL 151
Cdd:COG2124    30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTL-DGPEHTRLRRLVQ-PAFTPRRV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 152 ERSRglraEELQRLYNRILDKAKMNENVEIGKE-ATMLMNNIFCRMsmgrsFSEENGEAERVRGLVAEsyalakkiFFAS 230
Cdd:COG2124   108 AALR----PRIREIADELLDRLAARGPVDLVEEfARPLPVIVICEL-----LGVPEEDRDRLRRWSDA--------LLDA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 231 VLRRLLKKLRiplfkkDIMDVSNRFNELLEKILVEHnekldEEHKDTDMMDVLLAAYADENaeyKITRNHIKSFFVELFV 310
Cdd:COG2124   171 LGPLPPERRR------RARRARAELDAYLRELIAER-----RAEPGDDLLSALLAARDDGE---RLSDEELRDELLLLLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 311 GGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqetdipnLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIK 390
Cdd:COG2124   237 AGHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDVELG 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712834 391 GFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:COG2124   299 GVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR--------------PPNAHLPFGGGPHRCLGAALA 353
 
Name Accession Description Interval E-value
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
74-504 0e+00

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: 744.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20655     1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKiFFASVLR 233
Cdd:cd20655    81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESAELAGK-FNASDFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 234 RLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKD--TDMMDVLLAAYADENAEYKITRNHIKSFFVELFVG 311
Cdd:cd20655   160 WPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRKEGgsKDLLDILLDAYEDENAEYKITRNHIKAFILDLFIA 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 312 GTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKG 391
Cdd:cd20655   240 GTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKING 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 392 FYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQ-VDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVM 470
Cdd:cd20655   320 YDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQeLDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAM 399
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1063712834 471 VQCFDW-GIKGDKINMEETfEGLTLTMVHPIKCTP 504
Cdd:cd20655   400 VQCFDWkVGDGEKVNMEEA-SGLTLPRAHPLKCVP 433
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
74-500 3.36e-142

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: 416.18  E-value: 3.36e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20618     1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKRLES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFS----EENGEAERVRGLVAESYALAKKIFFA 229
Cdd:cd20618    81 FQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFgeseKESEEAREFKELIDEAFELAGAFNIG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 230 SVLRrLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAYaDENAEYKITRNHIKSFFVELF 309
Cdd:cd20618   161 DYIP-WLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLL-DLDGEGKLSDDNIKALLLDML 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 310 VGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT-RKFEERCE 388
Cdd:cd20618   239 AAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLpHESTEDCK 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 389 IKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlgqVDE-REEAQKYIPFGGGRRGCPGANLASIFVGTAI 467
Cdd:cd20618   319 VAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESD----IDDvKGQDFELLPFGSGRRMCPGMPLGLRMVQLTL 394
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1063712834 468 GVMVQCFDW---GIKGDKINMEETFeGLTLTMVHPI 500
Cdd:cd20618   395 ANLLHGFDWslpGPKPEDIDMEEKF-GLTVPRAVPL 429
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
72-499 1.30e-129

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: 384.12  E-value: 1.30e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVL 151
Cdd:cd11072     1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAKRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 152 ERSRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEENGEaeRVRGLVAESYALAKKIFFASV 231
Cdd:cd11072    81 QSFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQD--KFKELVKEALELLGGFSVGDY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 232 LRRLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAA-YADENAEYKITRNHIKSFFVELFV 310
Cdd:cd11072   159 FPSLGWIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRlQKEGDLEFPLTRDNIKAIILDMFL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 311 GGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT-RKFEERCEI 389
Cdd:cd11072   239 AGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLpRECREDCKI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 390 KGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlgqVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGV 469
Cdd:cd11072   319 NGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSS----IDFKGQDFELIPFGAGRRICPGITFGLANVELALAN 394
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1063712834 470 MVQCFDW----GIKGDKINMEETFeGLTLTMVHP 499
Cdd:cd11072   395 LLYHFDWklpdGMKPEDLDMEEAF-GLTVHRKNP 427
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
70-504 1.14e-121

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: 363.78  E-value: 1.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  70 SSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQ 149
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 150 VLERSRGLRAEELQRLYNRILDKAKMNENVEIGKEA--TML--MNNIFCRMSMgrsFSEENGEAERVRGLVAESYALAKK 225
Cdd:cd11073    81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAflTSLnlISNTLFSVDL---VDPDSESGSEFKELVREIMELAGK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 226 I----FFaSVLRRL-LKKLRiplfkKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAYADENAEYKITRNH 300
Cdd:cd11073   158 PnvadFF-PFLKFLdLQGLR-----RRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSESELTRNH 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT 380
Cdd:cd11073   232 IKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 381 -RKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlgqVDEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11073   312 pRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSE----IDFKGRDFELIPFGSGRRICPGLPLA 387
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1063712834 460 SIFVGTAIGVMVQCFDW----GIKGDKINMEETFeGLTLTMVHPIKCTP 504
Cdd:cd11073   388 ERMVHLVLASLLHSFDWklpdGMKPEDLDMEEKF-GLTLQKAVPLKAIP 435
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
74-507 1.64e-108

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: 330.15  E-value: 1.64e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20657     1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMG-RSFSEENG-EAERVRGLVAESYALAkKIF---- 227
Cdd:cd20657    81 WAHVRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSkRVFAAKAGaKANEFKEMVVELMTVA-GVFnigd 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 228 FASVLRRL--------LKKLRiplfkkdimdvsNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAYADENAEYKITRN 299
Cdd:cd20657   160 FIPSLAWMdlqgvekkMKRLH------------KRFDALLTKILEEHKATAQERKGKPDFLDFVLLENDDNGEGERLTDT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 300 HIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL- 378
Cdd:cd20657   228 NIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLn 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgSSRLGQVDEREEAQKYIPFGGGRRGCPGANL 458
Cdd:cd20657   308 LPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFL-PGRNAKVDVRGNDFELIPFGAGRRICAGTRM 386
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 459 ASIFVGTAIGVMVQCFDWGIKG----DKINMEETFeGLTLTMVHPIKCTPIPR 507
Cdd:cd20657   387 GIRMVEYILATLVHSFDWKLPAgqtpEELNMEEAF-GLALQKAVPLVAHPTPR 438
PLN02687 PLN02687
flavonoid 3'-monooxygenase
69-510 1.84e-101

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 314.83  E-value: 1.84e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  69 ISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRP 148
Cdd:PLN02687   62 LAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSA 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 149 QVLERSRGLRAEELQrLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRS-FSEENGE-AERVRGLVAESYALAKkI 226
Cdd:PLN02687  142 KALDDFRHVREEEVA-LLVRELARQHGTAPVNLGQLVNVCTTNALGRAMVGRRvFAGDGDEkAREFKEMVVELMQLAG-V 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 227 F----FASVLRRL--------LKKLRiplfkkdimdvsNRFNELLEKILVEHN-EKLDEEHKDTDMMDVLLAAYADENA- 292
Cdd:PLN02687  220 FnvgdFVPALRWLdlqgvvgkMKRLH------------RRFDAMMNGIIEEHKaAGQTGSEEHKDLLSTLLALKREQQAd 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 293 --EYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGL 370
Cdd:PLN02687  288 geGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETF 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 371 RLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFL-GSSRLGqVDEREEAQKYIPFGG 448
Cdd:PLN02687  368 RLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpGGEHAG-VDVKGSDFELIPFGA 446
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712834 449 GRRGCPGANLASIFVGTAIGVMVQCFDW----GIKGDKINMEETFeGLTLTMVHPIKCTPIPRTLP 510
Cdd:PLN02687  447 GRRICAGLSWGLRMVTLLTATLVHAFDWeladGQTPDKLNMEEAY-GLTLQRAVPLMVHPRPRLLP 511
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
74-500 2.29e-100

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: 308.76  E-value: 2.29e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20653     1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMN-ENVEIGKEATMLMNNIFCRMSMGRSFSEENG----EAERVRGLVAESYALAKKIFF 228
Cdd:cd20653    81 FSSIRRDEIRRLLKRLARDSKGGfAKVELKPLFSELTFNNIMRMVAGKRYYGEDVsdaeEAKLFRELVSEIFELSGAGNP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 229 ASVLRrLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKldEEHKDTDMMDVLLAAYADENAEYkiTRNHIKSFFVEL 308
Cdd:cd20653   161 ADFLP-ILRWFDFQGLEKRVKKLAKRRDAFLQGLIDEHRKN--KESGKNTMIDHLLSLQESQPEYY--TDEIIKGLILVM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 309 FVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT-RKFEERC 387
Cdd:cd20653   236 LLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVpHESSEDC 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 388 EIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGssrlgqvdEREEAQKYIPFGGGRRGCPGANLASIFVGTAI 467
Cdd:cd20653   316 KIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEG--------EEREGYKLIPFGLGRRACPGAGLAQRVVGLAL 387
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1063712834 468 GVMVQCFDW-GIKGDKINMEETfEGLTLTMVHPI 500
Cdd:cd20653   388 GSLIQCFEWeRVGEEEVDMTEG-KGLTMPKAIPL 420
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
74-507 1.05e-91

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: 287.20  E-value: 1.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20654     1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQ----RLYNRILDKAKMNEN--VEIGKEATMLMNNIFCRMSMG-RSFS----EENGEAERVRGLVAESYAL 222
Cdd:cd20654    81 LKHVRVSEVDtsikELYSLWSNNKKGGGGvlVEMKQWFADLTFNVILRMVVGkRYFGgtavEDDEEAERYKKAIREFMRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 223 AKkIFFASVLRRLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHK---DTDMMDVLLAAYADENAEYKITRN 299
Cdd:cd20654   161 AG-TFVVSDAIPFLGWLDFGGHEKAMKRTAKELDSILEEWLEEHRQKRSSSGKsknDEDDDDVMMLSILEDSQISGYDAD 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 300 H-IKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL 378
Cdd:cd20654   240 TvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPL 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LT-RKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRlgQVDEREEAQKYIPFGGGRRGCPGAN 457
Cdd:cd20654   320 LGpREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHK--DIDVRGQNFELIPFGSGRRSCPGVS 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 458 LASIFVGTAIGVMVQCFDwgIK---GDKINMEETFeGLTLTMVHPIKCTPIPR 507
Cdd:cd20654   398 FGLQVMHLTLARLLHGFD--IKtpsNEPVDMTEGP-GLTNPKATPLEVLLTPR 447
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
68-510 6.64e-89

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 281.74  E-value: 6.64e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  68 KISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLR 147
Cdd:PLN00110   58 KMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLG 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 148 PQVLERSRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRS-FSEENGEAERVRGLVAESYALAKKI 226
Cdd:PLN00110  138 GKALEDWSQVRTVELGHMLRAMLELSQRGEPVVVPEMLTFSMANMIGQVILSRRvFETKGSESNEFKDMVVELMTTAGYF 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 227 ----FFASV-------LRRLLKKLRiplfkkdimdvsNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAYADENAEyK 295
Cdd:PLN00110  218 nigdFIPSIawmdiqgIERGMKHLH------------KKFDKLLTRMIEEHTASAHERKGNPDFLDVVMANQENSTGE-K 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 296 ITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPP 375
Cdd:PLN00110  285 LTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPS 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 376 FPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgSSRLGQVDEREEAQKYIPFGGGRRGCP 454
Cdd:PLN00110  365 TPLnLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFL-SEKNAKIDPRGNDFELIPFGAGRRICA 443
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712834 455 GANLASIFVGTAIGVMVQCFDWGI-KGDKINMEETFeGLTLTMVHPIKCTPIPRTLP 510
Cdd:PLN00110  444 GTRMGIVLVEYILGTLVHSFDWKLpDGVELNMDEAF-GLALQKAVPLSAMVTPRLHQ 499
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
72-510 1.14e-84

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 271.31  E-value: 1.14e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVL 151
Cdd:PLN03112   63 KYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTLAAVHLAYGCGDVALAPLGPHWKRMRRICMEHLLTTKRL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 152 ERSRGLRAEELQRLYNRILDKAKMNENVEIgKE--ATMLMNNIfCRMSMGRSF----SEENGEAERVRGLVAESYALAKK 225
Cdd:PLN03112  143 ESFAKHRAEEARHLIQDVWEAAQTGKPVNL-REvlGAFSMNNV-TRMLLGKQYfgaeSAGPKEAMEFMHITHELFRLLGV 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 226 IFfasvLRRLLKKLR-IPL--FKKDIMDVSNRFNELLEKILVEH----NEKLDEEhKDTDMMDVLLAaYADENAEYKITR 298
Cdd:PLN03112  221 IY----LGDYLPAWRwLDPygCEKKMREVEKRVDEFHDKIIDEHrrarSGKLPGG-KDMDFVDVLLS-LPGENGKEHMDD 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 299 NHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL 378
Cdd:PLN03112  295 VEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPF 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LT-RKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFL--GSSRLGQVDEREeaQKYIPFGGGRRGCPG 455
Cdd:PLN03112  375 LIpHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWpaEGSRVEISHGPD--FKILPFSAGKRKCPG 452
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712834 456 ANLASIFVGTAIGVMVQCFDW----GIKGDKINMEETFeGLTLTMVHPIKCTPIPRTLP 510
Cdd:PLN03112  453 APLGVTMVLMALARLFHCFDWsppdGLRPEDIDTQEVY-GMTMPKAKPLRAVATPRLAP 510
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
72-501 2.01e-77

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: 249.85  E-value: 2.01e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLV-FGSSGVVYAPYGDYLKFVKKIIATKLLRPQV 150
Cdd:cd11075     1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLFsSNKHMVNSSPYGPLWRTLRRNLVSEVLSPSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 151 LERSRGLRAEELQRLYNRILDKAKMNEN-VEIGKEATMLMNNIFCRMSMGRSFSEEngeaeRVRGLVAESYALAKKI--- 226
Cdd:cd11075    81 LKQFRPARRRALDNLVERLREEAKENPGpVNVRDHFRHALFSLLLYMCFGERLDEE-----TVRELERVQRELLLSFtdf 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 227 ----FFASVLRRLLKKlriplFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAYADENAE---YKITRN 299
Cdd:cd11075   156 dvrdFFPALTWLLNRR-----RWKKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFLLLDLLDLKEEggeRKLTDE 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 300 HIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPP-FPL 378
Cdd:cd11075   231 ELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPgHFL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQVDEREEAQKYIPFGGGRRGCPGANL 458
Cdd:cd11075   311 LPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAADIDTGSKEIKMMPFGAGRRICPGLGL 390
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1063712834 459 ASIFVGTAIGVMVQCFDWG-IKGDKINMEETFEgLTLTMVHPIK 501
Cdd:cd11075   391 ATLHLELFVARLVQEFEWKlVEGEEVDFSEKQE-FTVVMKNPLR 433
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
73-501 1.20e-72

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: 237.38  E-value: 1.20e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLE 152
Cdd:cd20656     1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 153 RSRGLRAEELQRLYNRILDKAKMNEN----VEIGKEATMLMNNIFCRMSMGRSFSEENGEAER----VRGLVAE------ 218
Cdd:cd20656    81 SLRPIREDEVTAMVESIFNDCMSPENegkpVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEqgveFKAIVSNglklga 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 219 SYALAKKIFFasvLRRLLkklriPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAyadeNAEYKITR 298
Cdd:cd20656   161 SLTMAEHIPW---LRWMF-----PLSEKAFAKHGARRDRLTKAIMEEHTLARQKSGGGQQHFVALLTL----KEQYDLSE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 299 NHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL 378
Cdd:cd20656   229 DTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPL 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 -LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSsrlgQVDEREEAQKYIPFGGGRRGCPGAN 457
Cdd:cd20656   309 mLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEE----DVDIKGHDFRLLPFGAGRRVCPGAQ 384
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1063712834 458 LASIFVGTAIGVMVQCFDW----GIKGDKINMEETfEGLTLTMVHPIK 501
Cdd:cd20656   385 LGINLVTLMLGHLLHHFSWtppeGTPPEEIDMTEN-PGLVTFMRTPLQ 431
PLN02183 PLN02183
ferulate 5-hydroxylase
68-507 4.50e-71

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 235.51  E-value: 4.50e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  68 KISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLR 147
Cdd:PLN02183   63 NLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKLFS 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 148 PQVLERSRGLRaEELQRLYNRIldKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEenGEAERVRGLVAESyalakKIF 227
Cdd:PLN02183  143 RKRAESWASVR-DEVDSMVRSV--SSNIGKPVNIGELIFTLTRNITYRAAFGSSSNE--GQDEFIKILQEFS-----KLF 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 228 FASVLRRLLKKL---RIPLFKKDIMDVSNRFNELLEKILVEHNEKL-------DEEHKDTDMMDVLLAAYADE------- 290
Cdd:PLN02183  213 GAFNVADFIPWLgwiDPQGLNKRLVKARKSLDGFIDDIIDDHIQKRknqnadnDSEEAETDMVDDLLAFYSEEakvnesd 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 291 --NAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKE 368
Cdd:PLN02183  293 dlQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKE 372
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 369 GLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssRLGQVDEREEAQKYIPFGG 448
Cdd:PLN02183  373 TLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFL---KPGVPDFKGSHFEFIPFGS 449
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 449 GRRGCPGANLASIFVGTAIGVMVQCFDW----GIKGDKINMEETFeGLTLTMVHPIKCTPIPR 507
Cdd:PLN02183  450 GRRSCPGMQLGLYALDLAVAHLLHCFTWelpdGMKPSELDMNDVF-GLTAPRATRLVAVPTYR 511
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
74-496 4.93e-71

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: 232.49  E-value: 4.93e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLvFGSSGVVYApYGDYLKFVKKIIATKLLRPQVLER 153
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEII-SGGKGILFS-NGDYWKELRRFALSSLTKTKLKKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEEN-GEAERVRGLVAESYALAKKIFFASVL 232
Cdd:cd20617    79 MEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDdGEFLKLVKPIEEIFKELGSGNPSDFI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 233 rrLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEhKDTDMMDVLLAAYADENAEYKITRNHIKSFFVELFVGG 312
Cdd:cd20617   159 --PILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPN-NPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLFLAG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 313 TDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKG 391
Cdd:cd20617   236 TDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLgLPRVTTEDTEIGG 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 392 FYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQVDEreeaqkYIPFGGGRRGCPGANLASIFVGTAIGVMV 471
Cdd:cd20617   316 YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSEQ------FIPFGIGKRNCVGENLARDELFLFFANLL 389
                         410       420
                  ....*....|....*....|....*
gi 1063712834 472 QCFDWGIKGDKINMEETFEGLTLTM 496
Cdd:cd20617   390 LNFKFKSSDGLPIDEKEVFGLTLKP 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
72-495 1.02e-68

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: 227.93  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAI--DESLVFGSSGVVYAPYGDYlKFVKKIIATKLLRPQ 149
Cdd:pfam00067  32 KYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfaTSRGPFLGKGIVFANGPRW-RQLRRFLTPTFTSFG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 150 VLE-RSRglRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSF-SEENGEAERVRGLVAESYALAKKIF 227
Cdd:pfam00067 111 KLSfEPR--VEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFgSLEDPKFLELVKAVQELSSLLSSPS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 228 FASVLR-RLLKKLRIPLFKKdIMDVSNRFNELLEKILVEHNEKLD-EEHKDTDMMDVLLAAYADENAEyKITRNHIKSFF 305
Cdd:pfam00067 189 PQLLDLfPILKYFPGPHGRK-LKRARKKIKDLLDKLIEERRETLDsAKKSPRDFLDALLLAKEEEDGS-KLTDEELRATV 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 306 VELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFP-LLTRKFE 384
Cdd:pfam00067 267 LELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVT 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 385 ERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQK---YIPFGGGRRGCPGANLASI 461
Cdd:pfam00067 347 KDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFL--------DENGKFRKsfaFLPFGAGPRNCLGERLARM 418
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1063712834 462 FVGTAIGVMVQCFDW-GIKGDKINMEETFEGLTLT 495
Cdd:pfam00067 419 EMKLFLATLLQNFEVeLPPGTDPPDIDETPGLLLP 453
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
80-507 2.81e-64

