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Conserved domains on  [gi|154146204|ref|NP_001093654|]
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cytochrome P450, family 2, subfamily t, polypeptide 4 [Mus musculus]

Protein Classification

cytochrome P450( domain architecture ID 15335077)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
74-498 0e+00

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: 813.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20669   81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20669  161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20669  241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20669  321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                        410       420
                 ....*....|....*....|....*
gi 154146204 474 VGSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd20669  401 LGAPEDIDLTPLSSGLGNVPRPFQL 425
 
Name Accession Description Interval E-value
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
74-498 0e+00

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: 813.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20669   81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20669  161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20669  241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20669  321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                        410       420
                 ....*....|....*....|....*
gi 154146204 474 VGSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd20669  401 LGAPEDIDLTPLSSGLGNVPRPFQL 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
63-498 1.35e-135

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: 399.73  E-value: 1.35e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204   63 LDRVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFT---CGNGIVFSNGPRWHSLRNF 139
Cdd:pfam00067  22 LHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRgpfLGKGIVFANGPRWRQLRRF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  140 ALGVLRelGVGRSTIEDRILEEAACVLDEFQATMGAP--FDPQQLLDSAVSNVICTVVFGKRYD-YGDPEFRRLLNLFSD 216
Cdd:pfam00067 102 LTPTFT--SFGKLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFGsLEDPKFLELVKAVQE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  217 NFCIMSSRWAEIYNMFPSFmDWIPGPHNRIFKNFQ----ELRLFISEQIQWHWQSRQtGEPRDFIDCFLDQMDKEQQdle 292
Cdd:pfam00067 180 LSSLLSSPSPQLLDLFPIL-KYFPGPHGRKLKRARkkikDLLDKLIEERRETLDSAK-KSPRDFLDALLLAKEEEDG--- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  293 SHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFI 372
Cdd:pfam00067 255 SKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLH 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  373 SVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAG 452
Cdd:pfam00067 335 PVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGER 414
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 154146204  453 LARSEIFLFLTAILQKFSL--LPVGSPANINLNPqctGLGNVPPAFQL 498
Cdd:pfam00067 415 LARMEMKLFLATLLQNFEVelPPGTDPPDIDETP---GLLLPPKPYKL 459
PTZ00404 PTZ00404
cytochrome P450; Provisional
65-471 1.51e-47

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 171.44  E-value: 1.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  65 RVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVL 144
Cdd:PTZ00404  52 RDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTSSGEYWKRNREIVGKAM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 145 RELGVgrSTIEDrILEEAACVL----DEFQATmGAPFDPQQLLDSAVSNVICTVVF----GKRYDYGDPEFRRLLNLFSD 216
Cdd:PTZ00404 132 RKTNL--KHIYD-LLDDQVDVLiesmKKIESS-GETFEPRYYLTKFTMSAMFKYIFnediSFDEDIHNGKLAELMGPMEQ 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 217 NFCIMSSrwAEIYNMF----PSFMDWIpgphNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLdqmdKEQQDlE 292
Cdd:PTZ00404 208 VFKDLGS--GSLFDVIeitqPLYYQYL----EHTDKNFKKIKKFIKEKYHEHLKTIDPEVPRDLLDLLI----KEYGT-N 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 293 SHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFI 372
Cdd:PTZ00404 277 TDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYK 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 373 SVLPLGLPRALTRDVNLKN-HFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLddhgEFQNNDAFMPFALGKRMCLGA 451
Cdd:PTZ00404 357 PVSPFGLPRSTSNDIIIGGgHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFL----NPDSNDAFMPFSIGPRNCVGQ 432
                        410       420
                 ....*....|....*....|
gi 154146204 452 GLARSEIFLFLTAILQKFSL 471
Cdd:PTZ00404 433 QFAQDELYLAFSNIILNFKL 452
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
74-472 2.88e-38

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 144.49  E-value: 2.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGP--LPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNG---IVFSNGPRWHSLRN-----FALGV 143
Cdd:COG2124   35 YGDYFTLRLPGpgDGFWVVSRPADVREVLRDPRFFSSALGAGLRPRLLRPVLGdgsLLTLDGPEHTRLRKllapaFTPRA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 144 LRELgvgrstiEDRILEEAACVLDEFQAtmGAPFDPQQLLDSAVSNVICTVvFGkrydYGDPEFRRLLnlfsdnfcimss 223
Cdd:COG2124  115 LRGY-------RPLIREIADRLLDDLWQ--GGADLVLDFAAELTLRVIAEL-LG----VPLEDRPQLL------------ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 224 RWAEIYNMFPSFMDWIPGPHNRIFKNFQELRLFISEQIQwhwqSRQTGEPRDFidcfLDQMDKEQQDLESHFQDETLVMT 303
Cdd:COG2124  169 RWSDALLLRLDPDLGPEEPWRRARAARRELDAYLRALIA----ERRAAPRDDL----LSLLLSAEDDGGGRLSDDEIRDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 304 THDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDAtvgrtwapriedrarlPYTNAVLHEIQRFISVLPLgLPRAL 383
Cdd:COG2124  241 LITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR----------------PLLEAVVEETLRLYPPVPL-ARRVA 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 384 TRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTnflddhgefQNNDAFMPFALGKRMCLGAGLARSEIFLFLT 463
Cdd:COG2124  304 TEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPE---------RFNNAHLPFGGGPHRCLGAALARLELKVALA 374

                 ....*....
gi 154146204 464 AILQKFSLL 472
Cdd:COG2124  375 ELLRRFPLL 383
 
Name Accession Description Interval E-value
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
74-498 0e+00

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: 813.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20669   81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20669  161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20669  241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20669  321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                        410       420
                 ....*....|....*....|....*
gi 154146204 474 VGSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd20669  401 LGAPEDIDLTPLSSGLGNVPRPFQL 425
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
75-498 0e+00

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: 649.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRSTI 154
Cdd:cd11026    2 GPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKRSI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 155 EDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFPS 234
Cdd:cd11026   82 EERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMFPP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 235 FMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTET 314
Cdd:cd11026  162 LLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAGTET 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 315 TSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFL 394
Cdd:cd11026  242 TSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYTI 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 395 HKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPV 474
Cdd:cd11026  322 PKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSP 401
                        410       420
                 ....*....|....*....|....
gi 154146204 475 GSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd11026  402 VGPKDPDLTPRFSGFTNSPRPYQL 425
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
74-498 0e+00

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: 590.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20665    1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20665   81 IEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20665  161 ALLDYLPGSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQEKHNQQSEFTLENLAVTVTDLFGAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20665  241 TTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20665  321 IPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKS 400
                        410       420
                 ....*....|....*....|....*
gi 154146204 474 VGSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd20665  401 LVDPKDIDTTPVVNGFASVPPPYQL 425
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
74-498 0e+00

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: 520.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALANGERWRILRRFSLTILRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20670   81 IEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20670  161 GIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLDPQNPRDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20670  241 TVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRGYL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20670  321 LPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRS 400
                        410       420
                 ....*....|....*....|....*
gi 154146204 474 VGSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd20670  401 LVPPADIDITPKISGFGNIPPTYEL 425
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
74-498 1.38e-176

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 502.77  E-value: 1.38e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFANGERWKTLRRFSLATMRDFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20672   81 VEERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20672  161 GFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHQNLMISVLSLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20672  241 TTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRGYL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20672  321 LPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVAS 400
                        410       420
                 ....*....|....*....|....*
gi 154146204 474 VGSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd20672  401 PVAPEDIDLTPKESGVGKIPPTYQI 425
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
74-498 2.12e-173

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: 494.70  E-value: 2.12e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20668    1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRDFGVGKRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20668   81 IEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20668  161 SVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEKKNPNTEFYMKNLVMTTLNLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20668  241 TVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRDFF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20668  321 LPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKS 400
                        410       420
                 ....*....|....*....|....*
gi 154146204 474 VGSPANINLNPQCTGLGNVPPAFQL 498
Cdd:cd20668  401 PQSPEDIDVSPKHVGFATIPRNYTM 425
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
74-483 3.11e-159

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: 458.89  E-value: 3.11e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNGENWKEMRRFTLTTLRDFGMGKKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20664   81 SEDKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWiPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20664  161 WLGPF-PGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFLVKQQEEEESSDSFFHDDNLTCSVGNLFGAGTD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20664  240 TTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSR-QPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRGYF 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20664  319 IPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQP 398
                        410
                 ....*....|
gi 154146204 474 VGSPANINLN 483
Cdd:cd20664  399 PPGVSEDDLD 408
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
74-473 2.71e-149

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: 433.45  E-value: 2.71e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20662   81 LEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEqQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20662  161 WIMKYLPGSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYLKEMAKY-PDPTTSFNEENLICSTLDLFFAGTE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20662  240 TTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLAGFH 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDhGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20662  320 LPKGTMILTNLTALHRDPKEWATPDTFNPGHFLEN-GQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKP 398
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
63-498 1.35e-135

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: 399.73  E-value: 1.35e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204   63 LDRVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFT---CGNGIVFSNGPRWHSLRNF 139
Cdd:pfam00067  22 LHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRgpfLGKGIVFANGPRWRQLRRF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  140 ALGVLRelGVGRSTIEDRILEEAACVLDEFQATMGAP--FDPQQLLDSAVSNVICTVVFGKRYD-YGDPEFRRLLNLFSD 216
Cdd:pfam00067 102 LTPTFT--SFGKLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFGsLEDPKFLELVKAVQE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  217 NFCIMSSRWAEIYNMFPSFmDWIPGPHNRIFKNFQ----ELRLFISEQIQWHWQSRQtGEPRDFIDCFLDQMDKEQQdle 292
Cdd:pfam00067 180 LSSLLSSPSPQLLDLFPIL-KYFPGPHGRKLKRARkkikDLLDKLIEERRETLDSAK-KSPRDFLDALLLAKEEEDG--- 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  293 SHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFI 372
Cdd:pfam00067 255 SKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLH 334
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  373 SVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAG 452
Cdd:pfam00067 335 PVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGER 414
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 154146204  453 LARSEIFLFLTAILQKFSL--LPVGSPANINLNPqctGLGNVPPAFQL 498
Cdd:pfam00067 415 LARMEMKLFLATLLQNFEVelPPGTDPPDIDETP---GLLLPPKPYKL 459
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
75-498 1.14e-130

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: 385.80  E-value: 1.14e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVgRSTI 154
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNGDYWKELRRFALSSLTKTKL-KKKM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 155 EDRILEEAACVLDEFQATM--GAPFDPQQLLDSAVSNVICTVVFGKRYD-YGDPEFRRLLNLFSDNFCIMSSRWAEIYNM 231
Cdd:cd20617   80 EELIEEEVNKLIESLKKHSksGEPFDPRPYFKKFVLNIINQFLFGKRFPdEDDGEFLKLVKPIEEIFKELGSGNPSDFIP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 232 FPSfmDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEqqDLESHFQDETLVMTTHDLFFGG 311
Cdd:cd20617  160 ILL--PFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKE--GDSGLFDDDSIISTCLDLFLAG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 312 TETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKN 391
Cdd:cd20617  236 TDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEIGG 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 392 HFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEfQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd20617  316 YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGN-KLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKF 394
                        410       420
                 ....*....|....*....|....*..
gi 154146204 472 LPVGSpaNINLNPQCTGLGNVPPAFQL 498
Cdd:cd20617  395 KSSDG--LPIDEKEVFGLTLKPKPFKV 419
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
74-477 5.08e-128

