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Conserved domains on  [gi|266618501|pdb|2WV2|A]
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Chain A, LANOSTEROL 14-ALPHA-DEMETHYLASE

Protein Classification

cytochrome P450( domain architecture ID 15296390)

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

CATH:  1.10.630.10
Gene Ontology:  GO:0004497|GO:0005506|GO:0020037|GO:0016712
PubMed:  16042601|8637843|17023115|27267697|8405421|7678494|28124606
SCOP:  4001206

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 45-459 0e+00

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: 512.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       45 CKRQLkSGIFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPREVYSFMVPVFGEGVAYAAPYPRMREQLNFLAEELTIAK 124
Cdd:cd11042   1 CRKKY-GDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFGLNILRRGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      125 FQNFVPAIQHEVRKFMAANWdkDEGEINLLEDCSTMIINTACQCLFGEDLRKRLDaRRFAQLLAKMESSLIPAAVFlpiL 204
Cdd:cd11042  80 LRGYVPLIVEEVEKYFAKWG--ESGEVDLFEEMSELTILTASRCLLGKEVRELLD-DEFAQLYHDLDGGFTPIAFF---F 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      205 LKLPLPQSARCHEARTELQKILSEIIIARKEEEvnkDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSI 284
Cdd:cd11042 154 PPLPLPSFRRRDRARAKLKEIFSEIIQKRRKSP---DKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      285 TTTWSMLHLMHpaNVKHLEALRKEIEEFPAQLN---YNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKV--GSYV 359
Cdd:cd11042 231 TSAWTGLELLR--NPEHLEALREEQKEVLGDGDdplTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVegGGYV 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      360 VPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEG--------AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDF 431
Cdd:cd11042 309 IPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAedskggkfAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDF 388

                       410       420
                ....*....|....*....|....*...
2WV2_A      432 QLLRDEVPDPDYHTMVVGPtASQCRVKY 459
Cdd:cd11042 389 ELVDSPFPEPDYTTMVVWP-KGPARVRY 415
 
Name Accession Description Interval E-value
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 45-459 0e+00

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: 512.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       45 CKRQLkSGIFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPREVYSFMVPVFGEGVAYAAPYPRMREQLNFLAEELTIAK 124
Cdd:cd11042   1 CRKKY-GDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFGLNILRRGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      125 FQNFVPAIQHEVRKFMAANWdkDEGEINLLEDCSTMIINTACQCLFGEDLRKRLDaRRFAQLLAKMESSLIPAAVFlpiL 204
Cdd:cd11042  80 LRGYVPLIVEEVEKYFAKWG--ESGEVDLFEEMSELTILTASRCLLGKEVRELLD-DEFAQLYHDLDGGFTPIAFF---F 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      205 LKLPLPQSARCHEARTELQKILSEIIIARKEEEvnkDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSI 284
Cdd:cd11042 154 PPLPLPSFRRRDRARAKLKEIFSEIIQKRRKSP---DKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      285 TTTWSMLHLMHpaNVKHLEALRKEIEEFPAQLN---YNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKV--GSYV 359
Cdd:cd11042 231 TSAWTGLELLR--NPEHLEALREEQKEVLGDGDdplTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVegGGYV 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      360 VPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEG--------AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDF 431
Cdd:cd11042 309 IPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAedskggkfAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDF 388

                       410       420
                ....*....|....*....|....*...
2WV2_A      432 QLLRDEVPDPDYHTMVVGPtASQCRVKY 459
Cdd:cd11042 389 ELVDSPFPEPDYTTMVVWP-KGPARVRY 415
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 18-449 2.50e-55

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: 190.95  E-value: 2.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A         18 PPvYPVTVPILGHIIQFGKS--PLGFMQECKRqlKSG-IFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPRE----VYS 90
Cdd:pfam00067   1 PP-GPPPLPLFGNLLQLGRKgnLHSVFTKLQK--KYGpIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPdepwFAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A         91 FMVPVFGEGVAYAApYPRMREQLNFLAEELTIAKFQNFVPAIQHEVRKFMAAnWDKDEGE---INLLEDCSTMIINTACQ 167
Cdd:pfam00067  78 SRGPFLGKGIVFAN-GPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEK-LRKTAGEpgvIDITDLLFRAALNVICS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        168 CLFGEDL-----RKRLDARRFAQLLAKMESSLIPAAVFLPILLKLP-LPQSARCHEARTELQKILSEIIIARKEEEVNKD 241
Cdd:pfam00067 156 ILFGERFgsledPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFpGPHGRKLKRARKKIKDLLDKLIEERRETLDSAK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        242 SSTSDLLSGLLSA-VYRDGTPMSLHEvcgmIVAA----MFAGQHTSSITTTWSMLHLM-HPanvKHLEALRKEIEE---F 312
Cdd:pfam00067 236 KSPRDFLDALLLAkEEEDGSKLTDEE----LRATvlelFFAGTDTTSSTLSWALYELAkHP---EVQEKLREEIDEvigD 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        313 PAQLNYNNVMDeMPFAERCARESIRRDPPLLM-LMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER- 390
Cdd:pfam00067 309 KRSPTYDDLQN-MPYLDAVIKETLRLHPVVPLlLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERf 387

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
2WV2_A        391 -DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDPDYHTMVVG 449
Cdd:pfam00067 388 lDENGKFrksfAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLL 451
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 33-452 6.99e-51

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: 177.78  E-value: 6.99e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       33 QFGKSPLGFMQECKRQlkSGIFTINIVGKRVTIVGDpHEHSRFFLPRNEVLSPREVYSFMVP---VFGEGVAYAAPyPRM 109
Cdd:COG2124  16 AFLRDPYPFYARLREY--GPVFRVRLPGGGAWLVTR-YEDVREVLRDPRTFSSDGGLPEVLRplpLLGDSLLTLDG-PEH 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      110 REQLNFLAEELTIAKFQNFVPAIQHEVRKFMAAnWDkDEGEINLLEDCSTMIINTACQCLFGEDLRkrlDARRFAQLLAK 189
Cdd:COG2124  92 TRLRRLVQPAFTPRRVAALRPRIREIADELLDR-LA-ARGPVDLVEEFARPLPVIVICELLGVPEE---DRDRLRRWSDA 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      190 MESSLIPAAvflpillklpLPQSARCHEARTELQKILSEIIIARKEEevnkdsSTSDLLSGLLSAVYrDGTPMSLHEVCG 269
Cdd:COG2124 167 LLDALGPLP----------PERRRRARRARAELDAYLRELIAERRAE------PGDDLLSALLAARD-DGERLSDEELRD 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      270 MIVAAMFAGQHTSSITTTWSMLHLM-HPAnvkHLEALRkeieefpaqlnynnvmDEMPFAERCARESIRRDPPLLMLMRK 348
Cdd:COG2124 230 ELLLLLLAGHETTANALAWALYALLrHPE---QLARLR----------------AEPELLPAAVEETLRLYPPVPLLPRT 290

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      349 VMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDekvEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRS 428
Cdd:COG2124 291 ATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRP---PNAHLPFGGGPHRCLGAALARLEARIALATLLRR 367

                       410       420
                ....*....|....*....|....*
2WV2_A      429 Y-DFQLLRDEVPDPDYHTMVVGPTA 452
Cdd:COG2124 368 FpDLRLAPPEELRWRPSLTLRGPKS 392
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 9-439 4.20e-23

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 101.55  E-value: 4.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A         9 SFNVTRPTDPPVYPVTV--PILGHIIQ-FGKSPLGFMQECKRQLKSgIFTINIVGKRVTIVGDPhEHSRFFL-PRNEVLS 84
Cdd:PLN02196  25 GFRRSSSTKLPLPPGTMgwPYVGETFQlYSQDPNVFFASKQKRYGS-VFKTHVLGCPCVMISSP-EAAKFVLvTKSHLFK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        85 P-----REVYSFMVPVFGEGVAYAApypRMREQL--NFLAEELtiakfQNFVPAIQhEVRKFMAANWDKDEgeINLLEDC 157
Cdd:PLN02196 103 PtfpasKERMLGKQAIFFHQGDYHA---KLRKLVlrAFMPDAI-----RNMVPDIE-SIAQESLNSWEGTQ--INTYQEM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       158 STMIINTACQCLFGED-LRKRLDARRFAQLLAKMESSL---IPAAVFLpillklplpqsaRCHEARTELQKILSEIIIAR 233
Cdd:PLN02196 172 KTYTFNVALLSIFGKDeVLYREDLKRCYYILEKGYNSMpinLPGTLFH------------KSMKARKELAQILAKILSKR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       234 KEeevnKDSSTSDLLSGLLSavyrDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANV-----KHLEALRKE 308
Cdd:PLN02196 240 RQ----NGSSHNDLLGSFMG----DKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVleavtEEQMAIRKD 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       309 IEEfPAQLNYNNVmDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIAcsPLLS--HHDEEAFPEPRRW 386
Cdd:PLN02196 312 KEE-GESLTWEDT-KKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVL--PLFRniHHSADIFSDPGKF 387

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
2WV2_A       387 DPERDEKV--EGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVP 439
Cdd:PLN02196 388 DPSRFEVApkPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTSNG 442
 
Name Accession Description Interval E-value
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 45-459 0e+00

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: 512.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       45 CKRQLkSGIFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPREVYSFMVPVFGEGVAYAAPYPRMREQLNFLAEELTIAK 124
Cdd:cd11042   1 CRKKY-GDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFGLNILRRGK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      125 FQNFVPAIQHEVRKFMAANWdkDEGEINLLEDCSTMIINTACQCLFGEDLRKRLDaRRFAQLLAKMESSLIPAAVFlpiL 204
Cdd:cd11042  80 LRGYVPLIVEEVEKYFAKWG--ESGEVDLFEEMSELTILTASRCLLGKEVRELLD-DEFAQLYHDLDGGFTPIAFF---F 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      205 LKLPLPQSARCHEARTELQKILSEIIIARKEEEvnkDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSI 284
Cdd:cd11042 154 PPLPLPSFRRRDRARAKLKEIFSEIIQKRRKSP---DKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      285 TTTWSMLHLMHpaNVKHLEALRKEIEEFPAQLN---YNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKV--GSYV 359
Cdd:cd11042 231 TSAWTGLELLR--NPEHLEALREEQKEVLGDGDdplTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVegGGYV 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      360 VPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEG--------AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDF 431
Cdd:cd11042 309 IPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAedskggkfAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDF 388

                       410       420
                ....*....|....*....|....*...
2WV2_A      432 QLLRDEVPDPDYHTMVVGPtASQCRVKY 459
Cdd:cd11042 389 ELVDSPFPEPDYTTMVVWP-KGPARVRY 415
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 53-451 6.67e-66

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: 217.00  E-value: 6.67e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       53 IFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPREVYSFMVPVFGEGVAYAAPYPRMREQLNFLAEELTIAKFQNFVPAI 132
Cdd:cd00302   3 VFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      133 QHEVRKFMAANWDKDEGEINLLEDCSTMIINTACQCLFGEDLRkrLDARRFAQLLAKMESSLIPAAVFLPILLKLplpqs 212
Cdd:cd00302  83 REIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLG--EDLEELAELLEALLKLLGPRLLRPLPSPRL----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      213 ARCHEARTELQKILSEIIIARKEEEvnkdsstSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd00302 156 RRLRRARARLRDYLEELIARRRAEP-------ADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYL 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 L-MHPanvKHLEALRKEIEEFPAQLNYNNVmDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPL 371
Cdd:cd00302 229 LaRHP---EVQERLRAEIDAVLGDGTPEDL-SKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLY 304

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      372 LSHHDEEAFPEPRRWDPER----DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDPDYHTMV 447
Cdd:cd00302 305 AAHRDPEVFPDPDEFDPERflpeREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRPSLGT 384


                ....
2WV2_A      448 VGPT 451
Cdd:cd00302 385 LGPA 388
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 18-449 2.50e-55

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: 190.95  E-value: 2.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A         18 PPvYPVTVPILGHIIQFGKS--PLGFMQECKRqlKSG-IFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPRE----VYS 90
Cdd:pfam00067   1 PP-GPPPLPLFGNLLQLGRKgnLHSVFTKLQK--KYGpIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPdepwFAT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A         91 FMVPVFGEGVAYAApYPRMREQLNFLAEELTIAKFQNFVPAIQHEVRKFMAAnWDKDEGE---INLLEDCSTMIINTACQ 167
Cdd:pfam00067  78 SRGPFLGKGIVFAN-GPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEK-LRKTAGEpgvIDITDLLFRAALNVICS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        168 CLFGEDL-----RKRLDARRFAQLLAKMESSLIPAAVFLPILLKLP-LPQSARCHEARTELQKILSEIIIARKEEEVNKD 241
Cdd:pfam00067 156 ILFGERFgsledPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFpGPHGRKLKRARKKIKDLLDKLIEERRETLDSAK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        242 SSTSDLLSGLLSA-VYRDGTPMSLHEvcgmIVAA----MFAGQHTSSITTTWSMLHLM-HPanvKHLEALRKEIEE---F 312
Cdd:pfam00067 236 KSPRDFLDALLLAkEEEDGSKLTDEE----LRATvlelFFAGTDTTSSTLSWALYELAkHP---EVQEKLREEIDEvigD 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        313 PAQLNYNNVMDeMPFAERCARESIRRDPPLLM-LMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER- 390
Cdd:pfam00067 309 KRSPTYDDLQN-MPYLDAVIKETLRLHPVVPLlLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERf 387

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
2WV2_A        391 -DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDPDYHTMVVG 449
Cdd:pfam00067 388 lDENGKFrksfAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLL 451
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 39-450 4.63e-53

cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410676 [Multi-domain]  Cd Length: 415  Bit Score: 183.94  E-value: 4.63e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       39 LGFMQECKRQLKSgIFTINIVGK-RVTIVGDPhEHSRF-FLPRNEVLSPREVYSFMVPVFGEG---VAYAAPYPRMREQL 113
Cdd:cd11053   1 VGFLERLRARYGD-VFTLRVPGLgPVVVLSDP-EAIKQiFTADPDVLHPGEGNSLLEPLLGPNsllLLDGDRHRRRRKLL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      114 --NFLAEELtiakfQNFVPAIQHEVRKfMAANWDKDEgEINLLEDCSTMIINTACQCLFGEDLRKRLDarRFAQLLAKME 191
Cdd:cd11053  79 mpAFHGERL-----RAYGELIAEITER-EIDRWPPGQ-PFDLRELMQEITLEVILRVVFGVDDGERLQ--ELRRLLPRLL 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      192 SSLIPAAVFLPILLKLPLPQS--ARCHEARTELQKILSEIIIARKEEevnKDSSTSDLLSGLLSAVYRDGTPMSLHEVCG 269
Cdd:cd11053 150 DLLSSPLASFPALQRDLGPWSpwGRFLRARRRIDALIYAEIAERRAE---PDAERDDILSLLLSARDEDGQPLSDEELRD 226

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      270 MIVAAMFAGQHTSSITTTWSMLHLM-HPAnVkhLEALRKEIEEFPAQLNYNNVmDEMPFAERCARESIRRDPPLLMLMRK 348
Cdd:cd11053 227 ELMTLLFAGHETTATALAWAFYWLHrHPE-V--LARLLAELDALGGDPDPEDI-AKLPYLDAVIKETLRLYPVAPLVPRR 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      349 VMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--DEKVE-GAFIGFGAGVHKCIGQKFGLLQVKTILATA 425
Cdd:cd11053 303 VKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERflGRKPSpYEYLPFGGGVRRCIGAAFALLEMKVVLATL 382

                       410       420
                ....*....|....*....|....*
2WV2_A      426 FRSYDFQLLRDEVPDPDYHTMVVGP 450
Cdd:cd11053 383 LRRFRLELTDPRPERPVRRGVTLAP 407
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 33-452 6.99e-51

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: 177.78  E-value: 6.99e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       33 QFGKSPLGFMQECKRQlkSGIFTINIVGKRVTIVGDpHEHSRFFLPRNEVLSPREVYSFMVP---VFGEGVAYAAPyPRM 109
Cdd:COG2124  16 AFLRDPYPFYARLREY--GPVFRVRLPGGGAWLVTR-YEDVREVLRDPRTFSSDGGLPEVLRplpLLGDSLLTLDG-PEH 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      110 REQLNFLAEELTIAKFQNFVPAIQHEVRKFMAAnWDkDEGEINLLEDCSTMIINTACQCLFGEDLRkrlDARRFAQLLAK 189
Cdd:COG2124  92 TRLRRLVQPAFTPRRVAALRPRIREIADELLDR-LA-ARGPVDLVEEFARPLPVIVICELLGVPEE---DRDRLRRWSDA 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      190 MESSLIPAAvflpillklpLPQSARCHEARTELQKILSEIIIARKEEevnkdsSTSDLLSGLLSAVYrDGTPMSLHEVCG 269
Cdd:COG2124 167 LLDALGPLP----------PERRRRARRARAELDAYLRELIAERRAE------PGDDLLSALLAARD-DGERLSDEELRD 229

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      270 MIVAAMFAGQHTSSITTTWSMLHLM-HPAnvkHLEALRkeieefpaqlnynnvmDEMPFAERCARESIRRDPPLLMLMRK 348
Cdd:COG2124 230 ELLLLLLAGHETTANALAWALYALLrHPE---QLARLR----------------AEPELLPAAVEETLRLYPPVPLLPRT 290

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      349 VMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDekvEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRS 428
Cdd:COG2124 291 ATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRP---PNAHLPFGGGPHRCLGAALARLEARIALATLLRR 367

                       410       420
                ....*....|....*....|....*
2WV2_A      429 Y-DFQLLRDEVPDPDYHTMVVGPTA 452
Cdd:COG2124 368 FpDLRLAPPEELRWRPSLTLRGPKS 392
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 38-442 7.02e-41

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: 151.26  E-value: 7.02e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       38 PLGFMQECkRQLkSGIFTINIVGKRVTIVGDPhEHSRFFLPRNEVLSPR-EVYSFMVPVFGEGVAyAAPYPRMREQLNFL 116
Cdd:cd11049   2 PLGFLSSL-RAH-GDLVRIRLGPRPAYVVTSP-ELVRQVLVNDRVFDKGgPLFDRARPLLGNGLA-TCPGEDHRRQRRLM 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      117 AEELTIAKFQNFVPAIQHEVRKfMAANWdKDEGEINLLEDCSTMIINTACQCLFGEDLrKRLDARRFAQLLAKMESSLIP 196
Cdd:cd11049  78 QPAFHRSRIPAYAEVMREEAEA-LAGSW-RPGRVVDVDAEMHRLTLRVVARTLFSTDL-GPEAAAELRQALPVVLAGMLR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      197 AAVFLPILLKLPLPQSARCHEARTELQKILSEIIIARKeeevNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMF 276
Cdd:cd11049 155 RAVPPKFLERLPTPGNRRFDRALARLRELVDEIIAEYR----ASGTDRDDLLSLLLAARDEEGRPLSDEELRDQVITLLT 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      277 AGQHTSSITTTWSmLHLM--HPAnvkHLEALRKEIEEF----PAqlNYNNVmDEMPFAERCARESIRRDPPLLMLMRKVM 350
Cdd:cd11049 231 AGTETTASTLAWA-FHLLarHPE---VERRLHAELDAVlggrPA--TFEDL-PRLTYTRRVVTEALRLYPPVWLLTRRTT 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      351 ADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILAT 424
Cdd:cd11049 304 ADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRwlpgraAAVPRGAFIPFGAGARKCIGDTFALTELTLALAT 383

                       410
                ....*....|....*...
2WV2_A      425 AFRSYDFQLlrdeVPDPD 442
Cdd:cd11049 384 IASRWRLRP----VPGRP 397
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 29-446 8.65e-41

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 150.90  E-value: 8.65e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       29 GHIIQFGKSPLGFMQecKRQLKSG-IFTINIVGKRVTIVGDPHEHSRFFLPRNEVLS---PREVYSfmvpVFGEG---VA 101
Cdd:cd11044   1 GETLEFLRDPEDFIQ--SRYQKYGpVFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRygwPRSVRR----LLGENslsLQ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      102 YAAPYPRMREQLnflAEELTIAKFQNFVPAIQHEVRKFMAAnWDKDeGEINLLEDCSTMIINTACQCLFGEDLRKrlDAR 181
Cdd:cd11044  75 DGEEHRRRRKLL---APAFSREALESYVPTIQAIVQSYLRK-WLKA-GEVALYPELRRLTFDVAARLLLGLDPEV--EAE 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      182 RFAQLLAKMESSL------IPAAVFlpillklplpqsARCHEARTELQKILSEIIIARKEEEvnkDSSTSDLLSGLLSAV 255
Cdd:cd11044 148 ALSQDFETWTDGLfslpvpLPFTPF------------GRAIRARNKLLARLEQAIRERQEEE---NAEAKDALGLLLEAK 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      256 YRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-HPAnvkHLEALRKEIEEFPAQLNYN-NVMDEMPFAERCAR 333
Cdd:cd11044 213 DEDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAqHPD---VLEKLRQEQDALGLEEPLTlESLKKMPYLDQVIK 289

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      334 ESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER-------DEKVEGAFIGFGAGVH 406
Cdd:cd11044 290 EVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERfsparseDKKKPFSLIPFGGGPR 369

                       410       420       430       440
                ....*....|....*....|....*....|....*....|
2WV2_A      407 KCIGQKFGLLQVKTILATAFRSYDFQLLRDEvpDPDYHTM 446
Cdd:cd11044 370 ECLGKEFAQLEMKILASELLRNYDWELLPNQ--DLEPVVV 407
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 221-431 1.13e-37