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: 215.69  E-value: 2.81e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  80 RIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLERSRGLRA 159
Cdd:cd20658     7 RLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQWLHGKRT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 160 EELQRLYNRILDKAKMN---ENVEIGKEATMLMNNIFCRMSMG-RSFSE--ENG-----EAERVrglvaESYALAKKIFF 228
Cdd:cd20658    87 EEADNLVAYVYNMCKKSnggGLVNVRDAARHYCGNVIRKLMFGtRYFGKgmEDGgpgleEVEHM-----DAIFTALKCLY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 229 ASVLRRLLKKLRI------PLFKKDIMDVSNRFNELL--EKILVEHNEKLDEEHkdtDMMDVLLAAyADENAEYKITRNH 300
Cdd:cd20658   162 AFSISDYLPFLRGldldghEKIVREAMRIIRKYHDPIidERIKQWREGKKKEEE---DWLDVFITL-KDENGNPLLTPDE 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHP--PF-- 376
Cdd:cd20658   238 IKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPvaPFnv 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 377 PLLTRkfeERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRlgQVDEREEAQKYIPFGGGRRGCPGA 456
Cdd:cd20658   318 PHVAM---SDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDS--EVTLTEPDLRFISFSTGRRGCPGV 392
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 457 NLASIFVGTAIGVMVQCFDWGIKGD--KINMEETFEGltLTMVHPIKCTPIPR 507
Cdd:cd20658   393 KLGTAMTVMLLARLLQGFTWTLPPNvsSVDLSESKDD--LFMAKPLVLVAKPR 443
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
127-500 1.61e-63

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: 212.96  E-value: 1.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 127 YAPYGDYLKFVKKIIATKLLRPQVLERSRGLRAEELQRLYNRILDKAKMNENVEIG---KEATMlmNNIFCRMsMGRS-- 201
Cdd:cd11076    53 FAPYGEYWRNLRRIASNHLFSPRRIAASEPQRQAIAAQMVKAIAKEMERSGEVAVRkhlQRASL--NNIMGSV-FGRRyd 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 202 FSEENGEAERVRGLVAESYAL-----------AKKIFFASVLRRLLKKLrIPlfkkdimdvsnRFNELLEKILVEHNEKL 270
Cdd:cd11076   130 FEAGNEEAEELGEMVREGYELlgafnwsdhlpWLRWLDLQGIRRRCSAL-VP-----------RVNTFVGKIIEEHRAKR 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 271 DE-EHKDTDMMDVLLAAYADEnaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSR 349
Cdd:cd11076   198 SNrARDDEDDVDVLLSLQGEE----KLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSR 273
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 350 MIQETDIPNLPYLQAVVKEGLRLHPPFPLLT--RKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLG 427
Cdd:cd11076   274 RVADSDVAKLPYLQAVVKETLRLHPPGPLLSwaRLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVA 353
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712834 428 SSRLGQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGDK-INMEETFeGLTLTMVHPI 500
Cdd:cd11076   354 AEGGADVSVLGSDLRLAPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDAKpVDLSEVL-KLSCEMKNPL 426
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
48-486 5.22e-63

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 213.78  E-value: 5.22e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  48 LPIIGHLHLLLSSLSHKSLQKISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVY 127
Cdd:PLN03234   36 LPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGF 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 128 APYGDYLKFVKKIIATKLLRPQVLERSRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEENG 207
Cdd:PLN03234  116 GQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGT 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 208 EAERVRGLVAESYALAKKIFFASVLRRL-----LKKLRIPLfKKDIMDVSNRFNELLEKILVEHNEKLDEEhkdtDMMDV 282
Cdd:PLN03234  196 EMKRFIDILYETQALLGTLFFSDLFPYFgfldnLTGLSARL-KKAFKELDTYLQELLDETLDPNRPKQETE----SFIDL 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 283 LLAAYADENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYL 362
Cdd:PLN03234  271 LMQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYL 350
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 363 QAVVKEGLRLHPPFP-LLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWED-PNEFKPERFLGSSRlgQVDEREEA 440
Cdd:PLN03234  351 KAVIKESLRLEPVIPiLLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMKEHK--GVDFKGQD 428
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063712834 441 QKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDW----GIKGDKINME 486
Cdd:PLN03234  429 FELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWslpkGIKPEDIKMD 478
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
74-499 2.14e-60

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: 203.90  E-value: 2.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSgvVYAPYGDYLKFVKKIIAtKLLRPQVLER 153
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDG--LLTLDGPEHRRLRRLLA-PAFTPRALAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 154 SRGLRAEELQRLYNRILDKAKMNENVEigKEATMLMNNIFCRMSMGrsfSEENGEAERVRGLVAESYALAKKIFFASVLR 233
Cdd:cd00302    78 LRPVIREIARELLDRLAAGGEVGDDVA--DLAQPLALDVIARLLGG---PDLGEDLEELAELLEALLKLLGPRLLRPLPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 234 RLLKKLRiplfkkdimDVSNRFNELLEKILvehNEKLDEEHKDTDMMDVllaayADENAEYKITRNHIKSFFVELFVGGT 313
Cdd:cd00302   153 PRLRRLR---------RARARLRDYLEELI---ARRRAEPADDLDLLLL-----ADADDGGGLSDEEIVAELLTLLLAGH 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 314 DTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSrmiQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFY 393
Cdd:cd00302   216 ETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYT 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 394 IPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGssrlgqvDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQC 473
Cdd:cd00302   293 IPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLP-------EREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRR 365
                         410       420
                  ....*....|....*....|....*.
gi 1063712834 474 FDWgIKGDKINMEETFEGLTLTMVHP 499
Cdd:cd00302   366 FDF-ELVPDEELEWRPSLGTLGPASL 390
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
73-459 1.35e-57

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: 197.43  E-value: 1.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVF-----------RIHDMNISSRGaaaideslvfgSSGVVYAPYGDYLKFVKKII 141
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALvkksadfagrpKLFTFDLFSRG-----------GKDIAFGDYSPTWKLHRKLA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 142 ATKL-LRPQVLERSRGLRAEELQRLYNRIldkAKMNEN-VEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVRGLVAES 219
Cdd:cd11027    70 HSALrLYASGGPRLEEKIAEEAEKLLKRL---ASQEGQpFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 220 YALAKKIFFASVLRrLLKKLRIPLFK--KDIMDvsnRFNELLEKILVEHNEKLDEEHKDtDMMDVLLAAYADENAEYK-- 295
Cdd:cd11027   147 FELLGAGSLLDIFP-FLKYFPNKALRelKELMK---ERDEILRKKLEEHKETFDPGNIR-DLTDALIKAKKEAEDEGDed 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 296 ---ITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRL 372
Cdd:cd11027   222 sglLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 373 HPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREEAqkYIPFGGGRR 451
Cdd:cd11027   302 SSVVPLaLPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDEN--GKLVPKPES--FLPFSAGRR 377

                  ....*...
gi 1063712834 452 GCPGANLA 459
Cdd:cd11027   378 VCLGESLA 385
PLN02655 PLN02655
ent-kaurene oxidase
68-507 7.05e-57

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 196.50  E-value: 7.05e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  68 KISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLR 147
Cdd:PLN02655   27 KWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDKSMVATSDYGDFHKMVKRYVMNNLLG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 148 PQVLERSRGLRAEELQRLYNRILDKAKMNENVEIGKEAtMLMNNIFcRMSMGRSFSEENgEAERVRGLVAEsyaLAKK-I 226
Cdd:PLN02655  107 ANAQKRFRDTRDMLIENMLSGLHALVKDDPHSPVNFRD-VFENELF-GLSLIQALGEDV-ESVYVEELGTE---ISKEeI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 227 FFASVL-----------RRLLKKLR-IP--LFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAyadena 292
Cdd:PLN02655  181 FDVLVHdmmmcaievdwRDFFPYLSwIPnkSFETRVQTTEFRRTAVMKALIKQQKKRIARGEERDCYLDFLLSE------ 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 293 EYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRmIQETDIPNLPYLQAVVKEGLRL 372
Cdd:PLN02655  255 ATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDER-VTEEDLPNLPYLNAVFHETLRK 333
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 373 HPPFPLL-TRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGsSRLGQVDereeAQKYIPFGGGRR 451
Cdd:PLN02655  334 YSPVPLLpPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLG-EKYESAD----MYKTMAFGAGKR 408
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712834 452 GCPGANLASIFVGTAIGVMVQCFDWGIKGDKINMEETFeGLTLTMVHPIKCTPIPR 507
Cdd:PLN02655  409 VCAGSLQAMLIACMAIARLVQEFEWRLREGDEEKEDTV-QLTTQKLHPLHAHLKPR 463
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
73-499 9.94e-56

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: 192.41  E-value: 9.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATkLLRPQVLE 152
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMPYGPRWRLHRRLFHQ-LLNPSAVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 153 RSRGLRAEELQRLYNRILDKakmNENVEigKEATMLMNNIFCRMSMGRSFSEENGEaervrgLVAESYALAKKIFFASV- 231
Cdd:cd11065    80 KYRPLQELESKQLLRDLLES---PDDFL--DHIRRYAASIILRLAYGYRVPSYDDP------LLRDAEEAMEGFSEAGSp 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 232 ----------LRRLLKKLRIPlFKKdIMDVSNRFNELLEKILVEHNEKLDEEHKDTD-MMDVLLAAyadENAEYKITRNH 300
Cdd:cd11065   149 gaylvdffpfLRYLPSWLGAP-WKR-KARELRELTRRLYEGPFEAAKERMASGTATPsFVKDLLEE---LDKEGGLSEEE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-L 379
Cdd:cd11065   224 IKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLgI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 380 TRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSsrlGQVDEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11065   304 PHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDD---PKGTPDPPDPPHFAFGFGRRICPGRHLA 380
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1063712834 460 --SIFVgtAIGVMVQCFD----WGIKGDKINMEETFEGLTLTMVHP 499
Cdd:cd11065   381 enSLFI--AIARLLWAFDikkpKDEGGKEIPDEPEFTDGLVSHPLP 424
PLN02966 PLN02966
cytochrome P450 83A1
16-504 2.48e-52

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 185.34  E-value: 2.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  16 ILLCFFSLLCYSLFF--KKPKDSRgCDLPPSPPSLPIIGHLHLLLSSLSHKSLQKISSKYGPLLHLRIFNVPIILVSSAS 93
Cdd:PLN02966    4 IIIGVVALAAVLLFFlyQKPKTKR-YKLPPGPSPLPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  94 VADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLERSRGLRAEELQRLYNRILDKA 173
Cdd:PLN02966   83 LAKELLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 174 KMNENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKIFFASVLrrllkklriPL--FKKDIMDV 251
Cdd:PLN02966  163 DKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFIKILYGTQSVLGKIFFSDFF---------PYcgFLDDLSGL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 252 SNRFNELLEK----ILVEHNEKLDEEH---KDTDMMDVLLAAYADENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTM 324
Cdd:PLN02966  234 TAYMKECFERqdtyIQEVVNETLDPKRvkpETESMIDLLMEIYKEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGM 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 325 AEIINNSDVLERLREEIDSVVGT--SRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT-RKFEERCEIKGFYIPEKTFLI 401
Cdd:PLN02966  314 TYLMKYPQVLKKAQAEVREYMKEkgSTFVTEDDVKNLPYFRALVKETLRIEPVIPLLIpRACIQDTKIAGYDIPAGTTVN 393
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 402 INAYAWMRDPDSW-EDPNEFKPERFLGSsrlgQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDW---- 476
Cdd:PLN02966  394 VNAWAVSRDEKEWgPNPDEFRPERFLEK----EVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFklpn 469
                         490       500
                  ....*....|....*....|....*...
gi 1063712834 477 GIKGDKINMeETFEGLTLTMVHPIKCTP 504
Cdd:PLN02966  470 GMKPDDINM-DVMTGLAMHKSQHLKLVP 496
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
69-475 3.74e-52

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 184.94  E-value: 3.74e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  69 ISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDEslVFGSSG--VVYAPYGDYLKFVKKIIATKLL 146
Cdd:PLN02394   59 MAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFD--IFTGKGqdMVFTVYGDHWRKMRRIMTVPFF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 147 RPQVLERSRGLRAEELQRLYNRILDKAKM-NENVEIGKEATMLMNNIFCRMSMGRSF-SEENGEAERVRGLVAESYALAK 224
Cdd:PLN02394  137 TNKVVQQYRYGWEEEADLVVEDVRANPEAaTEGVVIRRRLQLMMYNIMYRMMFDRRFeSEDDPLFLKLKALNGERSRLAQ 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 225 KI---------FFASVLRRLLKKL------RIPLFKkdimdvsNRFNELLEKILvehNEKLDEEHKDTDMMDVLLAAyaD 289
Cdd:PLN02394  217 SFeynygdfipILRPFLRGYLKICqdvkerRLALFK-------DYFVDERKKLM---SAKGMDKEGLKCAIDHILEA--Q 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 290 ENAEykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEG 369
Cdd:PLN02394  285 KKGE--INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKET 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 370 LRLHPPFPLLTRKFE-ERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREEAQKYIPFGG 448
Cdd:PLN02394  363 LRLHMAIPLLVPHMNlEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEE--AKVEANGNDFRFLPFGV 440
                         410       420
                  ....*....|....*....|....*..
gi 1063712834 449 GRRGCPGANLASIFVGTAIGVMVQCFD 475
Cdd:PLN02394  441 GRRSCPGIILALPILGIVLGRLVQNFE 467
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
72-475 3.92e-50

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: 177.66  E-value: 3.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDEslVFGSSG--VVYAPYGDYLKFVKKIIATKLLRPQ 149
Cdd:cd11074     2 KFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFD--IFTGKGqdMVFTVYGEHWRKMRRIMTVPFFTNK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 150 VLERSRGLRAEELQRLYNRILDKAKMNEN-VEIGKEATMLMNNIFCRMSMGRSF-SEENGEAERVRGLVAESYALAKKIF 227
Cdd:cd11074    80 VVQQYRYGWEEEAARVVEDVKKNPEAATEgIVIRRRLQLMMYNNMYRIMFDRRFeSEDDPLFVKLKALNGERSRLAQSFE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 228 -----FASVLRRLLKKlriplFKKDIMDVSNRFNELLEKILVEHNEKLdEEHKDTDMMDVLLAAYADENAEYK--ITRNH 300
Cdd:cd11074   160 ynygdFIPILRPFLRG-----YLKICKEVKERRLQLFKDYFVDERKKL-GSTKSTKNEGLKCAIDHILDAQKKgeINEDN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT 380
Cdd:cd11074   234 VLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 381 RKFE-ERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11074   314 PHMNlHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEE--SKVEANGNDFRYLPFGVGRRSCPGIILA 391
                         410
                  ....*....|....*.
gi 1063712834 460 SIFVGTAIGVMVQCFD 475
Cdd:cd11074   392 LPILGITIGRLVQNFE 407
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
72-459 7.60e-45

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: 163.08  E-value: 7.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFR------IHDMNIS------SRGaaaIDESLVFGSsgvvyapyGDYLKFVKK 139
Cdd:cd11054     3 KYGPIVREKLGGRDIVHLFDPDDIEKVFRnegkypIRPSLEPlekyrkKRG---KPLGLLNSN--------GEEWHRLRS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 140 IIATKLLRPQVLER-SRGLR--AEEL-QRLYNRILDKAKMNENV--EIGK---EATmlmnnifCRMSMGRSFS--EENGE 208
Cdd:cd11054    72 AVQKPLLRPKSVASyLPAINevADDFvERIRRLRDEDGEEVPDLedELYKwslESI-------GTVLFGKRLGclDDNPD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 209 AErvrglvAESYALAKKIFFASVLR-----RLLKKLRIPLFKK--DIMDVSNRF-NELLEKILVEHNEKLDEEHKDTDMM 280
Cdd:cd11054   145 SD------AQKLIEAVKDIFESSAKlmfgpPLWKYFPTPAWKKfvKAWDTIFDIaSKYVDEALEELKKKDEEDEEEDSLL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 281 DVLLAayadenaEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLP 360
Cdd:cd11054   219 EYLLS-------KPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMP 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 361 YLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlgqvDEREEA 440
Cdd:cd11054   292 YLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDD-----SENKNI 366
                         410       420
                  ....*....|....*....|.
gi 1063712834 441 QKY--IPFGGGRRGCPGANLA 459
Cdd:cd11054   367 HPFasLPFGFGPRMCIGRRFA 387
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
72-476 1.40e-44

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: 162.39  E-value: 1.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSsGVVYAPYGDYLKFVKKIIATklLRPQVL 151
Cdd:cd11042     4 KYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGG-VVYYAPFAEQKEQLKFGLNI--LRRGKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 152 ERSRGLRAEELQRLYNRiLDKAKMNENVEIGKEATMLmnnIFCRMSMGRSFSEENGEAervrglVAESYA-LAKKIFFAS 230
Cdd:cd11042    81 RGYVPLIVEEVEKYFAK-WGESGEVDLFEEMSELTIL---TASRCLLGKEVRELLDDE------FAQLYHdLDGGFTPIA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 231 VLrrlLKKLRIPLFKK-DimDVSNRFNELLEKILVEhnEKLDEEHKDTDMMDVLLaayadeNAEYK----ITRNHIKSFF 305
Cdd:cd11042   151 FF---FPPLPLPSFRRrD--RARAKLKEIFSEIIQK--RRKSPDKDEDDMLQTLM------DAKYKdgrpLTDDEIAGLL 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 306 VELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTS-RMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRK-- 382
Cdd:cd11042   218 IALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGdDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKar 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 383 --FEerCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQK-----YIPFGGGRRGCPG 455
Cdd:cd11042   298 kpFE--VEGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFL--------KGRAEDSKggkfaYLPFGAGRHRCIG 367
                         410       420
                  ....*....|....*....|.
gi 1063712834 456 ANLASIFVGTAIGVMVQCFDW 476
Cdd:cd11042   368 ENFAYLQIKTILSTLLRNFDF 388
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
72-474 2.61e-44

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: 161.60  E-value: 2.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLvFGSSgVVYAPyGDYLKFVKKIIAT-------K 144
Cdd:cd11055     1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEP-FDSS-LLFLK-GERWKRLRTTLSPtfssgklK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 145 LLRPQVLERSRglraeelqRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMG-RSFSEENGEAERVRGlvaesyalA 223
Cdd:cd11055    78 LMVPIINDCCD--------ELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGiDVDSQNNPDDPFLKA--------A 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 224 KKIFFASVLRRLLKKLRIPLFKKDI--------MDVSNRFNELLEKIlVEHNEKLDEEHKdTDMMDVLLAAYADENAEY- 294
Cdd:cd11055   142 KKIFRNSIIRLFLLLLLFPLRLFLFllfpfvfgFKSFSFLEDVVKKI-IEQRRKNKSSRR-KDLLQLMLDAQDSDEDVSk 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 295 -KITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLH 373
Cdd:cd11055   220 kKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLY 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 374 PPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQ---KYIPFGGGR 450
Cdd:cd11055   300 PPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFS--------PENKAKRhpyAYLPFGAGP 371
                         410       420
                  ....*....|....*....|....
gi 1063712834 451 RGCPGANLASIFVGTAIGVMVQCF 474
Cdd:cd11055   372 RNCIGMRFALLEVKLALVKILQKF 395
PLN02971 PLN02971
tryptophan N-hydroxylase
79-486 4.58e-44