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: 379.42  E-value: 5.08e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCG---NGIVFSN-GPRWHSLRNFALGVLRELGV 149
Cdd:cd20663    1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGpksQGVVLARyGPAWREQRRFSVSTLRNFGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 GRSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIY 229
Cdd:cd20663   81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 230 NMFPSFMDwIPGPHNRIFKNFQELRLFISEQIQWHWQSRQ-TGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLF 308
Cdd:cd20663  161 NAFPVLLR-IPGLAGKVFPGQKAFLALLDELLTEHRTTWDpAQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 309 FGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVN 388
Cdd:cd20663  240 SAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 389 LKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQK 468
Cdd:cd20663  320 VQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQR 399
                        410
                 ....*....|
gi 154146204 469 FSL-LPVGSP 477
Cdd:cd20663  400 FSFsVPAGQP 409
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
75-477 9.27e-127

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: 375.79  E-value: 9.27e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDalVLQADAFSGRGAMAVFDRFTCGN--GIVFSNGPRWHSLRNFALGVLRELGVGRS 152
Cdd:cd20651    1 GDVVGLKLGKDKVVVVSGYEAVRE--VLSREEFDGRPDGFFFRLRTFGKrlGITFTDGPFWKEQRRFVLRHLRDFGFGRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 153 TIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFsdnfcIMSSRWAEIYNMF 232
Cdd:cd20651   79 SMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELV-----HLLFRNFDMSGGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 233 PSFMDWI----PG--PHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMdKEQQDLESHFQDETLVMTTHD 306
Cdd:cd20651  154 LNQFPWLrfiaPEfsGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNPRDLIDAYLREM-KKKEPPSSSFTDDQLVMICLD 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 307 LFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRD 386
Cdd:cd20651  233 LFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKD 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 387 VNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAIL 466
Cdd:cd20651  313 TTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLL 392
                        410
                 ....*....|.
gi 154146204 467 QKFSLLPVGSP 477
Cdd:cd20651  393 QNFTFSPPNGS 403
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
74-476 2.24e-124

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: 369.94  E-value: 2.24e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20667    1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLRELGLGKQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20667   81 LESQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 SFMDWIPGPHNRIFKNFQELRLFISEQIQWHwQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20667  161 WLMRYLPGPHQKIFAYHDAVRSFIKKEVIRH-ELRTNEAPQDFIDCYLAQITKTKDDPVSTFSEENMIQVVIDLFLGGTE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHF 393
Cdd:cd20667  240 TTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHGYY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL-L 472
Cdd:cd20667  320 VEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFqL 399

                 ....
gi 154146204 473 PVGS 476
Cdd:cd20667  400 PEGV 403
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
74-499 6.38e-124

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: 368.74  E-value: 6.38e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRST 153
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 154 IEDRILEEAACVLDEFQATMGAPFdPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFP 233
Cdd:cd20671   81 IEDKILEELQFLNGQIDSFNGKPF-PLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 234 sFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLdQMDKEQQDLESHFQDETLVMTTHDLFFGGTE 313
Cdd:cd20671  160 -VLGAFLKLHKPILDKVEEVCMILRTLIEARRPTIDGNPLHSYIEALI-QKQEEDDPKETLFHDANVLACTLDLVMAGTE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPlGLPRALTRDVNLKNHF 393
Cdd:cd20671  238 TTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRCTAADTQFKGYL 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLL- 472
Cdd:cd20671  317 IPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLp 396
                        410       420
                 ....*....|....*....|....*...
gi 154146204 473 -PVGSPANINLNPQctglgnvpPAFQLR 499
Cdd:cd20671  397 pPGVSPADLDATPA--------AAFTMR 416
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
75-477 8.00e-122

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: 363.45  E-value: 8.00e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFT-CGNGIVFSN-GPRWHSLRNFALGVLRELGVGRS 152
Cdd:cd11027    2 GDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSrGGKDIAFGDySPTWKLHRKLAHSALRLYASGGP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 153 TIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLfSDNF--CIMSSRwaeIYN 230
Cdd:cd11027   82 RLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDL-NDKFfeLLGAGS---LLD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 231 MFPsFMDWIPGPHNRIFKNFQELRL-FISEQIQWHWQSRQTGEPRDFIDCFLD-QMDKEQQDLESH--FQDETLVMTTHD 306
Cdd:cd11027  158 IFP-FLKYFPNKALRELKELMKERDeILRKKLEEHKETFDPGNIRDLTDALIKaKKEAEDEGDEDSglLTDDHLVMTISD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 307 LFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRD 386
Cdd:cd11027  237 IFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTCD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 387 VNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQN-NDAFMPFALGKRMCLGAGLARSEIFLFLTAI 465
Cdd:cd11027  317 TTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPkPESFLPFSAGRRVCLGESLAKAELFLFLARL 396
                        410
                 ....*....|...
gi 154146204 466 LQKFSL-LPVGSP 477
Cdd:cd11027  397 LQKFRFsPPEGEP 409
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
74-473 2.86e-118

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: 354.08  E-value: 2.86e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSN-GPRWHSLRNFALGVLRELGVGRS 152
Cdd:cd20666    1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPyGPVWRQQRKFSHSTLRHFGLGKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 153 TIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMF 232
Cdd:cd20666   81 SLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAAILVNIC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 233 PsFMDWIP-GPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQ-DLESHFQDETLVMTTHDLFFG 310
Cdd:cd20666  161 P-WLYYLPfGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLHIEEEQKnNAESSFNEDYLFYIIGDLFIA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 311 GTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLK 390
Cdd:cd20666  240 GTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQ 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 391 NHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFS 470
Cdd:cd20666  320 GYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFT 399

                 ...
gi 154146204 471 LLP 473
Cdd:cd20666  400 FLL 402
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
74-473 2.47e-110

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: 333.88  E-value: 2.47e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFS-NGPRWHSLRNFALGVLRELGVGRS 152
Cdd:cd11028    1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSMAFSdYGPRWKLHRKLAQNALRTFSNART 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 153 T--IEDRILEEAACVLDEFQATMG--APFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLfSDNFcimsSRWAEI 228
Cdd:cd11028   81 HnpLEEHVTEEAEELVTELTENNGkpGPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVKS-NDDF----GAFVGA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 229 YNMFpSFMDWIPGPHNRIFKNFQEL--RL--FISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDL--ESHFQDETLVM 302
Cdd:cd11028  156 GNPV-DVMPWLRYLTRRKLQKFKELlnRLnsFILKKVKEHLDTYDKGHIRDITDALIKASEEKPEEEkpEVGLTDEHIIS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 303 TTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRA 382
Cdd:cd11028  235 TVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIPHA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 383 LTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNN--DAFMPFALGKRMCLGAGLARSEIFL 460
Cdd:cd11028  315 TTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTkvDKFLPFGAGRRRCLGEELARMELFL 394
                        410
                 ....*....|....*
gi 154146204 461 FLTAILQ--KFSLLP 473
Cdd:cd11028  395 FFATLLQqcEFSVKP 409
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
71-480 6.80e-109

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: 330.62  E-value: 6.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  71 SSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSN-GPRWHSLRNFALGVLRELGV 149
Cdd:cd20661    9 SQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKyGRGWTEHRKLAVNCFRYFGY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 GRSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIY 229
Cdd:cd20661   89 GQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWVFLY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 230 NMFPsFMDWIP-GPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLF 308
Cdd:cd20661  169 NAFP-WIGILPfGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFSVGELI 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 309 FGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVN 388
Cdd:cd20661  248 IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSKDAV 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 389 LKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQK 468
Cdd:cd20661  328 VRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQR 407
                        410
                 ....*....|...
gi 154146204 469 FSL-LPVGSPANI 480
Cdd:cd20661  408 FHLhFPHGLIPDL 420
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
75-498 2.55e-85

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: 269.66  E-value: 2.55e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALvlQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELG-----V 149
Cdd:cd20652    1 GSIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGGNGIICAEGDLWRDQRRFVHDWLRQFGmtkfgN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 GRSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSrwAEIY 229
Cdd:cd20652   79 GRAKMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLIGV--AGPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 230 NMFPsFMDWIPG---PHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRD---FIDCFLDQMDKEQQDLE---SHFQDETL 300
Cdd:cd20652  157 NFLP-FLRHLPSykkAIEFLVQGQAKTHAIYQKIIDEHKRRLKPENPRDaedFELCELEKAKKEGEDRDlfdGFYTDEQL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 301 VMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLP 380
Cdd:cd20652  236 HHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLGIP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 381 RALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFL 460
Cdd:cd20652  316 HGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFL 395
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 154146204 461 FLTAILQKFSL-LPVGSPANInLNPQCtGLGNVPPAFQL 498
Cdd:cd20652  396 FTARILRKFRIaLPDGQPVDS-EGGNV-GITLTPPPFKI 432
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
74-498 3.94e-81

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: 258.87  E-value: 3.94e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSN--GPRWHSLRNFALGVLRELGVGR 151
Cdd:cd20677    1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSEkyGESWKLHKKIAKNALRTFSKEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 152 ST-------IEDRILEEA---ACVLDEFQATMGApFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLfsDNFCIM 221
Cdd:cd20677   81 AKsstcsclLEEHVCAEAselVKTLVELSKEKGS-FDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVEI--NNDLLK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 222 SSRWAEIYNMFPSFMdWIPGPHNRIFKNF-QELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESH-FQDET 299
Cdd:cd20677  158 ASGAGNLADFIPILR-YLPSPSLKALRKFiSRLNNFIAKSVQDHYATYDKNHIRDITDALIALCQERKAEDKSAvLSDEQ 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 300 LVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGL 379
Cdd:cd20677  237 IISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPFTI 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 380 PRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNN--DAFMPFALGKRMCLGAGLARSE 457
Cdd:cd20677  317 PHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSlvEKVLIFGMGVRKCLGEDVARNE 396
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 154146204 458 IFLFLTAILQKFSLlpVGSP-ANINLNPQcTGLGNVPPAFQL 498
Cdd:cd20677  397 IFVFLTTILQQLKL--EKPPgQKLDLTPV-YGLTMKPKPYRL 435
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
74-485 3.11e-80

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 256.48  E-value: 3.11e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSN--GPRWHSLRNFALGVLRELGVGR 151
Cdd:cd20676    1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLTFSTdsGPVWRARRKLAQNALKTFSIAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 152 ST-------IEDRILEEAACVLDEFQATMGAP--FDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLfSDNF--CI 220
Cdd:cd20676   81 SPtssssclLEEHVSKEAEYLVSKLQELMAEKgsFDPYRYIVVSVANVICAMCFGKRYSHDDQELLSLVNL-SDEFgeVA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 221 MSSRWAEiynmFPSFMDWIPGPHNRIFKNF-QELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQ--D 297
Cdd:cd20676  160 GSGNPAD----FIPILRYLPNPAMKRFKDInKRFNSFLQKIVKEHYQTFDKDNIRDITDSLIEHCQDKKLDENANIQlsD 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 298 ETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPL 377
Cdd:cd20676  236 EKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPF 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 378 GLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQN---NDAFMPFALGKRMCLGAGLA 454
Cdd:cd20676  316 TIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINkteSEKVMLFGLGKRRCIGESIA 395
                        410       420       430
                 ....*....|....*....|....*....|...
gi 154146204 455 RSEIFLFLTAILQK--FSLLPvGSPanINLNPQ 485
Cdd:cd20676  396 RWEVFLFLAILLQQleFSVPP-GVK--VDMTPE 425
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
74-466 3.23e-77