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: 142.66  E-value: 1.13e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      221 ELQKILSEIIIARKEE-EVNKDSSTSDLLSG---------LLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSM 290
Cdd:cd20628 174 VLHDFTNKVIKERREElKAEKRNSEEDDEFGkkkrkafldLLLEAHEDGGPLTDEDIREEVDTFMFAGHDTTASAISFTL 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      291 LHL-MHPanvKHLEALRKEIEEFPAQLNYNNVMD---EMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDII 366
Cdd:cd20628 254 YLLgLHP---EVQEKVYEELDEIFGDDDRRPTLEdlnKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTV 330

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2WV2_A      367 ACSPLLSHHDEEAFPEPRRWDPER--DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDF 431
Cdd:cd20628 331 VISIYALHRNPEYFPDPEKFDPDRflPENSAKrhpyAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRV 401
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 126-442 4.63e-37

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: 140.41  E-value: 4.63e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      126 QNFVPAIQHEVRKfMAANWD--KDEGEINLLEDCSTMIINTACQCLFGEDLRKrlDARRFAQLL-AKMESSLIPAAVFLP 202
Cdd:cd20620  75 AAYADAMVEATAA-LLDRWEagARRGPVDVHAEMMRLTLRIVAKTLFGTDVEG--EADEIGDALdVALEYAARRMLSPFL 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      203 ILLKLPLPQSARCHEARTELQKILSEIIIARKEEevnkDSSTSDLLSGLLSAVYRD-GTPMSLHEVCGMIVAAMFAGQHT 281
Cdd:cd20620 152 LPLWLPTPANRRFRRARRRLDEVIYRLIAERRAA----PADGGDLLSMLLAARDEEtGEPMSDQQLRDEVMTLFLAGHET 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      282 SSITTTWSmLHLM--HPAnvkHLEALRKEIEEF-------PAQLnynnvmDEMPFAERCARESIRRDPPLLMLMRKVMAD 352
Cdd:cd20620 228 TANALSWT-WYLLaqHPE---VAARLRAEVDRVlggrpptAEDL------PQLPYTEMVLQESLRLYPPAWIIGREAVED 297

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      353 VKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAF 426
Cdd:cd20620 298 DEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERftPEREAArpryAYFPFGGGPRICIGNHFAMMEAVLLLATIA 377

                       330
                ....*....|....*.
2WV2_A      427 RSYDFQLLRDEVPDPD 442
Cdd:cd20620 378 QRFRLRLVPGQPVEPE 393
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 80-433 2.16e-36

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: 139.33  E-value: 2.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       80 NEVLS--------PREVYSFMVPVFGEGV--AYAAPYPRMREQLN--FlaeelTIAKFQNFVPAIQHEVRKfMAANWDKD 147
Cdd:cd11069  25 KHILVtnsydfekPPAFRRLLRRILGDGLlaAEGEEHKRQRKILNpaF-----SYRHVKELYPIFWSKAEE-LVDKLEEE 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      148 -------EGEINLLEDCSTMIINTACQCLFGEDLR--KRLDARrFAQLLAKM-----ESSLIPAAVFLPILLKLPLPQSA 213
Cdd:cd11069  99 ieesgdeSISIDVLEWLSRATLDIIGLAGFGYDFDslENPDNE-LAEAYRRLfeptlLGSLLFILLLFLPRWLVRILPWK 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHE---ARTELQKILSEIIIARKEE-EVNKDSSTSDLLSGLLSA-VYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTW 288
Cdd:cd11069 178 ANREirrAKDVLRRLAREIIREKKAAlLEGKDDSGKDILSILLRAnDFADDERLSDEELIDQILTFLAAGHETTSTALTW 257

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      289 sMLHLM--HPAnVKhlEALRKEIEEF----PAQLNYNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPK 362
Cdd:cd11069 258 -ALYLLakHPD-VQ--ERLREEIRAAlpdpPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPK 333

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      363 GDIIACSPLLSHHDEEAF-PEPRRWDPER----DEKVE-------GAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYD 430
Cdd:cd11069 334 GTVVLIPPAAINRSPEIWgPDAEEFNPERwlepDGAASpggagsnYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFE 413


                ...
2WV2_A      431 FQL 433
Cdd:cd11069 414 FEL 416
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 213-446 6.46e-36

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: 137.45  E-value: 6.46e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      213 ARCHEARTELQKILSEIIIARKEeevnkdSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd11045 164 WRGLRGRRYLEEYFRRRIPERRA------GGGDDLFSALCRAEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYF 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LmhpanVKHLE---ALRKEIEEFP-AQLNYNNvMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIAC 368
Cdd:cd11045 238 L-----ARHPEwqeRLREESLALGkGTLDYED-LGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAV 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      369 SPLLSHHDEEAFPEPRRWDPER--DEKVEG-----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDP 441
Cdd:cd11045 312 SPGVTHYMPEYWPNPERFDPERfsPERAEDkvhryAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGYYPPW 391


                ....*
2WV2_A      442 DYHTM 446
Cdd:cd11045 392 WQSPL 396
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 47-418 7.01e-36

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: 137.31  E-value: 7.01e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       47 RQLK-SGIFTINIVGKRVTIVGDPhEHSRFFLpRNE--VLSPREVYSFMvPVFGE---GVAYAAPYPRMR-EQLNFL-AE 118
Cdd:cd11043   1 RIKRyGPVFKTSLFGRPTVVSADP-EANRFIL-QNEgkLFVSWYPKSVR-KLLGKsslLTVSGEEHKRLRgLLLSFLgPE 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      119 ELTiakfQNFVPAIQHEVRKFMAANWDKdeGEINLLEDCSTMIINTACQCLFGEDLRKRLDArrFAQLLAKMESSL---- 194
Cdd:cd11043  78 ALK----DRLLGDIDELVRQHLDSWWRG--KSVVVLELAKKMTFELICKLLLGIDPEEVVEE--LRKEFQAFLEGLlsfp 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      195 --IPAAVFlpillklplpqsARCHEARTELQKILSEIIIARKEEEvNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIV 272
Cdd:cd11043 150 lnLPGTTF------------HRALKARKRIRKELKKIIEERRAEL-EKASPKGDLLDVLLEEKDEDGDSLTDEEILDNIL 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      273 AAMFAGQHTSSITTTWSMLHLM-HPanvKHLEALRKEIEEF------PAQLNYNNVMdEMPFAERCARESIRRDPPLLML 345
Cdd:cd11043 217 TLLFAGHETTSTTLTLAVKFLAeNP---KVLQELLEEHEEIakrkeeGEGLTWEDYK-SMKYTWQVINETLRLAPIVPGV 292

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2WV2_A      346 MRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER----DEKVEGAFIGFGAGVHKCIGQKFGLLQV 418
Cdd:cd11043 293 FRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRwegkGKGVPYTFLPFGGGPRLCPGAELAKLEI 369
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 222-437 2.68e-32

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: 127.70  E-value: 2.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      222 LQKILSEIIIARKEEEVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-HPANvk 300
Cdd:cd11060 178 LMRFALEAVAERLAEDAESAKGRKDMLDSFLEAGLKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLkNPRV-- 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      301 hLEALRKEIEEFPAQLNYNNVMD-----EMPFAERCARESIRRDPPLLMLM-RKVMA--DVKVGSYVvPKGDIIACSPLL 372
Cdd:cd11060 256 -YAKLRAEIDAAVAEGKLSSPITfaeaqKLPYLQAVIKEALRLHPPVGLPLeRVVPPggATICGRFI-PGGTIVGVNPWV 333

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2WV2_A      373 SHHDEEAFPE------PRRW---DPERDEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDE 437
Cdd:cd11060 334 IHRDKEVFGEdadvfrPERWleaDEEQRRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVDPE 407
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 222-433 4.05e-32

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: 127.27  E-value: 4.05e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      222 LQKILSEIIIARKEEEVNKDsstsDLLSGLLSA-----VYRDGTPMSLHEvcGMIVAAMF----AGQHTSSITTTWSMLH 292
Cdd:cd11056 182 FRKLVRDTIEYREKNNIVRN----DFIDLLLELkkkgkIEDDKSEKELTD--EELAAQAFvfflAGFETSSSTLSFALYE 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LMHpaNVKHLEALRKEIEE----FPAQLNYNNVMdEMPFAERCARESIRRDPPLLMLMRKVMADVKVGS--YVVPKGDII 366
Cdd:cd11056 256 LAK--NPEIQEKLREEIDEvlekHGGELTYEALQ-EMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPV 332

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
2WV2_A      367 ACSPLLSHHDEEAFPEPRRWDPER------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd11056 333 IIPVYALHHDPKYYPEPEKFDPERfspenkKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEP 405
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 53-450 2.01e-30

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: 122.47  E-value: 2.01e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       53 IFTINIVGKRVTIVGDPhEHSRFFLPRNEVLSPrevYSFMVPVFG------------EGVAYAAPYPRMREQL--NFLAE 118
Cdd:cd11040  14 IFTIRLGGQKIYVITDP-ELISAVFRNPKTLSF---DPIVIVVVGrvfgspesakkkEGEPGGKGLIRLLHDLhkKALSG 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      119 ELTIAKFQN-FVPAIQHEVRKfMAANWDKDEGEINLLEDCSTMIINTACQCLFGEDLRKRLDA---------RRFAQLLA 188
Cdd:cd11040  90 GEGLDRLNEaMLENLSKLLDE-LSLSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPELDPDlvedfwtfdRGLPKLLL 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      189 KMESSLIPAAvflpillklplpqsarcHEARTELQKILSEIIIARKEEEVNkdsstsdlLSGLLSAVYRDGTPMSLHEV- 267
Cdd:cd11040 169 GLPRLLARKA-----------------YAARDRLLKALEKYYQAAREERDD--------GSELIRARAKVLREAGLSEEd 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      268 CGMIVAAMFAGQHTSSI-TTTWSMLHLMHPANVkhLEALRKEIEEF-------PAQLNYNNVMDEMPFAERCARESIRrd 339
Cdd:cd11040 224 IARAELALLWAINANTIpAAFWLLAHILSDPEL--LERIREEIEPAvtpdsgtNAILDLTDLLTSCPLLDSTYLETLR-- 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      340 pplLMLM----RKVMAD-VKVGSYVVPKGDIIACSPLLSHHDEEAF-PEPRRWDPER---------DEKVEGAFIGFGAG 404
Cdd:cd11040 300 ---LHSSstsvRLVTEDtVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERflkkdgdkkGRGLPGAFRPFGGG 376

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
2WV2_A      405 VHKCIGQKFGLLQVKTILATAFRSYDFQLLRD---EVPDPDYhTMVVGP 450
Cdd:cd11040 377 ASLCPGRHFAKNEILAFVALLLSRFDVEPVGGgdwKVPGMDE-SPGLGI 424
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 228-448 3.34e-29

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: 118.81  E-value: 3.34e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      228 EIIIARKEE-EVNKDSSTS-----DLLSGLLSAVYRDGTPMSLHEvcgmIVAA----MFAGQHTSSITTTWSMLHL-MHP 296
Cdd:cd20659 183 EIIKKRRKElEDNKDEALSkrkylDFLDILLTARDEDGKGLTDEE----IRDEvdtfLFAGHDTTASGISWTLYSLaKHP 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      297 anvKHLEALRKEIEEFPAQLN--YNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSH 374
Cdd:cd20659 259 ---EHQQKCREEVDEVLGDRDdiEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALH 335

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      375 HDEEAFPEPRRWDPER--DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLlrDEVPDPDYHTMVV 448
Cdd:cd20659 336 HNPTVWEDPEEFDPERflPENIKKrdpfAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSV--DPNHPVEPKPGLV 413
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 127-463 1.46e-28

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


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 117.39  E-value: 1.46e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      127 NFVPAIQHEVRKFMAANWDKDEG--EINLLEDCSTMIINTACQCLFGEDL---RKRLD-ARRFAQLL--AKMESSLIP-- 196
Cdd:cd11041  82 KLLPDLQEELRAALDEELGSCTEwtEVNLYDTVLRIVARVSARVFVGPPLcrnEEWLDlTINYTIDVfaAAAALRLFPpf 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      197 ----AAVFLPillklplpQSARCHEARTELQKILSEIIIARKEEEV-NKDSSTSDLLSGLLSAVYRDG--TPMSL-HEVC 268
Cdd:cd11041 162 lrplVAPFLP--------EPRRLRRLLRRARPLIIPEIERRRKLKKgPKEDKPNDLLQWLIEAAKGEGerTPYDLaDRQL 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      269 GMIVAAMfagqHTSSITTTWSMLHLM-HPanvKHLEALRKEIEEFPAQLNYNNV--MDEMPFAERCARESIRRDPP-LLM 344
Cdd:cd11041 234 ALSFAAI----HTTSMTLTHVLLDLAaHP---EYIEPLREEIRSVLAEHGGWTKaaLNKLKKLDSFMKESQRLNPLsLVS 306

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      345 LMRKVMADVKVGS-YVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER----DEKVEGA-----------FIGFGAGVHKC 408
Cdd:cd11041 307 LRRKVLKDVTLSDgLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRfyrlREQPGQEkkhqfvstspdFLGFGHGRHAC 386

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
2WV2_A      409 IGQKFGLLQVKTILATAFRSYDFQLLRDEVPDPDYHTMVVGPTASQCRVKYIRRK 463
Cdd:cd11041 387 PGRFFASNEIKLILAHLLLNYDFKLPEGGERPKNIWFGEFIMPDPNAKVLVRRRE 441
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 220-431 6.64e-27

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: 112.29  E-value: 6.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      220 TELQKILSEIIIARKEeevNKDSSTSDLLSGLLSAVYRDGT----PMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-M 294
Cdd:cd11055 179 SFLEDVVKKIIEQRRK---NKSSRRKDLLQLMLDAQDSDEDvskkKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLaT 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      295 HPaNVKhlEALRKEI-EEFPAQ--LNYNNVMDeMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPL 371
Cdd:cd11055 256 NP-DVQ--EKLIEEIdEVLPDDgsPTYDTVSK-LKYLDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVY 331

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2WV2_A      372 LSHHDEEAFPEPRRWDPER---DEKVE---GAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDF 431
Cdd:cd11055 332 AIHHDPEFWPDPEKFDPERfspENKAKrhpYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRF 397
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 220-433 3.10e-26

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: 110.51  E-value: 3.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      220 TELQKILSEIIIARKEEEV--NKDSSTSDLLSGLLSA--VYRDGTPMSLHEV---CGMIvaaMFAGQHTSSITTTWS-ML 291
Cdd:cd11052 182 KEIEDSLLEIIKKREDSLKmgRGDDYGDDLLGLLLEAnqSDDQNKNMTVQEIvdeCKTF---FFAGHETTALLLTWTtML 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      292 HLMHPanvKHLEALRKEIEEFPAQlnynnvmdEMPFAERCAR---------ESIRRDPPLLMLMRKVMADVKVGSYVVPK 362
Cdd:cd11052 259 LAIHP---EWQEKAREEVLEVCGK--------DKPPSDSLSKlktvsmvinESLRLYPPAVFLTRKAKEDIKLGGLVIPK 327

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      363 GDIIACSPLLSHHDEEAFPE------PRRWD--PERDEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd11052 328 GTSIWIPVLALHHDEEIWGEdanefnPERFAdgVAKAAKHPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTL 406
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 228-439 1.32e-25

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: 108.50  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      228 EIIIARKEE-----EVNKDSSTSDLLSG--------LLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSmLHLM 294
Cdd:cd20660 181 KVIQERKAElqkslEEEEEDDEDADIGKrkrlafldLLLEASEEGTKLSDEDIREEVDTFMFEGHDTTAAAINWA-LYLI 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      295 --HPaNVKhlEALRKEIEEFPAQLNYNNVMD---EMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACS 369
Cdd:cd20660 260 gsHP-EVQ--EKVHEELDRIFGDSDRPATMDdlkEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVL 336

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A      370 PLLSHHDEEAFPEPRRWDPER--DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLL--RDEVP 439
Cdd:cd20660 337 TYALHRDPRQFPDPEKFDPDRflPENSAGrhpyAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVqkREDLK 414
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 275-457 1.34e-25

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: 108.54  E-value: 1.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      275 MFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEEFPAQLNYNNV---MDEMPFAERCARESIRRDPPLLMLMRKVMA 351
Cdd:cd11059 230 IVAGHDTTAVTLTYLIWELSRPPNLQ--EKLREELAGLPGPFRGPPDledLDKLPYLNAVIRETLRLYPPIPGSLPRVVP 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      352 D--VKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTI 421
Cdd:cd11059 308 EggATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERwldpsgetAREMKRAFWPFGSGSRMCIGMNLALMEMKLA 387

                       170       180       190
                ....*....|....*....|....*....|....*....
2WV2_A      422 LATAFRSYDFqllrDEVPDPDYHTM---VVGPTASQCRV 457
Cdd:cd11059 388 LAAIYRNYRT----STTTDDDMEQEdafLAAPKGRRCLL 422
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 88-432 2.62e-25

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: 107.69  E-value: 2.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       88 VYSFMVpvFGEGVaYAAPYPRMREQLNFLAEELTIAKFQNFVPAIQhEVRKFMAANWDK--DEGEINLLEDCSTMIINTA 165
Cdd:cd11057  37 FYDFFR--LGRGL-FSAPYPIWKLQRKALNPSFNPKILLSFLPIFN-EEAQKLVQRLDTyvGGGEFDILPDLSRCTLEMI 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      166 CQCLFGEDLRKR-LDARRFAQLLAKMeSSLIPAAVFLPILLKLPLPQ----SARCHEARTELQKILSEII---IARKEEE 237
Cdd:cd11057 113 CQTTLGSDVNDEsDGNEEYLESYERL-FELIAKRVLNPWLHPEFIYRltgdYKEEQKARKILRAFSEKIIekkLQEVELE 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      238 VNKDSSTSD-------LLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPanvKHLEALRKEI 309
Cdd:cd11057 192 SNLDSEEDEengrkpqIFIDQLLELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLaMHP---EVQEKVYEEI 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      310 -EEFPA--QLNYNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGS-YVVPKGDIIACSPLLSHHDEEAF-PEPR 384
Cdd:cd11057 269 mEVFPDdgQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNgVVIPKGTTIVIDIFNMHRRKDIWgPDAD 348

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
2WV2_A      385 RWDPER--DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQ 432
Cdd:cd11057 349 QFDPDNflPERSAQrhpyAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLK 402
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 38-443 1.31e-24

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: 105.47  E-value: 1.31e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       38 PLGFMQECKRQLKSgIFTINIVGKRVTIVGDPHEHSRFFL------------PRNEVLS-PREvySFMvpvfgegvayaA 104
Cdd:cd20635   1 PLEFIEKARQKLGP-VFTVKAAGERMTFVTDEEDFHVFFKskdvdfqkavqdPVQNTASiSKE--SFF-----------E 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      105 PYPRMREqlnFLAEELTIAKFQNFVPAIQHEVRKFMAaNWDKDEGE--INLLEdcSTM---IINtacqCLFGEDL--RKR 177
Cdd:cd20635  67 YHTKIHD---MMKGKLASSNLAPLSDKLCEEFKEQLE-LLGSEGTGdlNDLVR--HVMypaVVN----NLFGKGLlpTSE 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      178 LDARRFAQLLAKME-----SSLIPAAVFLPILlklplpqsarchEARTELQKILSEIIIARKEEEVNKDSSTSdLLSGLL 252
Cdd:cd20635 137 EEIKEFEEHFVKFDeqfeyGSQLPEFFLRDWS------------SSKQWLLSLFEKVVPDAEKTKPLENNSKT-LLQHLL 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      253 SAVYRDGTPmslhevcGMIVAAMFAGQHTSSITTTWSMLHLMHPANVkhLEALRKEIEE-FPAQLNYN-----NVMDEMP 326
Cdd:cd20635 204 DTVDKENAP-------NYSLLLLWASLANAIPITFWTLAFILSHPSV--YKKVMEEISSvLGKAGKDKikiseDDLKKMP 274

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      327 FAERCARESIRRDPPLlMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEK--------VEGaF 398
Cdd:cd20635 275 YIKRCVLEAIRLRSPG-AITRKVVKPIKIKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKadleknvfLEG-F 352

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
2WV2_A      399 IGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLrDEVPDPDY 443
Cdd:cd20635 353 VAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLL-DPVPKPSP 396
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 228-448 3.01e-24

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: 104.53  E-value: 3.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      228 EIIIARKEEEVNKDSSTSDLLSGLLSavyRDGtpMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPanvKHLEALR 306
Cdd:cd11054 198 DEALEELKKKDEEDEEEDSLLEYLLS---KPG--LSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLaKNP---EVQEKLY 269

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      307 KEIEEFPAQLNY--NNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPR 384
Cdd:cd11054 270 EEIRSVLPDGEPitAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPE 349

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2WV2_A      385 RWDPER---DEKVEG-----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDfqlLRDEVPDPDYHTMVV 448
Cdd:cd11054 350 EFIPERwlrDDSENKnihpfASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFK---VEYHHEELKVKTRLI 418
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 214-443 3.22e-24

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 104.06  E-value: 3.22e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHEARTELQKILSEIIiarkeEEVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL 293
Cdd:cd20614 161 RSRRARAWIDARLSQLV-----ATARANGARTGLVAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIML 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      294 M-HPAnvkHLEALRKEIEEFPAQLNYNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLL 372
Cdd:cd20614 236 AeHPA---VWDALCDEAAAAGDVPRTPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLL 312