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 163.67  E-value: 4.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  79 LRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQvleRSRGL- 157
Cdd:PLN02971   98 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPA---RHRWLh 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 158 --RAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMG-RSFSEENG-----EAERVRGLVAESYALAKKIFFA 229
Cdd:PLN02971  175 dnRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGtRTFSEKTEpdggpTLEDIEHMDAMFEGLGFTFAFC 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 230 -SVLRRLLKKLRIPLFKKdIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVL--LAAYADENAEYKITRNHIKSFFV 306
Cdd:PLN02971  255 iSDYLPMLTGLDLNGHEK-IMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLdiFISIKDEAGQPLLTADEIKPTIK 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 307 ELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHP--PFPLLTRKFE 384
Cdd:PLN02971  334 ELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPvaAFNLPHVALS 413
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 385 ErCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgsSRLGQVDEREEAQKYIPFGGGRRGCPGANLASIFVG 464
Cdd:PLN02971  414 D-TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHL--NECSEVTLTENDLRFISFSTGKRGCAAPALGTAITT 490
                         410       420
                  ....*....|....*....|..
gi 1063712834 465 TAIGVMVQCFDWGIKGDKINME 486
Cdd:PLN02971  491 MMLARLLQGFKWKLAGSETRVE 512
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
113-502 1.70e-42

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: 156.69  E-value: 1.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 113 AIDESLVFGSSGVVYApygdylkfVKKIIATKLLRPQVLERSRGLRAE----ELQRLYNRILDKAKMNENVEIGKEATML 188
Cdd:cd11028    47 SNGKSMAFSDYGPRWK--------LHRKLAQNALRTFSNARTHNPLEEhvteEAEELVTELTENNGKPGPFDPRNEIYLS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 189 MNNIFCRMSMGRSFSEENgeaERVRGLVAESYALAKKI----------FFASVLRRLLKKLRiplfkkdimDVSNRFNEL 258
Cdd:cd11028   119 VGNVICAICFGKRYSRDD---PEFLELVKSNDDFGAFVgagnpvdvmpWLRYLTRRKLQKFK---------ELLNRLNSF 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 259 LEKILVEHNEKLDEEHKdTDMMDVLLAAYADENAEYK----ITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVL 334
Cdd:cd11028   187 ILKKVKEHLDTYDKGHI-RDITDALIKASEEKPEEEKpevgLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQ 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 335 ERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDS 413
Cdd:cd11028   266 EKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFtIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKL 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 414 WEDPNEFKPERFLGSSrlGQVDEReEAQKYIPFGGGRRGCPGANLA--SIFVGTAIgVMVQCFDWGIKGDKINMEETFeG 491
Cdd:cd11028   346 WPDPSVFRPERFLDDN--GLLDKT-KVDKFLPFGAGRRRCLGEELArmELFLFFAT-LLQQCEFSVKPGEKLDLTPIY-G 420
                         410
                  ....*....|.
gi 1063712834 492 LTLtmvHPIKC 502
Cdd:cd11028   421 LTM---KPKPF 428
PLN03018 PLN03018
homomethionine N-hydroxylase
87-510 3.02e-42

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 158.25  E-value: 3.02e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  87 ILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLLRPQVLERSRGLRAEELQRLY 166
Cdd:PLN03018   89 ITINSDEIAREAFRERDADLADRPQLSIMETIGDNYKSMGTSPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLI 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 167 NRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRS-FSEENGEAERVRGLVAESYALaKKIF--------FASV--LRRL 235
Cdd:PLN03018  169 AYIHSMYQRSETVDVRELSRVYGYAVTMRMLFGRRhVTKENVFSDDGRLGKAEKHHL-EVIFntlnclpgFSPVdyVERW 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 236 LKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVL--LAAYADENAEYKITRNHIKSFFVELFVGGT 313
Cdd:PLN03018  248 LRGWNIDGQEERAKVNVNLVRSYNNPIIDERVELWREKGGKAAVEDWLdtFITLKDQNGKYLVTPDEIKAQCVEFCIAAI 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 314 DTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPF----PLLTRkfeERCEI 389
Cdd:PLN03018  328 DNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAhyvpPHVAR---QDTTL 404
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 390 KGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFL-GSSRLGQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIG 468
Cdd:PLN03018  405 GGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLqGDGITKEVTLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLA 484
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1063712834 469 VMVQCFDWGIKGD--KINMEEtfEGLTLTMVHPIKCTPIPRTLP 510
Cdd:PLN03018  485 RFLQGFNWKLHQDfgPLSLEE--DDASLLMAKPLLLSVEPRLAP 526
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
144-455 7.47e-42

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: 154.99  E-value: 7.47e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 144 KLLRP----QVLERSRGLRAEELQRLYNRILDKAKmNENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVRGLVAE- 218
Cdd:cd20628    62 KLLTPafhfKILESFVEVFNENSKILVEKLKKKAG-GGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRi 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 219 SYALAKKIF-----------FASVLRRLLKKLRIplfkkdIMDVSN-----RFNELLEKILVEHNEKLDEEHKDTDMMDV 282
Cdd:cd20628   141 LEIILKRIFspwlrfdfifrLTSLGKEQRKALKV------LHDFTNkvikeRREELKAEKRNSEEDDEFGKKKRKAFLDL 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 283 LLAAYADENaeyKIT----RNHIKSFFVElfvgGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTS-RMIQETDIP 357
Cdd:cd20628   215 LLEAHEDGG---PLTdediREEVDTFMFA----GHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDdRRPTLEDLN 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 358 NLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvdeR 437
Cdd:cd20628   288 KMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFL----------P 357
                         330       340
                  ....*....|....*....|...
gi 1063712834 438 EEAQK-----YIPFGGGRRGCPG 455
Cdd:cd20628   358 ENSAKrhpyaYIPFSAGPRNCIG 380
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
72-459 1.21e-41

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: 154.28  E-value: 1.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNV-PIILVSSASVADEVFRIHDmNISSRGAAaiDESL--VFGSSGVVYAPyGDYLKfvkkiIATKLLRP 148
Cdd:cd11053    10 RYGDVFTLRVPGLgPVVVLSDPEAIKQIFTADP-DVLHPGEG--NSLLepLLGPNSLLLLD-GDRHR-----RRRKLLMP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 149 qvlersrGLRAEELQR-------LYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAER-VRGLVAESY 220
Cdd:cd11053    81 -------AFHGERLRAygeliaeITEREIDRWPPGQPFDLRELMQEITLEVILRVVFGVDDGERLQELRRlLPRLLDLLS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 221 ALAkkiFFASVLRRLLkkLRIPLFKKdIMDVSNRFNELLEKILVEHNEKLDEEhkDTDMMDVLLAAyADENAEyKITRNH 300
Cdd:cd11053   154 SPL---ASFPALQRDL--GPWSPWGR-FLRARRRIDALIYAEIAERRAEPDAE--RDDILSLLLSA-RDEDGQ-PLSDEE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSrmiQETDIPNLPYLQAVVKEGLRLHPPFPLLT 380
Cdd:cd11053   224 LRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDP---DPEDIAKLPYLDAVIKETLRLYPVAPLVP 300
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712834 381 RKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGssrlgqvdEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11053   301 RRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLG--------RKPSPYEYLPFGGGVRRCIGAAFA 371
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
248-483 2.24e-41

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: 153.53  E-value: 2.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 248 IMDVSNRFNELLEKILVEHNEKLDEEHKDtDMMDVLLAAYADENA-EYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAE 326
Cdd:cd20651   173 LVELNQKLIEFLKEEIKEHKKTYDEDNPR-DLIDAYLREMKKKEPpSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLY 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 327 IINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAY 405
Cdd:cd20651   252 LLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIgIPHRALKDTTLGGYRIPKDTTILASLY 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 406 AWMRDPDSWEDPNEFKPERFLGSSRLGQVDEReeaqkYIPFGGGRRGCPGANLA--SIFVGTAigVMVQCFDWGIKGDKI 483
Cdd:cd20651   332 SVHMDPEYWGDPEEFRPERFLDEDGKLLKDEW-----FLPFGAGKRRCLGESLArnELFLFFT--GLLQNFTFSPPNGSL 404
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
162-459 2.41e-41

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: 153.51  E-value: 2.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 162 LQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFS-EENGEaeRVRGLVAESYALAKKIFFASV---LRRLLK 237
Cdd:cd11060    84 IDLLVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGfLEAGT--DVDGYIASIDKLLPYFAVVGQipwLDRLLL 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 238 KLRIPLFKKDI--MdvsNRFNELLEKILVEHNEKLDEEHKD-TDMMDVLLAAYadENAEYKITRNHIKSFFVELFVGGTD 314
Cdd:cd11060   162 KNPLGPKRKDKtgF---GPLMRFALEAVAERLAEDAESAKGrKDMLDSFLEAG--LKDPEKVTDREVVAEALSNILAGSD 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 315 TSVQTTQWTMAEIINNSDVLERLREEIDSVVGT---SRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKF-EERCEI 389
Cdd:cd11060   237 TTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEgklSSPITFAEAQKLPYLQAVIKEALRLHPPVGLpLERVVpPGGATI 316
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712834 390 KGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGSsrlGQVDEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11060   317 CGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEA---DEEQRRMMDRADLTFGAGSRTCLGKNIA 384
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
73-494 3.30e-41

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: 153.39  E-value: 3.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIdESLVFGSSGVVYAPYGDYLKFVKKIIATKL------- 145
Cdd:cd20666     1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPL-VTILTKGKGIVFAPYGPVWRQQRKFSHSTLrhfglgk 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 146 --LRPQVLERSRGLRaEELQRLYNRILDKAKMNENVeigkeatmlMNNIFCRMSMGRSFSEENGEAERVRGLVAESYALA 223
Cdd:cd20666    80 lsLEPKIIEEFRYVK-AEMLKHGGDPFNPFPIVNNA---------VSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEIS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 224 KKIFFASV-LRRLLKKLRIPLFKkDIMDVSNRFNELLEKILVEHNEKLDEEHKdTDMMDVLLAAYADE---NAEYKITRN 299
Cdd:cd20666   150 VNSAAILVnICPWLYYLPFGPFR-ELRQIEKDITAFLKKIIADHRETLDPANP-RDFIDMYLLHIEEEqknNAESSFNED 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 300 HIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL- 378
Cdd:cd20666   228 YLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLs 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGCPGANL 458
Cdd:cd20666   308 IPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDEN--GQLIKKE---AFIPFGIGRRVCMGEQL 382
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1063712834 459 ASIFVGTAIGVMVQCFDWGIKGD--KINMEETFeGLTL 494
Cdd:cd20666   383 AKMELFLMFVSLMQSFTFLLPPNapKPSMEGRF-GLTL 419
PLN00168 PLN00168
Cytochrome P450; Provisional
67-508 5.01e-41

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 154.72  E-value: 5.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  67 QKISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLL 146
Cdd:PLN00168   64 RRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRNLVAETL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 147 RPQVLERSRGLRAEELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEEN----GEAER--------VRG 214
Cdd:PLN00168  144 HPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAvraiAAAQRdwllyvskKMS 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 215 LVAESYALAKKIF-----FASVLRRLLKKLRIPLfkkdiMDVSNRFNELLEKILVEHNEKLDEEHKdtdMMDVLLAAYAD 289
Cdd:PLN00168  224 VFAFFPAVTKHLFrgrlqKALALRRRQKELFVPL-----IDARREYKNHLGQGGEPPKKETTFEHS---YVDTLLDIRLP 295
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 290 ENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGT-SRMIQETDIPNLPYLQAVVKE 368
Cdd:PLN00168  296 EDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDdQEEVSEEDVHKMPYLKAVVLE 375
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 369 GLRLHPP--FpLLTRKFEERCEIKGFYIPEKT---FLIinayAWM-RDPDSWEDPNEFKPERFLGSSRLGQVD-EREEAQ 441
Cdd:PLN00168  376 GLRKHPPahF-VLPHKAAEDMEVGGYLIPKGAtvnFMV----AEMgRDEREWERPMEFVPERFLAGGDGEGVDvTGSREI 450
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712834 442 KYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDW-GIKGDKINMEETFEgLTLTMVHPIKCTPIPRT 508
Cdd:PLN00168  451 RMMPFGVGRRICAGLGIAMLHLEYFVANMVREFEWkEVPGDEVDFAEKRE-FTTVMAKPLRARLVPRR 517
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
159-459 2.24e-40

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: 151.15  E-value: 2.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 159 AEELQRLynrILDKAKMNENVEIGKEATMLMNNIFCRMSMG---RSFSEENGEAERV-RGLVAESYALAKKIFFASVLRR 234
Cdd:cd11056    88 GDELVDY---LKKQAEKGKELEIKDLMARYTTDVIASCAFGldaNSLNDPENEFREMgRRLFEPSRLRGLKFMLLFFFPK 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 235 LLKKLRIPLFKKDimdVSNRFNELLEKIlVEHNEKldEEHKDTDMMDVLLAAY-----ADENAEYKITRNHI--KSFFve 307
Cdd:cd11056   165 LARLLRLKFFPKE---VEDFFRKLVRDT-IEYREK--NNIVRNDFIDLLLELKkkgkiEDDKSEKELTDEELaaQAFV-- 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 308 LFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVvgtsrmIQETD-------IPNLPYLQAVVKEGLRLHPPFPLLT 380
Cdd:cd11056   237 FFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEV------LEKHGgeltyeaLQEMKYLDQVVNETLRKYPPLPFLD 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 381 RKFEERCEI--KGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGssrlgqvderEEAQK-----YIPFGGGRRGC 453
Cdd:cd11056   311 RVCTKDYTLpgTDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSP----------ENKKKrhpytYLPFGDGPRNC 380

                  ....*.
gi 1063712834 454 PGANLA 459
Cdd:cd11056   381 IGMRFG 386
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
228-502 1.05e-39

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: 148.50  E-value: 1.05e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 228 FASVLRRLLKKLRIPLFKKDIM---------DVSNRFNELLEKILVEHNEKLDEEHKDTDMmdvLLAAyADENAEYKITR 298
Cdd:cd20620   135 LDVALEYAARRMLSPFLLPLWLptpanrrfrRARRRLDEVIYRLIAERRAAPADGGDLLSM---LLAA-RDEETGEPMSD 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 299 NHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTsRMIQETDIPNLPYLQAVVKEGLRLHPPFPL 378
Cdd:cd20620   211 QQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGG-RPPTAEDLPQLPYTEMVLQESLRLYPPAWI 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQ---KYIPFGGGRRGCPG 455
Cdd:cd20620   290 IGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFT--------PEREAARpryAYFPFGGGPRICIG 361
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1063712834 456 ANLASIFVGTAIGVMVQCFDW-GIKGDKINMEETfegLTLTMVHPIKC 502
Cdd:cd20620   362 NHFAMMEAVLLLATIAQRFRLrLVPGQPVEPEPL---ITLRPKNGVRM 406
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
73-466 8.47e-39

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: 146.40  E-value: 8.47e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASV---------ADEVFRIHDMN--ISSRGAAaiDESLvfgssgvvyapyGDY---LKFVK 138
Cdd:cd20674     1 YGPIYRLRLGLQDVVVLNSKRTirealvrkwADFAGRPHSYTgkLVSQGGQ--DLSL------------GDYsllWKAHR 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 139 KIIATKLLR-------PQVLERSRGLRaeelQRLynrildKAKMNENVEIGKEATMLMNNIFCRMSMGRSFSEENgEAER 211
Cdd:cd20674    67 KLTRSALQLgirnslePVVEQLTQELC----ERM------RAQAGTPVDIQEEFSLLTCSIICCLTFGDKEDKDT-LVQA 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 212 VRGLVAEsyaLAKKIFFASV----LRRLLKKLRIPLFKKdIMDVSNRFNELLEKILVEHNEKLDEEhKDTDMMDVLLAAY 287
Cdd:cd20674   136 FHDCVQE---LLKTWGHWSIqaldSIPFLRFFPNPGLRR-LKQAVENRDHIVESQLRQHKESLVAG-QWRDMTDYMLQGL 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 288 AD---ENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQA 364
Cdd:cd20674   211 GQprgEKGMGQLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNA 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 365 VVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQKY 443
Cdd:cd20674   291 TIAEVLRLRPVVPLaLPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFL--------EPGAANRAL 362
                         410       420
                  ....*....|....*....|....*
gi 1063712834 444 IPFGGGRRGCPGANLA--SIFVGTA 466
Cdd:cd20674   363 LPFGCGARVCLGEPLArlELFVFLA 387
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
71-486 8.61e-39

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: 146.17  E-value: 8.61e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  71 SKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDEslVFGSSGVVyAPYGDYLKFVKKIIATkLLRPQV 150
Cdd:cd11043     3 KRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRK--LLGKSSLL-TVSGEEHKRLRGLLLS-FLGPEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 151 LeRSRGLraEELQRLYNRILDKAKMNENVEIgKEATMLMN-NIFCRMSMGrsfseeNGEAERVRGLVAESYALAKKIFfa 229
Cdd:cd11043    79 L-KDRLL--GDIDELVRQHLDSWWRGKSVVV-LELAKKMTfELICKLLLG------IDPEEVVEELRKEFQAFLEGLL-- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 230 SVlrrllkKLRIP--LFKKDIMdVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAyaDENAEYKITRNHIKSFFVE 307
Cdd:cd11043   147 SF------PLNLPgtTFHRALK-ARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEE--KDEDGDSLTDEEILDNILT 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 308 LFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGT---SRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFE 384
Cdd:cd11043   218 LLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRkeeGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKAL 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 385 ERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGqvdereeAQKYIPFGGGRRGCPGANLASIFVG 464
Cdd:cd11043   298 QDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV-------PYTFLPFGGGPRLCPGAELAKLEIL 370
                         410       420
                  ....*....|....*....|...
gi 1063712834 465 TAIGVMVQCFDW-GIKGDKINME 486
Cdd:cd11043   371 VFLHHLVTRFRWeVVPDEKISRF 393
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
73-459 1.01e-38

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: 146.70  E-value: 1.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYAPYGDYLKFVKKIIATKLlrpqvle 152
Cdd:cd20673     1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGKDIAFADYSATWQLHRKLVHSAF------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 153 rsrGLRAEELQRLYNRILDKAKM---------NENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVR----GLVAes 219
Cdd:cd20673    74 ---ALFGEGSQKLEKIICQEASSlcdtlathnGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILnyneGIVD-- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 220 yALAK----------KIFFASVLRRLLKKlriplfkkdimdVSNRfNELLEKILVEHNEKLDEeHKDTDMMDVLLAAY-- 287
Cdd:cd20673   149 -TVAKdslvdifpwlQIFPNKDLEKLKQC------------VKIR-DKLLQKKLEEHKEKFSS-DSIRDLLDALLQAKmn 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 288 ADEN------AEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPY 361
Cdd:cd20673   214 AENNnagpdqDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPL 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 362 LQAVVKEGLRLHPPFPLLT-RKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQvDEREEA 440
Cdd:cd20673   294 LEATIREVLRIRPVAPLLIpHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPT--GS-QLISPS 370
                         410
                  ....*....|....*....
gi 1063712834 441 QKYIPFGGGRRGCPGANLA 459
Cdd:cd20673   371 LSYLPFGAGPRVCLGEALA 389
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
215-461 1.73e-37