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


Pssm-ID: 410768  Cd Length: 434  Bit Score: 248.77  E-value: 3.23e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSN-GPRWHSLRNFALGVLRELGVG-- 150
Cdd:cd20675    1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFGGySERWKAHRRVAHSTVRAFSTRnp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 151 --RSTIEDRILEEAACVLDEF--QATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLfSDNFCiMSSRWA 226
Cdd:cd20675   81 rtRKAFERHVLGEARELVALFlrKSAGGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLGR-NDQFG-RTVGAG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 227 EIYNMFPsFMDWIPGPHNRIFKNFQELR----LFISEQIQWHWQSRQTGEPRDFIDCFLDQMDK-EQQDLESHFQDETLV 301
Cdd:cd20675  159 SLVDVMP-WLQYFPNPVRTVFRNFKQLNrefyNFVLDKVLQHRETLRGGAPRDMMDAFILALEKgKSGDSGVGLDKEYVP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 302 MTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPR 381
Cdd:cd20675  238 STVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTIPH 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 382 ALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGeFQNNDA---FMPFALGKRMCLGAGLARSEI 458
Cdd:cd20675  318 ATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENG-FLNKDLassVMIFSVGKRRCIGEELSKMQL 396

                 ....*...
gi 154146204 459 FLFlTAIL 466
Cdd:cd20675  397 FLF-TSIL 403
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
74-477 1.88e-76

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: 246.46  E-value: 1.88e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFT-CGNGIVFSN-GPRWHSLRNFALGVLRELGVGR 151
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSrNGKDIAFADySATWQLHRKLVHSAFALFGEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 152 STIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNlFSDNFCIMSSRwAEIYNM 231
Cdd:cd20673   81 QKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILN-YNEGIVDTVAK-DSLVDI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 232 FPsfmdWIpgphnRIFKNfQELRLF----------ISEQIQWHWQSRQTGEPRDFIDCFLD-QMDKEQQDLESH-----F 295
Cdd:cd20673  159 FP----WL-----QIFPN-KDLEKLkqcvkirdklLQKKLEEHKEKFSSDSIRDLLDALLQaKMNAENNNAGPDqdsvgL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 296 QDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVL 375
Cdd:cd20673  229 SDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVA 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 376 PLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGE--FQNNDAFMPFALGKRMCLGAGL 453
Cdd:cd20673  309 PLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSqlISPSLSYLPFGAGPRVCLGEAL 388
                        410       420
                 ....*....|....*....|....*
gi 154146204 454 ARSEIFLFLTAILQKFSL-LPVGSP 477
Cdd:cd20673  389 ARQELFLFMAWLLQRFDLeVPDGGQ 413
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
74-500 4.80e-76

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: 245.40  E-value: 4.80e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDrFTCGNGIVFSNG---PRWHSLRNFALGVLrELGVg 150
Cdd:cd20674    1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGK-LVSQGGQDLSLGdysLLWKAHRKLTRSAL-QLGI- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 151 RSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDyGDPEFRRLLNLFSDNFCIMSSRWAEIYN 230
Cdd:cd20674   78 RNSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKED-KDTLVQAFHDCVQELLKTWGHWSIQALD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 231 MFPsFMDWIPGPHNRIFKNFQELR-LFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLE-SHFQDETLVMTTHDLF 308
Cdd:cd20674  157 SIP-FLRFFPNPGLRRLKQAVENRdHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQPRGEKGmGQLLEGHVHMAVVDLF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 309 FGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVN 388
Cdd:cd20674  236 IGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRDSS 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 389 LKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQK 468
Cdd:cd20674  316 IAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPG---AANRALLPFGCGARVCLGEPLARLELFVFLARLLQA 392
                        410       420       430
                 ....*....|....*....|....*....|..
gi 154146204 469 FSLLPVGSPANINLNPQCTGLGNVPPaFQLRL 500
Cdd:cd20674  393 FTLLPPSDGALPSLQPVAGINLKVQP-FQVRL 423
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
75-477 4.41e-68

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


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 223.55  E-value: 4.41e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGRstI 154
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAA--L 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 155 EDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDnfcimssrwaeiYNMFPS 234
Cdd:cd00302   79 RPVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLK------------LLGPRL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 235 FMDWIPGPHNRIFKNFQELRLFISEQIQwhwqsrqtgEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTET 314
Cdd:cd00302  147 LRPLPSPRLRRLRRARARLRDYLEELIA---------RRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHET 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 315 TSTTLRYGLLIMLKYPEVAAKVQEELDATVGRtwaPRIEDRARLPYTNAVLHEIQRFISVLPlGLPRALTRDVNLKNHFL 394
Cdd:cd00302  218 TASLLAWALYLLARHPEVQERLRAEIDAVLGD---GTPEDLSKLPYLEAVVEETLRLYPPVP-LLPRVATEDVELGGYTI 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 395 HKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEfqNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPV 474
Cdd:cd00302  294 PAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREE--PRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELV 371

                 ...
gi 154146204 475 GSP 477
Cdd:cd00302  372 PDE 374
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
75-496 5.74e-62

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: 208.59  E-value: 5.74e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRF-TCGNGIVFSN-GPRWHSLRNFALGVLRELGVgrS 152
Cdd:cd11065    2 GPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELmGWGMRLLLMPyGPRWRLHRRLFHQLLNPSAV--R 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 153 TIEDRILEEAACVLDEFqatMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMF 232
Cdd:cd11065   80 KYRPLQELESKQLLRDL---LESPDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGAYLVDFF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 233 PsFMDWIPGPHNRIFKNF-QELRLFISEQIQWHWQS-RQTGEPRDFIDCFLDQMdKEQQDLESHFQDETLVMTTHDLFFG 310
Cdd:cd11065  157 P-FLRYLPSWLGAPWKRKaRELRELTRRLYEGPFEAaKERMASGTATPSFVKDL-LEELDKEGGLSEEEIKYLAGSLYEA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 311 GTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLK 390
Cdd:cd11065  235 GSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPHALTEDDEYE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 391 NHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDD--HGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQK 468
Cdd:cd11065  315 GYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDpkGTPDPPDPPHFAFGFGRRICPGRHLAENSLFIAIARLLWA 394
                        410       420       430
                 ....*....|....*....|....*....|.
gi 154146204 469 FSLLPVGSPANINLNPQ---CTGLGNVPPAF 496
Cdd:cd11065  395 FDIKKPKDEGGKEIPDEpefTDGLVSHPLPF 425
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
75-482 1.22e-57

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: 197.01  E-value: 1.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGN-GIVFS-NGPRWHSLRN------FALGVLRE 146
Cdd:cd20618    1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGqDIVFApYGPHWRHLRKictlelFSAKRLES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 147 LGVGRStiedrilEEAACVLDEF--QATMGAPFDPQQLLDSAVSNVICTVVFGKRY----DYGDPEFRRLLNLFSDNFCI 220
Cdd:cd20618   81 FQGVRK-------EELSHLVKSLleESESGKPVNLREHLSDLTLNNITRMLFGKRYfgesEKESEEAREFKELIDEAFEL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 221 MSSRWAEIYNMFPSFMDWipGPHNRIFKNFQ-ELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDkeQQDLESHFQDET 299
Cdd:cd20618  154 AGAFNIGDYIPWLRWLDL--QGYEKRMKKLHaKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLL--DLDGEGKLSDDN 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 300 LVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGL 379
Cdd:cd20618  230 IKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 380 PRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLD-DHGEFQNND-AFMPFALGKRMCLGAGLARSE 457
Cdd:cd20618  310 PHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLEsDIDDVKGQDfELLPFGSGRRMCPGMPLGLRM 389
                        410       420
                 ....*....|....*....|....*.
gi 154146204 458 IFLFLTAILQKFSL-LPVGSPANINL 482
Cdd:cd20618  390 VQLTLANLLHGFDWsLPGPKPEDIDM 415
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
75-454 7.48e-49

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: 173.42  E-value: 7.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGN-GIVFSN-GPRWHSLRNfaLGVLRELGVGR- 151
Cdd:cd11072    3 GPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGkDIAFAPyGEYWRQMRK--ICVLELLSAKRv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 152 ---STIEDrilEEAACVLDEFQATMGA--PFDPQQLLDSAVSNVICTVVFGKRYDYGD-PEFRRLLNLFSDN---FCIMs 222
Cdd:cd11072   81 qsfRSIRE---EEVSLLVKKIRESASSssPVNLSELLFSLTNDIVCRAAFGRKYEGKDqDKFKELVKEALELlggFSVG- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 223 srwaeiyNMFPS--FMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETL 300
Cdd:cd11072  157 -------DYFPSlgWIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNI 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 301 VMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLP 380
Cdd:cd11072  230 KAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLP 309
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 154146204 381 RALTRDVNLKNHFLHKGTFVIpllVSA---HRDPTQFKDPDHFNPTNFLDDHGEFQNND-AFMPFALGKRMCLGAGLA 454
Cdd:cd11072  310 RECREDCKINGYDIPAKTRVI---VNAwaiGRDPKYWEDPEEFRPERFLDSSIDFKGQDfELIPFGAGRRICPGITFG 384
PTZ00404 PTZ00404
cytochrome P450; Provisional
65-471 1.51e-47

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 171.44  E-value: 1.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  65 RVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVL 144
Cdd:PTZ00404  52 RDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTSSGEYWKRNREIVGKAM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 145 RELGVgrSTIEDrILEEAACVL----DEFQATmGAPFDPQQLLDSAVSNVICTVVF----GKRYDYGDPEFRRLLNLFSD 216
Cdd:PTZ00404 132 RKTNL--KHIYD-LLDDQVDVLiesmKKIESS-GETFEPRYYLTKFTMSAMFKYIFnediSFDEDIHNGKLAELMGPMEQ 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 217 NFCIMSSrwAEIYNMF----PSFMDWIpgphNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLdqmdKEQQDlE 292
Cdd:PTZ00404 208 VFKDLGS--GSLFDVIeitqPLYYQYL----EHTDKNFKKIKKFIKEKYHEHLKTIDPEVPRDLLDLLI----KEYGT-N 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 293 SHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFI 372
Cdd:PTZ00404 277 TDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYK 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 373 SVLPLGLPRALTRDVNLKN-HFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLddhgEFQNNDAFMPFALGKRMCLGA 451
Cdd:PTZ00404 357 PVSPFGLPRSTSNDIIIGGgHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFL----NPDSNDAFMPFSIGPRNCVGQ 432
                        410       420
                 ....*....|....*....|
gi 154146204 452 GLARSEIFLFLTAILQKFSL 471
Cdd:PTZ00404 433 QFAQDELYLAFSNIILNFKL 452
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
75-482 5.03e-43