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      373 SHHDEEAFPEPRRWDPER----DEK---VEGAfiGFGAGVHKCIGQKFGLLQVKTILATAFRSYD----FQLLRDEVPDP 441
Cdd:cd20614 313 FSRDPELYPDPDRFRPERwlgrDRApnpVELL--QFGGGPHFCLGYHVACVELVQFIVALARELGaagiRPLLVGVLPGR 390


                ..
2WV2_A      442 DY 443
Cdd:cd20614 391 RY 392
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 162-444 1.03e-23

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: 103.18  E-value: 1.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      162 INTACQCLFGEDLRKRLDAR-RFAQLLAKMESSLIPAAV----FLPILLKLPLPQSARCHEARTELQKILSEIIIARKEE 236
Cdd:cd11070 115 LNVIGEVGFGFDLPALDEEEsSLHDTLNAIKLAIFPPLFlnfpFLDRLPWVLFPSRKRAFKDVDEFLSELLDEVEAELSA 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      237 EVNKDSSTSDLLSGLLSAVYRDGTpMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPaNVKhlEALRKEI----EE 311
Cdd:cd11070 195 DSKGKQGTESVVASRLKRARRSGG-LTEKELLGNLFIFFIAGHETTANTLSFALYLLaKHP-EVQ--DWLREEIdsvlGD 270

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      312 FPAQLNYNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKV-----GSYVVPKGDIIACSPLLSHHDEEA-FPEPRR 385
Cdd:cd11070 271 EPDDWDYEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIwGPDADE 350

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2WV2_A      386 WDPER-------------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYdfqllRDEVpDPDYH 444
Cdd:cd11070 351 FDPERwgstsgeigaatrFTPARGAFIPFSAGPRACLGRKFALVEFVAALAELFRQY-----EWRV-DPEWE 416
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 53-446 1.77e-23

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: 102.33  E-value: 1.77e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       53 IFTINIVGKRVTIVGDPhEHSRFFLPRNEVLSPREVYSFMVPVFGEGVAYAaPYPRMREQLNFLAEELTIAKFQNFVPAI 132
Cdd:cd20621   5 IIVSNLGSKPLISLVDP-EYIKEFLQNHHYYKKKFGPLGIDRLFGKGLLFS-EGEEWKKQRKLLSNSFHFEKLKSRLPMI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      133 QhEVRKFMAANWDKDEGEI-NLLEDCSTMIIntaCQCLFGEDLRK-------------RLDARRFAQLlakMESSL--IP 196
Cdd:cd20621  83 N-EITKEKIKKLDNQNVNIiQFLQKITGEVV---IRSFFGEEAKDlkingkeiqvelvEILIESFLYR---FSSPYfqLK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      197 AAVFLPILLKLPLPQSARCHEART-ELQKILSEIIIARKEEEVNKDSSTSDLLSGLLSAVYRDG---TPMSLHEVCGMIV 272
Cdd:cd20621 156 RLIFGRKSWKLFPTKKEKKLQKRVkELRQFIEKIIQNRIKQIKKNKDEIKDIIIDLDLYLLQKKkleQEITKEEIIQQFI 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      273 AAMFAGQHTSSITTTWSMLHLmhpANVKHL-EALRKEIEEF---PAQLNYNNvMDEMPFAERCARESIRRDPPLLMLM-R 347
Cdd:cd20621 236 TFFFAGTDTTGHLVGMCLYYL---AKYPEIqEKLRQEIKSVvgnDDDITFED-LQKLNYLNAFIKEVLRLYNPAPFLFpR 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      348 KVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER---DEKVEG---AFIGFGAGVHKCIGQKFGLLQVKTI 421
Cdd:cd20621 312 VATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERwlnQNNIEDnpfVFIPFSAGPRNCIGQHLALMEAKII 391

                       410       420
                ....*....|....*....|....*
2WV2_A      422 LATAFRSYDFQllrdEVPDPDYHTM 446
Cdd:cd20621 392 LIYILKNFEIE----IIPNPKLKLI 412
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 217-433 2.96e-23

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: 101.90  E-value: 2.96e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEII---IARKEEEVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMlHL 293
Cdd:cd11064 178 EAIRVIDDFVYEVIsrrREELNSREEENNVREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFF-WL 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      294 M--HPaNVkhLEALRKEIEE-FPAQLNYNNV---MDE---MPFAERCARESIRRDPPLLMLMRKVM-ADVKVGSYVVPKG 363
Cdd:cd11064 257 LskNP-RV--EEKIREELKSkLPKLTTDESRvptYEElkkLVYLHAALSESLRLYPPVPFDSKEAVnDDVLPDGTFVKKG 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      364 DIIacspLLSHH-----------DEEAF-PEprRW-DPERDEKVEGA--FIGFGAGVHKCIGQKFGLLQVKTILATAFRS 428
Cdd:cd11064 334 TRI----VYSIYamgrmesiwgeDALEFkPE--RWlDEDGGLRPESPykFPAFNAGPRICLGKDLAYLQMKIVAAAILRR 407


                ....*
2WV2_A      429 YDFQL 433
Cdd:cd11064 408 FDFKV 412
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 9-439 4.20e-23

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 101.55  E-value: 4.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A         9 SFNVTRPTDPPVYPVTV--PILGHIIQ-FGKSPLGFMQECKRQLKSgIFTINIVGKRVTIVGDPhEHSRFFL-PRNEVLS 84
Cdd:PLN02196  25 GFRRSSSTKLPLPPGTMgwPYVGETFQlYSQDPNVFFASKQKRYGS-VFKTHVLGCPCVMISSP-EAAKFVLvTKSHLFK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        85 P-----REVYSFMVPVFGEGVAYAApypRMREQL--NFLAEELtiakfQNFVPAIQhEVRKFMAANWDKDEgeINLLEDC 157
Cdd:PLN02196 103 PtfpasKERMLGKQAIFFHQGDYHA---KLRKLVlrAFMPDAI-----RNMVPDIE-SIAQESLNSWEGTQ--INTYQEM 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       158 STMIINTACQCLFGED-LRKRLDARRFAQLLAKMESSL---IPAAVFLpillklplpqsaRCHEARTELQKILSEIIIAR 233
Cdd:PLN02196 172 KTYTFNVALLSIFGKDeVLYREDLKRCYYILEKGYNSMpinLPGTLFH------------KSMKARKELAQILAKILSKR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       234 KEeevnKDSSTSDLLSGLLSavyrDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANV-----KHLEALRKE 308
Cdd:PLN02196 240 RQ----NGSSHNDLLGSFMG----DKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVleavtEEQMAIRKD 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       309 IEEfPAQLNYNNVmDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIAcsPLLS--HHDEEAFPEPRRW 386
Cdd:PLN02196 312 KEE-GESLTWEDT-KKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVL--PLFRniHHSADIFSDPGKF 387

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
2WV2_A       387 DPERDEKV--EGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVP 439
Cdd:PLN02196 388 DPSRFEVApkPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTSNG 442
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 265-451 4.51e-23

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: 100.78  E-value: 4.51e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      265 HEVCGMIVAAMFAGQHTSSITTTWSMLHLM-HPaNVkhLEALRKEIEEF----PAQLNYNnVMDEMPFAERCARESIRRD 339
Cdd:cd11082 219 EEIAGTLLDFLFASQDASTSSLVWALQLLAdHP-DV--LAKVREEQARLrpndEPPLTLD-LLEEMKYTRQVVKEVLRYR 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      340 PPLLMLMRKVMADVKVG-SYVVPKGDIIACSPLLSHHDEeaFPE-----PRRWDPERDEKVEGA--FIGFGAGVHKCIGQ 411
Cdd:cd11082 295 PPAPMVPHIAKKDFPLTeDYTVPKGTIVIPSIYDSCFQG--FPEpdkfdPDRFSPERQEDRKYKknFLVFGAGPHQCVGQ 372

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
2WV2_A      412 KFGLLQVKTILATAFRSYDFQllRDEVPDPDyhTMVVGPT 451
Cdd:cd11082 373 EYAINHLMLFLALFSTLVDWK--RHRTPGSD--EIIYFPT 408
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 52-432 7.47e-23

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: 100.36  E-value: 7.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       52 GIFTINIVGKRVTIVGDP-------HEHSRFFLPRNEVLSPREVYSFMVPVFGEGvayaapyPRMREQLNFLAEELTIAK 124
Cdd:cd20617   2 GIFTLWLGDVPTVVLSDPeiikeafVKNGDNFSDRPLLPSFEIISGGKGILFSNG-------DYWKELRRFALSSLTKTK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      125 FQN-FVPAIQHEVRKFMAA--NWDKDEGEINLLEDCSTMIINTACQCLFGEDLrKRLDARRFAQLLAKME-----SSLIP 196
Cdd:cd20617  75 LKKkMEELIEEEVNKLIESlkKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRF-PDEDDGEFLKLVKPIEeifkeLGSGN 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      197 AAVFLPILLKLPLPQSARCHEARTELQKILSEIIIARKEEevNKDSSTSDLLSGLLSAVYRDGTPMSLHE--VCGMIVAA 274
Cdd:cd20617 154 PSDFIPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKT--IDPNNPRDLIDDELLLLLKEGDSGLFDDdsIISTCLDL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      275 MFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEEF-----PAQLNYnnvMDEMPFAERCARESIRRDPPLLM-LMRK 348
Cdd:cd20617 232 FLAGTDTTSTTLEWFLLYLANNPEIQ--EKIYEEIDNVvgndrRVTLSD---RSKLPYLNAVIKEVLRLRPILPLgLPRV 306

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      349 VMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER---DEKVEG--AFIGFGAGVHKCIGQKFGLLQVKTILA 423
Cdd:cd20617 307 TTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERfleNDGNKLseQFIPFGIGKRNCVGENLARDELFLFFA 386


                ....*....
2WV2_A      424 TAFRSYDFQ 432
Cdd:cd20617 387 NLLLNFKFK 395
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 130-437 3.58e-22

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: 98.45  E-value: 3.58e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      130 PAIQHEVRKFMAAnWDKDEGE-----INLLEDCSTMIINTACQCLFGED---LRKRLDARRFAQLLAKMESSLI---PAA 198
Cdd:cd11061  75 PRILSHVEQLCEQ-LDDRAGKpvswpVDMSDWFNYLSFDVMGDLAFGKSfgmLESGKDRYILDLLEKSMVRLGVlghAPW 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      199 VFLPILLKLPLPQSARcheARTELQKILSEIIIARKEeevNKDSSTSDLLSGLLSA-VYRDGTPMSLHEVCGMIVAAMFA 277
Cdd:cd11061 154 LRPLLLDLPLFPGATK---ARKRFLDFVRAQLKERLK---AEEEKRPDIFSYLLEAkDPETGEGLDLEELVGEARLLIVA 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      278 GQHTSSITTTWSMLHLMHpaNVKHLEALRKEIEE-FPAQLN---YNNVMDeMPFAERCARESIRRDPPLL-MLMRKVMAD 352
Cdd:cd11061 228 GSDTTATALSAIFYYLAR--NPEAYEKLRAELDStFPSDDEirlGPKLKS-LPYLRACIDEALRLSPPVPsGLPRETPPG 304

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      353 -VKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER----DEKV---EGAFIGFGAGVHKCIGQKFGLLQVKTILAT 424
Cdd:cd11061 305 gLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERwlsrPEELvraRSAFIPFSIGPRGCIGKNLAYMELRLVLAR 384

                       330
                ....*....|...
2WV2_A      425 AFRSYDFQLLRDE 437
Cdd:cd11061 385 LLHRYDFRLAPGE 397
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 122-433 5.76e-22

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: 97.74  E-value: 5.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      122 IAKFQNFVPAIQHEVRKfMAANWDK-----DEGEINLLEDCSTMIINTACQCLFGEDLRkrlDARRFAQLLAK------- 189
Cdd:cd20642  80 LEKLKNMLPAFYLSCSE-MISKWEKlvsskGSCELDVWPELQNLTSDVISRTAFGSSYE---EGKKIFELQKEqgeliiq 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      190 -MESSLIPAAVFLPILLKLplpqsaRCHEARTELQKILSEIIIARKEEEVNKDSSTSDLLSGLLSAVYRD-------GTP 261
Cdd:cd20642 156 aLRKVYIPGWRFLPTKRNR------RMKEIEKEIRSSLRGIINKREKAMKAGEATNDDLLGILLESNHKEikeqgnkNGG 229

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      262 MSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHP-----ANVKHLEALRKEIEEFPAqLNYNNVMDeMPFaercaRES 335
Cdd:cd20642 230 MSTEDVIEECKLFYFAGQETTSVLLVWTMVLLsQHPdwqerAREEVLQVFGNNKPDFEG-LNHLKVVT-MIL-----YEV 302

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      336 IRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPE-PRRWDPER-------DEKVEGAFIGFGAGVHK 407
Cdd:cd20642 303 LRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERfaegiskATKGQVSYFPFGWGPRI 382

                       330       340
                ....*....|....*....|....*.
2WV2_A      408 CIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd20642 383 CIGQNFALLEAKMALALILQRFSFEL 408
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 214-446 9.99e-22

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: 97.44  E-value: 9.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHEARTELQKILSEIIIARK----EEEVN---------KDSStsdLLSGLLSAVYRDGTPMSLH-EVCGMIVAamfaGQ 279
Cdd:cd11046 181 KFLRDLKLLNDTLDDLIRKRKemrqEEDIElqqedylneDDPS---LLRFLVDMRDEDVDSKQLRdDLMTMLIA----GH 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      280 HTSSITTTWSMLHLMhpanvKHLEALRKEIEEFPAQL-----NYNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVK 354
Cdd:cd11046 254 ETTAAVLTWTLYELS-----QNPELMAKVQAEVDAVLgdrlpPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDK 328

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      355 V--GSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEG----------AFIGFGAGVHKCIGQKFGLLQVKTIL 422
Cdd:cd11046 329 LpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFInppneviddfAFLPFGGGPRKCLGDQFALLEATVAL 408

                       250       260
                ....*....|....*....|....*....
2WV2_A      423 ATAFRSYDFQLLRDE-----VPDPDYHTM 446
Cdd:cd11046 409 AMLLRRFDFELDVGPrhvgmTTGATIHTK 437
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 224-430 4.59e-21

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: 95.21  E-value: 4.59e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      224 KILSEIIIARKEEEVNKDSSTSDL---------LSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSmLHLM 294
Cdd:cd20680 192 NVIAERAEEMKAEEDKTGDSDGESpskkkrkafLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWS-LYLL 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      295 --HPanvkhlEALRK---EIEEFPAQLNYNNVMDEMP---FAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDII 366
Cdd:cd20680 271 gsHP------EVQRKvhkELDEVFGKSDRPVTMEDLKklrYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNA 344

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      367 ACSPLLSHHDEEAFPEPRRWDPER--DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYD 430
Cdd:cd20680 345 VIIPYALHRDPRYFPEPEEFRPERffPENSSGrhpyAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFW 414
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 240-442 5.30e-21

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: 95.14  E-value: 5.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      240 KDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPanvKHLEALRKEIEEF-----P 313
Cdd:cd20679 218 AKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLaRHP---EYQERCRQEVQELlkdreP 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      314 AQLNYNNvMDEMPFAERCARESIRRDPPLLMLMRKVMADVKV-GSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER-- 390
Cdd:cd20679 295 EEIEWDD-LAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRfd 373

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
2WV2_A      391 DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILAtafrsydFQLLRDEVPDPD 442
Cdd:cd20679 374 PENSQGrsplAFIPFSAGPRNCIGQTFAMAEMKVVLA-------LTLLRFRVLPDD 422
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 126-423 1.92e-20

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: 92.54  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      126 QNFVPAIQHEVRKFMAANwdKDEGEINLLED-CSTMIINTACQCLfgeDLRKRlDARRFAQL---LAKMESSLipaavfl 201
Cdd:cd11080  73 DHLLPLIKENAEELIAPF--LERGRVDLVNDfGKPFAVNVTMDML---GLDKR-DHEKIHEWhssVAAFITSL------- 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      202 pillklPLPQSARCHEART--ELQKILSEIIIARKEEevnkdsSTSDLLSGLLSAVYrDGTPMSLHEVCGMIVAAMFAGQ 279
Cdd:cd11080 140 ------SQDPEARAHGLRCaeQLSQYLLPVIEERRVN------PGSDLISILCTAEY-EGEALSDEDIKALILNVLLAAT 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      280 HTSSITTTWSMLHL-MHPAnvkhlealrkeieefpaQLNynNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSY 358
Cdd:cd11080 207 EPADKTLALMIYHLlNNPE-----------------QLA--AVRADRSLVPRAIAETLRYHPPVQLIPRQASQDVVVSGM 267

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2WV2_A      359 VVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKV-EGAF------IGFGAGVHKCIGQKFGLLQVKTILA 423
Cdd:cd11080 268 EIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREDLGiRSAFsgaadhLAFGSGRHFCVGAALAKREIEIVAN 339
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 217-411 3.10e-20

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: 91.59  E-value: 3.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIIARKEEEvnkdssTSDLLSGLLSAVYrDGTPMSLHEVCGMIVAAMFAGqhtsSITTTW---SMLHL 293
Cdd:cd20629 150 AAAAELYDYVLPLIAERRRAP------GDDLISRLLRAEV-EGEKLDDEEIISFLRLLLPAG----SDTTYRalaNLLTL 218

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      294 M--HPAnvkHLEALRKEIEEFPAQLnynnvmdempfaercaRESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPL 371
Cdd:cd20629 219 LlqHPE---QLERVRRDRSLIPAAI----------------EEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVG 279

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
2WV2_A      372 LSHHDEEAFPEPRRWDPERDEKvegAFIGFGAGVHKCIGQ 411
Cdd:cd20629 280 SANRDEDVYPDPDVFDIDRKPK---PHLVFGGGAHRCLGE 316
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 221-433 3.21e-20

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: 92.51  E-value: 3.21e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      221 ELQKILSEIIIARKE--EEVNKDSSTSDLLSGLLSA-VYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHP 296
Cdd:cd20639 184 EIRKSLLKLIERRQTaaDDEKDDEDSKDLLGLMISAkNARNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLaMHP 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      297 anvKHLEALRKEIEEFPAQlnynnvmDEMPFAERCAR---------ESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIA 367
Cdd:cd20639 264 ---EWQERARREVLAVCGK-------GDVPTKDHLPKlktlgmilnETLRLYPPAVATIRRAKKDVKLGGLDIPAGTELL 333

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2WV2_A      368 CSPLLSHHDEEAFPE------PRRW--DPERDEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd20639 334 IPIMAIHHDAELWGNdaaefnPARFadGVARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRL 407
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 213-452 4.00e-20

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: 91.84  E-value: 4.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      213 ARCHEARTELQKILSEIIIARKEEevNKDsstsDLLSGLLSAVyRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd20625 155 ARANAAAAELAAYFRDLIARRRAD--PGD----DLISALVAAE-EDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLA 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LM-HPAnvkHLEALRKEIEEFPaqlnynNVMDEMpfaercaresIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACspL 371
Cdd:cd20625 228 LLrHPE---QLALLRADPELIP------AAVEEL----------LRYDSPVQLTARVALEDVEIGGQTIPAGDRVLL--L 286

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      372 LS--HHDEEAFPEPRRWDPERDekvEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRsyDFQLLRDEVPDPDY-HTMVV 448
Cdd:cd20625 287 LGaaNRDPAVFPDPDRFDITRA---PNRHLAFGAGIHFCLGAPLARLEAEIALRALLR--RFPDLRLLAGEPEWrPSLVL 361


                ....*
2WV2_A      449 -GPTA 452
Cdd:cd20625 362 rGLRS 366
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 217-411 1.03e-19

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 90.34  E-value: 1.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIIARKEEEVNkdsstsDLLSGLLSAvYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MH 295
Cdd:cd11035 148 AAAQAVLDYLTPLIAERRANPGD------DLISAILNA-EIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLaRH 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      296 PAnvkhleaLRKEIEEFPAQLNynNVMDEMpfaercaresIRRDPPLLmLMRKVMADVKVGSYVVPKGDIIACSPLLSHH 375
Cdd:cd11035 221 PE-------DRRRLREDPELIP--AAVEEL----------LRRYPLVN-VARIVTRDVEFHGVQLKAGDMVLLPLALANR 280

                       170       180       190
                ....*....|....*....|....*....|....*.
2WV2_A      376 DEEAFPEPRRWDPERDEKVEgafIGFGAGVHKCIGQ 411
Cdd:cd11035 281 DPREFPDPDTVDFDRKPNRH---LAFGAGPHRCLGS 313
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 214-433 1.20e-19

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: 91.04  E-value: 1.20e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHEARTELQKILSEIIIARKEEEVNKDSSTSDLLSGLLSAvYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL 293
Cdd:cd20613 183 EVREAIKFLRETGRECIEERLEALKRGEEVPNDILTHILKA-SEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLEL 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      294 -MHPanvKHLEALRKEIEEFPAQLNYNNVMD--EMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSP 370
Cdd:cd20613 262 gRHP---EILKRLQAEVDEVLGSKQYVEYEDlgKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVST 338

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      371 LLSHHDEEAFPEPRRWDPER------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd20613 339 YVMGRMEEYFEDPLKFDPERfspeapEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFEL 407
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 212-444 1.26e-19