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 143.16  E-value: 1.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 215 LVAESYALAKKIFFASVLRRLL--KKLRIPLFK--KDIMDVSNRFNELLEKILVEHNEKLDEE--HKDTDMMDVLLAAYA 288
Cdd:cd20621   138 ILIESFLYRFSSPYFQLKRLIFgrKSWKLFPTKkeKKLQKRVKELRQFIEKIIQNRIKQIKKNkdEIKDIIIDLDLYLLQ 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 289 DENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKE 368
Cdd:cd20621   218 KKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKE 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 369 GLRLHPPFP-LLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlgQVDEREEAqkYIPFG 447
Cdd:cd20621   298 VLRLYNPAPfLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQN---NIEDNPFV--FIPFS 372
                         250
                  ....*....|....
gi 1063712834 448 GGRRGCPGANLASI 461
Cdd:cd20621   373 AGPRNCIGQHLALM 386
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
138-459 2.80e-37

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: 142.44  E-value: 2.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 138 KKIIAtKLLRPQVLerSRGLRAEELQRLYNRILDKAKMN----ENVEIGKEATMLMNNIFCRMSMGRSFSEENGEAERVR 213
Cdd:cd11059    59 RRLLS-GVYSKSSL--LRAAMEPIIRERVLPLIDRIAKEagksGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSR 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 214 GLVAESYALAkkiFFASVLRRLLKKLRIPLFKKDIMDVSNRFNELLE--KILVEHNEKLDEEHKDTDMMDVLLAAYADEN 291
Cdd:cd11059   136 ERELLRRLLA---SLAPWLRWLPRYLPLATSRLIIGIYFRAFDEIEEwaLDLCARAESSLAESSDSESLTVLLLEKLKGL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 292 AEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQE-TDIPNLPYLQAVVKEGL 370
Cdd:cd11059   213 KKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPPDlEDLDKLPYLNAVIRETL 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 371 RLHPPFPLLtrkfEER------CEIKGFYIPEKTflIINAYAWM--RDPDSWEDPNEFKPERFLGSSRLGQvderEEAQK 442
Cdd:cd11059   293 RLYPPIPGS----LPRvvpeggATIGGYYIPGGT--IVSTQAYSlhRDPEVFPDPEEFDPERWLDPSGETA----REMKR 362
                         330
                  ....*....|....*...
gi 1063712834 443 -YIPFGGGRRGCPGANLA 459
Cdd:cd11059   363 aFWPFGSGSRMCIGMNLA 380
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
73-459 4.92e-37

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: 142.02  E-value: 4.92e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLR-IFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSsGVVYApYGDYLKFVKKIIATKLLRPQVl 151
Cdd:cd11069     1 YGGLIRYRgLFGSERLLVTDPKALKHILVTNSYDFEKPPAFRRLLRRILGD-GLLAA-EGEEHKRQRKILNPAFSYRHV- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 152 ersRGLR------AEEL-QRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSF-SEENGEAErvrglVAESY--- 220
Cdd:cd11069    78 ---KELYpifwskAEELvDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFdSLENPDNE-----LAEAYrrl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 221 ---ALAKKIFFA---SVLRRLLKKLRIPLfKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDT--DMMDVLLAAYADENA 292
Cdd:cd11069   150 fepTLLGSLLFIlllFLPRWLVRILPWKA-NREIRRAKDVLRRLAREIIREKKAALLEGKDDSgkDILSILLRANDFADD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 293 EyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSR--MIQETDIPNLPYLQAVVKEGL 370
Cdd:cd11069   229 E-RLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPdgDLSYDDLDRLPYLNAVCRETL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 371 RLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGssrLGQVDEREEAQKY---IPF 446
Cdd:cd11069   308 RLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLE---PDGAASPGGAGSNyalLTF 384
                         410
                  ....*....|...
gi 1063712834 447 GGGRRGCPGANLA 459
Cdd:cd11069   385 LHGPRSCIGKKFA 397
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
256-461 8.84e-37

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: 141.12  E-value: 8.84e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 256 NELLEKILvehneKLDEEHKDTDMMDVLlaayaDEnaeykitrnhiksfFVELFVGGTDTSVQTTQWTMAEIINNSDVLE 335
Cdd:cd20613   214 NDILTHIL-----KASEEEPDFDMEELL-----DD--------------FVTFFIAGQETTANLLSFTLLELGRHPEILK 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 336 RLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWE 415
Cdd:cd20613   270 RLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFE 349
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1063712834 416 DPNEFKPERFLGSSrlgqvDEREEAQKYIPFGGGRRGCPGANLASI 461
Cdd:cd20613   350 DPLKFDPERFSPEA-----PEKIPSYAYFPFSLGPRSCIGQQFAQI 390
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
72-459 4.58e-36

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: 138.49  E-value: 4.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSGVVYApYGDYLKFVKKIIAtKLLRPQVL 151
Cdd:COG2124    30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTL-DGPEHTRLRRLVQ-PAFTPRRV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 152 ERSRglraEELQRLYNRILDKAKMNENVEIGKE-ATMLMNNIFCRMsmgrsFSEENGEAERVRGLVAEsyalakkiFFAS 230
Cdd:COG2124   108 AALR----PRIREIADELLDRLAARGPVDLVEEfARPLPVIVICEL-----LGVPEEDRDRLRRWSDA--------LLDA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 231 VLRRLLKKLRiplfkkDIMDVSNRFNELLEKILVEHnekldEEHKDTDMMDVLLAAYADENaeyKITRNHIKSFFVELFV 310
Cdd:COG2124   171 LGPLPPERRR------RARRARAELDAYLRELIAER-----RAEPGDDLLSALLAARDDGE---RLSDEELRDELLLLLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 311 GGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqetdipnLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIK 390
Cdd:COG2124   237 AGHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDVELG 298
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712834 391 GFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:COG2124   299 GVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR--------------PPNAHLPFGGGPHRCLGAALA 353
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
254-459 4.79e-36

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: 138.55  E-value: 4.79e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 254 RFNELLEKILVEHNEklDEEHKDtDMMDVLLAAYADENAeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDV 333
Cdd:cd11049   179 RLRELVDEIIAEYRA--SGTDRD-DLLSLLLAARDEEGR--PLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEV 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 334 LERLREEIDSVVGTsRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDS 413
Cdd:cd11049   254 ERRLHAELDAVLGG-RPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEV 332
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1063712834 414 WEDPNEFKPERFLgssrlgqvDEREEAQ---KYIPFGGGRRGCPGANLA 459
Cdd:cd11049   333 YPDPERFDPDRWL--------PGRAAAVprgAFIPFGAGARKCIGDTFA 373
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
160-480 6.29e-36

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: 138.54  E-value: 6.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 160 EELQRLYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFS---EENGEAERVRGL--VAESYALAKkiFFaSVLRR 234
Cdd:cd11062    80 EKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGyldEPDFGPEFLDALraLAEMIHLLR--HF-PWLLK 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 235 LLKKLRIPLFKK--DIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLAAYADENAEYKITRNHIKSFFVELFVGG 312
Cdd:cd11062   157 LLRSLPESLLKRlnPGLAVFLDFQESIAKQVDEVLRQVSAGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTLIGAG 236
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 313 TDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQE-TDIPNLPYLQAVVKEGLRLHPPFPL-LTRKF-EERCEI 389
Cdd:cd11062   237 TETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSPPSlAELEKLPYLTAVIKEGLRLSYGVPTrLPRVVpDEGLYY 316
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 390 KGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQVDereeaQKYIPFGGGRRGCPGANLASIFVGTAIGV 469
Cdd:cd11062   317 KGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGKLD-----RYLVPFSKGSRSCLGINLAYAELYLALAA 391
                         330
                  ....*....|.
gi 1063712834 470 MVQCFDWGIKG 480
Cdd:cd11062   392 LFRRFDLELYE 402
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
210-498 2.63e-34

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: 133.84  E-value: 2.63e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 210 ERVRGLVAESYALAKKIF---FASVLRRLLKKLRI-PLF-------KKDIMDVSNRF-NELLEKILVEHNEKLDEEHKDT 277
Cdd:cd11063   121 ESVDSLKPGGDSPPAARFaeaFDYAQKYLAKRLRLgKLLwllrdkkFREACKVVHRFvDPYVDKALARKEESKDEESSDR 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 278 DmmdVLLAAYADENAEYKITRNHIksffVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIP 357
Cdd:cd11063   201 Y---VFLDELAKETRDPKELRDQL----LNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLK 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 358 NLPYLQAVVKEGLRLHPPFPLLTRkfeerCEIK--------------GFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKP 422
Cdd:cd11063   274 NMKYLRAVINETLRLYPPVPLNSR-----VAVRdttlprgggpdgksPIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRP 348
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712834 423 ERFLGSSRLGQvdereeaqKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGDKINMEetfEGLTLTMVH 498
Cdd:cd11063   349 ERWEDLKRPGW--------EYLPFNGGPRICLGQQFALTEASYVLVRLLQTFDRIESRDVRPPE---ERLTLTLSN 413
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
72-502 1.78e-33

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: 132.07  E-value: 1.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  72 KYGPLLhlrIFNVP--IILVSSASVADEVFRIHDMNISSRGAAAIDEslVFGSSgvVYAPYGDYLKFVKKIIAtkllrPQ 149
Cdd:cd11070     1 KLGAVK---ILFVSrwNILVTKPEYLTQIFRRRDDFPKPGNQYKIPA--FYGPN--VISSEGEDWKRYRKIVA-----PA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 150 VLERSRGLRAEEL----QRLYNRILDKAKMNENVEIgkeatmLMNNIFCRMSM---GRS-FSEENGEAERVRGLVAESYA 221
Cdd:cd11070    69 FNERNNALVWEESirqaQRLIRYLLEEQPSAKGGGV------DVRDLLQRLALnviGEVgFGFDLPALDEEESSLHDTLN 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 222 LAKKIFFASVLRRL--LKKLRIPLFKKDIM---DVSNRFNELLEKILVEHN-EKLDEEHKDTDMMDVLLAAYADEnaeyK 295
Cdd:cd11070   143 AIKLAIFPPLFLNFpfLDRLPWVLFPSRKRafkDVDEFLSELLDEVEAELSaDSKGKQGTESVVASRLKRARRSG----G 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 296 ITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQET--DIPNLPYLQAVVKEGLRLH 373
Cdd:cd11070   219 LTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYeeDFPKLPYLLAVIYETLRLY 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 374 PPFPLLTRKFEERCEI-----KGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGSSRLGQVDEREEAQK--YIP 445
Cdd:cd11070   299 PPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGEIGAATRFTPARgaFIP 378
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712834 446 FGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGDKiNMEETFEGLTLTMVHPIKC 502
Cdd:cd11070   379 FSAGPRACLGRKFALVEFVAALAELFRQYEWRVDPEW-EEGETPAGATRDSPAKLRL 434
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
196-491 2.47e-33

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: 131.19  E-value: 2.47e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 196 MSMGRSFSEENGEAERVRGLVAESYALAKKIF-FASVLRRLLKKLriPLFKKDIMDVsNRFNELLEKILVEHNEKLDEEH 274
Cdd:cd11061   117 LAFGKSFGMLESGKDRYILDLLEKSMVRLGVLgHAPWLRPLLLDL--PLFPGATKAR-KRFLDFVRAQLKERLKAEEEKR 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 275 KDtdMMDVLLAAYaDENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGT-SRMIQE 353
Cdd:cd11061   194 PD--IFSYLLEAK-DPETGEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSdDEIRLG 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 354 TDIPNLPYLQAVVKEGLRLHPPFP-LLTRKF-EERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrl 431
Cdd:cd11061   271 PKLKSLPYLRACIDEALRLSPPVPsGLPRETpPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWL----- 345
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712834 432 gqvDEREEAQK----YIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGDkiNMEETFEG 491
Cdd:cd11061   346 ---SRPEELVRarsaFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPG--EDGEAGEG 404
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
73-459 6.52e-32

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: 127.50  E-value: 6.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFG--SSGVVYAPYGDYLKFVKKIIATKL----- 145
Cdd:cd20663     1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGpkSQGVVLARYGPAWREQRRFSVSTLrnfgl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 146 ----LRPQVLERSRGLRA---EELQRLY--NRILDKAkmnenveigkeatmlMNNIFCRMSMGRSFSEENGEAERVRGLV 216
Cdd:cd20663    81 gkksLEQWVTEEAGHLCAaftDQAGRPFnpNTLLNKA---------------VCNVIASLIFARRFEYEDPRFIRLLKLL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 217 AESYAlAKKIFFASVLRRLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDTDMMDVLLA--AYADENAEY 294
Cdd:cd20663   146 EESLK-EESGFLPEVLNAFPVLLRIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPPRDLTDAFLAemEKAKGNPES 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 295 KITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHP 374
Cdd:cd20663   225 SFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGD 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 375 PFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGC 453
Cdd:cd20663   305 IVPLgVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQ--GHFVKPE---AFMPFSAGRRAC 379

                  ....*.
gi 1063712834 454 PGANLA 459
Cdd:cd20663   380 LGEPLA 385
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
191-494 7.04e-32

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: 127.44  E-value: 7.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 191 NIFCRMSMGRSFSEENGEAERVRGL------VAESYALAKkifFASVLRRL----LKKlriplFKkdimDVSNRFNELLE 260
Cdd:cd20676   127 NVICAMCFGKRYSHDDQELLSLVNLsdefgeVAGSGNPAD---FIPILRYLpnpaMKR-----FK----DINKRFNSFLQ 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 261 KILVEHNEKLDEEHKdTDMMDVLLA----AYADENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLER 336
Cdd:cd20676   195 KIVKEHYQTFDKDNI-RDITDSLIEhcqdKKLDENANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKK 273
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 337 LREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRlHPPF-----PLLTRKfeeRCEIKGFYIPEKTFLIINAYAWMRDP 411
Cdd:cd20676   274 IQEELDEVIGRERRPRLSDRPQLPYLEAFILETFR-HSSFvpftiPHCTTR---DTSLNGYYIPKDTCVFINQWQVNHDE 349
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 412 DSWEDPNEFKPERFLGSSrlGQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIK-GDKINMEETFe 490
Cdd:cd20676   350 KLWKDPSSFRPERFLTAD--GTEINKTESEKVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPpGVKVDMTPEY- 426

                  ....
gi 1063712834 491 GLTL 494
Cdd:cd20676   427 GLTM 430
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
253-479 1.13e-31

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: 126.63  E-value: 1.13e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 253 NRFNELLEKILVEHNEKLDEEHKDTdmMDVLLAAyADENAeYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSD 332
Cdd:cd11044   180 NKLLARLEQAIRERQEEENAEAKDA--LGLLLEA-KDEDG-EPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPD 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 333 VLERLREEIDSVvGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPD 412
Cdd:cd11044   256 VLEKLRQEQDAL-GLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPE 334
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712834 413 SWEDPNEFKPERFLgssrlgqvDEREEAQK----YIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIK 479
Cdd:cd11044   335 LYPDPERFDPERFS--------PARSEDKKkpfsLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELL 397
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
278-475 2.42e-31

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: 125.75  E-value: 2.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 278 DMMDVLLAAyADENAEyKIT----RNHIKSFFVElfvgGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQE 353
Cdd:cd20659   207 DFLDILLTA-RDEDGK-GLTdeeiRDEVDTFLFA----GHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEW 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 354 TDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgq 433
Cdd:cd20659   281 DDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL------- 353
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063712834 434 vdeREEAQK-----YIPFGGGRRGCPGANLASIFVGTAIGVMVQCFD 475
Cdd:cd20659   354 ---PENIKKrdpfaFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFE 397
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
192-459 2.98e-31

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: 125.45  E-value: 2.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 192 IFCRMSMGRSFS-EENGEAERVRGLVAESYALAKKI----FFASVLRRLLKKLRipLFKKDIMDVSNRFNELLEKILVEH 266
Cdd:cd20660   113 IICETAMGKSVNaQQNSDSEYVKAVYRMSELVQKRQknpwLWPDFIYSLTPDGR--EHKKCLKILHGFTNKVIQERKAEL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 267 NEKLDEEHKDTDM-----------MDVLLAAYADENaeyKIT----RNHIKSFFVElfvgGTDTSVQTTQWTMAEIINNS 331
Cdd:cd20660   191 QKSLEEEEEDDEDadigkrkrlafLDLLLEASEEGT---KLSdediREEVDTFMFE----GHDTTAAAINWALYLIGSHP 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 332 DVLERLREEIDSVVGTS-RMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRD 410
Cdd:cd20660   264 EVQEKVHEELDRIFGDSdRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRD 343
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063712834 411 PDSWEDPNEFKPERFLGssrlgqvdEREEAQK---YIPFGGGRRGCPGANLA 459
Cdd:cd20660   344 PRQFPDPEKFDPDRFLP--------ENSAGRHpyaYIPFSAGPRNCIGQKFA 387
PTZ00404 PTZ00404
cytochrome P450; Provisional
68-494 7.26e-31

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 125.22  E-value: 7.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  68 KISSKYGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAideSLVFGS--SGVVyAPYGDYLKFVKKII--AT 143
Cdd:PTZ00404   56 KMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIP---SIKHGTfyHGIV-TSSGEYWKRNREIVgkAM 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 144 K---------LLRPQVLERSRGLRAEELQ------RLYNRILDKAKM-----------NENVEIGKEA--TMLMNNIFCR 195
Cdd:PTZ00404  132 RktnlkhiydLLDDQVDVLIESMKKIESSgetfepRYYLTKFTMSAMfkyifnedisfDEDIHNGKLAelMGPMEQVFKD 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 196 MSMGRSFSEENgeaervrglVAESYALAKKIFFASVLRRLLKKLRiplfkkdimdvsNRFNEllekilveHNEKLDEEhK 275
Cdd:PTZ00404  212 LGSGSLFDVIE---------ITQPLYYQYLEHTDKNFKKIKKFIK------------EKYHE--------HLKTIDPE-V 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 276 DTDMMDVLLAAYADENAEYKITrnhIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETD 355
Cdd:PTZ00404  262 PRDLLDLLIKEYGTNTDDDILS---ILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSD 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 356 IPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEI-KGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSsrlgq 433
Cdd:PTZ00404  339 RQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNP----- 413
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712834 434 vderEEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDW-GIKGDKINMEETFeGLTL 494
Cdd:PTZ00404  414 ----DSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLkSIDGKKIDETEEY-GLTL 470
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
187-495 1.54e-30