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: 157.69  E-value: 5.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRdaLVLQADAFSGRGAmaVFDRFTC--GNGIVFSNGPRWHSLRN-----FALGVLRE- 146
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIE--VILSSSKLITKSF--LYDFLKPwlGDGLLTSTGEKWRKRRKlltpaFHFKILESf 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 147 LGVgrstiedrILEEAACVLDEFQATMGAP-FDPQQLLDSAVSNVICTVVFGKRYDY---GDPEFRRLLNLFSDnfcIMS 222
Cdd:cd20628   77 VEV--------FNENSKILVEKLKKKAGGGeFDIFPYISLCTLDIICETAMGVKLNAqsnEDSEYVKAVKRILE---IIL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 223 SRWAEIYnMFPSFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFID---------CFLDQMdkeqqdLES 293
Cdd:cd20628  146 KRIFSPW-LRFDFIFRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDdefgkkkrkAFLDLL------LEA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 294 HFQDETL--------VMTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGR-TWAPRIEDRARLPYTNAV 364
Cdd:cd20628  219 HEDGGPLtdedireeVDT---FMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDdDRRPTLEDLNKMKYLERV 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 365 LHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALG 444
Cdd:cd20628  296 IKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAG 374
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 154146204 445 KRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPANINL 482
Cdd:cd20628  375 PRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGEDLKL 412
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
75-478 4.14e-41

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


Pssm-ID: 410676 [Multi-domain]  Cd Length: 415  Bit Score: 152.35  E-value: 4.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGY-EALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRwHSLRnfalgvlRELGV---- 149
Cdd:cd11053   12 GDVFTLRVPGLGPVVVLSDpEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLLLLDGDR-HRRR-------RKLLMpafh 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 GRS--TIEDRILEEAACVLDEFQatMGAPFDPQQLLDSAVSNVICTVVFGKrydYGDPEFRRLLNLFSDNFCIMSSRWAe 227
Cdd:cd11053   84 GERlrAYGELIAEITEREIDRWP--PGQPFDLRELMQEITLEVILRVVFGV---DDGERLQELRRLLPRLLDLLSSPLA- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 228 iynMFPSFM-DWIP-GPHNRIFKNFQELRLFISEQIQWHwqSRQTGEPRDFIdcfLDQMDKEQQDLESHFQDETL---VM 302
Cdd:cd11053  158 ---SFPALQrDLGPwSPWGRFLRARRRIDALIYAEIAER--RAEPDAERDDI---LSLLLSARDEDGQPLSDEELrdeLM 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 303 TthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGrtwAPRIEDRARLPYTNAVLHEIQRFISVLPLgLPRA 382
Cdd:cd11053  230 T---LLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGG---DPDPEDIAKLPYLDAVIKETLRLYPVAPL-VPRR 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 383 LTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDdhGEFQNNdAFMPFALGKRMCLGAGLARSEIFLFL 462
Cdd:cd11053  303 VKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLG--RKPSPY-EYLPFGGGVRRCIGAAFALLEMKVVL 379
                        410
                 ....*....|....*.
gi 154146204 463 TAILQKFSLLPVGSPA 478
Cdd:cd11053  380 ATLLRRFRLELTDPRP 395
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
75-485 2.59e-40

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: 150.04  E-value: 2.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTcGNGIVFSNGPRWHSLRN-----FALGVLRELGv 149
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYERLKLLL-GNGLLTSEGDLWRRQRRlaqpaFHRRRIAAYA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 grstieDRILEEAACVLDEFQATMG-APFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFcimssrwAEI 228
Cdd:cd20620   79 ------DAMVEATAALLDRWEAGARrGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGDALDVALEYA-------ARR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 229 YNMFPSFMDWIPGPHNRIF-KNFQELRLFISEQIQwhwQSRQTGEPR-DFIDCFLD--------QMDKEQqdleshFQDE 298
Cdd:cd20620  146 MLSPFLLPLWLPTPANRRFrRARRRLDEVIYRLIA---ERRAAPADGgDLLSMLLAardeetgePMSDQQ------LRDE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 299 tlVMTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEIQRFISVLPLg 378
Cdd:cd20620  217 --VMT---LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGR-PPTAEDLPQLPYTEMVLQESLRLYPPAWI- 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 379 LPRALTRDVNLKNHFLHKGT--FVIPLLVsaHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARS 456
Cdd:cd20620  290 IGREAVEDDEIGGYRIPAGStvLISPYVT--HRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMM 367
                        410       420       430
                 ....*....|....*....|....*....|....
gi 154146204 457 EIFLFLTAILQKFSLLPVGSP-----ANINLNPQ 485
Cdd:cd20620  368 EAVLLLATIAQRFRLRLVPGQpvepePLITLRPK 401
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
124-471 5.87e-40

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: 149.21  E-value: 5.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 124 GIVFSNGPRWHSLRnfalgvlrelgvgrSTIEDRIL--EEAAC-------VLDEFQATMGAPFDPQQLLDSAVSN----- 189
Cdd:cd11054   57 GLLNSNGEEWHRLR--------------SAVQKPLLrpKSVASylpaineVADDFVERIRRLRDEDGEEVPDLEDelykw 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 190 ---VICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRWAEIYNMFPSFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQ 266
Cdd:cd11054  123 sleSIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIFESSAKLMFGPPLWKYFPTPAWKKFVKAWDTIFDIASKYVDEALE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 267 SRQTGEPRDFID-CFLDQMdKEQQDLEShfqDETLVMTThDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVG 345
Cdd:cd11054  203 ELKKKDEEDEEEdSLLEYL-LSKPGLSK---KEIVTMAL-DLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLP 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 346 RTWAPRIEDRARLPYTNAVLHEIQRFISVLPlGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNF 425
Cdd:cd11054  278 DGEPITAEDLKKMPYLKACIKESLRLYPVAP-GNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERW 356
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 154146204 426 LDDHGEFQNNDAF--MPFALGKRMCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd11054  357 LRDDSENKNIHPFasLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKV 404
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
74-475 1.54e-39

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: 148.55  E-value: 1.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRG-AMAVFDRFTCGNGIVFSN--GPRWHSLR-NFALGVLRELGV 149
Cdd:cd11075    2 YGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPpANPLRVLFSSNKHMVNSSpyGPLWRTLRrNLVSEVLSPSRL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 GR-STIEDRILEEaacVLDEFQATMGAPFDPQQLLD---SAVSNVICTVVFGKRYDygDPEFRRLLNLFSDnfCIMSSRW 225
Cdd:cd11075   82 KQfRPARRRALDN---LVERLREEAKENPGPVNVRDhfrHALFSLLLYMCFGERLD--EETVRELERVQRE--LLLSFTD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 226 AEIYNMFPSFMdWIPgphNRIFKN-FQELRlfiSEQ-------IQWHWQSRQTGE--PRDFIDCFLDQMDKEQQDLESHF 295
Cdd:cd11075  155 FDVRDFFPALT-WLL---NRRRWKkVLELR---RRQeevllplIRARRKRRASGEadKDYTDFLLLDLLDLKEEGGERKL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 296 QDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVL 375
Cdd:cd11075  228 TDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 376 PLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLdDHGEFQNNDA------FMPFALGKRMCL 449
Cdd:cd11075  308 HFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFL-AGGEAADIDTgskeikMMPFGAGRRICP 386
                        410       420
                 ....*....|....*....|....*.
gi 154146204 450 GAGLARSEIFLFLTAILQKFSLLPVG 475
Cdd:cd11075  387 GLGLATLHLELFVARLVQEFEWKLVE 412
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
74-472 2.88e-38

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 144.49  E-value: 2.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGP--LPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNG---IVFSNGPRWHSLRN-----FALGV 143
Cdd:COG2124   35 YGDYFTLRLPGpgDGFWVVSRPADVREVLRDPRFFSSALGAGLRPRLLRPVLGdgsLLTLDGPEHTRLRKllapaFTPRA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 144 LRELgvgrstiEDRILEEAACVLDEFQAtmGAPFDPQQLLDSAVSNVICTVvFGkrydYGDPEFRRLLnlfsdnfcimss 223
Cdd:COG2124  115 LRGY-------RPLIREIADRLLDDLWQ--GGADLVLDFAAELTLRVIAEL-LG----VPLEDRPQLL------------ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 224 RWAEIYNMFPSFMDWIPGPHNRIFKNFQELRLFISEQIQwhwqSRQTGEPRDFidcfLDQMDKEQQDLESHFQDETLVMT 303
Cdd:COG2124  169 RWSDALLLRLDPDLGPEEPWRRARAARRELDAYLRALIA----ERRAAPRDDL----LSLLLSAEDDGGGRLSDDEIRDE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 304 THDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDAtvgrtwapriedrarlPYTNAVLHEIQRFISVLPLgLPRAL 383
Cdd:COG2124  241 LITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR----------------PLLEAVVEETLRLYPPVPL-ARRVA 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 384 TRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTnflddhgefQNNDAFMPFALGKRMCLGAGLARSEIFLFLT 463
Cdd:COG2124  304 TEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPE---------RFNNAHLPFGGGPHRCLGAALARLELKVALA 374

                 ....*....
gi 154146204 464 AILQKFSLL 472
Cdd:COG2124  375 ELLRRFPLL 383
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
67-474 1.01e-36

cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 140.09  E-value: 1.01e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  67 LMELSSHwGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGrGamAVFDRF--TCGNGIVFSNGPrwHSLRNfalgvl 144
Cdd:cd11049    6 LSSLRAH-GDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKG-G--PLFDRArpLLGNGLATCPGE--DHRRQ------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 145 relgvgRSTIE-----DRILEEAACVLDEFQATMGApFDPQQLLD------SAVSNVICTVVFGKRYDYGD-PEFRRLLN 212
Cdd:cd11049   74 ------RRLMQpafhrSRIPAYAEVMREEAEALAGS-WRPGRVVDvdaemhRLTLRVVARTLFSTDLGPEAaAELRQALP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 213 LFSDNFCIMSSrwaeiynmFPSFMDWIPGPHNRIF-KNFQELRLFISEQIQwhwQSRQTGEPR-DFIDCFLDQMDKEQQD 290
Cdd:cd11049  147 VVLAGMLRRAV--------PPKFLERLPTPGNRRFdRALARLRELVDEIIA---EYRASGTDRdDLLSLLLAARDEEGRP 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 291 L-ESHFQDEtlVMTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEIQ 369
Cdd:cd11049  216 LsDEELRDQ--VIT---LLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGGR-PATFEDLPRLTYTRRVVTEAL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 370 RFISVLPLgLPRALTRDVNLKNHFLHKGTFVI--PLLVsaHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRM 447
Cdd:cd11049  290 RLYPPVWL-LTRRTTADVELGGHRLPAGTEVAfsPYAL--HRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARK 366
                        410       420
                 ....*....|....*....|....*..
gi 154146204 448 CLGAGLARSEIFLFLTAILQKFSLLPV 474
Cdd:cd11049  367 CIGDTFALTELTLALATIASRWRLRPV 393
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
75-472 1.52e-36