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: 90.09  E-value: 1.26e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      212 SARCHEARTELQKILSEIIIARKEEEVNkdsstsDLLSGLLSAVYrDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSML 291
Cdd:cd11034 143 PEEGAAAFAELFGHLRDLIAERRANPRD------DLISRLIEGEI-DGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALL 215

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      292 HLM-HPAN----VKHLEALRKEIEEFpaqlnynnvmdempfaercaresIRRDPPLLMLMRKVMADVKVGSYVVPKGDII 366
Cdd:cd11034 216 WLAqHPEDrrrlIADPSLIPNAVEEF-----------------------LRFYSPVAGLARTVTQEVEVGGCRLKPGDRV 272

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      367 ACSPLLSHHDEEAFPEPRRWDPERDEKVEgafIGFGAGVHKCIGQKFGLLQVKTILATAF-RSYDFQLlrDEVPDPDYH 444
Cdd:cd11034 273 LLAFASANRDEEKFEDPDRIDIDRTPNRH---LAFGSGVHRCLGSHLARVEARVALTEVLkRIPDFEL--DPGATCEFL 346
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 211-439 5.00e-19

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: 88.43  E-value: 5.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      211 QSARCHEARTELQKILSEIIIARKEEEvnkdssTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSM 290
Cdd:cd11078 160 EQVEAAAAVGELWAYFADLVAERRREP------RDDLISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAV 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      291 LHLM-HPAnvkhleaLRKEIEEFPAQLNynnvmdemPFAErcarESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACS 369
Cdd:cd11078 234 KLLLeHPD-------QWRRLRADPSLIP--------NAVE----ETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLL 294

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2WV2_A      370 PLLSHHDEEAFPEPRRWDPERDEkvEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSY-DFQLLRDEVP 439
Cdd:cd11078 295 FGSANRDERVFPDPDRFDIDRPN--ARKHLTFGHGIHFCLGAALARMEARIALEELLRRLpGMRVPGQEVV 363
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 217-442 6.77e-19

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: 88.01  E-value: 6.77e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIIARKEEevnkdsSTSDLLSGLLSAVYRDGTpMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-H 295
Cdd:cd11031 164 AARQELRGYMAELVAARRAE------PGDDLLSALVAARDDDDR-LSEEELVTLAVGLLVAGHETTASQIGNGVLLLLrH 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      296 PAnvkHLEALRKEIEEFPAQLNynnvmdempfaercarESIRRDPP--LLMLMRKVMADVKVGSYVVPKGDIIACSPLLS 373
Cdd:cd11031 237 PE---QLARLRADPELVPAAVE----------------ELLRYIPLgaGGGFPRYATEDVELGGVTIRAGEAVLVSLNAA 297

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      374 HHDEEAFPEPRRWDPERDEKvegAFIGFGAGVHKCIGQKFGLLQVKTILATAFRsyDFQLLRDEVPDPD 442
Cdd:cd11031 298 NRDPEVFPDPDRLDLDREPN---PHLAFGHGPHHCLGAPLARLELQVALGALLR--RLPGLRLAVPEEE 361
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 214-440 1.10e-18

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: 87.97  E-value: 1.10e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHEARTELQKILSEIIIARKEE-EVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd11073 178 RMAEHFGKLFDIFDGFIDERLAErEAGGDKKKDDDLLLLLDLELDSESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAE 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LMHpaNVKHLEALRKEIEEFpaqLNYNNVMDE-----MPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGdii 366
Cdd:cd11073 258 LLR--NPEKMAKARAELDEV---IGKDKIVEEsdiskLPYLQAVVKETLRLHPPApLLLPRKAEEDVEVMGYTIPKG--- 329

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      367 acSPLL-----SHHDEEAFPEPRRWDPER----DEKVEGA---FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLL 434
Cdd:cd11073 330 --TQVLvnvwaIGRDPSVWEDPLEFKPERflgsEIDFKGRdfeLIPFGSGRRICPGLPLAERMVHLVLASLLHSFDWKLP 407


                ....*.
2WV2_A      435 RDEVPD 440
Cdd:cd11073 408 DGMKPE 413
PLN02290 PLN02290
cytokinin trans-hydroxylase
 219-431 8.39e-18

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 86.02  E-value: 8.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       219 RTELQKILSEIIIARKE-EEVNKDSSTSDLLSGLLSAVYR----DGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL 293
Cdd:PLN02290 264 KGEVERLLMEIIQSRRDcVEIGRSSSYGDDLLGMLLNEMEkkrsNGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLL 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       294 MHpaNVKHLEALRKEIEEFpaqlnynnVMDEMPFAERCAR---------ESIRRDPPLLMLMRKVMADVKVGSYVVPKGD 364
Cdd:PLN02290 344 AS--NPTWQDKVRAEVAEV--------CGGETPSVDHLSKltllnmvinESLRLYPPATLLPRMAFEDIKLGDLHIPKGL 413

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2WV2_A       365 IIACSPLLSHHDEEAF-PEPRRWDPER----DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDF 431
Cdd:PLN02290 414 SIWIPVLAIHHSEELWgKDANEFNPDRfagrPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSF 485
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 19-440 1.03e-17

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 85.51  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        19 PVYPVTVPILGHIIQFGK-SPLGFMQECKRqLKSGIFTINIVGKRVTIVGDPhEHSRFFLPRNEV-------LSPREVYS 90
Cdd:PLN03234  30 PPGPKGLPIIGNLHQMEKfNPQHFLFRLSK-LYGPIFTMKIGGRRLAVISSA-ELAKELLKTQDLnftarplLKGQQTMS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        91 FMVPVFGEGvAYAAPYPRMREQLnfLAEELTIAKFQNFVPAIQHEVRKFMAANWDKDE--GEINLLEDCSTMIINTACQC 168
Cdd:PLN03234 108 YQGRELGFG-QYTAYYREMRKMC--MVNLFSPNRVASFRPVREEECQRMMDKIYKAADqsGTVDLSELLLSFTNCVVCRQ 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       169 LFGEDLRKR-LDARRFAQLLAKME--------SSLIPAAVFLPILLKLplpqSARCHEARTELQKILSEIIiaRKEEEVN 239
Cdd:PLN03234 185 AFGKRYNEYgTEMKRFIDILYETQallgtlffSDLFPYFGFLDNLTGL----SARLKKAFKELDTYLQELL--DETLDPN 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       240 KDSSTSDLLSGLLSAVYRDgTPMSL---HE-VCGMIVAAMFAGQHTSSITTTWSMLHLmhpanVKHLEALRKEIEEFPAQ 315
Cdd:PLN03234 259 RPKQETESFIDLLMQIYKD-QPFSIkftHEnVKAMILDIVVPGTDTAAAVVVWAMTYL-----IKYPEAMKKAQDEVRNV 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       316 LNYNNVMDE-----MPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPE-PRRWDP 388
Cdd:PLN03234 333 IGDKGYVSEedipnLPYLKAVIKESLRLEPVIpILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIP 412

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2WV2_A       389 ER--DEKVEGAFIG-------FGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPD 440
Cdd:PLN03234 413 ERfmKEHKGVDFKGqdfellpFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPE 473
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 245-444 1.99e-17

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: 84.04  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      245 SDLLSGLLSA------VYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPanvKHLEALRKEI-EEFPAql 316
Cdd:cd20641 208 DDLLGLMLEAassnegGRRTERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLsLHP---DWQEKLREEVfRECGK-- 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      317 nynnvmDEMPFAERCAR---------ESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPE----- 382
Cdd:cd20641 283 ------DKIPDADTLSKlklmnmvlmETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWGSdadef 356

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
2WV2_A      383 -PRRWDP--ERDEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDPDYH 444
Cdd:cd20641 357 nPLRFANgvSRAATHPNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPEYVHAPADH 421
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 217-410 2.31e-17

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: 83.73  E-value: 2.31e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIiARKEEEvNKDsstsDLLSGLLSAVyRDGTPMSLHEVCGMIVAAMFAGQHTSS--ITTtwSMLHLM 294
Cdd:cd11029 169 AALRELVDYLAELV-ARKRAE-PGD----DLLSALVAAR-DEGDRLSEEELVSTVFLLLVAGHETTVnlIGN--GVLALL 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      295 -HPAnvkHLEALRKEIEEFPAqlnynnVMDEMpfaercaresIRRDPPLLML-MRKVMADVKVGSYVVPKGDIIACSPLL 372
Cdd:cd11029 240 tHPD---QLALLRADPELWPA------AVEEL----------LRYDGPVALAtLRFATEDVEVGGVTIPAGEPVLVSLAA 300

                       170       180       190
                ....*....|....*....|....*....|....*...
2WV2_A      373 SHHDEEAFPEPRRWDPERDekvEGAFIGFGAGVHKCIG 410
Cdd:cd11029 301 ANRDPARFPDPDRLDITRD---ANGHLAFGHGIHYCLG 335
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 219-423 2.50e-17

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: 83.83  E-value: 2.50e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      219 RTELQKILSEIIIARKE--EEVNKDSSTSDLLSGLLSAVYRDGTPMSL--HEVCGMIVAAMFAGQHTSSITTTWSMLHLM 294
Cdd:cd11075 180 RRRQEEVLLPLIRARRKrrASGEADKDYTDFLLLDLLDLKEEGGERKLtdEELVSLCSEFLNAGTDTTATALEWAMAELV 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      295 HPANVKhlEALRKEIEEFPAQlnyNNVMDE-----MPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIAC 368
Cdd:cd11075 260 KNPEIQ--EKLYEEIKEVVGD---EAVVTEedlpkMPYLKAVVLETLRRHPPGhFLLPHAVTEDTVLGGYDIPAGAEVNF 334

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
2WV2_A      369 SPLLSHHDEEAFPEPRRWDPER---DEKVEGAFIG--------FGAGVHKCIGQKFGLLQVKTILA 423
Cdd:cd11075 335 NVAAIGRDPKVWEDPEEFKPERflaGGEAADIDTGskeikmmpFGAGRRICPGLGLATLHLELFVA 400
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 261-439 3.14e-17

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: 83.73  E-value: 3.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      261 PMSLHEVCGMIVAAMFAGQHTSSITTTW-SMLHLMHPanvKHLEALRKEIEEFPAQ---LNYNNVmDEMPFAERCARESI 336
Cdd:cd20649 256 MLTEDEIVGQAFIFLIAGYETTTNTLSFaTYLLATHP---ECQKKLLREVDEFFSKhemVDYANV-QELPYLDMVIAETL 331

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      337 RRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER---DEKVEG---AFIGFGAGVHKCIG 410
Cdd:cd20649 332 RMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERftaEAKQRRhpfVYLPFGAGPRSCIG 411

                       170       180       190
                ....*....|....*....|....*....|
2WV2_A      411 QKFGLLQVKTILATAFRSYDFQLLRD-EVP 439
Cdd:cd20649 412 MRLALLEIKVTLLHILRRFRFQACPEtEIP 441
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 221-450 6.70e-17

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: 82.46  E-value: 6.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      221 ELQKILSEIIIARKEEEvnkdSSTSDLLSGLLSAVYRDGTPMSLHE--VCGMIVAAMFAGQHTSSITTTWS-MLHLMHP- 296
Cdd:cd20640 187 EIRSLILEIVKEREEEC----DHEKDLLQAILEGARSSCDKKAEAEdfIVDNCKNIYFAGHETTAVTAAWClMLLALHPe 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      297 ----ANVKHLEALRKEIEEFPAQLNYNNVMdempfaeRCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLL 372
Cdd:cd20640 263 wqdrVRAEVLEVCKGGPPDADSLSRMKTVT-------MVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVST 335

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      373 SHHDEEAF-PEPRRWDPER-DEKVEGA------FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLlrdevpDPDY- 443
Cdd:cd20640 336 LHLDPEIWgPDANEFNPERfSNGVAAAckpphsYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSFTL------SPEYq 409

                       250
                ....*....|.
2WV2_A      444 ----HTMVVGP 450
Cdd:cd20640 410 hspaFRLIVEP 420
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 218-422 8.45e-17

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 82.45  E-value: 8.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       218 ARTELQKILSEIIIARK-EEEVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-H 295
Cdd:PLN02302 238 ARKKLVALFQSIVDERRnSRKQNISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQeH 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       296 PANVKHLEALRKEI-EEFPAQLNYNNVMD--EMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLL 372
Cdd:PLN02302 318 PEVLQKAKAEQEEIaKKRPPGQKGLTLKDvrKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQ 397

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
2WV2_A       373 SHHDEEAFPEPRRWDPERDEKVE---GAFIGFGAGVHKCIGQKFGLLQVKTIL 422
Cdd:PLN02302 398 VHMDPEVYPNPKEFDPSRWDNYTpkaGTFLPFGLGSRLCPGNDLAKLEISIFL 450
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 221-433 1.00e-16

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: 81.92  E-value: 1.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      221 ELQKILSEIIIARKEEEvnKDSSTSDLLSGLLSAVYRDGTP---MSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPA 297
Cdd:cd11062 178 DFQESIAKQVDEVLRQV--SAGDPPSIVTSLFHALLNSDLPpseKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNP 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      298 NVkhLEALRKEIEEfpAQLNYNNVMD-----EMPFAERCARESIRRDPPLL-MLMRKV-MADVKVGSYVVPKGDIIACSP 370
Cdd:cd11062 256 EI--LERLREELKT--AMPDPDSPPSlaeleKLPYLTAVIKEGLRLSYGVPtRLPRVVpDEGLYYKGWVIPPGTPVSMSS 331

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      371 LLSHHDEEAFPEPRRWDPER--DEKVEGA----FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd11062 332 YFVHHDEEIFPDPHEFRPERwlGAAEKGKldryLVPFSKGSRSCLGINLAYAELYLALAALFRRFDLEL 400
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 130-447 2.79e-16

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 80.16  E-value: 2.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      130 PAIQHEVRKFMAANwdKDEGEINLLEDCSTMIINTACQCLFGEDLRKRLDARRFAQllaKMESSLIPAAVflpillklpL 209
Cdd:cd20630  87 AEIQAIVDQLLDEL--GEPEEFDVIREIAEHIPFRVISAMLGVPAEWDEQFRRFGT---ATIRLLPPGLD---------P 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      210 PQSARCHEARTELQKILSEIIIARKEEEVNkdsstSDLLSGLLSAvYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWS 289
Cdd:cd20630 153 EELETAAPDVTEGLALIEEVIAERRQAPVE-----DDLLTTLLRA-EEDGERLSEDELMALVAALIVAGTDTTVHLITFA 226

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      290 MLHLM-HPanvKHLEALRKEIEEFPaqlnynNVMDEmpfaercareSIRRDPPLLM-LMRKVMADVKVGSYVVPKGDIIA 367
Cdd:cd20630 227 VYNLLkHP---EALRKVKAEPELLR------NALEE----------VLRWDNFGKMgTARYATEDVELCGVTIRKGQMVL 287

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      368 CSPLLSHHDEEAFPEPRRWDPERDEKvegAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSY-DFQLLrdEVPDPDYHTM 446
Cdd:cd20630 288 LLLPSALRDEKVFSDPDRFDVRRDPN---ANIAFGYGPHFCIGAALARLELELAVSTLLRRFpEMELA--EPPVFDPHPV 362


                .
2WV2_A      447 V 447
Cdd:cd20630 363 L 363
PLN02936 PLN02936
epsilon-ring hydroxylase
 225-451 3.17e-16

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 80.99  E-value: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       225 ILSEIIIARkeEEVNKDSSTSDLLSgllsavyrdgtpmslhevcgMIVAamfaGQHTSSITTTWSMLHLMhpanvKHLEA 304
Cdd:PLN02936 263 VLRFLLASR--EEVSSVQLRDDLLS--------------------MLVA----GHETTGSVLTWTLYLLS-----KNPEA 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       305 LRKEIEEFPAQLN-----YNNvMDEMPFAERCARESIRRDP-PLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEE 378
Cdd:PLN02936 312 LRKAQEELDRVLQgrpptYED-IKELKYLTRCINESMRLYPhPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPE 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       379 AFP-----EPRRWDPE----RDEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLlrdeVPDPDYhTMVVG 449
Cdd:PLN02936 391 VWEraeefVPERFDLDgpvpNETNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLEL----VPDQDI-VMTTG 465


                 ..
2WV2_A       450 PT 451
Cdd:PLN02936 466 AT 467
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 217-442 5.92e-16

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 79.10  E-value: 5.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIiARKEEEvnkdsSTSDLLSGLLSAVYRDGtPMSLHEVCGMIVAAMFAGQHTSS--ITT-TWSMLHl 293
Cdd:cd11030 166 AAGAELRAYLDELV-ARKRRE-----PGDDLLSRLVAEHGAPG-ELTDEELVGIAVLLLVAGHETTAnmIALgTLALLE- 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      294 mHPAnvkHLEALRKEIEEFPaqlnynNVMDEMpfaERCAreSIRRDPpllmLMRKVMADVKVGSYVVPKGDIIACSPLLS 373
Cdd:cd11030 238 -HPE---QLAALRADPSLVP------GAVEEL---LRYL--SIVQDG----LPRVATEDVEIGGVTIRAGEGVIVSLPAA 298

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      374 HHDEEAFPEPRRWDPERDekvEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSydFQLLRDEVPDPD 442
Cdd:cd11030 299 NRDPAVFPDPDRLDITRP---ARRHLAFGHGVHQCLGQNLARLELEIALPTLFRR--FPGLRLAVPAEE 362
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 222-443 6.25e-16

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: 79.54  E-value: 6.25e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      222 LQKILSEIIIARKEeevNKDSSTSDLLSGLLSAVYRD-GTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMhpanvK 300
Cdd:cd11068 188 MRDLVDEIIAERRA---NPDGSPDDLLNLMLNGKDPEtGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLL-----K 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      301 HLEALRKEIEEF-----PAQLNYNNVMdEMPFAERCARESIRRDPPLLMLMRKVMADVKV-GSYVVPKGDIIACSPLLSH 374
Cdd:cd11068 260 NPEVLAKARAEVdevlgDDPPPYEQVA-KLRYIRRVLDETLRLWPTAPAFARKPKEDTVLgGKYPLKKGDPVLVLLPALH 338

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2WV2_A      375 HDEEAF---PE---PRRWDPERDEKV-EGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFqllrdeVPDPDY 443
Cdd:cd11068 339 RDPSVWgedAEefrPERFLPEEFRKLpPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDF------EDDPDY 408
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 214-442 6.67e-16

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: 79.63  E-value: 6.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHEARTELQKILSEIIIARK-----EEEVNKDSSTS--DLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITT 286
Cdd:cd20678 180 RFRRACQLAHQHTDKVIQQRKeqlqdEGELEKIKKKRhlDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTASGI 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      287 TWSMLHL-MHPanvKHLEALRKEIEEF---PAQLNYNNvMDEMPFAERCARESIRRDPPLLMLMRKVMADVK-VGSYVVP 361
Cdd:cd20678 260 SWILYCLaLHP---EHQQRCREEIREIlgdGDSITWEH-LDQMPYTTMCIKEALRLYPPVPGISRELSKPVTfPDGRSLP 335

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      362 KGDIIACSPLLSHHDEEAFPEPRRWDPER--DEKVEG----AFIGFGAGVHKCIGQKFGLLQVKTILAtafrsydFQLLR 435
Cdd:cd20678 336 AGITVSLSIYGLHHNPAVWPNPEVFDPLRfsPENSSKrhshAFLPFSAGPRNCIGQQFAMNEMKVAVA-------LTLLR 408


                ....*...
2WV2_A      436 DEV-PDPD 442
Cdd:cd20678 409 FELlPDPT 416
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 262-439 1.00e-15

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: 79.00  E-value: 1.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      262 MSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPanvKHLEALRKEIEE-FP--AQLNYNNVMdEMPFAERCARESIR 337
Cdd:cd20650 224 LSDLEILAQSIIFIFAGYETTSSTLSFLLYELaTHP---DVQQKLQEEIDAvLPnkAPPTYDTVM-QMEYLDMVVNETLR 299

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      338 RDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER------DEKVEGAFIGFGAGVHKCIGQ 411
Cdd:cd20650 300 LFPIAGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERfskknkDNIDPYIYLPFGSGPRNCIGM 379

                       170       180
                ....*....|....*....|....*....
2WV2_A      412 KFGLLQVKTILATAFRSYDFQLLRD-EVP 439
Cdd:cd20650 380 RFALMNMKLALVRVLQNFSFKPCKEtQIP 408
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 214-422 3.34e-15

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 77.71  E-value: 3.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       214 RCHEARTELQKILSEIIIARKEEEVNKDSSTSDLLSGLLSAvyrdGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL 293
Cdd:PLN02987 219 RAIQARTKVAEALTLVVMKRRKEEEEGAEKKKDMLAALLAS----DDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       294 MHPANVkhLEALRKEIEEFPAQLNYNNVMD-----EMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIAC 368
Cdd:PLN02987 295 TETPLA--LAQLKEEHEKIRAMKSDSYSLEwsdykSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFA 372

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       369 SPLLSHHDEEAFPEPRRWDPERDEKVEGA------FIGFGAGVHKCIGQKFGLLQVKTIL 422
Cdd:PLN02987 373 SFRAVHLDHEYFKDARTFNPWRWQSNSGTtvpsnvFTPFGGGPRLCPGYELARVALSVFL 432
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 213-433 4.25e-15

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: 77.21  E-value: 4.25e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      213 ARCHEARTELQKILSEIIIARKEEEVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd20618 176 KRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAE 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LMhpanvKHLEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDII 366
Cdd:cd20618 256 LL-----RHPEVMRKAQEELDSVVGRERLVEEsdlpkLPYLQAVVKETLRLHPPGpLLLPHESTEDCKVAGYDIPAGTRV 330