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: 123.29  E-value: 1.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 187 MLMN---NIFCRMSMGRSFSEENGEAERVRGLVAESYAL---AKKIFFASVLRRLLKKLRIPLFKKDIMDVSNRFnelLE 260
Cdd:cd20652   111 VLMHslgNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLigvAGPVNFLPFLRHLPSYKKAIEFLVQGQAKTHAI---YQ 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 261 KILVEHNEKLDEEHKDTDMMDVLlaaYADENAEYKIT-RNHIKSFFVE---------LFVGGTDTSVQTTQWTMAEIINN 330
Cdd:cd20652   188 KIIDEHKRRLKPENPRDAEDFEL---CELEKAKKEGEdRDLFDGFYTDeqlhhlladLFGAGVDTTITTLRWFLLYMALF 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 331 SDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMR 409
Cdd:cd20652   265 PKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHM 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 410 DPDSWEDPNEFKPERFLGSSrlGQVDEREEaqkYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGI-KGDKINMEET 488
Cdd:cd20652   345 DPNLWEEPEEFRPERFLDTD--GKYLKPEA---FIPFQTGKRMCLGDELARMILFLFTARILRKFRIALpDGQPVDSEGG 419

                  ....*..
gi 1063712834 489 FEGLTLT 495
Cdd:cd20652   420 NVGITLT 426
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
190-502 1.56e-30

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


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 123.44  E-value: 1.56e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 190 NNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKI------FFASVLRRLlkklriPLFKKDIMDVSNRFNELLEKIL 263
Cdd:cd11026   115 SNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPwgqlynMFPPLLKHL------PGPHQKLFRNVEEIKSFIRELV 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 264 VEHNEKLD---------------EEHKDTdmmdvLLAAYADENAEYKItrnhiksffVELFVGGTDTSVQTTQWTMAEII 328
Cdd:cd11026   189 EEHRETLDpssprdfidcfllkmEKEKDN-----PNSEFHEENLVMTV---------LDLFFAGTETTSTTLRWALLLLM 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 329 NNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAW 407
Cdd:cd11026   255 KYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLgVPHAVTRDTKFRGYTIPKGTTVIPNLTSV 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 408 MRDPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGCPGANLAS-----IFVGtaigvMVQCFD--WGIKG 480
Cdd:cd11026   335 LRDPKQWETPEEFNPGHFLDEQ--GKFKKNE---AFMPFSAGKRVCLGEGLARmelflFFTS-----LLQRFSlsSPVGP 404
                         330       340
                  ....*....|....*....|..
gi 1063712834 481 DKINMEETFEGLTLtMVHPIKC 502
Cdd:cd11026   405 KDPDLTPRFSGFTN-SPRPYQL 425
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
191-459 7.33e-30

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: 121.79  E-value: 7.33e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 191 NIFCRMSMGRSF-SEENGEAERVRGLvaesYALAKKIFfasvlrrllKKLRIPLFKKDIMdvSNRFNELLE-----KIL- 263
Cdd:cd20680   123 DIICETAMGKKIgAQSNKDSEYVQAV----YRMSDIIQ---------RRQKMPWLWLDLW--YLMFKEGKEhnknlKILh 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 264 ----------VEHNEKLDEEHKDTD-----------MMDVLLAAYADENAE--YKITRNHIKSFFVElfvgGTDTSVQTT 320
Cdd:cd20680   188 tftdnviaerAEEMKAEEDKTGDSDgespskkkrkaFLDMLLSVTDEEGNKlsHEDIREEVDTFMFE----GHDTTAAAM 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 321 QWTMAEIINNSDVLERLREEIDSVVGTS-RMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTF 399
Cdd:cd20680   264 NWSLYLLGSHPEVQRKVHKELDEVFGKSdRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVN 343
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 400 LIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd20680   344 AVIIPYALHRDPRYFPEPEEFRPERFFPENSSGR-----HPYAYIPFSAGPRNCIGQRFA 398
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
73-499 1.53e-29

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: 120.93  E-value: 1.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSsGVVYAPYGDYLKFVKKIIATklLRPQVLE 152
Cdd:cd11046    10 YGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGK-GLIPADGEIWKKRRRALVPA--LHKDYLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 153 RSRGLRAEELQRLYNRILDKAKMNENVEigkeatmlMNNIFCRMSM---GRS-FSEENGEAERVRGLVAESYALakkIFF 228
Cdd:cd11046    87 MMVRVFGRCSERLMEKLDAAAETGESVD--------MEEEFSSLTLdiiGLAvFNYDFGSVTEESPVIKAVYLP---LVE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 229 ASVLRRLLkklrIPLFKKD-IMDVSNRF----------NELLEKILVEHNEKLDEEH-----------KDTDMMDVLLAA 286
Cdd:cd11046   156 AEHRSVWE----PPYWDIPaALFIVPRQrkflrdlkllNDTLDDLIRKRKEMRQEEDielqqedylneDDPSLLRFLVDM 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 287 yADENAEYKITRNHIKSFFVelfvGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVV 366
Cdd:cd11046   232 -RDEDVDSKQLRDDLMTMLI----AGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 367 KEGLRLHPPFPLLTRKFEERCEIKG--FYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssRLGQVDEREEAQ--K 442
Cdd:cd11046   307 NESLRLYPQPPVLIRRAVEDDKLPGggVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFL---DPFINPPNEVIDdfA 383
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712834 443 YIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGDKINMEETfeglTLTMVHP 499
Cdd:cd11046   384 FLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGMT----TGATIHT 436
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
155-459 2.51e-29

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: 119.61  E-value: 2.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 155 RGLRAEE--LQR----LYNRILDKAKMNENVEIGKEATMLMNNIFCRMSMGRSF-SEENGEAER-VRGLVAESYALAKKI 226
Cdd:cd11058    72 KALREQEpiIQRyvdlLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGESFgCLENGEYHPwVALIFDSIKALTIIQ 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 227 FFASV--LRRLLKKLRIPLFKKDIMDVsnrFNELLEKIlvehNEKLDEEHKDTDMMDVLLAAyadENAEYKITRNHIKSF 304
Cdd:cd11058   152 ALRRYpwLLRLLRLLIPKSLRKKRKEH---FQYTREKV----DRRLAKGTDRPDFMSYILRN---KDEKKGLTREELEAN 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 305 FVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIdsvvgTSRMIQETDI-----PNLPYLQAVVKEGLRLHPPFPL- 378
Cdd:cd11058   222 ASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEI-----RSAFSSEDDItldslAQLPYLNAVIQEALRLYPPVPAg 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LTRkfeeRC-----EIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQVDEREEAqkYIPFGGGRRGC 453
Cdd:cd11058   297 LPR----VVpaggaTIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNDKKEA--FQPFSVGPRNC 370

                  ....*.
gi 1063712834 454 PGANLA 459
Cdd:cd11058   371 IGKNLA 376
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
173-474 1.35e-27

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: 114.75  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 173 AKMNENVEIGKEATMLMNNIFCRMSMGRSFSEengeaervrglvaesyalAKKIFfaSVLRRLLK-------KLRIPLFK 245
Cdd:cd11052   108 GEEGEEVDVFEEFKALTADIISRTAFGSSYEE------------------GKEVF--KLLRELQKicaqanrDVGIPGSR 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 246 -------KDIMDVSNRFNELLEKILVEHNEKLDEEHKD---TDMMDVLLAAYADENAEYKITRNHI----KSFFvelFVG 311
Cdd:cd11052   168 flptkgnKKIKKLDKEIEDSLLEIIKKREDSLKMGRGDdygDDLLGLLLEANQSDDQNKNMTVQEIvdecKTFF---FAG 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 312 GTDTSVQTTqWTMAEIINNSDVLERLREEIDSVVGTSrmIQETD-IPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIK 390
Cdd:cd11052   245 HETTALLLT-WTTMLLAIHPEWQEKAREEVLEVCGKD--KPPSDsLSKLKTVSMVINESLRLYPPAVFLTRKAKEDIKLG 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 391 GFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGssrlGQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGV 469
Cdd:cd11052   322 GLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFAD----GVAKAAKHPMAFLPFGLGPRNCIGQNFATMEAKIVLAM 397

                  ....*
gi 1063712834 470 MVQCF 474
Cdd:cd11052   398 ILQRF 402
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
226-500 1.81e-27

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: 114.43  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 226 IFFASVLRRLLKKLRIPLFKKDIMDVsnrFNELLEKIlveHNEKLDEEHKD-TDMMDVLLAAYADENAE-YKITRNH--I 301
Cdd:cd20650   157 ITVFPFLTPILEKLNISVFPKDVTNF---FYKSVKKI---KESRLDSTQKHrVDFLQLMIDSQNSKETEsHKALSDLeiL 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 302 KSFFVELFvGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTR 381
Cdd:cd20650   231 AQSIIFIF-AGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLER 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 382 KFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRlGQVDEreeaQKYIPFGGGRRGCPGANLASI 461
Cdd:cd20650   310 VCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNK-DNIDP----YIYLPFGSGPRNCIGMRFALM 384
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1063712834 462 FVGTAIGVMVQCFDWGI-KGDKINMEETFEGLTLTMVhPI 500
Cdd:cd20650   385 NMKLALVRVLQNFSFKPcKETQIPLKLSLQGLLQPEK-PI 423
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
74-500 3.03e-27

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: 114.00  E-value: 3.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  74 GPLLHLRIFNVPIILVSSASVADEVFRiHDMNISSRGAAAIDESLVFGSSGVVYA-----PYGDYLKFVKKIIATKLLRP 148
Cdd:cd11040    12 GPIFTIRLGGQKIYVITDPELISAVFR-NPKTLSFDPIVIVVVGRVFGSPESAKKkegepGGKGLIRLLHDLHKKALSGG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 149 QVLERSRGLRAEELQRLYNRILDKaKMNENVEIGKEAtmLMNNIFCRMSM----GRSFSEENGEaervrgLVAESYAlak 224
Cdd:cd11040    91 EGLDRLNEAMLENLSKLLDELSLS-GGTSTVEVDLYE--WLRDVLTRATTealfGPKLPELDPD------LVEDFWT--- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 225 kifFASVLRRLLKKLRIPLFKKdimdVSNRFNELLEKILVEHNEKLDEEHKDTDMMdvllAAYADENAEYKITRNHIKSF 304
Cdd:cd11040   159 ---FDRGLPKLLLGLPRLLARK----AYAARDRLLKALEKYYQAAREERDDGSELI----RARAKVLREAGLSEEDIARA 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 305 FVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIP-----NLPYLQAVVKEGLRLHPPFPlL 379
Cdd:cd11040   228 ELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDLtdlltSCPLLDSTYLETLRLHSSST-S 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 380 TRKFEERC-EIKGFYIPEKTFLIINAYAWMRDPDSWE-DPNEFKPERFLGSSRLGQVDEReeAQKYIPFGGGRRGCPGAN 457
Cdd:cd11040   307 VRLVTEDTvLGGGYLLRKGSLVMIPPRLLHMDPEIWGpDPEEFDPERFLKKDGDKKGRGL--PGAFRPFGGGASLCPGRH 384
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1063712834 458 LASIFVGTAIGVMVQCFDWGIKGDKinmEETFEGLTLTMVHPI 500
Cdd:cd11040   385 FAKNEILAFVALLLSRFDVEPVGGG---DWKVPGMDESPGLGI 424
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
222-461 6.76e-27

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: 112.70  E-value: 6.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 222 LAKKIFFASVLRRLLKKLrIPLFKKDIMDVSNrFNELLEKIL------VEHNEKLDEEHKDTD------MMDVLLAAYAD 289
Cdd:cd11057   142 IAKRVLNPWLHPEFIYRL-TGDYKEEQKARKI-LRAFSEKIIekklqeVELESNLDSEEDEENgrkpqiFIDQLLELARN 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 290 ENaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTS-RMIQETDIPNLPYLQAVVKE 368
Cdd:cd11057   220 GE---EFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDgQFITYEDLQQLVYLEMVLKE 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 369 GLRLHPPFPLLTRKFEERCEIK-GFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGssrlgqvderEEAQK---- 442
Cdd:cd11057   297 TMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLP----------ERSAQrhpy 366
                         250       260
                  ....*....|....*....|
gi 1063712834 443 -YIPFGGGRRGCPGANLASI 461
Cdd:cd11057   367 aFIPFSAGPRNCIGWRYAMI 386
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
73-459 1.72e-26

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: 111.43  E-value: 1.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESlVFGSSGVVYAPyGDYLKFVKKIIATKLLRPQVLE 152
Cdd:cd20662     1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRER-IFNKNGLIFSS-GQTWKEQRRFALMTLRNFGLGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 153 RSRGLR-AEELQRLYNRILDKA--KMNENVEIGKEatmlMNNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKI--- 226
Cdd:cd20662    79 KSLEERiQEECRHLVEAIREEKgnPFNPHFKINNA----VSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPmsq 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 227 ---FFASVLRRLlkklriPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEhKDTDMMDVLL---AAYADENAEYKItRNH 300
Cdd:cd20662   155 lynAFPWIMKYL------PGSHQTVFSNWKKLKLFVSDMIDKHREDWNPD-EPRDFIDAYLkemAKYPDPTTSFNE-ENL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFfVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-L 379
Cdd:cd20662   227 ICST-LDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLnV 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 380 TRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSsrlGQVDEREeaqKYIPFGGGRRGCPGANLA 459
Cdd:cd20662   306 PREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLEN---GQFKKRE---AFLPFSMGKRACLGEQLA 379
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
67-475 6.43e-26

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: 109.97  E-value: 6.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  67 QKISSKYGPLLHLRIFNVPIILVSSASVADEV-----FRIHDMnissrgaAAIDESLVFGSSGVVYApYGDYLKFVKkii 141
Cdd:cd11068     6 LRLADELGPIFKLTLPGRRVVVVSSHDLIAELcdesrFDKKVS-------GPLEELRDFAGDGLFTA-YTHEPNWGK--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 142 ATKLLRPqvlersrGLRAEELQRLYNRILDKA--------KMN--ENVEIGKEATMLMNNIFCRMSMGRSF-SEENGEA- 209
Cdd:cd11068    75 AHRILMP-------AFGPLAMRGYFPMMLDIAeqlvlkweRLGpdEPIDVPDDMTRLTLDTIALCGFGYRFnSFYRDEPh 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 210 ----ERVRGLvAESYALAKKIFFASVLRRLLKKLriplFKKDImdvsnRFNELLEKILVEHNEKLDEEHKDtDMMDVLLA 285
Cdd:cd11068   148 pfveAMVRAL-TEAGRRANRPPILNKLRRRAKRQ----FREDI-----ALMRDLVDEIIAERRANPDGSPD-DLLNLMLN 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 286 AYADENAEyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGtSRMIQETDIPNLPYLQAV 365
Cdd:cd11068   217 GKDPETGE-KLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLG-DDPPPYEQVAKLRYIRRV 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 366 VKEGLRLHPPFPLLTRKFEERCEIKGFY-IPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLgssrlgqvDEREE---A 440
Cdd:cd11068   295 LDETLRLWPTAPAFARKPKEDTVLGGKYpLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFL--------PEEFRklpP 366
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1063712834 441 QKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFD 475
Cdd:cd11068   367 NAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFD 401
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
280-476 6.96e-26

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: 109.65  E-value: 6.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 280 MDVLLAAYADENAEYKITRNHIKSFfveLFvGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVG-----TSRMIQET 354
Cdd:cd11051   169 LDRYLKPEVRKRFELERAIDQIKTF---LF-AGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGpdpsaAAELLREG 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 355 D--IPNLPYLQAVVKEGLRLHPP----------FPLLTRKfeerceiKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKP 422
Cdd:cd11051   245 PelLNQLPYTTAVIKETLRLFPPagtarrgppgVGLTDRD-------GKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIP 317
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 423 ERFLGSsrlgqvderEEAQKYI------PFGGGRRGCPGANLASIFVGTAIGVMVQCFDW 476
Cdd:cd11051   318 ERWLVD---------EGHELYPpksawrPFERGPRNCIGQELAMLELKIILAMTVRRFDF 368
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
272-475 1.35e-25

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: 109.13  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 272 EEHKDTDMMDVLLAAYADENaeykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMI 351
Cdd:cd20645   202 QRYSQGPANDFLCDIYHDNE----LSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTP 277
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 352 QETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrl 431
Cdd:cd20645   278 RAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWL----- 352
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1063712834 432 gqvderEEAQK-----YIPFGGGRRGCPGANLASIFVGTAIGVMVQCFD 475
Cdd:cd20645   353 ------QEKHSinpfaHVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQ 395
PLN02738 PLN02738
carotene beta-ring hydroxylase
156-521 1.95e-25

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 110.39  E-value: 1.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 156 GLRAEELQRLYNRiLDKAKMN-ENVEigkeatmlMNNIFCRMSM---GRS-FSEENGEAERVRGLVAESYALAKKIFFAS 230
Cdd:PLN02738  243 SLFGQASDRLCQK-LDAAASDgEDVE--------MESLFSRLTLdiiGKAvFNYDFDSLSNDTGIVEAVYTVLREAEDRS 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 231 VlrRLLKKLRIPLFKkDIMDVSNRFNELLEKI-------------LVE------HNEKLDEehKDTDMMDVLLAAYADen 291
Cdd:PLN02738  314 V--SPIPVWEIPIWK-DISPRQRKVAEALKLIndtlddliaickrMVEeeelqfHEEYMNE--RDPSILHFLLASGDD-- 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 292 aeykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGtSRMIQETDIPNLPYLQAVVKEGLR 371
Cdd:PLN02738  387 ----VSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-DRFPTIEDMKKLKYTTRVINESLR 461
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 372 LHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFlgssRLGQVDEREEAQ--KYIPFGGG 449
Cdd:PLN02738  462 LYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERW----PLDGPNPNETNQnfSYLPFGGG 537
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712834 450 RRGCPGANLASIFVGTAIGVMVQCFDWGIKGDK--INME-----ETFEGLTLTMVHPIKCTPIPRTLPFVTSNLQSPSS 521
Cdd:PLN02738  538 PRKCVGDMFASFENVVATAMLVRRFDFQLAPGAppVKMTtgatiHTTEGLKMTVTRRTKPPVIPNLPMTPISDSPENVS 616
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
267-475 3.03e-25

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: 107.79  E-value: 3.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 267 NEKLDEEHkdTDMMDVLLAAYADENAeykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVG 346
Cdd:cd11083   194 NPALAEAP--ETLLAMMLAEDDPDAR---LTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLG 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 347 TSRM-IQETDIPNLPYLQAVVKEGLRLHPPFPLLtrkFEERCE---IKGFYIPEKT--FLIINAYAwmRDPDSWEDPNEF 420
Cdd:cd11083   269 GARVpPLLEALDRLPYLEAVARETLRLKPVAPLL---FLEPNEdtvVGDIALPAGTpvFLLTRAAG--LDAEHFPDPEEF 343
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063712834 421 KPERFLGSSRLGqvdEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFD 475
Cdd:cd11083   344 DPERWLDGARAA---EPHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFD 395
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
219-499 6.44e-25

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: 106.91  E-value: 6.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 219 SYALAKKIFFASVLRRLLKKLRIPLFKK--DIMDVSNRF-NELLEKILVEHNEKLDEEHKDTDMMDVLLAAYADENAEY- 294
Cdd:cd11064   148 SEAVAKRFIVPPWLWKLKRWLNIGSEKKlrEAIRVIDDFvYEVISRRREELNSREEENNVREDLLSRFLASEEEEGEPVs 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 295 -KITRNHIKSFFVelfvGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVV-----GTSRMIQETDIPNLPYLQAVVKE 368
Cdd:cd11064   228 dKFLRDIVLNFIL----AGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSE 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 369 GLRLHPPFPlltrkFEERCEIK------GFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGSSRLGQvdeREEAQ 441
Cdd:cd11064   304 SLRLYPPVP-----FDSKEAVNddvlpdGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLR---PESPY 375
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 442 KYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDwgikgdkINMEETFE-----GLTLTMVHP 499
Cdd:cd11064   376 KFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFD-------FKVVPGHKvepkmSLTLHMKGG 431
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
307-475 1.04e-24