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: 140.44  E-value: 1.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGN-GIVFSN-GPRWHSLRNFA------------ 140
Cdd:cd20654    1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYaMFGFAPyGPYWRELRKIAtlellsnrrlek 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 141 LGVLRElgvgrSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRY-----DYGDPEFRRLLNLFS 215
Cdd:cd20654   81 LKHVRV-----SEVDTSIKELYSLWSNNKKGGGGVLVEMKQWFADLTFNVILRMVVGKRYfggtaVEDDEEAERYKKAIR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 216 DNFCIMssrwAEIY--NMFPS--FMDWipGPHNRIFK-NFQELRLFISEQIQWHWQSRQTGE-PRDFIDCFLDQMDKEQQ 289
Cdd:cd20654  156 EFMRLA----GTFVvsDAIPFlgWLDF--GGHEKAMKrTAKELDSILEEWLEEHRQKRSSSGkSKNDEDDDDVMMLSILE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 290 DLESHFQDETLVM--TTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHE 367
Cdd:cd20654  230 DSQISGYDADTVIkaTCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKE 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 368 IQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEF----QNNDaFMPFAL 443
Cdd:cd20654  310 TLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKDIdvrgQNFE-LIPFGS 388
                        410       420
                 ....*....|....*....|....*....
gi 154146204 444 GKRMCLGAGLARSEIFLFLTAILQKFSLL 472
Cdd:cd20654  389 GRRSCPGVSFGLQVMHLTLARLLHGFDIK 417
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
64-473 5.46e-36

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: 138.42  E-value: 5.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  64 DRVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALV---LQADAFSGRGAMAVF-DRFTcGNGIVF-SNGPRWHSLRN 138
Cdd:cd20613    1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLItlnLPKPPRVYSRLAFLFgERFL-GNGLVTeVDHEKWKKRRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 139 -----FALGVLRELGVGRSTIEDR---ILEEAA------CVLDEF-QATMgapfdpqqlldsavsNVICTVVFGKRYD-Y 202
Cdd:cd20613   80 ilnpaFHRKYLKNLMDEFNESADLlveKLSKKAdgktevNMLDEFnRVTL---------------DVIAKVAFGMDLNsI 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 203 GDPEfrrllNLFSDNFCIMssrwaeIYNMFPSFMD--WIPGPHNRIFKN-----FQELRLFISEQIQWHWQSRQTGE--P 273
Cdd:cd20613  145 EDPD-----SPFPKAISLV------LEGIQESFRNplLKYNPSKRKYRRevreaIKFLRETGRECIEERLEALKRGEevP 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 274 RDFidcfLDQMDKEQQDLEShFQDETLV---MTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAP 350
Cdd:cd20613  214 NDI----LTHILKASEEEPD-FDMEELLddfVT---FFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYV 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 351 RIEDRARLPYTNAVLHEIQRFISVLPlGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHG 430
Cdd:cd20613  286 EYEDLGKLEYLSQVLKETLRLYPPVP-GTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAP 364
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 154146204 431 EFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQ--KFSLLP 473
Cdd:cd20613  365 EKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQnfKFELVP 409
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
71-483 1.11e-35

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: 137.66  E-value: 1.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  71 SSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRG---AMAVFDrfTCGNGIVF-SNGPRWHSLR--------- 137
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDvpdAVRALG--HHKSSIVWpPYGPRWRMLRkicttelfs 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 138 NFALGVLRELgvgRSTIEDRILEEAACVLDEfqatmGAPFDPQQLLDSAVSNVICTVVFGKR-YDYGDPEFRRLLNLFSD 216
Cdd:cd11073   79 PKRLDATQPL---RRRKVRELVRYVREKAGS-----GEAVDIGRAAFLTSLNLISNTLFSVDlVDPDSESGSEFKELVRE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 217 nfcIMssRWAEIYNM---FP--SFMDWiPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPR---DFIDCFLDQMDKEQ 288
Cdd:cd11073  151 ---IM--ELAGKPNVadfFPflKFLDL-QGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKkkdDDLLLLLDLELDSE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 289 QDLESHfQDETLVMtthDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRtwAPRIE--DRARLPYTNAVLH 366
Cdd:cd11073  225 SELTRN-HIKALLL---DLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGK--DKIVEesDISKLPYLQAVVK 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 367 EIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFViplLVSA---HRDPTQFKDPDHFNPTNFLDDHGEFQNNDA-FMPFA 442
Cdd:cd11073  299 ETLRLHPPAPLLLPRKAEEDVEVMGYTIPKGTQV---LVNVwaiGRDPSVWEDPLEFKPERFLGSEIDFKGRDFeLIPFG 375
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 154146204 443 LGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVG-SPANINLN 483
Cdd:cd11073  376 SGRRICPGLPLAERMVHLVLASLLHSFDWkLPDGmKPEDLDME 418
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
75-474 1.43e-35

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: 137.33  E-value: 1.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTcGNGIVFSNGPRWHSLRN-----FALGVLRELgv 149
Cdd:cd11055    3 GKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEPF-DSSLLFLKGERWKRLRTtlsptFSSGKLKLM-- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 gRSTIED------RILEEAACVldefqatmGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCimSS 223
Cdd:cd11055   80 -VPIINDccdelvEKLEKAAET--------GKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFR--NS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 224 RWAEIYNMFPSFMDWIPGpHNRIFKNFQELRLFISEQIQWHWQSR---QTGEPRDFIDCFLDQMDKEQQDLESHFQDETL 300
Cdd:cd11055  149 IIRLFLLLLLFPLRLFLF-LLFPFVFGFKSFSFLEDVVKKIIEQRrknKSSRRKDLLQLMLDAQDSDEDVSKKKLTDDEI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 301 VMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQR------FISv 374
Cdd:cd11055  228 VAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRlyppafFIS- 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 375 lplglpRALTRDVNLKNHFLHKGTFV-IPllVSA-HRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAG 452
Cdd:cd11055  307 ------RECKEDCTINGVFIPKGVDVvIP--VYAiHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMR 378
                        410       420
                 ....*....|....*....|..
gi 154146204 453 LARSEIFLFLTAILQKFSLLPV 474
Cdd:cd11055  379 FALLEVKLALVKILQKFRFVPC 400
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
122-485 5.63e-34

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: 132.76  E-value: 5.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 122 GNGIVFSNGPRWHSLRNFalgvlrelgVGRS----TIEDRI--LEEAacVLDEFQATMGAPFDPQQLLDSAVSNVICTVV 195
Cdd:cd20621   48 GKGLLFSEGEEWKKQRKL---------LSNSfhfeKLKSRLpmINEI--TKEKIKKLDNQNVNIIQFLQKITGEVVIRSF 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 196 FGKR----YDYGDPEFRRLLNLFSDNFC-IMSSRWAEIYNMF---PSFmDWIPGPHNRIF-KNFQELRLFISEQIQWHW- 265
Cdd:cd20621  117 FGEEakdlKINGKEIQVELVEILIESFLyRFSSPYFQLKRLIfgrKSW-KLFPTKKEKKLqKRVKELRQFIEKIIQNRIk 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 266 QSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVG 345
Cdd:cd20621  196 QIKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVG 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 346 RTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNF 425
Cdd:cd20621  276 NDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERW 355
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 426 LDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLlpvgspaNINLNPQ 485
Cdd:cd20621  356 LNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEI-------EIIPNPK 408
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
189-471 2.63e-32

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: 128.22  E-value: 2.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 189 NVICTVVFGKRYDYGDPE---FRRLLNLFSDNfcIMSsrwaEIYNMFPsFMDWIPGPHNR-IFKNFQELRLFISEQIQwh 264
Cdd:cd11070  116 NVIGEVGFGFDLPALDEEessLHDTLNAIKLA--IFP----PLFLNFP-FLDRLPWVLFPsRKRAFKDVDEFLSELLD-- 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 265 wQSRQTGEPRDFIDcfLDQMDKEQQDLESHFQDETLvmtTHD--------LFFGGTETTSTTLRYGLLIMLKYPEVAAKV 336
Cdd:cd11070  187 -EVEAELSADSKGK--QGTESVVASRLKRARRSGGL---TEKellgnlfiFFIAGHETTANTLSFALYLLAKHPEVQDWL 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 337 QEELDATVGRT--WAPRIEDRARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNL-----KNHFLHKGTFVIPLLVSAHR 409
Cdd:cd11070  261 REEIDSVLGDEpdDWDYEEDFPKLPYLLAVIYETLRLYPPVQL-LNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHR 339
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 410 DPTQ-FKDPDHFNPTNFLDDHGEFQNND-------AFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd11070  340 DPTIwGPDADEFDPERWGSTSGEIGAATrftpargAFIPFSAGPRACLGRKFALVEFVAALAELFRQYEW 409
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
75-470 3.88e-32

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: 127.30  E-value: 3.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVF-TVWLGPlPAVVLCGYEALRdaLVLQADA--FSGrGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRELGVGR 151
Cdd:cd11043    6 GPVFkTSLFGR-PTVVSADPEANR--FILQNEGklFVS-WYPKSVRKLLGKSSLLTVSGEEHKRLRGLLLSFLGPEALKD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 152 STIEDrILEEAACVLDEFQAtmGAPFDPQQLLDSAVSNVICTVVFGkrydYGDPEFRRllnlfsdnfcIMSSRWAEIYNM 231
Cdd:cd11043   82 RLLGD-IDELVRQHLDSWWR--GKSVVVLELAKKMTFELICKLLLG----IDPEEVVE----------ELRKEFQAFLEG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 232 FPSFMDWIPG-PHNRIFKNFQELRLFISEQIQWHWQSRQTGEPR-DFIDCFLDQMDKEQQDLEshfqDE---TLVMTthd 306
Cdd:cd11043  145 LLSFPLNLPGtTFHRALKARKRIRKELKKIIEERRAELEKASPKgDLLDVLLEEKDEDGDSLT----DEeilDNILT--- 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 307 LFFGGTETTSTTLryglLIMLKY----PEVAAKVQEELDATVGR-------TWapriEDRARLPYTNAVLHEIQRFISVL 375
Cdd:cd11043  218 LLFAGHETTSTTL----TLAVKFlaenPKVLQELLEEHEEIAKRkeegeglTW----EDYKSMKYTWQVINETLRLAPIV 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 376 PlGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFlDDHGEFQNNdAFMPFALGKRMCLGAGLAR 455
Cdd:cd11043  290 P-GVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW-EGKGKGVPY-TFLPFGGGPRLCPGAELAK 366
                        410
                 ....*....|....*
gi 154146204 456 SEIFLFLTAILQKFS 470
Cdd:cd11043  367 LEILVFLHHLVTRFR 381
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
75-487 1.28e-31

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: 126.33  E-value: 1.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRW--------HSLRNFALGVLRE 146
Cdd:cd11046   11 GPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADGEIWkkrrralvPALHKDYLEMMVR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 147 LgVGRSTieDRILEEaacvLDEFQATmGAPFDPQQLLDSAVSNVICTVVFGkrYDYG-----DPEFRRLLNlfsdnfCIM 221
Cdd:cd11046   91 V-FGRCS--ERLMEK----LDAAAET-GESVDMEEEFSSLTLDIIGLAVFN--YDFGsvteeSPVIKAVYL------PLV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 222 S----SRWAEIYNMFPSFMDWIPGpHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDC-----------FLDQMDK 286
Cdd:cd11046  155 EaehrSVWEPPYWDIPAALFIVPR-QRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDylneddpsllrFLVDMRD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 287 EQQDLeSHFQDEtlVMTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLH 366
Cdd:cd11046  234 EDVDS-KQLRDD--LMT---MLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLN 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 367 EIQRFISVLPLGLPRALTRDVnlknhfLHKGTFVIP----LLVS---AHRDPTQFKDPDHFNPTNFLDDHGEFQN----N 435
Cdd:cd11046  308 ESLRLYPQPPVLIRRAVEDDK------LPGGGVKVPagtdIFISvynLHRSPELWEDPEEFDPERFLDPFINPPNevidD 381
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154146204 436 DAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPANINLNPQCT 487
Cdd:cd11046  382 FAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGMTTGAT 433
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
94-477 6.65e-31