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      367 acspLLS----HHDEEAFPEPRRWDPER--DEKVEGA------FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd20618 331 ----LVNvwaiGRDPKVWEDPLEFKPERflESDIDDVkgqdfeLLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFDWSL 405
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 270-442 5.19e-15

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: 76.87  E-value: 5.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      270 MIVAAMF-AGQHTSSITTTWSMLHLMHPANVkhLEALRKEIEEF--PAQLNYNNVMDEMPFAERCARESIRRDP--PLlM 344
Cdd:cd20651 228 MICLDLFiAGSETTSNTLGFAFLYLLLNPEV--QRKVQEEIDEVvgRDRLPTLDDRSKLPYTEAVILEVLRIFTlvPI-G 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      345 LMRKVMADVKVGSYVVPKGDIIacspLLS----HHDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKCIGQKFG 414
Cdd:cd20651 305 IPHRALKDTTLGGYRIPKDTTI----LASlysvHMDPEYWGDPEEFRPERFLDEDGkllkdeWFLPFGAGKRRCLGESLA 380

                       170       180
                ....*....|....*....|....*...
2WV2_A      415 LLQVKTILATAFRSYDFQLLRDEVPDPD 442
Cdd:cd20651 381 RNELFLFFTGLLQNFTFSPPNGSLPDLE 408
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 122-443 9.58e-15

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: 76.09  E-value: 9.58e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      122 IAKFQNFVPAIQHEVRKFMAaNWDKDEGE-INLLEDCSTMIINTACQCLFGEdlRKRLDARRFAQLL------AKMESSL 194
Cdd:cd11027  77 ASGGPRLEEKIAEEAEKLLK-RLASQEGQpFDPKDELFLAVLNVICSITFGK--RYKLDDPEFLRLLdlndkfFELLGAG 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      195 IPAAVFLPILLKLPlpqsarchEARTELQKILSEI--IIARKEEEvNKDSSTS----DLLSGLLSAVY----RDGTPMSL 264
Cdd:cd11027 154 SLLDIFPFLKYFPN--------KALRELKELMKERdeILRKKLEE-HKETFDPgnirDLTDALIKAKKeaedEGDEDSGL 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      265 ----HeVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEI-----EEFPAQLNynnvmD--EMPFAERCAR 333
Cdd:cd11027 225 ltddH-LVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQ--AKLHAELddvigRDRLPTLS-----DrkRLPYLEATIA 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      334 ESIRRDPPLLMLM-RKVMADVKVGSYVVPKGDIIACSpLLS-HHDEEAFPEPRRWDPER--DEKVE-----GAFIGFGAG 404
Cdd:cd11027 297 EVLRLSSVVPLALpHKTTCDTTLRGYTIPKGTTVLVN-LWAlHHDPKEWDDPDEFRPERflDENGKlvpkpESFLPFSAG 375

                       330       340       350
                ....*....|....*....|....*....|....*....
2WV2_A      405 VHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPdPDY 443
Cdd:cd11027 376 RRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPP-PEL 413
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 211-448 1.93e-14

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: 74.92  E-value: 1.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      211 QSARCHEARTELQKILSEIIIARKEEEVNKDSSTSDLLSGLlsavyRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSM 290
Cdd:cd11065 173 KARELRELTRRLYEGPFEAAKERMASGTATPSFVKDLLEEL-----DKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFI 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      291 LHL-MHPanvkhlEALRK---EIEEF--PAQLNYNNVMDEMPFAERCARESIRRDPPLLM-LMRKVMADVKVGSYVVPKG 363
Cdd:cd11065 248 LAMaLHP------EVQKKaqeELDRVvgPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKG 321

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      364 DIIacspLLS----HHDEEAFPEPRRWDPER---DEKVEGA-----FIGFGAGVHKCIGQKFG----LLQVKTILATafr 427
Cdd:cd11065 322 TTV----IPNawaiHHDPEVYPDPEEFDPERyldDPKGTPDppdppHFAFGFGRRICPGRHLAenslFIAIARLLWA--- 394

                       250       260
                ....*....|....*....|....*.
2WV2_A      428 sYDFQLLRDE-----VPDPDYHTMVV 448
Cdd:cd11065 395 -FDIKKPKDEggkeiPDEPEFTDGLV 419
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 116-453 3.98e-14

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: 74.27  E-value: 3.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      116 LAEELTIAKFQNFVPAIQHEVRKFMAANW-DKDEG--EINLLEDCSTMIINTACQCLFGedlrKRLDARRFAQLLA---K 189
Cdd:cd11066  71 AASALNRPAVQSYAPIIDLESKSFIRELLrDSAEGkgDIDPLIYFQRFSLNLSLTLNYG----IRLDCVDDDSLLLeiiE 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      190 MESSL-------------IPaavfLPILLKLPLPQSARCHEARTELQKILSEIIIARKEEEVNKDSSTSdllsgLLSAVY 256
Cdd:cd11066 147 VESAIskfrstssnlqdyIP----ILRYFPKMSKFRERADEYRNRRDKYLKKLLAKLKEEIEDGTDKPC-----IVGNIL 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      257 RD-GTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANVKHLEALRKEIEE----FPAQlnYNNVMDEM--PFAE 329
Cdd:cd11066 218 KDkESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGQEIQEKAYEEILEaygnDEDA--WEDCAAEEkcPYVV 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      330 RCARESIRRDPPLLMLM-RKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER------DEKVEGAFIGFG 402
Cdd:cd11066 296 ALVKETLRYFTVLPLGLpRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERwldasgDLIPGPPHFSFG 375

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      403 AGVHKCIGQKFG-----LLQVKTILAtafrsydFQLLRDEVPDP---DYHTMVVGPTAS 453
Cdd:cd11066 376 AGSRMCAGSHLAnrelyTAICRLILL-------FRIGPKDEEEPmelDPFEYNACPTAL 427
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 225-440 4.11e-14

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 74.46  E-value: 4.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       225 ILSEIIIARKEEEVNKDSSTSDLLSGLLSAVYR-----DGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLmhpanV 299
Cdd:PLN02687 251 MMNGIIEEHKAAGQTGSEEHKDLLSTLLALKREqqadgEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAEL-----I 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       300 KHLEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLS 373
Cdd:PLN02687 326 RHPDILKKAQEELDAVVGRDRLVSEsdlpqLTYLQAVIKETFRLHPSTpLSLPRMAAEECEINGYHIPKGATLLVNVWAI 405

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A       374 HHDEEAFPEPRRWDPER--------DEKVEGA---FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPD 440
Cdd:PLN02687 406 ARDPEQWPDPLEFRPDRflpggehaGVDVKGSdfeLIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTPD 483
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 218-442 4.44e-14

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: 73.93  E-value: 4.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      218 ARTELQKILSEI--IIARKEEEVnkdsstSDLLSGLLSAvyrdgTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMH 295
Cdd:cd20646 194 GKKLIDKKMEEIeeRVDRGEPVE------GEYLTYLLSS-----GKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLAR 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      296 PANVKhlEALRKEI------EEFPAQLNYNnvmdEMPFAERCARESIRRDPPLLMLMRKVM-ADVKVGSYVVPKGDIIac 368
Cdd:cd20646 263 DPEIQ--ERLYQEVisvcpgDRIPTAEDIA----KMPLLKAVIKETLRLYPVVPGNARVIVeKEVVVGDYLFPKNTLF-- 334

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      369 spLLSH----HDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQllrdev 438
Cdd:cd20646 335 --HLCHyavsHDETNFPEPERFKPERWLRDGGlkhhpfGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVR------ 406


                ....
2WV2_A      439 PDPD 442
Cdd:cd20646 407 PDPS 410
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 214-440 1.10e-13

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: 72.74  E-value: 1.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHEARTE-LQKILSEiiiaRKEEevNKDSSTSDLLSGLLSAVYR--DGTPMSLHEVCG-------MIVAAMF-AGQHTS 282
Cdd:cd20673 175 QCVKIRDKlLQKKLEE----HKEK--FSSDSIRDLLDALLQAKMNaeNNNAGPDQDSVGlsddhilMTVGDIFgAGVETT 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      283 SITTTWSMLHLMHPANVKhlEALRKEIEEF-----PAQLNYNNvmdEMPFAERCARESIRRDP--PLLmLMRKVMADVKV 355
Cdd:cd20673 249 TTVLKWIIAFLLHNPEVQ--KKIQEEIDQNigfsrTPTLSDRN---HLPLLEATIREVLRIRPvaPLL-IPHVALQDSSI 322

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      356 GSYVVPKGD--IIACSPLlsHHDEEAFPEPRRWDPER--DE------KVEGAFIGFGAGVHKCIGQKFGLLQVKTILATA 425
Cdd:cd20673 323 GEFTIPKGTrvVINLWAL--HHDEKEWDQPDQFMPERflDPtgsqliSPSLSYLPFGAGPRVCLGEALARQELFLFMAWL 400

                       250
                ....*....|....*
2WV2_A      426 FRSYDFqllrdEVPD 440
Cdd:cd20673 401 LQRFDL-----EVPD 410
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 53-436 1.11e-13

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: 72.74  E-value: 1.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       53 IFTINIVGKRVTIVGDPHehsrffLPRnEVLSPR----EVYSFMVPVFGE----GVaYAAPYPRMREQLNFLAEELTIAK 124
Cdd:cd11083   3 AYRFRLGRQPVLVISDPE------LIR-EVLRRRpdefRRISSLESVFREmginGV-FSAEGDAWRRQRRLVMPAFSPKH 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      125 FQNFVPAIQHEVRKFMAAnWDK--DEGE-INLLEDCSTMIINTACQCLFGED----------LRKRLDaRRFAQLLAKME 191
Cdd:cd11083  75 LRYFFPTLRQITERLRER-WERaaAEGEaVDVHKDLMRYTVDVTTSLAFGYDlntlerggdpLQEHLE-RVFPMLNRRVN 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      192 SSlIPAAVFLPILlklplpQSARCHEARTELQKILSEIIiARKEEEVNKDSSTSD---LLSGLLSAVYRDGTPMSLHEVC 268
Cdd:cd11083 153 AP-FPYWRYLRLP------ADRALDRALVEVRALVLDII-AAARARLAANPALAEapeTLLAMMLAEDDPDARLTDDEIY 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      269 GMIVAAMFAGQHTSSITTTWsMLHLMHpANVKHLEALRKEIEEF--PAQLNYN-NVMDEMPFAERCARESIRRDP--PLL 343
Cdd:cd11083 225 ANVLTLLLAGEDTTANTLAW-MLYYLA-SRPDVQARVREEVDAVlgGARVPPLlEALDRLPYLEAVARETLRLKPvaPLL 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      344 MLmrKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEGA--------FIGFGAGVHKCIGQKFGL 415
Cdd:cd11083 303 FL--EPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAaephdpssLLPFGAGPRLCPGRSLAL 380

                       410       420
                ....*....|....*....|.
2WV2_A      416 LQVKTILATAFRSYDFQLLRD 436
Cdd:cd11083 381 MEMKLVFAMLCRNFDIELPEP 401
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 244-422 3.07e-13

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: 71.02  E-value: 3.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      244 TSDLLSGLLSAVyRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-HPAnvkHLEALRKEieefPAQLNynNVM 322
Cdd:cd11033 188 GDDLISVLANAE-VDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAeHPD---QWERLRAD----PSLLP--TAV 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      323 DEMpfaercaresIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIacspLLSH----HDEEAFPEPRRWDPERDEkveGAF 398
Cdd:cd11033 258 EEI----------LRWASPVIHFRRTATRDTELGGQRIRAGDKV----VLWYasanRDEEVFDDPDRFDITRSP---NPH 320

                       170       180
                ....*....|....*....|....
2WV2_A      399 IGFGAGVHKCIGQKFGLLQVKTIL 422
Cdd:cd11033 321 LAFGGGPHFCLGAHLARLELRVLF 344
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 263-438 4.01e-13

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: 70.75  E-value: 4.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      263 SLHEVCGMIVAAMFAGQHTSSITTTWsMLHLMHpanvKH---LEALRKE---------------IEEFPAQLNynnvmdE 324
Cdd:cd11051 182 ELERAIDQIKTFLFAGHDTTSSTLCW-AFYLLS----KHpevLAKVRAEhdevfgpdpsaaaelLREGPELLN------Q 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      325 MPFAERCARESIRRDPPLlMLMRKVMADVKV----GSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER---DEKVE-- 395
Cdd:cd11051 251 LPYTTAVIKETLRLFPPA-GTARRGPPGVGLtdrdGKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERwlvDEGHEly 329

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
2WV2_A      396 ---GAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEV 438
Cdd:cd11051 330 ppkSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFEKAYDEW 375
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 80-422 7.75e-13

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: 70.13  E-value: 7.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       80 NEVLSPREVYSFmVPVFGEGVayaapyprmreqlnflaeeltiakfQNFVPAIQHEVRKFMAANWDKDegeinLLEDCST 159
Cdd:cd20643  75 KEVLAPKVIDNF-VPLLNEVS-------------------------QDFVSRLHKRIKKSGSGKWTAD-----LSNDLFR 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      160 MIINTACQCLFGEDLRKRLD-----ARRFAQLLAKMESSLIPAAVFLPILLKLPLPQSARCHEARTELQKILSEIIIARK 234
Cdd:cd20643 124 FALESICNVLYGERLGLLQDyvnpeAQRFIDAITLMFHTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNI 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      235 EEEVNKDSSTSDLLSGLLSAVYRDGTpMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEI--EEF 312
Cdd:cd20643 204 YRDLRQKGKNEHEYPGILANLLLQDK-LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQ--EMLRAEVlaARQ 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      313 PAQLNYNNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDE 392
Cdd:cd20643 281 EAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWL 360

                       330       340       350
                ....*....|....*....|....*....|...
2WV2_A      393 KVEGAF---IGFGAGVHKCIGQKFGLLQVKTIL 422
Cdd:cd20643 361 SKDITHfrnLGFGFGPRQCLGRRIAETEMQLFL 393
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 110-433 9.62e-13

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: 69.86  E-value: 9.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      110 REQLNFLAEELTIAKFQNFVPAIQHEVRKFMAAnWDKDEGEINLLEDCSTMIINTACQCLFG---EDLRKRLDARRFAQL 186
Cdd:cd20636  81 RQRRKVLARVFSRAALESYLPRIQDVVRSEVRG-WCRGPGPVAVYTAAKSLTFRIAVRILLGlrlEEQQFTYLAKTFEQL 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      187 LAKMESslIPAAV-FLPILLKLplpqsarchEARTELQKILSEIIiaRKEEEVNKDSSTSDLLSGLLSAVYRDGTPMSLH 265
Cdd:cd20636 160 VENLFS--LPLDVpFSGLRKGI---------KARDILHEYMEKAI--EEKLQRQQAAEYCDALDYMIHSARENGKELTMQ 226

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      266 EVCGMIVAAMFAGQHTS-SITTTWSMLHLMHPANvkhLEALRKEIEE---------FPAQLNYNNvMDEMPFAERCARES 335
Cdd:cd20636 227 ELKESAVELIFAAFSTTaSASTSLVLLLLQHPSA---IEKIRQELVShglidqcqcCPGALSLEK-LSRLRYLDCVVKEV 302

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      336 IRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAF--PE---PRRWDPERDEKVEGAF--IGFGAGVHKC 408
Cdd:cd20636 303 LRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYqnPEgfdPDRFGVEREESKSGRFnyIPFGGGVRSC 382

                       330       340
                ....*....|....*....|....*
2WV2_A      409 IGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd20636 383 IGKELAQVILKTLAVELVTTARWEL 407
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 217-451 9.93e-13

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 69.17  E-value: 9.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIIARKEeevnkdSSTSDLLSGLLSAvYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-H 295
Cdd:cd11032 156 EALRELNAYLLEHLEERRR------NPRDDLISRLVEA-EVDGERLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDeD 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      296 PanvKHLEALRKEIEEFPAQLNynnvmdempfaercarESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHH 375
Cdd:cd11032 229 P---EVAARLRADPSLIPGAIE----------------EVLRYRPPVQRTARVTTEDVELGGVTIPAGQLVIAWLASANR 289

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A      376 DEEAFPEPRRWDPERDEKvegAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDfQLLRDEVPDPDYH--TMVVGPT 451
Cdd:cd11032 290 DERQFEDPDTFDIDRNPN---PHLSFGHGIHFCLGAPLARLEARIALEALLDRFP-RIRVDPDVPLELIdsPVVFGVR 363
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 222-440 1.20e-12

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: 69.37  E-value: 1.20e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      222 LQKILSEIIIARKEEEVNKDSSTSDLLSGLLSAvyrDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMhpanvKH 301
Cdd:cd20657 187 LTKILEEHKATAQERKGKPDFLDFVLLENDDNG---EGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELI-----RH 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      302 LEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHH 375
Cdd:cd20657 259 PDILKKAQEEMDQVIGRDRRLLEsdipnLPYLQAICKETFRLHPSTpLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGR 338

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2WV2_A      376 DEEAFPEPRRWDPER-------DEKVEGA---FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPD 440
Cdd:cd20657 339 DPDVWENPLEFKPERflpgrnaKVDVRGNdfeLIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPAGQTPE 413
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 251-437 1.77e-12

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: 69.07  E-value: 1.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      251 LLSAVYRDGTpMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEE--FPAQLNYNNVMDEMPFA 328
Cdd:cd20645 212 FLCDIYHDNE-LSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQ--QKLLQEIQSvlPANQTPRAEDLKNMPYL 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      329 ERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER---DEKVEGAF--IGFGA 403
Cdd:cd20645 289 KACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERwlqEKHSINPFahVPFGI 368

                       170       180       190
                ....*....|....*....|....*....|....
2WV2_A      404 GVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDE 437
Cdd:cd20645 369 GKRMCIGRRLAELQLQLALCWIIQKYQIVATDNE 402
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 269-410 1.93e-12

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: 68.79  E-value: 1.93e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      269 GMIVAAMFAGQHTSSITTTWSMLHLmhpanVKHLEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPPL- 342
Cdd:cd20653 230 GLILVMLLAGTDTSAVTLEWAMSNL-----LNHPEVLKKAREEIDTQVGQDRLIEEsdlpkLPYLQNIISETLRLYPAAp 304

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2WV2_A      343 LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVE---GAFIGFGAGVHKCIG 410
Cdd:cd20653 305 LLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEregYKLIPFGLGRRACPG 375
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 221-443 2.44e-12

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: 68.48  E-value: 2.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      221 ELQKILSEIIIARKEEEVN--KDSSTSDLLSGLLSAVyrDGTPMSLHEVCGM----IVAAMF----AGQHTSSITTTWSM 290
Cdd:cd11028 178 ELLNRLNSFILKKVKEHLDtyDKGHIRDITDALIKAS--EEKPEEEKPEVGLtdehIISTVQdlfgAGFDTISTTLQWSL 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      291 LHLMHpaNVKHLEALRKEIEEFPAQLNYNNVMD--EMPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIA 367
Cdd:cd11028 256 LYMIR--YPEIQEKVQAELDRVIGRERLPRLSDrpNLPYTEAFILETMRHSSFVpFTIPHATTRDTTLNGYFIPKGTVVF 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      368 CSPLLSHHDEEAFPEPRRWDPER--------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVP 439
Cdd:cd11028 334 VNLWSVNHDEKLWPDPSVFRPERflddngllDKTKVDKFLPFGAGRRRCLGEELARMELFLFFATLLQQCEFSVKPGEKL 413


                ....
2WV2_A      440 DPDY 443
Cdd:cd11028 414 DLTP 417
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 226-432 2.66e-12

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: 68.41  E-value: 2.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      226 LSEIIIARKEEEVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLmhpanVKHLEAL 305
Cdd:cd20647 197 FSQIHVDNRLREIQKQMDRGEEVKGGLLTYLLVSKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLL-----ARHPEVQ 271

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      306 RKEIEEFPAQLNYNNV-----MDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAF 380
Cdd:cd20647 272 QQVYEEIVRNLGKRVVptaedVPKLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENF 351

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      381 PEPRRWDPER------DEKVEG-AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQ 432
Cdd:cd20647 352 PRAEEFRPERwlrkdaLDRVDNfGSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIK 410
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 216-430 4.03e-12

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: 67.97  E-value: 4.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      216 HEARTELQKILSEII---IARKEEEVNKDSSTSDLLSGLLSAVYRDgtpmsLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd11063 168 REACKVVHRFVDPYVdkaLARKEESKDEESSDRYVFLDELAKETRD-----PKELRDQLLNILLAGRDTTASLLSFLFYE 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LMHPANVkhLEALRKEI-EEFPA----------QLNY-NNVMDE-------MPFAERCAResirRD------------PP 341
Cdd:cd11063 243 LARHPEV--WAKLREEVlSLFGPeptptyedlkNMKYlRAVINEtlrlyppVPLNSRVAV----RDttlprgggpdgkSP 316

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      342 LLmlmrkvmadvkvgsyvVPKGDIIACSPLLSHHDEEAF-PEPRRWDPER--DEKVEG-AFIGFGAGVHKCIGQKFGLLQ 417
Cdd:cd11063 317 IF----------------VPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERweDLKRPGwEYLPFNGGPRICLGQQFALTE 380

                       250
                ....*....|...
2WV2_A      418 VKTILATAFRSYD 430
Cdd:cd11063 381 ASYVLVRLLQTFD 393
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 217-433 6.50e-12