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: 106.38  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 307 ELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEER 386
Cdd:cd20648   241 ELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDR 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 387 -CEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGssrlgqvdEREEAQKY--IPFGGGRRGCPGANLASIFV 463
Cdd:cd20648   321 dIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLG--------KGDTHHPYasLPFGFGKRSCIGRRIAELEV 392
                         170
                  ....*....|..
gi 1063712834 464 GTAIGVMVQCFD 475
Cdd:cd20648   393 YLALARILTHFE 404
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
253-494 3.48e-24

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: 105.09  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 253 NR--FNELLEKILvEHNEKLDEEHKdTDMMDVLLAAY---ADENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEI 327
Cdd:cd20675   185 NRefYNFVLDKVL-QHRETLRGGAP-RDMMDAFILALekgKSGDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 328 INNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLL----TRKfeeRCEIKGFYIPEKTFLIIN 403
Cdd:cd20675   263 VRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTiphaTTA---DTSILGYHIPKDTVVFVN 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 404 AYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDeREEAQKYIPFGGGRRGCPGANLASI--FVGTAIgVMVQCFDWGIKGD 481
Cdd:cd20675   340 QWSVNHDPQKWPNPEVFDPTRFLDEN--GFLN-KDLASSVMIFSVGKRRCIGEELSKMqlFLFTSI-LAHQCNFTANPNE 415
                         250
                  ....*....|...
gi 1063712834 482 KINMEETFeGLTL 494
Cdd:cd20675   416 PLTMDFSY-GLTL 427
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
253-463 4.20e-24

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: 104.79  E-value: 4.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 253 NRFNELLEKILVEHNEKLDEEHKdTDMMDVLLAAYADENAEYK---ITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIIN 329
Cdd:cd20677   187 SRLNNFIAKSVQDHYATYDKNHI-RDITDALIALCQERKAEDKsavLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIK 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 330 NSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRlHPPF-----PLLTRKfeeRCEIKGFYIPEKTFLIINA 404
Cdd:cd20677   266 YPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFR-HSSFvpftiPHCTTA---DTTLNGYFIPKDTCVFINM 341
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712834 405 YAWMRDPDSWEDPNEFKPERFLGSSrlGQVDeREEAQKYIPFGGGRRGCPGANLA--SIFV 463
Cdd:cd20677   342 YQVNHDETLWKDPDLFMPERFLDEN--GQLN-KSLVEKVLIFGMGVRKCLGEDVArnEIFV 399
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
314-476 8.59e-24

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 103.55  E-value: 8.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 314 DTSVQTTQWTMAEIINNSDVLERLREEIDSVvGTSRMIQEtDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFY 393
Cdd:cd11045   225 DTTTSTLTSMAYFLARHPEWQERLREESLAL-GKGTLDYE-DLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYR 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 394 IPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQK----YIPFGGGRRGCPGANLASIFVGTAIGV 469
Cdd:cd11045   303 IPAGTLVAVSPGVTHYMPEYWPNPERFDPERFS--------PERAEDKVhryaWAPFGGGAHKCIGLHFAGMEVKAILHQ 374

                  ....*..
gi 1063712834 470 MVQCFDW 476
Cdd:cd11045   375 MLRRFRW 381
PLN02936 PLN02936
epsilon-ring hydroxylase
248-485 1.12e-23

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 104.10  E-value: 1.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 248 IMDVSNRFNELLEKILVEHNEKLDEEH----KDTDMMDVLLAAYADenaeykITRNHIKSFFVELFVGGTDTSVQTTQWT 323
Cdd:PLN02936  228 IRETVEDLVDKCKEIVEAEGEVIEGEEyvndSDPSVLRFLLASREE------VSSVQLRDDLLSMLVAGHETTGSVLTWT 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 324 MAEIINNSDVLERLREEIDSVVGTsRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFY-IPEKTFLII 402
Cdd:PLN02936  302 LYLLSKNPEALRKAQEELDRVLQG-RPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYkVNAGQDIMI 380
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 403 NAYAWMRDPDSWEDPNEFKPERFlgSSRLGQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGD- 481
Cdd:PLN02936  381 SVYNIHRSPEVWERAEEFVPERF--DLDGPVPNETNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPDq 458

                  ....
gi 1063712834 482 KINM 485
Cdd:PLN02936  459 DIVM 462
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
73-511 3.31e-23

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: 102.01  E-value: 3.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834  73 YGPLLHLRIFNVPIILVSSASVADEVFRIHDMNISSRGAAAIDESLVFGSSG--VVYAPYGDYLKFVKKIIATKLLRPQV 150
Cdd:cd11066     1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTFHKVVSSTQGftIGTSPWDESCKRRRKAAASALNRPAV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 151 LERSRGLRAEE---LQRLYNrilDKAKMNENVEIGKEATMLMNNIFCRMSMGRSFsEENGEAErvrgLVAESYALAKKIf 227
Cdd:cd11066    81 QSYAPIIDLESksfIRELLR---DSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRL-DCVDDDS----LLLEIIEVESAI- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 228 faSVLRRLLKKLR--IPLFK--KDIMDVSNRFNELLEKILVEHN---EKLDEEHKDTDMMDVLLAAyADENAEYKITRNH 300
Cdd:cd11066   152 --SKFRSTSSNLQdyIPILRyfPKMSKFRERADEYRNRRDKYLKkllAKLKEEIEDGTDKPCIVGN-ILKDKESKLTDAE 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFFVELFVGGTDTSVQTTQWTMAEII--NNSDVLERLREEIDSVVGTSRMIQE--TDIPNLPYLQAVVKEGLRLHPPF 376
Cdd:cd11066   229 LQSICLTMVSAGLDTVPLNLNHLIGHLShpPGQEIQEKAYEEILEAYGNDEDAWEdcAAEEKCPYVVALVKETLRYFTVL 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 377 PL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRlgqvDEREEAQKYiPFGGGRRGCPG 455
Cdd:cd11066   309 PLgLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASG----DLIPGPPHF-SFGAGSRMCAG 383
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712834 456 ANLASIFVGTAIGVMVQCFDWGIKGDKINMEetfegltltmVHPIKCTPIPRTLPF 511
Cdd:cd11066   384 SHLANRELYTAICRLILLFRIGPKDEEEPME----------LDPFEYNACPTALVA 429
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
316-455 3.53e-23

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: 101.62  E-value: 3.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 316 SVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRM----IQETDIPNLPYLQAVVKEGLRLHPPfPLLTRKFEERCEIKG 391
Cdd:cd20635   226 AIPITFWTLAFILSHPSVYKKVMEEISSVLGKAGKdkikISEDDLKKMPYIKRCVLEAIRLRSP-GAITRKVVKPIKIKN 304
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712834 392 FYIPEKTFLIINAYaWM-RDPDSWEDPNEFKPERFLGSSrlgqVDEREEAQKYIPFGGGRRGCPG 455
Cdd:cd20635   305 YTIPAGDMLMLSPY-WAhRNPKYFPDPELFKPERWKKAD----LEKNVFLEGFVAFGGGRYQCPG 364
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
232-482 6.12e-23

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


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 101.22  E-value: 6.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 232 LRRLLKKLRiplfkkdimdvsnrfnELLEKILVEH--NEKLDEEHKDTDMMDVLLAAyADENAEYKITRNHIKSFFveLF 309
Cdd:cd11041   176 LRRLLRRAR----------------PLIIPEIERRrkLKKGPKEDKPNDLLQWLIEA-AKGEGERTPYDLADRQLA--LS 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 310 VGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT-RKFEERCE 388
Cdd:cd11041   237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLrRKVLKDVT 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 389 IK-GFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssRLGQVDEREEA-------QKYIPFGGGRRGCPGANLAS 460
Cdd:cd11041   317 LSdGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFY---RLREQPGQEKKhqfvstsPDFLGFGHGRHACPGRFFAS 393
                         250       260
                  ....*....|....*....|..
gi 1063712834 461 IFVGTAIGVMVQCFDWGIKGDK 482
Cdd:cd11041   394 NEIKLILAHLLLNYDFKLPEGG 415
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
307-459 1.70e-22

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: 99.73  E-value: 1.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 307 ELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEER 386
Cdd:cd20646   240 ELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEK 319
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712834 387 CEIKGFYI-PEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLgqvdeREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd20646   320 EVVVGDYLfPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGL-----KHHPFGSIPFGYGVRACVGRRIA 388
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
184-459 2.70e-22

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: 99.11  E-value: 2.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 184 EATMLMN----NIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKiffASV-LRRLLKKLR-IPLFKKDIMDVSNRFNE 257
Cdd:cd20664   105 ETTLSMNvavsNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGS---PSVqLYNMFPWLGpFPGDINKLLRNTKELND 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 258 LLEKILVEHNEKLDEeHKDTDMMDVLLA----------AYADENAEYKITRNhiksffveLFVGGTDTSVQTTQWTMAEI 327
Cdd:cd20664   182 FLMETFMKHLDVLEP-NDQRGFIDAFLVkqqeeeessdSFFHDDNLTCSVGN--------LFGAGTDTTGTTLRWGLLLM 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 328 INNSDVLERLREEIDSVVGtSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYA 406
Cdd:cd20664   253 MKYPEIQKKVQEEIDRVIG-SRQPQVEHRKNMPYTDAVIHEIQRFANIVPMnLPHATTRDVTFRGYFIPKGTYVIPLLTS 331
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 407 WMRDPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGCPGANLA 459
Cdd:cd20664   332 VLQDKTEWEKPEEFNPEHFLDSQ--GKFVKRD---AFMPFSAGRRVCIGETLA 379
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
306-461 4.12e-22

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: 98.76  E-value: 4.12e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 306 VELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFE 384
Cdd:cd20667   231 IDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCV 310
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712834 385 ERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGCPGANLASI 461
Cdd:cd20667   311 TSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKD--GNFVMNE---AFLPFSAGHRVCLGEQLARM 382
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
295-475 5.36e-22

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: 98.45  E-value: 5.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 295 KITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHP 374
Cdd:cd20647   232 ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFP 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 375 PFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRLGQVDEREEaqkyIPFGGGRRGCP 454
Cdd:cd20647   312 VLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGS----IPFGYGIRSCI 387
                         170       180
                  ....*....|....*....|.
gi 1063712834 455 GANLASIFVGTAIGVMVQCFD 475
Cdd:cd20647   388 GRRIAELEIHLALIQLLQNFE 408
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
189-459 5.73e-22

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: 98.30  E-value: 5.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 189 MNNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKIF------FASVLRRllkklrIPLFKKDIMDVSNRFNELLEKI 262
Cdd:cd20669   114 VSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWgelyniFPSVMDW------LPGPHQRIFQNFEKLRDFIAES 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 263 LVEHNEKLDEEhKDTDMMDVLLAAYADENaeykitRNHIKSFFVE--------LFVGGTDTSVQTTQWTMAEIINNSDVL 334
Cdd:cd20669   188 VREHQESLDPN-SPRDFIDCFLTKMAEEK------QDPLSHFNMEtlvmtthnLLFGGTETVSTTLRYGFLILMKYPKVA 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 335 ERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDS 413
Cdd:cd20669   261 ARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMsLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQ 340
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1063712834 414 WEDPNEFKPERFLgssrlgqvDEREEAQK---YIPFGGGRRGCPGANLA 459
Cdd:cd20669   341 FKDPQEFNPEHFL--------DDNGSFKKndaFMPFSAGKRICLGESLA 381
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
156-475 5.85e-22

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: 98.29  E-value: 5.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 156 GLRAEELQRlYNRILDKAKMNENV-----EIGKEATMLMNNIFCRMSMGRSFseENGEAERVRGLVAE---------SYA 221
Cdd:cd20639    63 SLRGEKWAH-HRRVITPAFHMENLkrlvpHVVKSVADMLDKWEAMAEAGGEG--EVDVAEWFQNLTEDvisrtafgsSYE 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 222 LAKKIF--------FASVLRRllkKLRIPLF-----KKdimdvsNRFNELLEK-------ILVEHNEKLDEEHKD----T 277
Cdd:cd20639   140 DGKAVFrlqaqqmlLAAEAFR---KVYIPGYrflptKK------NRKSWRLDKeirksllKLIERRQTAADDEKDdedsK 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 278 DMMDVLLAAYADENaEYKITRNHI----KSFFvelFVGGTDTSVQTTqWTMAEIINNSDVLERLREEIDSVVGTSRMIQE 353
Cdd:cd20639   211 DLLGLMISAKNARN-GEKMTVEEIieecKTFF---FAGKETTSNLLT-WTTVLLAMHPEWQERARREVLAVCGKGDVPTK 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 354 TDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGssrlG 432
Cdd:cd20639   286 DHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFAD----G 361
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1063712834 433 QVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFD 475
Cdd:cd20639   362 VARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFE 404
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
308-459 7.10e-21

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: 94.82  E-value: 7.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 308 LFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRmiQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERC 387
Cdd:cd20614   216 LVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAGDVPR--TPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEI 293
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 388 EIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSR-LGQVderEEAQkyipFGGGRRGCPGANLA 459
Cdd:cd20614   294 ELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRaPNPV---ELLQ----FGGGPHFCLGYHVA 359
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
259-459 2.42e-20

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


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 93.24  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 259 LEKILVEHNEKLDEEHKDTDMMDVLLAayadenaEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLR 338
Cdd:cd20643   200 IQNIYRDLRQKGKNEHEYPGILANLLL-------QDKLPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLR 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 339 EEidsvVGTSRMIQETDIPNL----PYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSW 414
Cdd:cd20643   273 AE----VLAARQEAQGDMVKMlksvPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVF 348
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063712834 415 EDPNEFKPERFLgssrlgqvdeREEAQ--KYIPFGGGRRGCPGANLA 459
Cdd:cd20643   349 PKPEKYDPERWL----------SKDIThfRNLGFGFGPRQCLGRRIA 385
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
307-476 5.54e-20

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 92.57  E-value: 5.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 307 ELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEE 385
Cdd:cd20661   245 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSK 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 386 RCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGCPGANLASIFVGT 465
Cdd:cd20661   325 DAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSN--GQFAKKE---AFVPFSLGRRHCLGEQLARMEMFL 399
                         170
                  ....*....|.
gi 1063712834 466 AIGVMVQCFDW 476
Cdd:cd20661   400 FFTALLQRFHL 410
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
310-459 1.31e-18

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: 88.36  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 310 VGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEI 389
Cdd:cd20649   271 IAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVV 350
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 390 KGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSRlgqvdEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd20649   351 LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAK-----QRRHPFVYLPFGAGPRSCIGMRLA 415
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
306-461 4.24e-18

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


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 86.39  E-value: 4.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 306 VELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEE 385
Cdd:cd20671   229 LDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAA 308
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712834 386 RCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGCPGANLASI 461
Cdd:cd20671   309 DTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAE--GKFVKKE---AFLPFSAGRRVCVGESLART 379
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
278-467 5.06e-18

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: 86.56  E-value: 5.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 278 DMMDVLLAAyADENAEY---KITRNHIKSFFVElfvgGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQET 354
Cdd:cd20678   219 DFLDILLFA-KDENGKSlsdEDLRAEVDTFMFE----GHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWE 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 355 DIPNLPYLQAVVKEGLRLHPPFPLLTRK------FEErceikGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGS 428
Cdd:cd20678   294 HLDQMPYTTMCIKEALRLYPPVPGISRElskpvtFPD-----GRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPE 368
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063712834 429 SrlgqVDEReEAQKYIPFGGGRRGCPGANLASIFVGTAI 467
Cdd:cd20678   369 N----SSKR-HSHAFLPFSAGPRNCIGQQFAMNEMKVAV 402
PLN02302 PLN02302
ent-kaurenoic acid oxidase
268-463 7.39e-18

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 86.31  E-value: 7.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 268 EKLDEEHKDTDMMDVLLAAyADENAEyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVG- 346
Cdd:PLN02302  257 RKQNISPRKKDMLDLLLDA-EDENGR-KLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKk 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 347 ---TSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIinayAWMR----DPDSWEDPNE 419
Cdd:PLN02302  335 rppGQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVL----AWFRqvhmDPEVYPNPKE 410
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063712834 420 FKPERFlgssrlgqvdEREEAQ--KYIPFGGGRRGCPGANLA----SIFV 463
Cdd:PLN02302  411 FDPSRW----------DNYTPKagTFLPFGLGSRLCPGNDLAkleiSIFL 450
PLN02290 PLN02290
cytokinin trans-hydroxylase
162-478 1.31e-17

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 85.64  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 162 LQRLYNRIldkAKMNENVEIGKEATMLMNNIFCRMSMGRSFseENGEA-----ERVRGLVAES---YALAKKIFFASVLR 233
Cdd:PLN02290  183 LQSLQKAV---ESGQTEVEIGEYMTRLTADIISRTEFDSSY--EKGKQifhllTVLQRLCAQAtrhLCFPGSRFFPSKYN 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 234 RLLKKLRIPL---------FKKDIMDV---SNRFNELLEKILVEHnekldeEHKDTDMMDVLLAAYADEnaeykitrnhI 301
Cdd:PLN02290  258 REIKSLKGEVerllmeiiqSRRDCVEIgrsSSYGDDLLGMLLNEM------EKKRSNGFNLNLQLIMDE----------C 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 302 KSFFvelFVGGTDTSVQTTqWTMAEIINNSDVLERLREEIDSVVGtsrmiQET----DIPNLPYLQAVVKEGLRLHPPFP 377
Cdd:PLN02290  322 KTFF---FAGHETTALLLT-WTLMLLASNPTWQDKVRAEVAEVCG-----GETpsvdHLSKLTLLNMVINESLRLYPPAT 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 378 LLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLGSSrlgqvdeREEAQKYIPFGGGRRGCPGA 456
Cdd:PLN02290  393 LLPRMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRP-------FAPGRHFIPFAAGPRNCIGQ 465
                         330       340
                  ....*....|....*....|..
gi 1063712834 457 NLASIFVGTAIGVMVQCFDWGI 478
Cdd:PLN02290  466 AFAMMEAKIILAMLISKFSFTI 487
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
264-459 2.15e-17

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: 84.46  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 264 VEHNEKLDEEHKDTDMMDVLLAAYADE----NAEYkitrnHIKSFF---VELFVGGTDTSVQTTQWTMAEIINNSDVLER 336
Cdd:cd20668   188 VEHNQRTLDPNSPRDFIDSFLIRMQEEkknpNTEF-----YMKNLVmttLNLFFAGTETVSTTLRYGFLLLMKHPEVEAK 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 337 LREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKT--FLIINAYawMRDPDS 413
Cdd:cd20668   263 VHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKDTKFRDFFLPKGTevFPMLGSV--LKDPKF 340
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1063712834 414 WEDPNEFKPERFLgssrlgqvDEREEAQK---YIPFGGGRRGCPGANLA 459
Cdd:cd20668   341 FSNPKDFNPQHFL--------DDKGQFKKsdaFVPFSIGKRYCFGEGLA 381
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
275-459 3.18e-17