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: 124.19  E-value: 6.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  94 EALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRN-----FALGVLRELGVgrstiedrILEEAACVLDE 168
Cdd:cd11056   22 ELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELRQkltpaFTSGKLKNMFP--------LMVEVGDELVD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 169 F---QATMGAPFDPQQLLDSAVSNVICTVVFGKRYD-YGDP--EFRRLLNLFSDNFCIMSSRWAeIYNMFPSFMDWIpgp 242
Cdd:cd11056   94 YlkkQAEKGKELEIKDLMARYTTDVIASCAFGLDANsLNDPenEFREMGRRLFEPSRLRGLKFM-LLFFFPKLARLL--- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 243 hnRIFKNFQELRLFISEQIQWHWQSRQTGEPR--DFIDCFLDQMDKEQQDLEshfqDETLVMTTHDL-------FFGGTE 313
Cdd:cd11056  170 --RLKFFPKEVEDFFRKLVRDTIEYREKNNIVrnDFIDLLLELKKKGKIEDD----KSEKELTDEELaaqafvfFLAGFE 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPrI--EDRARLPYTNAVLHEIQRFISVLPLgLPRALTRD--VNL 389
Cdd:cd11056  244 TSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGE-LtyEALQEMKYLDQVVNETLRKYPPLPF-LDRVCTKDytLPG 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 390 KNHFLHKGTFV-IPLLvSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQK 468
Cdd:cd11056  322 TDVVIEKGTPViIPVY-ALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSN 400

                 ....*....
gi 154146204 469 FSLLPVGSP 477
Cdd:cd11056  401 FRVEPSSKT 409
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
65-503 8.14e-31

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 125.32  E-value: 8.14e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  65 RVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAM--AVFDRFTCGNGIVFSNGPRWHSLRNFALG 142
Cdd:PLN03112  55 RDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTlaAVHLAYGCGDVALAPLGPHWKRMRRICME 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 143 VLRELGVGRSTIEDRILEEAACVLDEF-QATMGAPFDPQQLLDSAVSNVICTVVFGKRY----DYGDPEFRRLLNLFSDN 217
Cdd:PLN03112 135 HLLTTKRLESFAKHRAEEARHLIQDVWeAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYfgaeSAGPKEAMEFMHITHEL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 218 FCIMSSrwaeIY-NMFPSFMDWIP--GPHNRIFKNFQELRLFISEQIQWHWQSRQ----TGEPRDFIDCFLDQmdkEQQD 290
Cdd:PLN03112 215 FRLLGV----IYlGDYLPAWRWLDpyGCEKKMREVEKRVDEFHDKIIDEHRRARSgklpGGKDMDFVDVLLSL---PGEN 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 291 LESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQR 370
Cdd:PLN03112 288 GKEHMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFR 367
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 371 FISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHG---EFQNNDAF--MPFALGK 445
Cdd:PLN03112 368 MHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGsrvEISHGPDFkiLPFSAGK 447
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 154146204 446 RMCLGAGLARSEIFLFLTAILQKF--SLLPVGSPANINLNP--QCTglgnVPPAFQLRLVAR 503
Cdd:PLN03112 448 RKCPGAPLGVTMVLMALARLFHCFdwSPPDGLRPEDIDTQEvyGMT----MPKAKPLRAVAT 505
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
75-469 2.12e-30

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


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 122.71  E-value: 2.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGN-GIVFSN-GPRWHSLRNF----ALGVlRELG 148
Cdd:cd20655    1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSsGFAFAPyGDYWKFMKKLcmteLLGP-RALE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 149 VGRSTIEDRILEEAACVLDefQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSD------NFCIMS 222
Cdd:cd20655   80 RFRPIRAQELERFLRRLLD--KAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKEsaelagKFNASD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 223 SRW--------------AEIYNMFPSFMDwipgphnRIFKNFQELRlfiseqiqwhwQSRQTGEPRDFIDCFLDQmdkeq 288
Cdd:cd20655  158 FIWplkkldlqgfgkriMDVSNRFDELLE-------RIIKEHEEKR-----------KKRKEGGSKDLLDILLDA----- 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 289 qdleshFQDET------------LVMtthDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwapRI---E 353
Cdd:cd20655  215 ------YEDENaeykitrnhikaFIL---DLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKT---RLvqeS 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 354 DRARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTfviPLLVSAH---RDPTQFKDPDHFNPTNFLDDHG 430
Cdd:cd20655  283 DLPNLPYLQAVVKETLRLHPPGPL-LVRESTEGCKINGYDIPEKT---TLFVNVYaimRDPNYWEDPLEFKPERFLASSR 358
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 154146204 431 EFQNNDA------FMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd20655  359 SGQELDVrgqhfkLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCF 403
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
67-490 1.48e-29

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 121.34  E-value: 1.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  67 LMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAvfdrftcGNGIVFSNGprwhslrnfalgvlRE 146
Cdd:PLN03234  54 LFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLK-------GQQTMSYQG--------------RE 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 147 LGVGRSTIEDRILEEAaCVLDEFQATMGAPFDP------QQLLD-------------------SAVSNVICTVVFGKRYD 201
Cdd:PLN03234 113 LGFGQYTAYYREMRKM-CMVNLFSPNRVASFRPvreeecQRMMDkiykaadqsgtvdlselllSFTNCVVCRQAFGKRYN 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 202 YGDPEFRRLLNLFSDNFCIMSSRWaeIYNMFP--SFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQ-SRQTGEPRDFID 278
Cdd:PLN03234 192 EYGTEMKRFIDILYETQALLGTLF--FSDLFPyfGFLDNLTGLSARLKKAFKELDTYLQELLDETLDpNRPKQETESFID 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 279 cFLDQMDKEQQdLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARL 358
Cdd:PLN03234 270 -LLMQIYKDQP-FSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNL 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 359 PYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKD-PDHFNPTNFLDDHG--EFQNN 435
Cdd:PLN03234 348 PYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMKEHKgvDFKGQ 427
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 154146204 436 D-AFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVG-SPANINLNPQcTGLG 490
Cdd:PLN03234 428 DfELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWsLPKGiKPEDIKMDVM-TGLA 484
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
73-471 1.68e-29

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: 120.14  E-value: 1.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  73 HW----GPVFTVWLGPLPAVVLCGYEALRDalVLQAD-AFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRN-----FALG 142
Cdd:cd11052    6 HWikqyGKNFLYWYGTDPRLYVTEPELIKE--LLSKKeGYFGKSPLQPGLKKLLGRGLVMSNGEKWAKHRRianpaFHGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 143 VLRELgvgrstiedrILEEAACV---LDEFQATMG---APFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLfsD 216
Cdd:cd11052   84 KLKGM----------VPAMVESVsdmLERWKKQMGeegEEVDVFEEFKALTADIISRTAFGSSYEEGKEVFKLLREL--Q 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 217 NFCIMSSRwaeiYNMFPsFMDWIPGPHNR-IFKNFQELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDleshf 295
Cdd:cd11052  152 KICAQANR----DVGIP-GSRFLPTKGNKkIKKLDKEIEDSLLEIIKKREDSLKMGRGDDYGDDLLGLLLEANQS----- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 296 QDETLVMTTHDL-------FFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEI 368
Cdd:cd11052  222 DDQNKNMTVQEIvdecktfFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKD-KPPSDSLSKLKTVSMVINES 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 369 QRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDD-HGEFQNNDAFMPFALGKR 446
Cdd:cd11052  301 LRLYPPAVF-LTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGvAKAAKHPMAFLPFGLGPR 379
                        410       420
                 ....*....|....*....|....*
gi 154146204 447 MCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd11052  380 NCIGQNFATMEAKIVLAMILQRFSF 404
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
74-484 3.78e-29

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: 119.13  E-value: 3.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFT-CGNGIVFSN-GPRWHSLR---NFALGVLRELG 148
Cdd:cd20656    1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSrNGQDLIWADyGPHYVKVRklcTLELFTPKRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 149 VGRSTIEDRILEEAACVLDEFQAT--MGAPFDPQQLLDSAVSNVICTVVFGKRY--DYG--DPEFRRLLNLFSDNFCIMS 222
Cdd:cd20656   81 SLRPIREDEVTAMVESIFNDCMSPenEGKPVVLRKYLSAVAFNNITRLAFGKRFvnAEGvmDEQGVEFKAIVSNGLKLGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 223 S-RWAEiynmFPSFMDWIPGPHNRIFKNFQELRLFISEQI-QWHWQSRQT-GEPRDFIDCFLDQmdKEQQDLeshfQDET 299
Cdd:cd20656  161 SlTMAE----HIPWLRWMFPLSEKAFAKHGARRDRLTKAImEEHTLARQKsGGGQQHFVALLTL--KEQYDL----SEDT 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 300 LVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGL 379
Cdd:cd20656  231 VIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLML 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 380 PRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNND-AFMPFALGKRMCLGAGLARSEI 458
Cdd:cd20656  311 PHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDfRLLPFGAGRRVCPGAQLGINLV 390
                        410       420       430
                 ....*....|....*....|....*....|
gi 154146204 459 FLFLTAILQKFSLLPVGS--PANINL--NP 484
Cdd:cd20656  391 TLMLGHLLHHFSWTPPEGtpPEEIDMteNP 420
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
75-471 6.87e-29

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: 118.52  E-value: 6.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRdaLVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHS-------------LRNFaL 141
Cdd:cd20660    1 GPIFRIWLGPKPIVVLYSAETVE--VILSSSKHIDKSFEYDFLHPWLGTGLLTSTGEKWHSrrkmltptfhfkiLEDF-L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 142 GVLRElgvgRSTIEDRILEEAAcvldefqatMGAPFDPQQLLDSAVSNVICTVVFGKRYDY---GDPEFRRLLNLFSDnf 218
Cdd:cd20660   78 DVFNE----QSEILVKKLKKEV---------GKEEFDIFPYITLCALDIICETAMGKSVNAqqnSDSEYVKAVYRMSE-- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 219 cIMSSR------WAE-IYNMFPsfMDWIPGPHNRIFKNFQelRLFISEQIQWHWQSR-QTGEPRDFID-------CFLDq 283
Cdd:cd20660  143 -LVQKRqknpwlWPDfIYSLTP--DGREHKKCLKILHGFT--NKVIQERKAELQKSLeEEEEDDEDADigkrkrlAFLD- 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 284 MDKEQQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVG-RTWAPRIEDRARLPYTN 362
Cdd:cd20660  217 LLLEASEEGTKLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGdSDRPATMDDLKEMKYLE 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 363 AVLHEIQR-FISVLPLGlpRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPF 441
Cdd:cd20660  297 CVIKEALRlFPSVPMFG--RTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPF 374
                        410       420       430
                 ....*....|....*....|....*....|
gi 154146204 442 ALGKRMCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd20660  375 SAGPRNCIGQKFALMEEKVVLSSILRNFRI 404
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
75-450 3.83e-28