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: 67.05  E-value: 6.50e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIIARKEEEV--NKDSSTSDLLSGLLSAVYR--DGTPMS-------LHEVcgmiVAAMF-AGQHTSSI 284
Cdd:cd20652 177 QGQAKTHAIYQKIIDEHKRRLKpeNPRDAEDFELCELEKAKKEgeDRDLFDgfytdeqLHHL----LADLFgAGVDTTIT 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      285 TTTWSMLHLMHpaNVKHLEALRKEIEEFPAQLNYNNV--MDEMPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVP 361
Cdd:cd20652 253 TLRWFLLYMAL--FPKEQRRIQRELDEVVGRPDLVTLedLSSLPYLQACISESQRIRSVVpLGIPHGCTEDAVLAGYRIP 330

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A      362 KGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd20652 331 KGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGkylkpeAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIAL 408
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 229-451 8.22e-12

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: 66.76  E-value: 8.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      229 IIIARKEEEVNK-------DSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPanvK 300
Cdd:cd20638 186 LIHAKIEENIRAkiqredtEQQCKDALQLLIEHSRRNGEPLNLQALKESATELLFGGHETTASAATSLIMFLgLHP---E 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      301 HLEALRKEIEE------FPAQLNYNN--VMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLL 372
Cdd:cd20638 263 VLQKVRKELQEkgllstKPNENKELSmeVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICD 342

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      373 SHHDEEAFPEPRRWDPER------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEvPdpdyhTM 446
Cdd:cd20638 343 THDVADIFPNKDEFNPDRfmsplpEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNGP-P-----TM 416


                ....*
2WV2_A      447 VVGPT 451
Cdd:cd20638 417 KTSPT 421
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 216-423 9.28e-12

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: 66.74  E-value: 9.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      216 HEARtelQKILSEIIIARKEEEVNKDSSTSDLLSGLLSavYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLmh 295
Cdd:cd20656 185 HGAR---RDRLTKAIMEEHTLARQKSGGGQQHFVALLT--LKEQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEM-- 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      296 panVKHLEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACS 369
Cdd:cd20656 258 ---IRNPRVQEKAQEELDRVVGSDRVMTEadfpqLPYLQCVVKEALRLHPPTpLMLPHKASENVKIGGYDIPKGANVHVN 334

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
2WV2_A      370 PLLSHHDEEAFPEPRRWDPER----DEKVEGA---FIGFGAGVHKCIGQKFGLLQVKTILA 423
Cdd:cd20656 335 VWAIARDPAVWKNPLEFRPERfleeDVDIKGHdfrLLPFGAGRRVCPGAQLGINLVTLMLG 395
PLN02966 PLN02966
cytochrome P450 83A1
 19-440 1.47e-11

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 66.31  E-value: 1.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        19 PVYPVTVPILGHIIQFGK-SPLGFMQECKRqlKSGIFTINIVGKRVTIVGDPHEHSRFFLPRNEV----LSPREVYSFMV 93
Cdd:PLN02966  31 PPGPSPLPVIGNLLQLQKlNPQRFFAGWAK--KYGPILSYRIGSRTMVVISSAELAKELLKTQDVnfadRPPHRGHEFIS 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        94 pvFGE---GVAYAAPYPRMREQLNfLAEELTIAKFQNFVPAIQHEVRKFM-AANWDKDEGEI-NLLEDCSTMIINTACQC 168
Cdd:PLN02966 109 --YGRrdmALNHYTPYYREIRKMG-MNHLFSPTRVATFKHVREEEARRMMdKINKAADKSEVvDISELMLTFTNSVVCRQ 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       169 LFGEDLRKR-LDARRFAQLLAKMESSL--------IPAAVFLPILLKLPLPQSARCHEARTELQKILSEIIIARKEEEvn 239
Cdd:PLN02966 186 AFGKKYNEDgEEMKRFIKILYGTQSVLgkiffsdfFPYCGFLDDLSGLTAYMKECFERQDTYIQEVVNETLDPKRVKP-- 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       240 KDSSTSDLLSGllsaVYRD---GTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-HPANVKHLEA-LRKEIEEFPA 314
Cdd:PLN02966 264 ETESMIDLLME----IYKEqpfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMkYPQVLKKAQAeVREYMKEKGS 339

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       315 QLNYNNVMDEMPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAF-PEPRRWDPER-- 390
Cdd:PLN02966 340 TFVTEDDVKNLPYFRALVKETLRIEPVIpLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERfl 419

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
2WV2_A       391 ----DEK-VEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPD 440
Cdd:PLN02966 420 ekevDFKgTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPD 474
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 334-411 1.50e-11

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 65.68  E-value: 1.50e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A      334 ESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDekvEGAFIGFGAGVHKCIGQ 411
Cdd:cd11037 252 EAVRLESPVQTFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITRN---PSGHVGFGHGVHACVGQ 326
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 226-437 1.95e-11

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: 65.70  E-value: 1.95e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      226 LSEIIIARKEEEVNKDSSTS--DLLSGLLsAVYRDGTP---MSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-HPaNV 299
Cdd:cd20655 184 LLERIIKEHEEKRKKRKEGGskDLLDILL-DAYEDENAeykITRNHIKAFILDLFIAGTDTSAATTEWAMAELInNP-EV 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      300 khLEALRKEIEefpAQLNYNNVMDE-----MPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSH 374
Cdd:cd20655 262 --LEKAREEID---SVVGKTRLVQEsdlpnLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIM 336

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2WV2_A      375 HDEEAFPEPRRWDPER---------DEKVEGA---FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDE 437
Cdd:cd20655 337 RDPNYWEDPLEFKPERflassrsgqELDVRGQhfkLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGE 411
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 221-431 2.23e-11

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: 65.72  E-value: 2.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      221 ELQKILSEII---IARKEEEVNKDSSTSDLLSGLLSAVyrDGTPMSLHE----VCGMIVAAMFAGQHTSSITTTWSM-LH 292
Cdd:cd20654 191 ELDSILEEWLeehRQKRSSSGKSKNDEDDDDVMMLSIL--EDSQISGYDadtvIKATCLELILGGSDTTAVTLTWALsLL 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LMHPanvkhlEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPP-LLMLMRKVMADVKVGSYVVPKGdii 366
Cdd:cd20654 269 LNNP------HVLKKAQEELDTHVGKDRWVEEsdiknLVYLQAIVKETLRLYPPgPLLGPREATEDCTVGGYHVPKG--- 339

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      367 acSPLLS-----HHDEEAFPEPRRWDPER------DEKVEGA---FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDF 431
Cdd:cd20654 340 --TRLLVnvwkiQRDPNVWSDPLEFKPERfltthkDIDVRGQnfeLIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDI 416
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 41-459 2.50e-11

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 65.40  E-value: 2.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       41 FMQECkrQLKSG-IFTINIVGKRVTIVGDP---------HEHSRFFLPRNEVLSPrevysfmvpVFGEGVAYAAPYPRMR 110
Cdd:cd20632   1 FLLAL--QKKHGdVFTVLIAGKYITFIMDPflypyvikhGKQLDFHEFSDRLASK---------TFGYPPLRSPKFPGLN 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      111 EQL----NFLAEELTIAKFQNFVPAIQHEVR-KFM-AANWDKDEgeinLLEDCSTMIINTACQCLFG-----------ED 173
Cdd:cd20632  70 EQIhrsyQYLQGENLDILTESMMGNLQLVLRqQFLgETDWETEE----LYEFCSRIMFEATFLTLYGkppdddrhkviSE 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      174 LRKRLDA--RRFAQLLAKMESSLIPAAvflpillklplpqsarcHEARTELQKIL-----------SEIIIARKE--EEV 238
Cdd:cd20632 146 LRKKFRKfdAMFPYLVANIPIELLGAT-----------------KSIREKLIKYFlpqkmakwsnpSEVIQARQEllEQY 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      239 nkdsstsDLLSGLLSAVYRDGTpmsLHEVCGMIVAAMFagqhtssitttWSMLHL-MHPANvkhLEALRKEIE------- 310
Cdd:cd20632 209 -------DVLQDYDKAAHHFAF---LWASVGNTIPATF-----------WAMYYLlRHPEA---LAAVRDEIDhvlqstg 264

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      311 -----EFPAQLNyNNVMDEMPFAERCARESIRrdpplL----MLMRKVMADVKV-----GSYVVPKGDIIACSPLLSHHD 376
Cdd:cd20632 265 qelgpDFDIHLT-REQLDSLVYLESAINESLR-----LssasMNIRVVQEDFTLklesdGSVNLRKGDIVALYPQSLHMD 338

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      377 EEAFPEPRRWDPER---DEKVEGAF-----------IGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVP-DP 441
Cdd:cd20632 339 PEIYEDPEVFKFDRfveDGKKKTTFykrgqklkyylMPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDLELLEEQKPpGL 418

                       490       500
                ....*....|....*....|
2WV2_A      442 DYHTMVVG--PTASQCRVKY 459
Cdd:cd20632 419 DNSRAGLGilPPNSDVRFRY 438
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 120-433 2.61e-11

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: 65.18  E-value: 2.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      120 LTIAKFQNFVPAIQHEVRKFMAANWDK--DEGEINLLEDCSTMIINTACQCLFGEDLRKrLDARRFAQLLAKME------ 191
Cdd:cd11072  75 LSAKRVQSFRSIREEEVSLLVKKIRESasSSSPVNLSELLFSLTNDIVCRAAFGRKYEG-KDQDKFKELVKEALellggf 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      192 --SSLIPAAVFLPILLKlplpQSARCHEARTELQKILSEIIIARKEEEVNKDSStSDLLSGLLSAVYRDGT---PMSLHE 266
Cdd:cd11072 154 svGDYFPSLGWIDLLTG----LDRKLEKVFKELDAFLEKIIDEHLDKKRSKDED-DDDDDLLDLRLQKEGDlefPLTRDN 228

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      267 VCGMIVAAMFAGQHTSSITTTWSMLHLM-HPANVKHLEA-LR------KEIEEfpaqlnynNVMDEMPFAERCARESIRR 338
Cdd:cd11072 229 IKAIILDMFLAGTDTSATTLEWAMTELIrNPRVMKKAQEeVRevvggkGKVTE--------EDLEKLKYLKAVIKETLRL 300

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      339 DPPL-LMLMRKVMADVKVGSYVVPKGDII-----ACspllsHHDEEAFPEPRRWDPERDEKVEGAFIG-------FGAGV 405
Cdd:cd11072 301 HPPApLLLPRECREDCKINGYDIPAKTRVivnawAI-----GRDPKYWEDPEEFRPERFLDSSIDFKGqdfelipFGAGR 375

                       330       340
                ....*....|....*....|....*...
2WV2_A      406 HKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd11072 376 RICPGITFGLANVELALANLLYHFDWKL 403
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 216-437 1.21e-10

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: 63.15  E-value: 1.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      216 HEARTELQKILsEIIIARKEEEVN---KDSSTSDLLSGLLSAVYRDgtPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd20616 174 EKAVKDLKDAI-EILIEQKRRRIStaeKLEDHMDFATELIFAQKRG--ELTAENVNQCVLEMLIAAPDTMSVSLFFMLLL 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LMHPANVKhlEALRKEIEEFPAQLNY-NNVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKG-DIIAcsP 370
Cdd:cd20616 251 IAQHPEVE--EAILKEIQTVLGERDIqNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKGtNIIL--N 326

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      371 LLSHHDEEAFPEPRRWDPERDEKV--EGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDE 437
Cdd:cd20616 327 IGRMHRLEFFPKPNEFTLENFEKNvpSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGR 395
PLN02774 PLN02774
brassinosteroid-6-oxidase
 26-422 1.50e-10

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 63.26  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        26 PILGHIIQFGKSPLGFMQecKRQLKSG-IFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPREVYSfMVPVFGE---GVA 101
Cdd:PLN02774  40 PLFGETTEFLKQGPDFMK--NQRLRYGsFFKSHILGCPTIVSMDPELNRYILMNEGKGLVPGYPQS-MLDILGTcniAAV 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       102 YAAPYPRMREQLNFLAEELTIAkfQNFVPAIQHEVRKFMAaNWDKDEgEINLLEDCSTMIINTACQCLFGEDLRKRLDA- 180
Cdd:PLN02774 117 HGSTHRYMRGSLLSLISPTMIR--DHLLPKIDEFMRSHLS-GWDGLK-TIDIQEKTKEMALLSALKQIAGTLSKPISEEf 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       181 -RRFAQLLAKMESSLI--PAAVFLpillklplpqsaRCHEARTELQKILSEIIIARKEEEVNKDsstsDLLSGLLSavyR 257
Cdd:PLN02774 193 kTEFFKLVLGTLSLPIdlPGTNYR------------SGVQARKNIVRMLRQLIQERRASGETHT----DMLGYLMR---K 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       258 DGT--PMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLM-HPanvKHLEALRKE---IEEFPAQ---LNYNNVmDEMPFA 328
Cdd:PLN02774 254 EGNryKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHdHP---KALQELRKEhlaIRERKRPedpIDWNDY-KSMRFT 329

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       329 ERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--DEKVEGA--FIGFGAG 404
Cdd:PLN02774 330 RAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRwlDKSLESHnyFFLFGGG 409

                        410
                 ....*....|....*...
2WV2_A       405 VHKCIGQKFGLLQVKTIL 422
Cdd:PLN02774 410 TRLCPGKELGIVEISTFL 427
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 14-440 1.58e-10

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 63.30  E-value: 1.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        14 RPTDPPVYPVTVPILGHIIQFGKSPLGFMQE-CKrqlKSGIFTINIVGKRVTIVGDPHEHSRFFLPR-NEVLSPREVYSF 91
Cdd:PLN03112  29 KSLRLPPGPPRWPIVGNLLQLGPLPHRDLASlCK---KYGPLVYLRLGSVDAITTDDPELIREILLRqDDVFASRPRTLA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        92 MVPV-FGEGVAYAAPY----PRMR----EQLnflaeeLTIAKFQNFVPAIQHEVRKFMAANWDKDE-GE-INLLEDCSTM 160
Cdd:PLN03112 106 AVHLaYGCGDVALAPLgphwKRMRricmEHL------LTTKRLESFAKHRAEEARHLIQDVWEAAQtGKpVNLREVLGAF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       161 IINTACQCL-----FGEDLRKRLDARRFAQLLAKMESSL--------IPAAVFLPILLKLPLPQSARcHEARTELQKILS 227
Cdd:PLN03112 180 SMNNVTRMLlgkqyFGAESAGPKEAMEFMHITHELFRLLgviylgdyLPAWRWLDPYGCEKKMREVE-KRVDEFHDKIID 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       228 EIIIARKEEEvnKDSSTSDLLSGLLSAVYRDGTP-MSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLmhpanVKHLEALR 306
Cdd:PLN03112 259 EHRRARSGKL--PGGKDMDFVDVLLSLPGENGKEhMDDVEIKALMQDMIAAATDTSAVTNEWAMAEV-----IKNPRVLR 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       307 KEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDP--PLLmLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEA 379
Cdd:PLN03112 332 KIQEELDSVVGRNRMVQEsdlvhLNYLRCVVRETFRMHPagPFL-IPHESLRATTINGYYIPAKTRVFINTHGLGRNTKI 410

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
2WV2_A       380 FPEPRRWDPERDEKVEGA-----------FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPD 440
Cdd:PLN03112 411 WDDVEEFRPERHWPAEGSrveishgpdfkILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGLRPE 482
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 231-423 2.04e-10

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: 62.46  E-value: 2.04e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      231 IARKEEEVNKDSSTSDLLSG--LLSAVYRDGTPMSlhEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANVKhlEALRKE 308
Cdd:cd20648 199 IDRRMAEVAAKLPRGEAIEGkyLTYFLAREKLPMK--SIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQ--TALHRE 274

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      309 IEEF--PAQLNYNNVMDEMPFAERCARESIRRDPPLLMLMRKVM-ADVKVGSYVVPKGDIIACSPLLSHHDEEAFPE--- 382
Cdd:cd20648 275 ITAAlkDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPdRDIQVGEYIIPKKTLITLCHYATSRDENQFPDpns 354

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
2WV2_A      383 --PRRWDPERDEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILA 423
Cdd:cd20648 355 frPERWLGKGDTHHPYASLPFGFGKRSCIGRRIAELEVYLALA 397
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 238-434 2.10e-10

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: 62.60  E-value: 2.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      238 VNKDSSTSDLLSGLLSAvYRDGTPMSLHEvcgMIVAA---MFAGQHTSSITTTWSMLHLMHPANVkhLEALRKEI-EEFP 313
Cdd:cd11058 190 LAKGTDRPDFMSYILRN-KDEKKGLTREE---LEANAsllIIAGSETTATALSGLTYYLLKNPEV--LRKLVDEIrSAFS 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      314 A--QLNYNNVmDEMPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYV-VPKGDIIACSPLLSHHDEEAFPEPRRWDPE 389
Cdd:cd11058 264 SedDITLDSL-AQLPYLNAVIQEALRLYPPVpAGLPRVVPAGGATIDGQfVPGGTSVSVSQWAAYRSPRNFHDPDEFIPE 342

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
2WV2_A      390 R---DEKVE------GAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLL 434
Cdd:cd11058 343 RwlgDPRFEfdndkkEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELD 396
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 212-441 2.27e-10

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: 62.13  E-value: 2.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      212 SARCHEARTELQKILSEIIIARKEeevNKDSStsdllsgLLSAVYRDGTPMSLHEVCGMIVAAMFAGQHT---SSITTTW 288
Cdd:cd11039 158 EARCDEATAGIDAAIDALIPVHRS---NPNPS-------LLSVMLNAGMPMSLEQIRANIKVAIGGGLNEprdAIAGTCW 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      289 SMLhlMHPAnvkhlealrkEIEEfpaqlnynnVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIAC 368
Cdd:cd11039 228 GLL--SNPE----------QLAE---------VMAGDVHWLRAFEEGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFL 286

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
2WV2_A      369 SPLLSHHDEEAFPEPRRWDPERDEKvegAFIGFGAGVHKCIGQKFGLLQVKTI-LATAFRsydfQLLRDEVPDP 441
Cdd:cd11039 287 MFGSANRDEARFENPDRFDVFRPKS---PHVSFGAGPHFCAGAWASRQMVGEIaLPELFR----RLPNLIRLDP 353
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 275-441 4.36e-10

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 61.61  E-value: 4.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      275 MFAGQHTSSITTTWSMLHLM-HPanvKHLEALRKEIEEF------------PAQLNYNNVMDEMPFAERCARESIR-RDP 340
Cdd:cd20633 233 LWASQGNTGPASFWLLLYLLkHP---EAMKAVREEVEQVlketgqevkpggPLINLTRDMLLKTPVLDSAVEETLRlTAA 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      341 PLLMlmRKVMADVKV-----GSYVVPKGDIIACSPLLSHH-DEEAFPEP------RRWDPERDEKVEGAFIG-------- 400
Cdd:cd20633 310 PVLI--RAVVQDMTLkmangREYALRKGDRLALFPYLAVQmDPEIHPEPhtfkydRFLNPDGGKKKDFYKNGkklkyynm 387

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
2WV2_A      401 -FGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDP 441
Cdd:cd20633 388 pWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLELVNPDEEIP 429
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 293-427 1.16e-09

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 60.05  E-value: 1.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LMHPANVKHLEA---LRKEIEEFPAQLnynnvmdempfaERCARESIRRDPPLLMLMRKVMADVKVGSYV-----VPKGD 364
Cdd:cd20612 214 YLRRPGAAHLAEiqaLARENDEADATL------------RGYVLEALRLNPIAPGLYRRATTDTTVADGGgrtvsIKAGD 281

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
2WV2_A      365 IIACSPLLSHHDEEAFPEPRRWDPERDEKvegAFIGFGAGVHKCIGQKFgllqVKTILATAFR 427
Cdd:cd20612 282 RVFVSLASAMRDPRAFPDPERFRLDRPLE---SYIHFGHGPHQCLGEEI----ARAALTEMLR 337
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 125-433 2.01e-09

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: 59.48  E-value: 2.01e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      125 FQNFVPAIQHEVRKFMAAnWDKDEGEINLLEDCSTMIINTACQCLFG-----EDLRKRLDArrFAQLLAKMESslIPAAV 199
Cdd:cd20637  95 LESYLPKIQQVIQDTLRV-WSSNPEPINVYQEAQKLTFRMAIRVLLGfrvseEELSHLFSV--FQQFVENVFS--LPLDL 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      200 flpillklPLPQSARCHEARTELQKILSEIIiaRKEEEVNKDSSTSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAMFAG- 278
Cdd:cd20637 170 --------PFSGYRRGIRARDSLQKSLEKAI--REKLQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAf 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      279 QHTSSITTTWSMLHLMHPANvkhLEALRKEI-------EEFPAQLNYN-NVMDEMPFAERCARESIRRDPPLLMLMRKVM 350
Cdd:cd20637 240 ATTASASTSLIMQLLKHPGV---LEKLREELrsngilhNGCLCEGTLRlDTISSLKYLDCVIKEVLRLFTPVSGGYRTAL 316

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      351 ADVKVGSYVVPKGDIIACSPLLSH------HDEEAFpEPRRWDPERDEKVEGAF--IGFGAGVHKCIGQKFGLLQVKTIL 422
Cdd:cd20637 317 QTFELDGFQIPKGWSVLYSIRDTHdtapvfKDVDAF-DPDRFGQERSEDKDGRFhyLPFGGGVRTCLGKQLAKLFLKVLA 395