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: 83.97  E-value: 3.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 275 KDTDMMDVLLAAyADENAEyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVG--TSRMIQ 352
Cdd:cd20679   221 KTLDFIDVLLLS-KDEDGK-ELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKdrEPEEIE 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 353 ETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEErcEIK---GFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFlgss 429
Cdd:cd20679   299 WDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQ--DIVlpdGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF---- 372
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063712834 430 rlgqvdEREEAQK-----YIPFGGGRRGCPGANLA 459
Cdd:cd20679   373 ------DPENSQGrsplaFIPFSAGPRNCIGQTFA 401
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
219-474 1.13e-16

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: 82.07  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 219 SYALAKKIFfaSVLRRLLKK-------LRIPLFKKDIMDVSNRFNELLEKI------LVEHNEKLDEEHKDTdMMDVLLA 285
Cdd:cd20640   140 SYSKGKEIF--SKLRELQKAvskqsvlFSIPGLRHLPTKSNRKIWELEGEIrslileIVKEREEECDHEKDL-LQAILEG 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 286 AYA--DENAEYKitrnhikSFFVE----LFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGtSRMIQETDIPNL 359
Cdd:cd20640   217 ARSscDKKAEAE-------DFIVDncknIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK-GGPPDADSLSRM 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 360 PYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFlgssRLGQVDERE 438
Cdd:cd20640   289 KTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERF----SNGVAAACK 364
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1063712834 439 EAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCF 474
Cdd:cd20640   365 PPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKF 400
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
180-500 2.67e-16

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: 81.03  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 180 EIGKEATMLMNNIFCRMSMGRSFSEENGEAE-RVRGLVAES-----YALAKKIFFASVLRRLLKkLRipLFKKDIMDVSN 253
Cdd:cd20636    78 ELHRQRRKVLARVFSRAALESYLPRIQDVVRsEVRGWCRGPgpvavYTAAKSLTFRIAVRILLG-LR--LEEQQFTYLAK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 254 RFNELLEKI---------------------LVEHNEKLDEE--HKD-----TDMMDVLLAAyADENAeYKITRNHIKSFF 305
Cdd:cd20636   155 TFEQLVENLfslpldvpfsglrkgikardiLHEYMEKAIEEklQRQqaaeyCDALDYMIHS-ARENG-KELTMQELKESA 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 306 VELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVvGTSR-------MIQETDIPNLPYLQAVVKEGLRLHPPFPL 378
Cdd:cd20636   233 VELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVSH-GLIDqcqccpgALSLEKLSRLRYLDCVVKEVLRLLPPVSG 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 379 LTRKFEERCEIKGFYIPeKTFLIInaYAwMRDPDS----WEDPNEFKPERFlGSSRlgqvdEREEAQK--YIPFGGGRRG 452
Cdd:cd20636   312 GYRTALQTFELDGYQIP-KGWSVM--YS-IRDTHEtaavYQNPEGFDPDRF-GVER-----EESKSGRfnYIPFGGGVRS 381
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1063712834 453 CPGANLASIFVGTAIGVMVQCFDWGIKgdkinmEETFEGL-TLTMVHPI 500
Cdd:cd20636   382 CIGKELAQVILKTLAVELVTTARWELA------TPTFPKMqTVPIVHPV 424
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
225-459 6.76e-16

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: 79.71  E-value: 6.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 225 KIFFasVLRRLLKKlriplFKKDIMDVSNRFNELLEK--ILVEHNEKLDEEHkdtDMMDVLLaaYADENAEykITRNHIK 302
Cdd:cd20616   161 DIFF--KISWLYKK-----YEKAVKDLKDAIEILIEQkrRRISTAEKLEDHM---DFATELI--FAQKRGE--LTAENVN 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 303 SFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGtSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRK 382
Cdd:cd20616   227 QCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRK 305
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712834 383 FEERCEIKGFYIPEKTFLIINAYAWMRDPdSWEDPNEFKPERFlgssrlgqvDEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd20616   306 ALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF---------EKNVPSRYFQPFGFGPRSCVGKYIA 372
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
264-476 7.45e-16

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: 79.86  E-value: 7.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 264 VEHN--EKLDEEHKDTDMMDVL--LAAYADENAEyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLRE 339
Cdd:cd20638   191 IEENirAKIQREDTEQQCKDALqlLIEHSRRNGE-PLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRK 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 340 EIDSVVGTSRMIQETD------IPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPeKTFLIINAYAWMRD-PD 412
Cdd:cd20638   270 ELQEKGLLSTKPNENKelsmevLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIP-KGWNVIYSICDTHDvAD 348
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063712834 413 SWEDPNEFKPERFLG-----SSRLGqvdereeaqkYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDW 476
Cdd:cd20638   349 IFPNKDEFNPDRFMSplpedSSRFS----------FIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDW 407
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
239-476 9.75e-16

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 79.64  E-value: 9.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 239 LRIPLFK---KDIMDVSNRFNELLEKILVEHNEKLDE-EHKDTDMMDVLLAA---YADEnaeykitrnHIKSFFVELFVG 311
Cdd:PLN02987  208 VPLPLFSttyRRAIQARTKVAEALTLVVMKRRKEEEEgAEKKKDMLAALLASddgFSDE---------EIVDFLVALLVA 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 312 GTDTSVQTTQWTMAEIINNSDVLERLREEIDSV---VGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCE 388
Cdd:PLN02987  279 GYETTSTIMTLAVKFLTETPLALAQLKEEHEKIramKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIE 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 389 IKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLGSSrlgqvDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIG 468
Cdd:PLN02987  359 VKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNS-----GTTVPSNVFTPFGGGPRLCPGYELARVALSVFLH 433

                  ....*...
gi 1063712834 469 VMVQCFDW 476
Cdd:PLN02987  434 RLVTRFSW 441
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
179-474 3.30e-15

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: 77.87  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 179 VEIGKEATMLMNNIFCRMSMGRSFsEENGEaervrglVAESYALAKKIFFASvlrrlLKKLRIPLFK-------KDIMDV 251
Cdd:cd20641   117 VEVSREFQDLTADIIATTAFGSSY-AEGIE-------VFLSQLELQKCAAAS-----LTNLYIPGTQylptprnLRVWKL 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 252 SNRFNELLEKILvehNEKLDEEHKD--TDMMDVLLAAYADE----NAEYKITRNHI----KSFFVelfvGGTDTSVQTTQ 321
Cdd:cd20641   184 EKKVRNSIKRII---DSRLTSEGKGygDDLLGLMLEAASSNeggrRTERKMSIDEIidecKTFFF----AGHETTSNLLT 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 322 WTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLI 401
Cdd:cd20641   257 WTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTII 336
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712834 402 INAYAWMRDPDSW-EDPNEFKPERFlgSSRLGQVDEREEAqkYIPFGGGRRGCPGANLASIFVGTAIGVMVQCF 474
Cdd:cd20641   337 IPIAKLHRDKEVWgSDADEFNPLRF--ANGVSRAATHPNA--LLSFSLGPRACIGQNFAMIEAKTVLAMILQRF 406
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
219-474 7.66e-15

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: 76.55  E-value: 7.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 219 SYALAKKIF-----FASVLRRLLKKLRIPLFK--------------KDIMDvsnrfneLLEKIlVEHNEKLDE--EHKDT 277
Cdd:cd20642   135 SYEEGKKIFelqkeQGELIIQALRKVYIPGWRflptkrnrrmkeieKEIRS-------SLRGI-INKREKAMKagEATND 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 278 DMMDVLLAAYADENAEYKITRNHI---------KSFFvelFVGGTDTSVQTTqWTMAEIINNSDVLERLREEIDSVVGTs 348
Cdd:cd20642   207 DLLGILLESNHKEIKEQGNKNGGMstedvieecKLFY---FAGQETTSVLLV-WTMVLLSQHPDWQERAREEVLQVFGN- 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 349 rmiQETDIPNLPYLQAV---VKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPER 424
Cdd:cd20642   282 ---NKPDFEGLNHLKVVtmiLYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPER 358
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063712834 425 F---LGSSRLGQVdereeaqKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCF 474
Cdd:cd20642   359 FaegISKATKGQV-------SYFPFGWGPRICIGQNFALLEAKMALALILQRF 404
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
107-459 8.61e-15

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: 76.36  E-value: 8.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 107 SSRGAAAIDEsLVFGSSGVVYAPyGDYLKFVKKI-IAT--------KLLRPQVLERSRGLrAEELQRLYNRILDKAKMNE 177
Cdd:cd20672    35 SGRGTIAVVD-PIFQGYGVIFAN-GERWKTLRRFsLATmrdfgmgkRSVEERIQEEAQCL-VEELRKSKGALLDPTFLFQ 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 178 NVeigkeatmlMNNIFCRMSMGRSFSEENGEAERVRGLVAESYALAKKifFASVLRRLLKKLrIPLFKKDIMDVSNRFNE 257
Cdd:cd20672   112 SI---------TANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISS--FSSQVFELFSGF-LKYFPGAHRQIYKNLQE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 258 LLEKI--LVE-HNEKLDEEHKdTDMMDVLLAAYADENAEYKITRNH--IKSFFVELFVGGTDTSVQTTQWTMAEIINNSD 332
Cdd:cd20672   180 ILDYIghSVEkHRATLDPSAP-RDFIDTYLLRMEKEKSNHHTEFHHqnLMISVLSLFFAGTETTSTTLRYGFLLMLKYPH 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 333 VLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKT--FLIINAYawMR 409
Cdd:cd20672   259 VAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIgVPHRVTKDTLFRGYLLPKNTevYPILSSA--LH 336
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063712834 410 DPDSWEDPNEFKPERFLGSSrlGQVDEREeaqKYIPFGGGRRGCPGANLA 459
Cdd:cd20672   337 DPQYFEQPDTFNPDHFLDAN--GALKKSE---AFMPFSTGKRICLGEGIA 381
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
234-493 1.22e-14

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: 76.18  E-value: 1.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 234 RLLKKLRIPLFKKDimdvsNRFNELLEKILvEHNEKLDEEHKDTDMMDVLLA---AYAD-ENAEYKITRNHIKSffvELF 309
Cdd:cd20622   198 RNQPSYRRAAKIKD-----DFLQREIQAIA-RSLERKGDEGEVRSAVDHMVRrelAAAEkEGRKPDYYSQVIHD---ELF 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 310 ---VGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSV----VGTSRM--IQETDIPNLPYLQAVVKEGLRLHPPFPLLT 380
Cdd:cd20622   269 gylIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAhpeaVAEGRLptAQEIAQARIPYLDAVIEEILRCANTAPILS 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 381 RKFEERCEIKGFYIPEKTFLIINAY---------------------AWMRDPDSWE--DPNEFKPERFLGSS-RLGQVDE 436
Cdd:cd20622   349 REATVDTQVLGYSIPKGTNVFLLNNgpsylsppieidesrrssssaAKGKKAGVWDskDIADFDPERWLVTDeETGETVF 428
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063712834 437 REEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGDKINMEETFEGLT 493
Cdd:cd20622   429 DPSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPEALSGYEAIDGLT 485
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
253-459 2.38e-14

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: 74.96  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 253 NRFNELLEKI------LVEHNEKLDEEHKDTDMMDV-LLAAYADENAEYkiTRNHIKSFFV---ELFVGGTDTSVQTTQW 322
Cdd:cd20670   171 NRIYYLIEELkdfiasRVKINEASLDPQNPRDFIDCfLIKMHQDKNNPH--TEFNLKNLVLttlNLFFAGTETVSSTLRY 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 323 TMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLI 401
Cdd:cd20670   249 GFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLgVPHNVIRDTQFRGYLLPKGTDVF 328
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063712834 402 INAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQK---YIPFGGGRRGCPGANLA 459
Cdd:cd20670   329 PLLGSVLKDPKYFRYPEAFYPQHFL--------DEQGRFKKneaFVPFSSGKRVCLGEAMA 381
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
301-459 6.48e-14

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: 73.72  E-value: 6.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 301 IKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLT 380
Cdd:cd20644   233 IKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQ 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 381 RKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQ--KYIPFGGGRRGCPGANL 458
Cdd:cd20644   313 RVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWL--------DIRGSGRnfKHLAFGFGMRQCLGRRL 384

                  .
gi 1063712834 459 A 459
Cdd:cd20644   385 A 385
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
277-463 9.97e-14

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: 72.96  E-value: 9.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 277 TDMMDVLLAAYADENAEykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEI--DSVVGTSRMIQET 354
Cdd:cd20637   205 ADALDILIESAKEHGKE--LTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrsNGILHNGCLCEGT 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 355 ----DIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINayawMRDPDS----WEDPNEFKPERFl 426
Cdd:cd20637   283 lrldTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYS----IRDTHDtapvFKDVDAFDPDRF- 357
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063712834 427 GSSRlgqVDEREEAQKYIPFGGGRRGCPGANLASIFV 463
Cdd:cd20637   358 GQER---SEDKDGRFHYLPFGGGVRTCLGKQLAKLFL 391
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
245-459 1.04e-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: 73.06  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 245 KKDIMDVSNRFNELLEKIlVEHNEKLDEEHKdTDMMDVLLAAYADENAEYKiTRNHIKSFFV---ELFVGGTDTSVQTTQ 321
Cdd:cd20665   171 NKLLKNVAYIKSYILEKV-KEHQESLDVNNP-RDFIDCFLIKMEQEKHNQQ-SEFTLENLAVtvtDLFGAGTETTSTTLR 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 322 WTMAEIINNSDVLERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPL-LTRkfEERCEIK--GFYIPEKT 398
Cdd:cd20665   248 YGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNnLPH--AVTCDTKfrNYLIPKGT 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063712834 399 FLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDEREEAQK---YIPFGGGRRGCPGANLA 459
Cdd:cd20665   326 TVITSLTSVLHDDKEFPNPEKFDPGHFL--------DENGNFKKsdyFMPFSAGKRICAGEGLA 381
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
314-497 1.19e-13

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: 72.70  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 314 DTSVQTTQWTMAEIINNSDVLERLREEI-----DSVVGTSRMIQETDIpnlpYLQAVVKEGLRLHP--PFPLLTRKFEER 386
Cdd:cd20615   229 DVTTGVLSWNLVFLAANPAVQEKLREEIsaareQSGYPMEDYILSTDT----LLAYCVLESLRLRPllAFSVPESSPTDK 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 387 cEIKGFYIPEKTFLIINAYAW-MRDPDSWEDPNEFKPERFLGSSRlgqvdeREEAQKYIPFGGGRRGCPGANLASIFVGT 465
Cdd:cd20615   305 -IIGGYRIPANTPVVVDTYALnINNPFWGPDGEAYRPERFLGISP------TDLRYNFWRFGFGPRKCLGQHVADVILKA 377
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063712834 466 AIGVMVQCFDWGIKGDKINMEETFEGLTLTMV 497
Cdd:cd20615   378 LLAHLLEQYELKLPDQGENEEDTFEGLPWIWV 409
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
273-472 1.62e-13

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: 71.95  E-value: 1.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 273 EHKDTDMMDVLLAAYA-DENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREeidsvvgtsrmi 351
Cdd:cd20629   164 AERRRAPGDDLISRLLrAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRR------------ 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 352 QETDIPnlpylqAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFkperflgssrl 431
Cdd:cd20629   232 DRSLIP------AAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVF----------- 294
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063712834 432 gqvDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQ 472
Cdd:cd20629   295 ---DIDRKPKPHLVFGGGAHRCLGEHLARVELREALNALLD 332
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
322-476 2.38e-13

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: 71.89  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 322 WTMAEIINNSDVLERLREEIDSVVG------TSRMIQEtdipnLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFY-I 394
Cdd:cd11082   242 WALQLLADHPDVLAKVREEQARLRPndepplTLDLLEE-----MKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTEDYtV 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 395 PEKTFLIINAYAWMRDPdsWEDPNEFKPERFLgssrlgqvDEREEAQKY----IPFGGGRRGCPGANLASIFVGTAIGVM 470
Cdd:cd11082   317 PKGTIVIPSIYDSCFQG--FPEPDKFDPDRFS--------PERQEDRKYkknfLVFGAGPHQCVGQEYAINHLMLFLALF 386

                  ....*.
gi 1063712834 471 VQCFDW 476
Cdd:cd11082   387 STLVDW 392
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
256-503 4.84e-13

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 71.19  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 256 NELLEKILV-EHNEKLDEEHKDTDMMDVLLAAYADENAEYKITR----NHIKSFFVELFVGGTDTSVQTTQWTMAEIINN 330
Cdd:PLN02169  252 NRMFAKIISsRRKEEISRAETEPYSKDALTYYMNVDTSKYKLLKpkkdKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKH 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 331 SDVLERLREEIDSvvgtsrMIQETDIPNLPYLQAVVKEGLRLHPPFPlLTRKFEERCEI--KGFYIPEKTFLIINAYAWM 408
Cdd:PLN02169  332 PQVMAKIRHEINT------KFDNEDLEKLVYLHAALSESMRLYPPLP-FNHKAPAKPDVlpSGHKVDAESKIVICIYALG 404
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 409 RDPDSW-EDPNEFKPERFLGSSrlGQVdEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWG-IKGDKInme 486
Cdd:PLN02169  405 RMRSVWgEDALDFKPERWISDN--GGL-RHEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKvIEGHKI--- 478
                         250
                  ....*....|....*..
gi 1063712834 487 ETFEGLTLTMVHPIKCT 503
Cdd:PLN02169  479 EAIPSILLRMKHGLKVT 495
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
335-459 5.48e-13

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: 70.75  E-value: 5.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 335 ERLREEIDSVVGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIK----GFYIPEKTFLIINAYAWMRD 410
Cdd:cd11071   261 ARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIEshdaSYKIKKGELLVGYQPLATRD 340
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712834 411 PDSWEDPNEFKPERFLGssrlgqvdEREEAQKYIPFGGGR---------RGCPGANLA 459
Cdd:cd11071   341 PKVFDNPDEFVPDRFMG--------EEGKLLKHLIWSNGPeteeptpdnKQCPGKDLV 390
PLN02774 PLN02774
brassinosteroid-6-oxidase
277-483 1.83e-12

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 69.42  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 277 TDMMDVLLAAyadENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEIDSVVGTSR---MIQE 353
Cdd:PLN02774  244 TDMLGYLMRK---EGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEHLAIRERKRpedPIDW 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 354 TDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPeKTFLIinaYAWMR----DPDSWEDPNEFKPERFLgss 429
Cdd:PLN02774  321 NDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIP-KGWRI---YVYTReinyDPFLYPDPMTFNPWRWL--- 393
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063712834 430 rlgqvDEREEAQKY-IPFGGGRRGCPGANLASIFVGTAIGVMVQCFDW-GIKGDKI 483
Cdd:PLN02774  394 -----DKSLESHNYfFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWeEVGGDKL 444
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
273-471 7.99e-12

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: 66.73  E-value: 7.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 273 EHKDTDMMDVLLAAYADENAeykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiq 352
Cdd:cd11080   169 VNPGSDLISILCTAEYEGEA---LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRAD------------ 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 353 etdiPNLpyLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKT--FLIINAYAwmRDPDSWEDPNEFKPERflgsSR 430
Cdd:cd11080   234 ----RSL--VPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTtvFCLIGAAN--RDPAAFEDPDTFNIHR----ED 301
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063712834 431 LGQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMV 471
Cdd:cd11080   302 LGIRSAFSGAADHLAFGSGRHFCVGAALAKREIEIVANQVL 342
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
334-475 9.26e-12