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: 116.16  E-value: 3.83e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDalVLQADAFSGRGAMAVFdrFTCGNGIVFSNGPRWHSLR-------------NFA- 140
Cdd:cd11057    1 GSPFRAWLGPRPFVITSDPEIVQV--VLNSPHCLNKSFFYDF--FRLGRGLFSAPYPIWKLQRkalnpsfnpkillSFLp 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 141 ---------LGVLRELgVGRSTIEdrILEEAA-CVLDE-FQATMGAPFDPQQLLDSAVS---NVICTVVFgkrydygdpe 206
Cdd:cd11057   77 ifneeaqklVQRLDTY-VGGGEFD--ILPDLSrCTLEMiCQTTLGSDVNDESDGNEEYLesyERLFELIA---------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 207 fRRLLN--LFSDNFCIMSSRWAE-------IYNMFPSFMDWIpgpHNRIFKNFQELRLFISEQIQwhwqsrqtgEPRDFI 277
Cdd:cd11057  144 -KRVLNpwLHPEFIYRLTGDYKEeqkarkiLRAFSEKIIEKK---LQEVELESNLDSEEDEENGR---------KPQIFI 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 278 DCFLDQMDKEQ----QDLESHFQdeTLVmtthdlfFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAP-RI 352
Cdd:cd11057  211 DQLLELARNGEeftdEEIMDEID--TMI-------FAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQFiTY 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 353 EDRARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNLKN-HFLHKGT-FVIPLLvSAHRDPTQF-KDPDHFNPTNFLDDH 429
Cdd:cd11057  282 EDLQQLVYLEMVLKETMRLFPVGPL-VGRETTADIQLSNgVVIPKGTtIVIDIF-NMHRRKDIWgPDADQFDPDNFLPER 359
                        410       420
                 ....*....|....*....|.
gi 154146204 430 GEFQNNDAFMPFALGKRMCLG 450
Cdd:cd11057  360 SAQRHPYAFIPFSAGPRNCIG 380
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
190-469 9.30e-28

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: 115.09  E-value: 9.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 190 VICTVVFGKRYD---YGDPEFRRLLNLFSDNFCIMSS-RWAEIYNMFPSFMDWIPGPHNRifknFQELRlfiseqiQWHW 265
Cdd:cd11059  114 VVSHLLFGESFGtllLGDKDSRERELLRRLLASLAPWlRWLPRYLPLATSRLIIGIYFRA----FDEIE-------EWAL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 266 QS--------RQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMtthDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQ 337
Cdd:cd11059  183 DLcaraesslAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEAL---DHIVAGHDTTAVTLTYLIWELSRPPNLQEKLR 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 338 EEL-DATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRD-VNLKNHFLHKGTFVIPLLVSAHRDPTQFK 415
Cdd:cd11059  260 EELaGLPGPFRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgATIGGYYIPGGTIVSTQAYSLHRDPEVFP 339
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 154146204 416 DPDHFNPTNFLDDHGEFQN--NDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd11059  340 DPEEFDPERWLDPSGETARemKRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNY 395
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
189-474 9.95e-28

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: 115.06  E-value: 9.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 189 NVICTVVFGkrYDYG---DPE------FRRLLNLFsdnfcIMSSRWAEIYNMFPSFM-DWIPGPHNRIFK-NFQELRLFI 257
Cdd:cd11069  121 DIIGLAGFG--YDFDsleNPDnelaeaYRRLFEPT-----LLGSLLFILLLFLPRWLvRILPWKANREIRrAKDVLRRLA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 258 SEQIQwhwQSRQTGE------PRDFIDCFLDQMDKEQQDLEShfqDETLV--MTThdLFFGGTETTSTTLRYGLLIMLKY 329
Cdd:cd11069  194 REIIR---EKKAALLegkddsGKDILSILLRANDFADDERLS---DEELIdqILT--FLAAGHETTSTALTWALYLLAKH 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 330 PEVAAKVQEELDATV--GRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFV-IPLLVs 406
Cdd:cd11069  266 PDVQERLREEIRAALpdPPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPL-TSREATKDTVIKGVPIPKGTVVlIPPAA- 343
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154146204 407 AHRDPTQF-KDPDHFNPTNFLDD-----HGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPV 474
Cdd:cd11069  344 INRSPEIWgPDAEEFNPERWLEPdgaasPGGAGSNYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELD 417
PLN02183 PLN02183
ferulate 5-hydroxylase
65-493 1.69e-27

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 115.33  E-value: 1.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  65 RVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNG-IVFSN-GPRWHSLRNfaLG 142
Cdd:PLN02183  59 RGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRAdMAFAHyGPFWRQMRK--LC 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 143 VLRELGVGRSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNFCIMS 222
Cdd:PLN02183 137 VMKLFSRKRAESWASVRDEVDSMVRSVSSNIGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDEFIKILQEFSKLFGAFN 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 223 srwaeIYNMFPsFMDWI--PGPHNRIFKNFQELRLFISEQIQWHWQSRQTGEPRDFID-CFLDQMDkeqqDLESHFQDET 299
Cdd:PLN02183 217 -----VADFIP-WLGWIdpQGLNKRLVKARKSLDGFIDDIIDDHIQKRKNQNADNDSEeAETDMVD----DLLAFYSEEA 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 300 LVMTTHDL------------------FFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYT 361
Cdd:PLN02183 287 KVNESDDLqnsikltrdnikaiimdvMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYL 366
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 362 NAVLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLD-DHGEFQNND-AFM 439
Cdd:PLN02183 367 KCTLKETLRLHPPIPL-LLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKpGVPDFKGSHfEFI 445
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154146204 440 PFALGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVG-SPANINLN-------PQCTGLGNVP 493
Cdd:PLN02183 446 PFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWeLPDGmKPSELDMNdvfgltaPRATRLVAVP 508
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
76-469 2.59e-27

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: 114.09  E-value: 2.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  76 PVFTVWLGPLPAVVLcgYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLR-----NFALGVLRELgvg 150
Cdd:cd20680   13 PLLKLWIGPVPFVIL--YHAENVEVILSSSKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRkmltpTFHFTILSDF--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 151 rstiEDRILEEAACVLDEFQATM-GAPFDPQQLLDSAVSNVICTVVFGKRY---DYGDPEFRRLLNLFSDnfcIMSSR-- 224
Cdd:cd20680   88 ----LEVMNEQSNILVEKLEKHVdGEAFNCFFDITLCALDIICETAMGKKIgaqSNKDSEYVQAVYRMSD---IIQRRqk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 225 ----WAE-IYNMFPSFMDwipgpHNrifKNFQELRLF----ISEQIQ-------WHWQSRQTGEP----RDFIDCFLDQM 284
Cdd:cd20680  161 mpwlWLDlWYLMFKEGKE-----HN---KNLKILHTFtdnvIAERAEemkaeedKTGDSDGESPSkkkrKAFLDMLLSVT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 285 DKEQQDLeSHFQDETLVMTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAP-RIEDRARLPYTNA 363
Cdd:cd20680  233 DEEGNKL-SHEDIREEVDT---FMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPvTMEDLKKLRYLEC 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 364 VLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFAL 443
Cdd:cd20680  309 VIKESLRLFPSVPL-FARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSA 387
                        410       420
                 ....*....|....*....|....*.
gi 154146204 444 GKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd20680  388 GPRNCIGQRFALMEEKVVLSCILRHF 413
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
75-469 3.49e-27

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: 113.47  E-value: 3.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEAlRDALVLQAD-AFSGRGAMAVFDRFTCGN-GIVF-SNGPRWHSLRNF-ALGVL--RELG 148
Cdd:cd20653    1 GPIFSLRFGSRLVVVVSSPSA-AEECFTKNDiVLANRPRFLTGKHIGYNYtTVGSaPYGDHWRNLRRItTLEIFssHRLN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 149 VGRSTIEDRILEEAACvLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYdYGD-----PEFRRLLNLFSDnfcIMSS 223
Cdd:cd20653   80 SFSSIRRDEIRRLLKR-LARDSKGGFAKVELKPLFSELTFNNIMRMVAGKRY-YGEdvsdaEEAKLFRELVSE---IFEL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 224 RWAEIYNMFPSFMDWI--PGPHNRIFKNFQELRLFISEQIQWHwQSRQTGEPRDFIDCFLDQmdkeQQDLESHFQDET-- 299
Cdd:cd20653  155 SGAGNPADFLPILRWFdfQGLEKRVKKLAKRRDAFLQGLIDEH-RKNKESGKNTMIDHLLSL----QESQPEYYTDEIik 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 300 -LVMTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwapRI---EDRARLPYTNAVLHEIQRFISVL 375
Cdd:cd20653  230 gLILV---MLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQD---RLieeSDLPKLPYLQNIISETLRLYPAA 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 376 PLGLPRALTRDVNLKNHFLHKGTFvipLLVSA---HRDPTQFKDPDHFNPTNFlddHGEFQNNDAFMPFALGKRMCLGAG 452
Cdd:cd20653  304 PLLVPHESSEDCKIGGYDIPRGTM---LLVNAwaiHRDPKLWEDPTKFKPERF---EGEEREGYKLIPFGLGRRACPGAG 377
                        410
                 ....*....|....*..
gi 154146204 453 LARSEIFLFLTAILQKF 469
Cdd:cd20653  378 LAQRVVGLALGSLIQCF 394
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
190-469 1.65e-26

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: 111.52  E-value: 1.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 190 VICTVVFGKRYDYGDPEfrrllnlfSDNFCIMSSRWAEIYNMFP-SFMDWIpgpHNRIFKNFQELRL-----------FI 257
Cdd:cd11060  114 VIGEITFGKPFGFLEAG--------TDVDGYIASIDKLLPYFAVvGQIPWL---DRLLLKNPLGPKRkdktgfgplmrFA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 258 SEQIQWHWQ--SRQTGEPRDFIDCFLDQMDKEQQDleshFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAK 335
Cdd:cd11060  183 LEAVAERLAedAESAKGRKDMLDSFLEAGLKDPEK----VTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAK 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 336 VQEELDATVGRTWAPRI---EDRARLPYTNAVLHEIQRFISVLPLGLPRALTRD-VNLKNHFLHKGTFVIPLLVSAHRDP 411
Cdd:cd11060  259 LRAEIDAAVAEGKLSSPitfAEAQKLPYLQAVIKEALRLHPPVGLPLERVVPPGgATICGRFIPGGTIVGVNPWVIHRDK 338
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154146204 412 TQF-KDPDHFNPTNFLDDHGE--FQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd11060  339 EVFgEDADVFRPERWLEADEEqrRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRF 399
PLN02966 PLN02966
cytochrome P450 83A1
49-490 5.88e-26