                       330
                ....*....|.
2WV2_A      423 ATAFRSYDFQL 433
Cdd:cd20637 396 VELASTSRFEL 406
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 216-442 2.23e-09

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: 59.62  E-value: 2.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      216 HEARTELQKILS-EIIIARKEeevnkdsstsDLLSGLLSAVYRDgtpmslhEVCGMIVAamfaGQHTSSITTTWSMLHLM 294
Cdd:cd20622 232 GEVRSAVDHMVRrELAAAEKE----------GRKPDYYSQVIHD-------ELFGYLIA----GHDTTSTALSWGLKYLT 290

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      295 HPANVKhlEALRKEIEE-FPAQLNYNNV--MDEM-----PFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDII 366
Cdd:cd20622 291 ANQDVQ--SKLRKALYSaHPEAVAEGRLptAQEIaqariPYLDAVIEEILRCANTAPILSREATVDTQVLGYSIPKGTNV 368

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      367 AC--------SPLLSH---------------------HDEEAFpEPRRW---DPERDEKV----EGAFIGFGAGVHKCIG 410
Cdd:cd20622 369 FLlnngpsylSPPIEIdesrrssssaakgkkagvwdsKDIADF-DPERWlvtDEETGETVfdpsAGPTLAFGLGPRGCFG 447

                       250       260       270
                ....*....|....*....|....*....|..
2WV2_A      411 QKFGLLQVKTILATAFRSYDFQLLRDEVPDPD 442
Cdd:cd20622 448 RRLAYLEMRLIITLLVWNFELLPLPEALSGYE 479
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 213-410 2.68e-09

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: 58.92  E-value: 2.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      213 ARCHEARTELQKILSEIIIARKEEEvnkdssTSDLLSGLLSAvYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLH 292
Cdd:cd11038 168 PRIEAAVEELYDYADALIEARRAEP------GDDLISTLVAA-EQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLT 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      293 LM-HPAnvkHLEALRkeieEFPAqlnynnvmdempFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPL 371
Cdd:cd11038 241 FAeHPD---QWRALR----EDPE------------LAPAAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSH 301

                       170       180       190
                ....*....|....*....|....*....|....*....
2WV2_A      372 LSHHDEEAFPEPrRWDPERDEKvegAFIGFGAGVHKCIG 410
Cdd:cd11038 302 AANRDPRVFDAD-RFDITAKRA---PHLGFGGGVHHCLG 336
PLN02738 PLN02738
carotene beta-ring hydroxylase
 275-439 3.80e-09

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 58.77  E-value: 3.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       275 MFAGQHTSSITTTWSMLHLMHPANVkhLEALRKEIEE-----FPAQLNynnvMDEMPFAERCARESIRRDPPLLMLMRKV 349
Cdd:PLN02738 400 LIAGHETSAAVLTWTFYLLSKEPSV--VAKLQEEVDSvlgdrFPTIED----MKKLKYTTRVINESLRLYPQPPVLIRRS 473

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       350 MADVKVGSYVVPKGDIIACSPLLSHH------DEEAFpEPRRW---DPERDEKVEG-AFIGFGAGVHKCIGQKFGLLQVK 419
Cdd:PLN02738 474 LENDMLGGYPIKRGEDIFISVWNLHRspkhwdDAEKF-NPERWpldGPNPNETNQNfSYLPFGGGPRKCVGDMFASFENV 552

                        170       180
                 ....*....|....*....|
2WV2_A       420 TILATAFRSYDFQLLRDEVP 439
Cdd:PLN02738 553 VATAMLVRRFDFQLAPGAPP 572
PLN02655 PLN02655
ent-kaurene oxidase
 281-425 3.81e-09

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 58.60  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       281 TSSITTTWSMLHLMHPANVKhlEALRKEIEEFPAQlnyNNVMDE----MPFAERCARESIRRDPPL-LMLMRKVMADVKV 355
Cdd:PLN02655 277 TTLVTTEWAMYELAKNPDKQ--ERLYREIREVCGD---ERVTEEdlpnLPYLNAVFHETLRKYSPVpLLPPRFVHEDTTL 351

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
2WV2_A       356 GSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--DEKVEGA----FIGFGAGVHKCIgqkfGLLQVKTILATA 425
Cdd:PLN02655 352 GGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERflGEKYESAdmykTMAFGAGKRVCA----GSLQAMLIACMA 423
PLN02183 PLN02183
ferulate 5-hydroxylase
 212-415 4.01e-09

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 58.71  E-value: 4.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       212 SARCHEARTELQKILSEII---IARKEEEVNKDSST---SDLLSGLLsAVYRDGTPMSLHE------------VCGMIVA 273
Cdd:PLN02183 233 NKRLVKARKSLDGFIDDIIddhIQKRKNQNADNDSEeaeTDMVDDLL-AFYSEEAKVNESDdlqnsikltrdnIKAIIMD 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       274 AMFAGQHTSSITTTWSMLHLMH-PANVKHLE-------ALRKEIEEfpaqlnynNVMDEMPFAERCARESIRRDPPLLML 345
Cdd:PLN02183 312 VMFGGTETVASAIEWAMAELMKsPEDLKRVQqeladvvGLNRRVEE--------SDLEKLTYLKCTLKETLRLHPPIPLL 383

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A       346 MRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--DEKV---EGA---FIGFGAGVHKCIGQKFGL 415
Cdd:PLN02183 384 LHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRflKPGVpdfKGShfeFIPFGSGRRSCPGMQLGL 461
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 41-441 1.32e-08

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: 57.00  E-value: 1.32e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       41 FMQEckRQLKSG-IFTINIVGKRVTIVGDPHEHSRFfLPRNEVLSPREV-YSFMVPVFG-------EGVAYAAPYPRMRE 111
Cdd:cd20631   1 FLRS--RQKKYGhIFTCKIAGKYVHFITDPFSYHSV-IRHGKHLDWKKFhFATSAKAFGhvsfdpsDGNTTENIHDTFIK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      112 QLNFLA-EELTIAKFQNfvpaIQHEVRKFMAANWDKDEGEI-NLLEDCSTMIINTACQCLFGEDLR------KRLDARRF 183
Cdd:cd20631  78 TLQGSAlDSLTESMMEN----LQYVMLQDKSSSSSTKAWVTeGLYSFCYRVMFEAGYLTLFGKELTaredknARLEAQRA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      184 AQLLAkMES-----SLIPAAVFLPILLKLPLPQSAR-------CHEARTElQKILSEIIIARkeEEVNKDSSTsdllsgl 251
Cdd:cd20631 154 LILNA-LENfkefdKVFPALVAGLPIHMFKTAKSARealaerlLHENLQK-RENISELISLR--MLLNDTLST------- 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      252 lsavyrdgtpMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHpaNVKHLEALRKEIEEF-------------PAQLNY 318
Cdd:cd20631 223 ----------LDEMEKARTHVAMLWASQANTLPATFWSLFYLLR--CPEAMKAATKEVKRTlektgqkvsdggnPIVLTR 290

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      319 NNvMDEMPFAERCARESIRRDPPLLMLmRKVMADVKV-----GSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--D 391
Cdd:cd20631 291 EQ-LDDMPVLGSIIKEALRLSSASLNI-RVAKEDFTLhldsgESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRylD 368

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
2WV2_A      392 E-------------KVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDP 441
Cdd:cd20631 369 EngkekttfykngrKLKYYYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYFDMELLDGNAKCP 431
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 276-411 1.84e-08

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: 56.50  E-value: 1.84e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      276 FAGQHTSSITTTWSMLHLM-HPanvkHLEA-LRKEIEEFPAQLNYNNVMD--EMPFAERCAREsIRRDPPLL--MLMRKV 349
Cdd:cd20665 236 GAGTETTSTTLRYGLLLLLkHP----EVTAkVQEEIDRVIGRHRSPCMQDrsHMPYTDAVIHE-IQRYIDLVpnNLPHAV 310

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      350 MADVKVGSYVVPKG-DIIAC-SPLLshHDEEAFPEPRRWDPER--DE----KVEGAFIGFGAGVHKCIGQ 411
Cdd:cd20665 311 TCDTKFRNYLIPKGtTVITSlTSVL--HDDKEFPNPEKFDPGHflDEngnfKKSDYFMPFSAGKRICAGE 378
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 229-462 2.51e-08

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 56.33  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       229 IIIARKEEEVNKDSSTSDLLSGLLSAVYR-------DGTPMSLHEVcgmIVAAMFAGQHTSSITTTWSMLHLM-HP---- 296
Cdd:PLN03195 251 VIRRRKAEMDEARKSGKKVKHDILSRFIElgedpdsNFTDKSLRDI---VLNFVIAGRDTTATTLSWFVYMIMmNPhvae 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       297 ----------------ANVKHLEALRKEIEEFPAQLNYNNVMdEMPFAERCARESIRRDPPLLMLMRKVMAD-VKVGSYV 359
Cdd:PLN03195 328 klyselkalekerakeEDPEDSQSFNQRVTQFAGLLTYDSLG-KLQYLHAVITETLRLYPAVPQDPKGILEDdVLPDGTK 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       360 VPKGDIIACSP-------LLSHHDEEAFpEPRRWdperdeKVEGAFI--------GFGAGVHKCIGQKFGLLQVKTILAT 424
Cdd:PLN03195 407 VKAGGMVTYVPysmgrmeYNWGPDAASF-KPERW------IKDGVFQnaspfkftAFQAGPRICLGKDSAYLQMKMALAL 479

                        250       260       270
                 ....*....|....*....|....*....|....*...
2WV2_A       425 AFRSYDFQLLrdEVPDPDYHTMVVGPTASQCRVKYIRR 462
Cdd:PLN03195 480 LCRFFKFQLV--PGHPVKYRMMTILSMANGLKVTVSRR 515
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 256-433 4.04e-08

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 55.63  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       256 YRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMhpanvKHLEALRKEIEEFPAQLNYNNVMDE-----MPFAER 330
Cdd:PLN00110 279 NSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEML-----KNPSILKRAHEEMDQVIGRNRRLVEsdlpkLPYLQA 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       331 CARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--DEKVEG--------AFI 399
Cdd:PLN00110 354 ICKESFRKHPSTpLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERflSEKNAKidprgndfELI 433

                        170       180       190
                 ....*....|....*....|....*....|....
2WV2_A       400 GFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:PLN00110 434 PFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKL 467
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 214-433 4.51e-08

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: 55.03  E-value: 4.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      214 RCHEARTELQKILSEIIIARKEEEVNKDSSTSDLLSGLLS-------------AVyrdgtpmsLHEvcgMIvaamFAGQH 280
Cdd:cd11076 174 RCSALVPRVNTFVGKIIEEHRAKRSNRARDDEDDVDVLLSlqgeeklsdsdmiAV--------LWE---MI----FRGTD 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      281 TSSITTTWSMLHL-MHPanvkhlEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPP--LLMLMRKVMAD 352
Cdd:cd11076 239 TVAILTEWIMARMvLHP------DIQSKAQAEIDAAVGGSRRVADsdvakLPYLQAVVKETLRLHPPgpLLSWARLAIHD 312

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      353 VKVGSYVVPKGDI-------IAcspllshHDEEAFPEPRRWDPER----DEKVEGAFIG-------FGAGVHKCIGQKFG 414
Cdd:cd11076 313 VTVGGHVVPAGTTamvnmwaIT-------HDPHVWEDPLEFKPERfvaaEGGADVSVLGsdlrlapFGAGRRVCPGKALG 385

                       250
                ....*....|....*....
2WV2_A      415 LLQVKTILATAFRSYDFQL 433
Cdd:cd11076 386 LATVHLWVAQLLHEFEWLP 404
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 222-427 4.92e-08

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 55.13  E-value: 4.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       222 LQKILSEIIIARKEEEVNKDSSTSDLLSGLLsavyRDGTPMSLHE-VCGMIVAAMFAGQHTSSITTTWSM---------L 291
Cdd:PLN03141 210 VKKIIEEKRRAMKNKEEDETGIPKDVVDVLL----RDGSDELTDDlISDNMIDMMIPGEDSVPVLMTLAVkflsdcpvaL 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       292 HLMHPANVKhleaLRKEIEEFPAQLNYNNVMdEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSPL 371
Cdd:PLN03141 286 QQLTEENMK----LKRLKADTGEPLYWTDYM-SLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFR 360

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
2WV2_A       372 LSHHDEEAFPEPRRWDPERDEKVE---GAFIGFGAGVHKCIGQKFGLLQVKTIL---ATAFR 427
Cdd:PLN03141 361 SVHLDEENYDNPYQFNPWRWQEKDmnnSSFTPFGGGQRLCPGLDLARLEASIFLhhlVTRFR 422
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 53-444 5.19e-08

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: 54.78  E-value: 5.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       53 IFTINIVGKRVTIVGDPHEHSRFFLPRNEVLSPREVYSFMVPVF-GEGVAYAAPYPRMREQLNFLAEELTIAKF--QNFV 129
Cdd:cd20666   4 IFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTkGKGIVFAPYGPVWRQQRKFSHSTLRHFGLgkLSLE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      130 PAIQHEVRKFMAANWDKDEGEINLLEDCSTMIINTACQCLFGedlrKRLDAR--RFAQLLAKM----ESSLIPAAVFLPI 203
Cdd:cd20666  84 PKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFG----RRFDYQdvEFKTMLGLMsrglEISVNSAAILVNI 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      204 LLKLPLPQSARCHEAR-------TELQKILSE-----------------IIIARKEEEVNKDSS-TSDLLSGLLSAVYrd 258
Cdd:cd20666 160 CPWLYYLPFGPFRELRqiekditAFLKKIIADhretldpanprdfidmyLLHIEEEQKNNAESSfNEDYLFYIIGDLF-- 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      259 gtpmslhevcgmivaamFAGQHTSSITTTWSMLHL-MHPaNVKhlEALRKEIEEFPAQLNYNNVMD--EMPFAERCARES 335
Cdd:cd20666 238 -----------------IAGTDTTTNTLLWCLLYMsLYP-EVQ--EKVQAEIDTVIGPDRAPSLTDkaQMPFTEATIMEV 297

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      336 IRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKC 408
Cdd:cd20666 298 QRMTVVVpLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGqlikkeAFIPFGIGRRVC 377

                       410       420       430
                ....*....|....*....|....*....|....*.
2WV2_A      409 IGQKFGLLQVKTILATAFRSYDFqLLRDEVPDPDYH 444
Cdd:cd20666 378 MGEQLAKMELFLMFVSLMQSFTF-LLPPNAPKPSME 412
PLN03018 PLN03018
homomethionine N-hydroxylase
 299-439 1.07e-07

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 54.25  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       299 VKHLEALRKEIEEFPAQLNYNNVMDE-----MPFAERCARESIRRDPPLLMLMRKVM-ADVKVGSYVVPKGD-IIACSPL 371
Cdd:PLN03018 342 LKNPEILRKALKELDEVVGKDRLVQEsdipnLNYLKACCRETFRIHPSAHYVPPHVArQDTTLGGYFIPKGShIHVCRPG 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       372 LShHDEEAFPEPRRWDPERDEKVEGA------------FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVP 439
Cdd:PLN03018 422 LG-RNPKIWKDPLVYEPERHLQGDGItkevtlvetemrFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDFGP 500
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 262-412 1.13e-07

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: 54.08  E-value: 1.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      262 MSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEEFPAQL--NYNNVMDEMPFAERCARESIRRD 339
Cdd:cd20644 228 LSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQ--QILRQESLAAAAQIseHPQKALTELPLLKAALKETLRLY 305

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A      340 PPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER---DEKVEGAF--IGFGAGVHKCIGQK 412
Cdd:cd20644 306 PVGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRwldIRGSGRNFkhLAFGFGMRQCLGRR 383
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 270-449 1.56e-07

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: 53.33  E-value: 1.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      270 MIVAAMF-AGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEEFPAQLNYNNVMD--EMPFAERCAREsIRR--DPPLLM 344
Cdd:cd11026 229 MTVLDLFfAGTETTSTTLRWALLLLMKYPHIQ--EKVQEEIDRVIGRNRTPSLEDraKMPYTDAVIHE-VQRfgDIVPLG 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      345 LMRKVMADVKVGSYVVPKGDIIAcsPLLS--HHDEEAFPEPRRWDPER--DE-----KVEgAFIGFGAGVHKCIGQKFGL 415
Cdd:cd11026 306 VPHAVTRDTKFRGYTIPKGTTVI--PNLTsvLRDPKQWETPEEFNPGHflDEqgkfkKNE-AFMPFSAGKRVCLGEGLAR 382

                       170       180       190
                ....*....|....*....|....*....|....
2WV2_A      416 LQVKTILATAFRSYDFQLLRDEvPDPDYHTMVVG 449
Cdd:cd11026 383 MELFLFFTSLLQRFSLSSPVGP-KDPDLTPRFSG 415
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 233-423 1.60e-07

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: 53.52  E-value: 1.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      233 RKEEEvnkdsstsDLLSGLLSAVYRDGTPM-SLHEVCGMIVAAMFAGQHTSSITTTWSMLHLmhpanVKHLEALRKEIEE 311
Cdd:cd20658 211 KKEEE--------DWLDVFITLKDENGNPLlTPDEIKAQIKELMIAAIDNPSNAVEWALAEM-----LNQPEILRKATEE 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      312 FP--------------AQLNYnnvmdempfAERCARESIRRDPPLLMLMRKV-MADVKVGSYVVPKGDIIacspLLSHH- 375
Cdd:cd20658 278 LDrvvgkerlvqesdiPNLNY---------VKACAREAFRLHPVAPFNVPHVaMSDTTVGGYFIPKGSHV----LLSRYg 344

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      376 ---DEEAFPEPRRWDPER----DEKV-----EGAFIGFGAGVHKCIGQKFGLLQVKTILA 423
Cdd:cd20658 345 lgrNPKVWDDPLKFKPERhlneDSEVtltepDLRFISFSTGRRGCPGVKLGTAMTVMLLA 404
PTZ00404 PTZ00404
cytochrome P450; Provisional
 276-432 2.24e-07

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 53.19  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       276 FAGQHTSSITTTWSMLHLM-HPanvKHLEALRKEIEEFPAQLNYNNVMDE--MPFAERCARESIRRDPPLLM-LMRKVMA 351
Cdd:PTZ00404 293 LAGVDTSATSLEWMVLMLCnYP---EIQEKAYNEIKSTVNGRNKVLLSDRqsTPYTVAIIKETLRYKPVSPFgLPRSTSN 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       352 DVKVGS-YVVPKGdiiaCSPLLSHH----DEEAFPEPRRWDPERDEKVEG--AFIGFGAGVHKCIGQKFGLLQVKTILAT 424
Cdd:PTZ00404 370 DIIIGGgHFIPKD----AQILINYYslgrNEKYFENPEQFDPSRFLNPDSndAFMPFSIGPRNCVGQQFAQDELYLAFSN 445


                 ....*...
2WV2_A       425 AFRSYDFQ 432
Cdd:PTZ00404 446 IILNFKLK 453
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 211-422 2.27e-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: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      211 QSARCHEART-----ELQKILSEIIIARKEEevnkDSSTSDLLSGLLSAVYRDGTPMSLHEvcgmIVAAM--FAGQHTSS 283
Cdd:cd11079 127 ATRSGDRAATaevaeEFDGIIRDLLADRRAA----PRDADDDVTARLLRERVDGRPLTDEE----IVSILrnWTVGELGT 198

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      284 ITTTWSML--HLMHpaNVKHLEALRKEIEEFPAqlnynnVMDEMpfaercaresIRRDPPLLMLMRKVMADVKVGSYVVP 361
Cdd:cd11079 199 IAACVGVLvhYLAR--HPELQARLRANPALLPA------AIDEI----------LRLDDPFVANRRITTRDVELGGRTIP 260

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
2WV2_A      362 KGDIIACSPLLSHHDEEAFPEPRRWDPERDEKvegAFIGFGAGVHKCIGQKFGLLQVKTIL 422
Cdd:cd11079 261 AGSRVTLNWASANRDERVFGDPDEFDPDRHAA---DNLVYGRGIHVCPGAPLARLELRILL 318
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 251-434 3.15e-07

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: 52.46  E-value: 3.15e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      251 LLSAVYRDGTPMSLHEVcgmivaaMFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEEFPAQLNYNNVMD--EMPFA 328
Cdd:cd20669 218 PLSHFNMETLVMTTHNL-------LFGGTETVSTTLRYGFLILMKYPKVA--ARVQEEIDRVVGRNRLPTLEDraRMPYT 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      329 ERCAREsIRR--DPPLLMLMRKVMADVKVGSYVVPKG-DIIacsPLLS--HHDEEAFPEPRRWDPER--DEKVE----GA 397
Cdd:cd20669 289 DAVIHE-IQRfaDIIPMSLPHAVTRDTNFRGFLIPKGtDVI---PLLNsvHYDPTQFKDPQEFNPEHflDDNGSfkknDA 364

                       170       180       190
                ....*....|....*....|....*....|....*..
2WV2_A      398 FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLL 434
Cdd:cd20669 365 FMPFSAGKRICLGESLARMELFLYLTAILQNFSLQPL 401
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 234-433 5.60e-07