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 66.72  E-value: 9.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 334 LERLREEIDSVVGTsrmiqetdiPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDS 413
Cdd:cd20624   225 AARAREEAAVPPGP---------LARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFAPFFHRDDEA 295
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063712834 414 WEDPNEFKPERFLgssrlgqvdeREEAQKY---IPFGGGRRGCPGANLASIFVGTAIGVMVQCFD 475
Cdd:cd20624   296 LPFADRFVPEIWL----------DGRAQPDeglVPFSAGPARCPGENLVLLVASTALAALLRRAE 350
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
137-466 4.40e-11

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: 64.37  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 137 VKKIIATKLlRPQVLERsrgLRAEeLQRLYNRILDKAKMNENVEIGKE-ATMLMNNIFCRMsMGrsFSEENGEAERVrgl 215
Cdd:cd20630    69 VRKLVAPAF-TPRAIDR---LRAE-IQAIVDQLLDELGEPEEFDVIREiAEHIPFRVISAM-LG--VPAEWDEQFRR--- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 216 vaesyalakkifFASVLRRLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEhkdtDMMDVLLAAYADENaeyK 295
Cdd:cd20630   138 ------------FGTATIRLLPPGLDPEELETAAPDVTEGLALIEEVIAERRQAPVED----DLLTTLLRAEEDGE---R 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 296 ITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqetdiPNLpyLQAVVKEGLRlHPP 375
Cdd:cd20630   199 LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE----------------PEL--LRNALEEVLR-WDN 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 376 FPL--LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvdereEAQKYIPFGGGRRGC 453
Cdd:cd20630   260 FGKmgTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR--------------DPNANIAFGYGPHFC 325
                         330
                  ....*....|....*..
gi 1063712834 454 PGANLAS----IFVGTA 466
Cdd:cd20630   326 IGAALARleleLAVSTL 342
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
243-481 5.31e-11

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 64.57  E-value: 5.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 243 LFKKDiMDVSNRFNELLEKILVEHNEkLDEEHKDtdmmdvLLAAYADENAEykITRNHIKSFFVELFVGGTDTSVQTTQW 322
Cdd:PLN02196  217 LFHKS-MKARKELAQILAKILSKRRQ-NGSSHND------LLGSFMGDKEG--LTDEQIADNIIGVIFAARDTTASVLTW 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 323 TMAEIINNSDVLERLREEIDSVVGTS---RMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPE--K 397
Cdd:PLN02196  287 ILKYLAENPSVLEAVTEEQMAIRKDKeegESLTWEDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKgwK 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 398 TF-LIINAYawmRDPDSWEDPNEFKPERFlgssrlgqvderEEAQK---YIPFGGGRRGCPGANLASIFVGTAIGVMVQC 473
Cdd:PLN02196  367 VLpLFRNIH---HSADIFSDPGKFDPSRF------------EVAPKpntFMPFGNGTHSCPGNELAKLEISVLIHHLTTK 431

                  ....*...
gi 1063712834 474 FDWGIKGD 481
Cdd:PLN02196  432 YRWSIVGT 439
PLN02500 PLN02500
cytochrome P450 90B1
258-476 5.84e-11

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 64.50  E-value: 5.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 258 LLEKILVEHNEKLDEEHKDTDMMDVLLAAYADENaeykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERL 337
Cdd:PLN02500  241 FIERKMEERIEKLKEEDESVEEDDLLGWVLKHSN----LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQEL 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 338 REEIDSVVGTSRMIQET-----DIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPE--KTFLIINAYAWmrD 410
Cdd:PLN02500  317 REEHLEIARAKKQSGESelnweDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSgwKVLPVIAAVHL--D 394
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712834 411 PDSWEDPNEFKPERFL--GSSRLGQVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDW 476
Cdd:PLN02500  395 SSLYDQPQLFNPWRWQqnNNRGGSSGSSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNW 462
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
329-496 1.28e-10

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 63.56  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 329 NNSDVLERLREEIDSVVGTSRMIQETD-IPNLPYLQAVVKEGLRLHPPFPlLTRKFEERCEI--KGFYIPEKTFLIINAY 405
Cdd:PLN02426  322 KHPEVASAIREEADRVMGPNQEAASFEeMKEMHYLHAALYESMRLFPPVQ-FDSKFAAEDDVlpDGTFVAKGTRVTYHPY 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 406 AWMRDPDSW-EDPNEFKPERFLGSSRLgqvdEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCFDWGIKGDKIN 484
Cdd:PLN02426  401 AMGRMERIWgPDCLEFKPERWLKNGVF----VPENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVGRSNR 476
                         170
                  ....*....|..
gi 1063712834 485 MEETFEGLTLTM 496
Cdd:PLN02426  477 APRFAPGLTATV 488
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
361-455 1.45e-10

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: 62.93  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 361 YLQAVVKEGLRLHPPFPLL----TRKFEerceIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERFLgssrlgqvDE 436
Cdd:cd11067   264 YAEAFVQEVRRFYPFFPFVgaraRRDFE----WQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFL--------GW 331
                          90       100
                  ....*....|....*....|...
gi 1063712834 437 REEAQKYIPFGGG--RRG--CPG 455
Cdd:cd11067   332 EGDPFDFIPQGGGdhATGhrCPG 354
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
265-459 1.80e-10

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: 62.62  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 265 EHNEKLDEEHKDTDMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsv 344
Cdd:cd11078   177 DLVAERRREPRDDLISDLLAAADGDGE---RLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRAD---- 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 345 vgtsrmiqETDIPNlpylqaVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPER 424
Cdd:cd11078   250 --------PSLIPN------AVEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR 315
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063712834 425 flgssrlgqvderEEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11078   316 -------------PNARKHLTFGHGIHFCLGAALA 337
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
254-483 2.79e-10

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 62.45  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 254 RFNELLEKILVEHNEKLDEEHKDT-----DMMDVLLAAYADEnaeykITRNHIKSFFVELFVGGTDtSVQTTQWTMAEII 328
Cdd:PLN03141  205 RMVKLVKKIIEEKRRAMKNKEEDEtgipkDVVDVLLRDGSDE-----LTDDLISDNMIDMMIPGED-SVPVLMTLAVKFL 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 329 NNSDV-LERLREEIDSV----VGTSRMIQETDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIIN 403
Cdd:PLN03141  279 SDCPVaLQQLTEENMKLkrlkADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAY 358
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 404 AYAWMRDPDSWEDPNEFKPERFlgssrlgqvDERE-EAQKYIPFGGGRRGCPGANLA----SIFVGTaigvMVQCFDWGI 478
Cdd:PLN03141  359 FRSVHLDEENYDNPYQFNPWRW---------QEKDmNNSSFTPFGGGQRLCPGLDLArleaSIFLHH----LVTRFRWVA 425

                  ....*
gi 1063712834 479 KGDKI 483
Cdd:PLN03141  426 EEDTI 430
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
276-459 2.34e-09

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: 59.14  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 276 DTDMMDVLLAAYADENAeykITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqetd 355
Cdd:cd11035   169 GDDLISAILNAEIDGRP---LTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRED--------------- 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 356 iPNLpyLQAVVKEGLRLHPPfPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvd 435
Cdd:cd11035   231 -PEL--IPAAVEELLRRYPL-VNVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR----------- 295
                         170       180
                  ....*....|....*....|....
gi 1063712834 436 ereEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11035   296 ---KPNRHLAFGAGPHRCLGSHLA 316
PLN02648 PLN02648
allene oxide synthase
330-463 1.46e-08

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 57.25  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 330 NSDVLERLREEIDSVV---GTSRMIQetDIPNLPYLQAVVKEGLRLHPPFPL---------LTRKFEERCEIK------G 391
Cdd:PLN02648  303 GEELQARLAEEVRSAVkagGGGVTFA--ALEKMPLVKSVVYEALRIEPPVPFqygraredfVIESHDAAFEIKkgemlfG 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 392 FyipektfliiNAYAwMRDPDSWEDPNEFKPERFLGssrlgqvDEREEAQKYIPFGGGR---------RGCPGANL---- 458
Cdd:PLN02648  381 Y----------QPLV-TRDPKVFDRPEEFVPDRFMG-------EEGEKLLKYVFWSNGRetesptvgnKQCAGKDFvvlv 442

                  ....*
gi 1063712834 459 ASIFV 463
Cdd:PLN02648  443 ARLFV 447
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
322-425 2.93e-08

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: 55.98  E-value: 2.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 322 WTMAEIINNSDVLERLREEIDSVVGTSRMIQEtDIPNLPYLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLI 401
Cdd:cd20627   224 WAIYFLTTSEEVQKKLYKEVDQVLGKGPITLE-KIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVL 302
                          90       100
                  ....*....|....*....|....
gi 1063712834 402 INAYAWMRDPDSWEDPNEFKPERF 425
Cdd:cd20627   303 YALGVVLQDNTTWPLPYRFDPDRF 326
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
274-459 6.33e-08

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: 54.68  E-value: 6.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 274 HKDTDMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqe 353
Cdd:cd11038   191 EPGDDLISTLVAAEQDGD---RLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALRED------------- 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 354 tdiPNLPylQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSwedpneFKPERFlgssrlgq 433
Cdd:cd11038   255 ---PELA--PAAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRDPRV------FDADRF-------- 315
                         170       180
                  ....*....|....*....|....*.
gi 1063712834 434 vDEREEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11038   316 -DITAKRAPHLGFGGGVHHCLGAFLA 340
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
234-459 1.13e-07

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: 53.76  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 234 RLLKKLRIPLFKKDIMDVSNRFNELLEKILVEHNEKLDEEHKDtDMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGT 313
Cdd:cd11032   136 ALVSGLGDDSFEEEEVEEMAEALRELNAYLLEHLEERRRNPRD-DLISRLVEAEVDGE---RLTDEEIVGFAILLLIAGH 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 314 DTSvqttqwTMAeiINNS--------DVLERLREEIDsvvgtsrmiqetDIPNlpylqaVVKEGLRLHPPFPLLTRKFEE 385
Cdd:cd11032   212 ETT------TNL--LGNAvlcldedpEVAARLRADPS------------LIPG------AIEEVLRYRPPVQRTARVTTE 265
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063712834 386 RCEIKGFYIPEKTFLIinayAWM----RDPDSWEDPNEFKPERflgssrlgqvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11032   266 DVELGGVTIPAGQLVI----AWLasanRDERQFEDPDTFDIDR--------------NPNPHLSFGHGIHFCLGAPLA 325
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
362-459 2.30e-07

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: 52.74  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 362 LQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvdereEAQ 441
Cdd:cd11079   227 LPAAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR--------------HAA 292
                          90
                  ....*....|....*...
gi 1063712834 442 KYIPFGGGRRGCPGANLA 459
Cdd:cd11079   293 DNLVYGRGIHVCPGAPLA 310
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
277-472 5.38e-07

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: 51.78  E-value: 5.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 277 TDMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqetdi 356
Cdd:cd20625   181 DDLISALVAAEEDGD---RLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALLRAD---------------- 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 357 PNLpyLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYIP--EKTFLIINAyAwMRDPDSWEDPNEFKPERflgssrlgqv 434
Cdd:cd20625   242 PEL--IPAAVEELLRYDSPVQLTARVALEDVEIGGQTIPagDRVLLLLGA-A-NRDPAVFPDPDRFDITR---------- 307
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063712834 435 dereEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQ 472
Cdd:cd20625   308 ----APNRHLAFGAGIHFCLGAPLARLEAEIALRALLR 341
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
278-459 7.64e-07

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: 51.37  E-value: 7.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 278 DMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqETDIP 357
Cdd:cd11033   190 DLISVLANAEVDGE---PLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRAD------------PSLLP 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 358 NLpylqavVKEGLRLHPPFPLLTRKFEERCEIKGFYIP--EKTFLII---NayawmRDPDSWEDPNEFKPERflgssrlg 432
Cdd:cd11033   255 TA------VEEILRWASPVIHFRRTATRDTELGGQRIRagDKVVLWYasaN-----RDEEVFDDPDRFDITR-------- 315
                         170       180
                  ....*....|....*....|....*..
gi 1063712834 433 qvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11033   316 ------SPNPHLAFGGGPHFCLGAHLA 336
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
363-475 1.52e-06

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: 50.48  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 363 QAVVKEGLRLHPPFPLLTRKFEErceiKGFYIPEKtfLIINAYAWMRDPDSW-EDPNEFKPERFlgsSRLgqVDEREEAq 441
Cdd:cd20626   259 KNLVKEALRLYPPTRRIYRAFQR----PGSSKPEI--IAADIEACHRSESIWgPDALEFNPSRW---SKL--TPTQKEA- 326
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1063712834 442 kYIPFGGGRRGCPG-ANLASIFVGTAIGVMVQCFD 475
Cdd:cd20626   327 -FLPFGSGPFRCPAkPVFGPRMIALLVGALLDALG 360
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
290-474 1.69e-06

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 50.55  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 290 ENAEYKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEI--------------DSVVGTSRMIQETD 355
Cdd:PLN03195  282 EDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELkalekerakeedpeDSQSFNQRVTQFAG 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 356 IPN------LPYLQAVVKEGLRLHPPFPLLTRK-FEERCEIKGFYIPEKTFLIINAYAWMRDPDSW-EDPNEFKPERFLG 427
Cdd:PLN03195  362 LLTydslgkLQYLHAVITETLRLYPAVPQDPKGiLEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIK 441
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063712834 428 SSrlgqVDEREEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQCF 474
Cdd:PLN03195  442 DG----VFQNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFF 484
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
362-469 1.78e-06

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: 50.03  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 362 LQAVVKEGLRLHPPFPLLTRKFEERCEIK-----GFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvde 436
Cdd:cd20612   240 LRGYVLEALRLNPIAPGLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR------------ 307
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063712834 437 reEAQKYIPFGGGRRGCPGANLASIFVGTAIGV 469
Cdd:cd20612   308 --PLESYIHFGHGPHQCLGEEIARAALTEMLRV 338
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
319-459 5.15e-06

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: 48.91  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 319 TTQWTMAEIINNSDVLERLREEIDSVVGTSR----------MIQETDIPNLPYLQAVVKEGLRLHPP---FPLLTRKFEE 385
Cdd:cd20631   246 ATFWSLFYLLRCPEAMKAATKEVKRTLEKTGqkvsdggnpiVLTREQLDDMPVLGSIIKEALRLSSAslnIRVAKEDFTL 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 386 RCEIKGFYIPEKTFlIINAYAWMR--DPDSWEDPNEFKPERFLGSSrlGQ------VDEREEAQKYIPFGGGRRGCPGAN 457
Cdd:cd20631   326 HLDSGESYAIRKDD-IIALYPQLLhlDPEIYEDPLTFKYDRYLDEN--GKekttfyKNGRKLKYYYMPFGSGTSKCPGRF 402

                  ..
gi 1063712834 458 LA 459
Cdd:cd20631   403 FA 404
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
271-468 1.24e-05

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: 47.33  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 271 DEEHKDTDMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGTDTSVQTTqwtmaeiinnSDVLERLREEIDSvvgTSRM 350
Cdd:cd11034   164 RRANPRDDLISRLIEGEIDGK---PLSDGEVIGFLTLLLLGGTDTTSSAL----------SGALLWLAQHPED---RRRL 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 351 IQETDIpnlpyLQAVVKEGLRLHPPFPLLTRKFEERCEIKGFYI-PEKTFLIINAYAwMRDPDSWEDPNEFKPERFlgss 429
Cdd:cd11034   228 IADPSL-----IPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLkPGDRVLLAFASA-NRDEEKFEDPDRIDIDRT---- 297
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063712834 430 rlgqvdereeAQKYIPFGGGRRGCPGANLASIFVGTAIG 468
Cdd:cd11034   298 ----------PNRHLAFGSGVHRCLGSHLARVEARVALT 326
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
273-459 1.44e-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: 47.14  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 273 EHKDTDMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiq 352
Cdd:cd11029   187 AEPGDDLLSALVAARDEGD---RLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRAD------------ 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 353 ETDIPnlpylqAVVKEGLRLHPPFPLLTRKFE-ERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrl 431
Cdd:cd11029   252 PELWP------AAVEELLRYDGPVALATLRFAtEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR------- 318
                         170       180
                  ....*....|....*....|....*...
gi 1063712834 432 gqvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11029   319 -------DANGHLAFGHGIHYCLGAPLA 339
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
364-470 1.47e-05

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: 47.10  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 364 AVVKEGLRLHPPFPLLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvdereEAQKY 443
Cdd:cd11036   223 AAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR--------------PTARS 288
                          90       100
                  ....*....|....*....|....*..
gi 1063712834 444 IPFGGGRRGCPGANLASIFVGTAIGVM 470
Cdd:cd11036   289 AHFGLGRHACLGAALARAAAAAALRAL 315
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
308-459 3.76e-05

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: 46.04  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 308 LFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqetdiPNLpyLQAVVKEGLRLHPPFPLLTRKFEERC 387
Cdd:cd11037   210 YLSAGLDTTISAIGNALWLLARHPDQWERLRAD----------------PSL--APNAFEEAVRLESPVQTFSRTTTRDT 271
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063712834 388 EIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11037   272 ELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR--------------NPSGHVGFGHGVHACVGQHLA 329
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
360-464 2.03e-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: 43.65  E-value: 2.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 360 PYLQAVvKEGLRLHPPFPLLTRKFEERCEIKGFYIP--EKTFLIINAYAwmRDPDSWEDPNEFkperflgssrlgqvDER 437
Cdd:cd11039   245 HWLRAF-EEGLRWISPIGMSPRRVAEDFEIRGVTLPagDRVFLMFGSAN--RDEARFENPDRF--------------DVF 307
                          90       100
                  ....*....|....*....|....*..
gi 1063712834 438 EEAQKYIPFGGGRRGCPGANLASIFVG 464
Cdd:cd11039   308 RPKSPHVSFGAGPHFCAGAWASRQMVG 334
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
278-472 2.42e-04

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: 43.32  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 278 DMMDVLLAAYADENaeyKITRNHIKSFFVELFVGGTDTSVQTTQWTMAEIINNSDVLERLREEidsvvgtsrmiqetdiP 357
Cdd:cd11031   187 DLLSALVAARDDDD---RLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRAD----------------P 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 358 NLpyLQAVVKEGLRLHPPFP--LLTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflgssrlgqvd 435
Cdd:cd11031   248 EL--VPAAVEELLRYIPLGAggGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR----------- 314
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063712834 436 ereEAQKYIPFGGGRRGCPGANLASIFVGTAIGVMVQ 472
Cdd:cd11031   315 ---EPNPHLAFGHGPHHCLGAPLARLELQVALGALLR 348
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
272-459 4.97e-03

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: 39.43  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 272 EEHKDTDMMDVLLAAYADENAeykITRNHIKSFFVELFVGGTDTSVQTTQ---WTMAEiinNSDVLERLREEIDSVVGts 348
Cdd:cd11030   183 RREPGDDLLSRLVAEHGAPGE---LTDEELVGIAVLLLVAGHETTANMIAlgtLALLE---HPEQLAALRADPSLVPG-- 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063712834 349 rmiqetdipnlpylqaVVKEGLRLHPPFPL-LTRKFEERCEIKGFYIPEKTFLIINAYAWMRDPDSWEDPNEFKPERflg 427
Cdd:cd11030   255 ----------------AVEELLRYLSIVQDgLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR--- 315
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1063712834 428 ssrlgqvdereEAQKYIPFGGGRRGCPGANLA 459
Cdd:cd11030   316 -----------PARRHLAFGHGVHQCLGQNLA 336
 
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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