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: 51.76  E-value: 5.60e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      234 KEEEVNKDSSTSDLLSGLLSAVYRD-GTPMSLHEVCGMI--VAAMF-AGQHTSSITTTWSMLHLMHPANVKhlEALRKEI 309
Cdd:cd20667 189 IRHELRTNEAPQDFIDCYLAQITKTkDDPVSTFSEENMIqvVIDLFlGGTETTATTLHWALLYMVHHPEIQ--EKVQQEL 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      310 EEF--PAQLNYNNVMDEMPFAERCARESIRRDPPLLM-LMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRW 386
Cdd:cd20667 267 DEVlgASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKF 346

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
2WV2_A      387 DPERDEKVEG------AFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQL 433
Cdd:cd20667 347 NPGHFLDKDGnfvmneAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQL 399
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 285-435 7.77e-07

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: 50.92  E-value: 7.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      285 TTTWSMLHLM--HPanvKHLEALRKEIEEFPAQLnynnvmdEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPK 362
Cdd:cd20624 209 MALLRALALLaaHP---EQAARAREEAAVPPGPL-------ARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPA 278

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
2WV2_A      363 GD-IIACSPLLsHHDEEAFPEPRRWDPE----RDEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLR 435
Cdd:cd20624 279 GTgFLIFAPFF-HRDDEALPFADRFVPEiwldGRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLE 355
PLN02500 PLN02500
cytochrome P450 90B1
 234-439 8.47e-07

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 51.40  E-value: 8.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       234 KEEEVNKDSSTSDLLSGLLSAvyrdgTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLMH-PANVK-----HLEALRK 307
Cdd:PLN02500 252 KLKEEDESVEEDDLLGWVLKH-----SNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGcPKAVQelreeHLEIARA 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       308 EIEEFPAQLNYNNvMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIAcsPLLS--HHDEEAFPEPRR 385
Cdd:PLN02500 327 KKQSGESELNWED-YKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVL--PVIAavHLDSSLYDQPQL 403

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2WV2_A       386 WDPER-------------DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVP 439
Cdd:PLN02500 404 FNPWRwqqnnnrggssgsSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEADQA 470
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 276-432 8.81e-07

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: 50.95  E-value: 8.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      276 FAGQHTSSITTTWSMLHLM-HPanvkHLEA-LRKEIEEFPA---QLNYNNVMdEMPFAERCAREsIRR--DPPLLMLMRK 348
Cdd:cd20668 236 FAGTETVSTTLRYGFLLLMkHP----EVEAkVHEEIDRVIGrnrQPKFEDRA-KMPYTEAVIHE-IQRfgDVIPMGLARR 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      349 VMADVKVGSYVVPKGDIIAcsPLLSH--HDEEAFPEPRRWDPER--DEKVE----GAFIGFGAGVHKCIGQKFGLLQVKT 420
Cdd:cd20668 310 VTKDTKFRDFFLPKGTEVF--PMLGSvlKDPKFFSNPKDFNPQHflDDKGQfkksDAFVPFSIGKRYCFGEGLARMELFL 387

                       170
                ....*....|..
2WV2_A      421 ILATAFRSYDFQ 432
Cdd:cd20668 388 FFTTIMQNFRFK 399
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 231-434 1.39e-06

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: 50.49  E-value: 1.39e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      231 IARKEEEVNKDSSTS----DLLSGLLSAV--YRDGTPMS-LHE--VCGMIVAAMFAGQHTSSITTTWSMLHLMHPANVKh 301
Cdd:cd20674 182 IVESQLRQHKESLVAgqwrDMTDYMLQGLgqPRGEKGMGqLLEghVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQ- 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      302 lEALRKEIEEF--PAQLNYNNVMDEMPFAERCARESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEE 378
Cdd:cd20674 261 -DRLQEELDRVlgPGASPSYKDRARLPLLNATIAEVLRLRPVVpLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDET 339

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      379 AFPEPRRWDPER---DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRsyDFQLL 434
Cdd:cd20674 340 VWEQPHEFRPERflePGAANRALLPFGCGARVCLGEPLARLELFVFLARLLQ--AFTLL 396
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 270-411 1.41e-06

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: 50.46  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      270 MIVAAMF-AGQHTSSITTTWS-MLHLMHPaNVKhlEALRKEIEEFPAQLNYNNVMDE--MPFAERCARESIR-RDPPLLM 344
Cdd:cd20663 233 LVVADLFsAGMVTTSTTLSWAlLLMILHP-DVQ--RRVQQEIDEVIGQVRRPEMADQarMPYTNAVIHEVQRfGDIVPLG 309

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
2WV2_A      345 LMRKVMADVKVGSYVVPKGD--IIACSPLLShhDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKCIGQ 411
Cdd:cd20663 310 VPHMTSRDIEVQGFLIPKGTtlITNLSSVLK--DETVWEKPLRFHPEHFLDAQGhfvkpeAFMPFSAGRRACLGE 382
PLN00168 PLN00168
Cytochrome P450; Provisional
 19-439 1.61e-06

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 50.33  E-value: 1.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        19 PVYPVTVPILGHIIQFGKSPLGFMQECKR-QLKSGIFTINIVGKRVTI-VGDPHEHSRFFLPRNEVLSPREVY--SFMVP 94
Cdd:PLN00168  37 PPGPPAVPLLGSLVWLTNSSADVEPLLRRlIARYGPVVSLRVGSRLSVfVADRRLAHAALVERGAALADRPAVasSRLLG 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A        95 VFGEGVAYAAPYPRMRE-QLNFLAEELTIAKFQNFVPAIQ--HEVRKFMAANWDKDEGEINLLEDCS-TMIINTACQClF 170
Cdd:PLN00168 117 ESDNTITRSSYGPVWRLlRRNLVAETLHPSRVRLFAPARAwvRRVLVDKLRREAEDAAAPRVVETFQyAMFCLLVLMC-F 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       171 GEDL-----RKRLDARRfaQLLAKMESSLIPAAVFLPILLKLPLPQSARCHEARTELQKILSEIIIARKEEEVNKD---- 241
Cdd:PLN00168 196 GERLdepavRAIAAAQR--DWLLYVSKKMSVFAFFPAVTKHLFRGRLQKALALRRRQKELFVPLIDARREYKNHLGqgge 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       242 ----------SSTSDLLSGLLSAvyRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHLmhpanVKHLEALRKEIEE 311
Cdd:PLN00168 274 ppkkettfehSYVDTLLDIRLPE--DGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAEL-----VKNPSIQSKLHDE 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       312 FPAQL--NYNNVMDE----MPFAERCARESIRRDPPLLMLM-RKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPR 384
Cdd:PLN00168 347 IKAKTgdDQEEVSEEdvhkMPYLKAVVLEGLRKHPPAHFVLpHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPM 426

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2WV2_A       385 RWDPER--------DEKVEGA----FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQllrdEVP 439
Cdd:PLN00168 427 EFVPERflaggdgeGVDVTGSreirMMPFGVGRRICAGLGIAMLHLEYFVANMVREFEWK----EVP 489
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 275-423 2.00e-06

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: 49.80  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      275 MFAGQHTSSITTTWSMLHLM-HPanvkHLEA-LRKEIEEF--PAQLNYNNVMDEMPFAERCARESIRRDPPLLMLMRKVM 350
Cdd:cd20671 232 VMAGTETTSTTLQWAVLLMMkYP----HIQKrVQEEIDRVlgPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTA 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      351 ADVKVGSYVVPKGDIIAcsPLLSH--HDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKCIGQKF--------- 413
Cdd:cd20671 308 ADTQFKGYLIPKGTPVI--PLLSSvlLDKTQWETPYQFNPNHFLDAEGkfvkkeAFLPFSAGRRVCVGESLartelfiff 385

                       170
                ....*....|.
2WV2_A      414 -GLLQVKTILA 423
Cdd:cd20671 386 tGLLQKFTFLP 396
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 222-440 2.18e-06

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: 49.80  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      222 LQKILSEIIIaRKEEEVNKDSStSDLLSGLLSAVYRDGTPMSLHEVCGMIVAAM---FAGQHTSSITTTWSMLHL-MHPA 297
Cdd:cd20662 180 LKLFVSDMID-KHREDWNPDEP-RDFIDAYLKEMAKYPDPTTSFNEENLICSTLdlfFAGTETTSTTLRWALLYMaLYPE 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      298 NVKHLEAlrkEIEEFPAQLNYNNVMDE--MPFAERCARESIRR-DPPLLMLMRKVMADVKVGSYVVPKGDIIACSPLLSH 374
Cdd:cd20662 258 IQEKVQA---EIDRVIGQKRQPSLADResMPYTNAVIHEVQRMgNIIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALH 334

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
2WV2_A      375 HDEEAFPEPRRWDPER-----DEKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPD 440
Cdd:cd20662 335 RDPKEWATPDTFNPGHflengQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPNEKLS 405
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 252-430 4.34e-06

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: 48.82  E-value: 4.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      252 LSAVYRDGTpMSLHEVCGMIVAAMFAGQHTSSITTTWSMLHL-MHPAnVKhlEALRKEIEEFPAQLNYNNVM---DEMPF 327
Cdd:cd20615 202 LYEAVEKGD-ITFEELLQTLDEMLFANLDVTTGVLSWNLVFLaANPA-VQ--EKLREEISAAREQSGYPMEDyilSTDTL 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      328 AERCARESIRRDPPLLMLMRKVMADVK-VGSYVVPKG-----DIIAcsplLSHHDEEAFPEPRRWDPERDEKVEGA---- 397
Cdd:cd20615 278 LAYCVLESLRLRPLLAFSVPESSPTDKiIGGYRIPANtpvvvDTYA----LNINNPFWGPDGEAYRPERFLGISPTdlry 353

                       170       180       190
                ....*....|....*....|....*....|....
2WV2_A      398 -FIGFGAGVHKCIGQKFGLLQVKTILATAFRSYD 430
Cdd:cd20615 354 nFWRFGFGPRKCLGQHVADVILKALLAHLLEQYE 387
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 218-441 6.13e-06

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 48.46  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       218 ARTELQKILSEIIIARKEEEVNK---DSSTSDLLSGLL---SAVYRDGTPMSLHEVCGMIVAAMFAGQHTSSITTTWSML 291
Cdd:PLN02169 247 ALATVNRMFAKIISSRRKEEISRaetEPYSKDALTYYMnvdTSKYKLLKPKKDKFIRDVIFSLVLAGRDTTSSALTWFFW 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       292 HLMhpanvKHLEALRKEIEEFPAQLNyNNVMDEMPFAERCARESIRRDPPLlMLMRKVMADVKV---GSYVVPKGDIIAC 368
Cdd:PLN02169 327 LLS-----KHPQVMAKIRHEINTKFD-NEDLEKLVYLHAALSESMRLYPPL-PFNHKAPAKPDVlpsGHKVDAESKIVIC 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       369 ----SPLLSHHDEEAFP-EPRRWDPERD---EKVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPD 440
Cdd:PLN02169 400 iyalGRMRSVWGEDALDfKPERWISDNGglrHEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKVIEGHKIE 479


                 .
2WV2_A       441 P 441
Cdd:PLN02169 480 A 480
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 303-430 1.18e-05

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: 47.64  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      303 EALRKEI-----EEFPAQLNynnVMDEMPFAERCARESIRRDPPLLMLMRKVMADVKV----GSYVVPKGDIIACSPLLS 373
Cdd:cd11071 261 ARLAEEIrsalgSEGGLTLA---ALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIeshdASYKIKKGELLVGYQPLA 337

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2WV2_A      374 HHDEEAFPEPRRWDPERDEKVEGAFI------------GFGAGVHKCIGQKFGLLQVKTILATAFRSYD 430
Cdd:cd11071 338 TRDPKVFDNPDEFVPDRFMGEEGKLLkhliwsngpeteEPTPDNKQCPGKDLVVLLARLFVAELFLRYD 406
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 158-442 3.65e-05

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: 46.07  E-value: 3.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      158 STMIINTACQCLFGedlrKRLD--ARRFAQLLAKMESSLI----PAAVFLPILLKLPLPQSARcHEARTELQKILSEIII 231
Cdd:cd20670 111 SRTVSNVISSVVFG----SRFDyeDKQFLSLLRMINESFIemstPWAQLYDMYSGIMQYLPGR-HNRIYYLIEELKDFIA 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      232 AR-KEEEVNKDSST-SDLLSGLLSAVYRD-GTPMSLHEVCGMIVAAM---FAGQHTSSITTTWSMLHLMHPANVKhlEAL 305
Cdd:cd20670 186 SRvKINEASLDPQNpRDFIDCFLIKMHQDkNNPHTEFNLKNLVLTTLnlfFAGTETVSSTLRYGFLLLMKYPEVE--AKI 263

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      306 RKEIEEF--PAQLNYNNVMDEMPFAERCAREsIRR--DPPLLMLMRKVMADVKVGSYVVPKG-DIIacsPLLSH--HDEE 378
Cdd:cd20670 264 HEEINQVigPHRLPSVDDRVKMPYTDAVIHE-IQRltDIVPLGVPHNVIRDTQFRGYLLPKGtDVF---PLLGSvlKDPK 339

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      379 AFPEPRRWDPER--DE----KVEGAFIGFGAGVHKCIGQKFGLLQVKTILATAFRSYDfqlLRDEVPDPD 442
Cdd:cd20670 340 YFRYPEAFYPQHflDEqgrfKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFS---LRSLVPPAD 406
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 53-443 5.70e-05

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 45.52  E-value: 5.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       53 IFTINIVGKRVTIVGDPH----------------EHSRFFLPRnevlspreVYSFMVPvfgegvAYAAPYPRMREQLNFL 116
Cdd:cd20634  13 IFTVQVAGRYVTVLLDPHsydavvwepstsldftSYARLLMDR--------IFDVQLP------SYDPTEEKKRMESHFQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      117 AEELTI---AKFQNFVPAIQHEvRKFMAANWdKDEGeinLLEDCSTMIINTACQCLFGEDLRKRLDA------------- 180
Cdd:cd20634  79 GANLTQltqAMFNNLQLLLLGD-AMGLSTEW-KKDG---LFNFCYSLLFRAGYLTLFGNENENSTHEsqnkdrahsaevy 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      181 ---RRFAQLLAKMESSLIPAAvflpillklplpQSARCHEARTELQKILSEIIIARKeeevnkdSSTSDLLSGLLSAVYR 257
Cdd:cd20634 154 hefRKLDQLLPKLARGTLSKE------------EKQEAASVKERLWKLLSPKRLNRK-------ANRSSWLESYLLHLEE 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      258 DGTPMSLHEVCgmIVAAMFAGQHTSSITTTWSMLHLM-HPANvkhLEALRKEIEEF---------PAQLNYNNVMDEMPF 327
Cdd:cd20634 215 EGVDEEMQARA--MLLQLWATQGNAGPAAFWLLLFLLkHPEA---MAAVRGEIQRIkhqrgqpvsQTLTINQELLDNTPV 289

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      328 AERCARESIRRDPPLLmLMRKVMADVKV-----GSYVVPKGDIIACSPLLS-HHDEEAFPEP------RRWDPERDEKVE 395
Cdd:cd20634 290 FDSVLSETLRLTAAPF-ITREVLQDMKLrladgQEYNLRRGDRLCLFPFLSpQMDPEIHQEPevfkydRFLNADGTEKKD 368

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
2WV2_A      396 ----GAFIGF-----GAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDPDY 443
Cdd:cd20634 369 fyknGKRLKYynmpwGAGDNVCIGRHFAVNSIKQFVFLILTHFDVELKDPEAEIPEF 425
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 334-420 2.72e-04

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


Pssm-ID: 410716 [Multi-domain]  Cd Length: 367  Bit Score: 43.02  E-value: 2.72e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      334 ESIRRDPPL-LMLMRKVMADVKVGSYVVPKGDIIACSPLLSHHDEEAFPeprrwDPERDEKVEGAFIGFGAGVHKCIGQK 412
Cdd:cd20623 246 EVLWRDPPLaNLAGRFAARDTELGGQWIRAGDLVVLGLAAANADPRVRP-----DPGASMSGNRAHLAFGAGPHRCPAQE 320


                ....*...
2WV2_A      413 FGLLQVKT 420
Cdd:cd20623 321 LAETIART 328
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 275-440 2.91e-04

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: 43.26  E-value: 2.91e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      275 MFAGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEeFPAQLNYNNVMDE---MPFAERCARESIRR-DPPLLMLMRKVM 350
Cdd:cd20661 247 IIAGTETTTNVLRWAILFMALYPNIQ--GQVQKEID-LVVGPNGMPSFEDkckMPYTEAVLHEVLRFcNIVPLGIFHATS 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      351 ADVKVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKCIGQKFGLLQVKTILAT 424
Cdd:cd20661 324 KDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGqfakkeAFVPFSLGRRHCLGEQLARMEMFLFFTA 403

                       170
                ....*....|....*.
2WV2_A      425 AFRSYDFQLLRDEVPD 440
Cdd:cd20661 404 LLQRFHLHFPHGLIPD 419
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 271-432 3.37e-04

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: 42.87  E-value: 3.37e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      271 IVAAMF-AGQHTSSITTTWSMLhLMhpanVKHLEALRKEIEEFPAQLNYNNVMDE----MPFAERCARESIRRDPPLLM- 344
Cdd:cd20664 229 SVGNLFgAGTDTTGTTLRWGLL-LM----MKYPEIQKKVQEEIDRVIGSRQPQVEhrknMPYTDAVIHEIQRFANIVPMn 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      345 LMRKVMADVKVGSYVVPKGDIIAcsPLLSH--HDEEAFPEPRRWDPERDEKVEG------AFIGFGAGVHKCIGQKFGLL 416
Cdd:cd20664 304 LPHATTRDVTFRGYFIPKGTYVI--PLLTSvlQDKTEWEKPEEFNPEHFLDSQGkfvkrdAFMPFSAGRRVCIGETLAKM 381

                       170
                ....*....|....*.
2WV2_A      417 QVKTILATAFRSYDFQ 432
Cdd:cd20664 382 ELFLFFTSLLQRFRFQ 397
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 277-424 3.71e-04

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: 42.78  E-value: 3.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      277 AGQHTSSITTTWSMLHLMHPANVKhlEALRKEIEEFPAQLNYNNVMD--EMPFAERCARESIRRDPPL-LMLMRKVMADV 353
Cdd:cd20677 247 AGFDTISTALQWSLLYLIKYPEIQ--DKIQEEIDEKIGLSRLPRFEDrkSLHYTEAFINEVFRHSSFVpFTIPHCTTADT 324

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      354 KVGSYVVPKGDIIACSPLLSHHDEEAFPEPRRWDPER--DEK-------VEGAFIgFGAGVHKCIGQKFGLLQVKTILAT 424
Cdd:cd20677 325 TLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERflDENgqlnkslVEKVLI-FGMGVRKCLGEDVARNEIFVFLTT 403
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 217-443 3.77e-04

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: 42.88  E-value: 3.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      217 EARTELQKILSEIIIARKEEEVNKDSSTSDLLSGLLS--AVYRDGTPMSLhevCGMIVAAMFAgqhtssittTWSMLHLM 294
Cdd:cd20627 163 DALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSeqQVLEDSMIFSL---AGCVITANLC---------TWAIYFLT 230

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      295 HPANVKhlEALRKEIEEF----PAQLNYnnvMDEMPFAERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIACSP 370
Cdd:cd20627 231 TSEEVQ--KKLYKEVDQVlgkgPITLEK---IEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYAL 305

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2WV2_A      371 LLSHHDEEAFPEPRRWDPER--DEKVEGAF--IGFgAGVHKCIGQKFGLLQVKTILATAFRSYDFQLLRDEVPDPDY 443
Cdd:cd20627 306 GVVLQDNTTWPLPYRFDPDRfdDESVMKSFslLGF-SGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKY 381
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 328-427 1.69e-03

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: 40.55  E-value: 1.69e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A      328 AERCARESIRRDPPLLMLMRKVMADVKVGSYVVPKGDIIAcspLL---SHHDEEAFPEPRRWDPERdekVEGAFIGFGAG 404
Cdd:cd11036 221 AAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVV---VLlaaANRDPEAFPDPDRFDLGR---PTARSAHFGLG 294

                        90       100
                ....*....|....*....|...
2WV2_A      405 VHKCIGQKFgllqVKTILATAFR 427
Cdd:cd11036 295 RHACLGAAL----ARAAAAAALR 313
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 228-453 4.21e-03

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 39.67  E-value: 4.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       228 EIIIARKEEEVnkdSSTSDLLSGLLSAV-----YRDgtpmslhevcgMIVAAMFAGQHT-SSITTTWSMLHLMHPANVkh 301
Cdd:PLN02426 264 EVIRQRRKLGF---SASKDLLSRFMASInddkyLRD-----------IVVSFLLAGRDTvASALTSFFWLLSKHPEVA-- 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       302 lEALRKEIEEF----PAQLNYNNvMDEMPFAERCARESIRRDPPllmlmrkVMADVK--VGSYVVPKGDIIACSPLLSHH 375
Cdd:PLN02426 328 -SAIREEADRVmgpnQEAASFEE-MKEMHYLHAALYESMRLFPP-------VQFDSKfaAEDDVLPDGTFVAKGTRVTYH 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2WV2_A       376 -------------DEEAFpEPRRWdperdeKVEGAFIG--------FGAGVHKCIGQKFGLLQVKTILATAFRSYDFQLL 434
Cdd:PLN02426 399 pyamgrmeriwgpDCLEF-KPERW------LKNGVFVPenpfkypvFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVV 471

                        250
                 ....*....|....*....
2WV2_A       435 RDEVPDPDYhtmVVGPTAS 453
Cdd:PLN02426 472 GRSNRAPRF---APGLTAT 487
 
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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