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 110.61  E-value: 5.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  49 LPLLGNLLQLQSGDLDRVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVFS 128
Cdd:PLN02966  37 LPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPHRGHEFISYGRRDMAL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 129 N--GPRWHSLRNFALGVLRElGVGRSTIEDRILEEAACVLDEFQ--ATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGD 204
Cdd:PLN02966 117 NhyTPYYREIRKMGMNHLFS-PTRVATFKHVREEEARRMMDKINkaADKSEVVDISELMLTFTNSVVCRQAFGKKYNEDG 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 205 PEFRRLLNLFSDNFCIMSSRWAEIYNMFPSFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQ-SRQTGEPRDFIDCFLDQ 283
Cdd:PLN02966 196 EEMKRFIKILYGTQSVLGKIFFSDFFPYCGFLDDLSGLTAYMKECFERQDTYIQEVVNETLDpKRVKPETESMIDLLMEI 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 284 MdkEQQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATV---GRTWAPRiEDRARLPY 360
Cdd:PLN02966 276 Y--KEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMkekGSTFVTE-DDVKNLPY 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 361 TNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDDHGEFQNND-AF 438
Cdd:PLN02966 353 FRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDyEF 432
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154146204 439 MPFALGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVG-SPANINLNPQcTGLG 490
Cdd:PLN02966 433 IPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFkLPNGmKPDDINMDVM-TGLA 485
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
311-473 5.89e-26

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 109.97  E-value: 5.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 311 GTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEIQRFISVLPlGLPRALTRDVNLK 390
Cdd:cd11068  242 GHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDD-PPPYEQVAKLRYIRRVLDETLRLWPTAP-AFARKPKEDTVLG 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 391 N-HFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQK 468
Cdd:cd11068  320 GkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQR 399

                 ....*
gi 154146204 469 FSLLP 473
Cdd:cd11068  400 FDFED 404
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
75-480 1.09e-25

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


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 108.95  E-value: 1.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSG-RGAMAVFDRFtCGNGIVFSNGPRWHSLRN-----FALGVLRELG 148
Cdd:cd11083    1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFRRiSSLESVFREM-GINGVFSAEGDAWRRQRRlvmpaFSPKHLRYFF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 149 VGRSTIEDRILEEaacvLDEFQATmGAPFDPQQLLDSAVSNVICTVVFGkrYDY------GDPEFRRLLNLFSdnfcIMS 222
Cdd:cd11083   80 PTLRQITERLRER----WERAAAE-GEAVDVHKDLMRYTVDVTTSLAFG--YDLntlergGDPLQEHLERVFP----MLN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 223 SRwaeIYNMFPsFMDWIPGPHNRIF-KNFQELRLFISEQIQwhwQSRQTG--------EPRDfidcfLDQMDKEQQDLES 293
Cdd:cd11083  149 RR---VNAPFP-YWRYLRLPADRALdRALVEVRALVLDIIA---AARARLaanpalaeAPET-----LLAMMLAEDDPDA 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 294 HFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRA-RLPYTNAVLHEIQRFI 372
Cdd:cd11083  217 RLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEALdRLPYLEAVARETLRLK 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 373 SVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNND--AFMPFALGKRMCLG 450
Cdd:cd11083  297 PVAPL-LFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEPHDpsSLLPFGAGPRLCPG 375
                        410       420       430
                 ....*....|....*....|....*....|
gi 154146204 451 AGLARSEIFLFLTAILQKFSLLPVGSPANI 480
Cdd:cd11083  376 RSLALMEMKLVFAMLCRNFDIELPEPAPAV 405
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
166-471 1.27e-25

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: 108.88  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 166 LDEFQATmGAPFDpqqlLDSAVS----NVICTVVFGKRYDY-GDPEFRrllNLFSDNFCIMSSRWAEIyNMFPSFMDWI- 239
Cdd:cd11062   89 LREAKGT-GEPVN----LDDAFRaltaDVITEYAFGRSYGYlDEPDFG---PEFLDALRALAEMIHLL-RHFPWLLKLLr 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 240 ---------PGPHNRIFKNFQElrlFISEQIQWHWQSRQTGEPRDFIDCFLDQM---DKEQQDL-ESHFQDETLVmtthd 306
Cdd:cd11062  160 slpesllkrLNPGLAVFLDFQE---SIAKQVDEVLRQVSAGDPPSIVTSLFHALlnsDLPPSEKtLERLADEAQT----- 231
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 307 LFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELD-ATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPR-ALT 384
Cdd:cd11062  232 LIGAGTETTARTLSVATFHLLSNPEILERLREELKtAMPDPDSPPSLAELEKLPYLTAVIKEGLRLSYGVPTRLPRvVPD 311
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 385 RDVNLKNHFLHKGTFV---IPLLvsaHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLF 461
Cdd:cd11062  312 EGLYYKGWVIPPGTPVsmsSYFV---HHDEEIFPDPHEFRPERWLGAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLA 388
                        330
                 ....*....|
gi 154146204 462 LTAILQKFSL 471
Cdd:cd11062  389 LAALFRRFDL 398
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
77-474 1.85e-25

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: 108.41  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  77 VFTVWLGPL-PAVVLCGYEALRDalVLQADAFSGRGAMAVFDRFTcGNGIVFSNGPRWHSLRN-----FALGVLRE-LGV 149
Cdd:cd20659    3 AYVFWLGPFrPILVLNHPDTIKA--VLKTSEPKDRDSYRFLKPWL-GDGLLLSNGKKWKRNRRlltpaFHFDILKPyVPV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 150 GRSTIeDRILE--EAACVldefqatMGAPFDpqqlLDSAVS----NVICTVVFGKRYDYGDPEFRrllNLFSDNFCIMSS 223
Cdd:cd20659   80 YNECT-DILLEkwSKLAE-------TGESVE----VFEDISlltlDIILRCAFSYKSNCQQTGKN---HPYVAAVHELSR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 224 RWAE-IYNmFPSFMDWIPG--PHNRIFKNFQELRLFISEQI---------QWHWQSRQTGEPRDFIDCFLDQMDKEQQ-- 289
Cdd:cd20659  145 LVMErFLN-PLLHFDWIYYltPEGRRFKKACDYVHKFAEEIikkrrkeleDNKDEALSKRKYLDFLDILLTARDEDGKgl 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 290 -DLEshFQDETlvmtthDLF-FGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGR----TWapriEDRARLPYTNA 363
Cdd:cd20659  224 tDEE--IRDEV------DTFlFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDrddiEW----DDLSKLPYLTM 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 364 VLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFAL 443
Cdd:cd20659  292 CIKESLRLYPPVPF-IARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSA 370
                        410       420       430
                 ....*....|....*....|....*....|.
gi 154146204 444 GKRMCLGAGLARSEIFLFLTAILQKFSLLPV 474
Cdd:cd20659  371 GPRNCIGQNFAMNEMKVVLARILRRFELSVD 401
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
74-473 1.53e-24

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: 105.44  E-value: 1.53e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVF-TVWLGPlPAVVLCGYEALRDALVLQADAFSGrGAMAVFDRFTCGNGIVFSNGPRwHSLRN------FALGVLRE 146
Cdd:cd11044   21 YGPVFkTHLLGR-PTVFVIGAEAVRFILSGEGKLVRY-GWPRSVRRLLGENSLSLQDGEE-HRRRRkllapaFSREALES 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 147 L-----GVGRSTIEDRILEEAACVLDEFQATMgapFDpqqlldsavsnVICTVVFGKRYDYGDPEFRRLLNLFSDNFciM 221
Cdd:cd11044   98 YvptiqAIVQSYLRKWLKAGEVALYPELRRLT---FD-----------VAARLLLGLDPEVEAEALSQDFETWTDGL--F 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 222 SSRWAeiynmfpsfmdwIPG-PHNRIFKNFQELRLFISEQIQwhwqSRQTGEPRDFIDCfLDQMDKEQQDLESHFQDETL 300
Cdd:cd11044  162 SLPVP------------LPFtPFGRAIRARNKLLARLEQAIR----ERQEEENAEAKDA-LGLLLEAKDEDGEPLSMDEL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 301 VMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDAtVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLp 380
Cdd:cd11044  225 KDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGF- 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 381 RALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNND-AFMPFALGKRMCLGAGLARSEIF 459
Cdd:cd11044  303 RKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPfSLIPFGGGPRECLGKEFAQLEMK 382
                        410
                 ....*....|....*.
gi 154146204 460 LFLTAILQKFS--LLP 473
Cdd:cd11044  383 ILASELLRNYDweLLP 398
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
72-486 1.55e-24

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: 105.61  E-value: 1.55e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  72 SHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTcGNGIVFSNGPRWHSLRN-----FALGVLRE 146
Cdd:cd20641    9 SQYGETFLYWQGTTPRICISDHELAKQVLSDKFGFFGKSKARPEILKLS-GKGLVFVNGDDWVRHRRvlnpaFSMDKLKS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 147 LGVGRSTIEDRILEEAacvldEFQATMGAPFDPQQLLDSAV----SNVICTVVFGKRYDYGDPEFRRLLNLfsdNFCIMS 222
Cdd:cd20641   88 MTQVMADCTERMFQEW-----RKQRNNSETERIEVEVSREFqdltADIIATTAFGSSYAEGIEVFLSQLEL---QKCAAA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 223 SrwaeIYNMFPSFMDWIPGPHN-RIFKNFQELRLFISEQIQwhwqSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETlV 301
Cdd:cd20641  160 S----LTNLYIPGTQYLPTPRNlRVWKLEKKVRNSIKRIID----SRLTSEGKGYGDDLLGLMLEAASSNEGGRRTER-K 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 302 MTTHDL-------FFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISV 374
Cdd:cd20641  231 MSIDEIidecktfFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGP 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 375 LPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDDHGEFQNN-DAFMPFALGKRMCLGAG 452
Cdd:cd20641  311 VIN-IARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHpNALLSFSLGPRACIGQN 389
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 154146204 453 LARSEIFLFLTAILQKF--SLLP--VGSPA-NINLNPQC 486
Cdd:cd20641  390 FAMIEAKTVLAMILQRFsfSLSPeyVHAPAdHLTLQPQY 428
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
67-477 2.23e-24

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: 105.10  E-value: 2.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  67 LMELSshwgpvftvwLGPLPAVVLCGYEALRDalVLQADAF-------SGRGAMavFDRftcgnGIVF-SNGPRWHSLRN 138
Cdd:cd11076    5 LMAFS----------LGETRVVITSHPETARE--ILNSPAFadrpvkeSAYELM--FNR-----AIGFaPYGEYWRNLRR 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 139 ------FALGVLRELGVGRSTIEDRILEEAAcvldEFQATMGAPFDPQQLLDSAVSNVICTVvFGKRYDY--GDPEFRRL 210
Cdd:cd11076   66 iasnhlFSPRRIAASEPQRQAIAAQMVKAIA----KEMERSGEVAVRKHLQRASLNNIMGSV-FGRRYDFeaGNEEAEEL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 211 LNLFSDNFCIMSS-RWAEiynMFPsFMDWI--PGPHNRIFKNFQELRLFISEQIQWHWQSRQTGePRDFIDCF--LDQMD 285
Cdd:cd11076  141 GEMVREGYELLGAfNWSD---HLP-WLRWLdlQGIRRRCSALVPRVNTFVGKIIEEHRAKRSNR-ARDDEDDVdvLLSLQ 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 286 KEQQdleshFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVL 365
Cdd:cd11076  216 GEEK-----LSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 366 HEIQRFISVLP-LGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGE-----FQNNDAFM 439
Cdd:cd11076  291 KETLRLHPPGPlLSWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGadvsvLGSDLRLA 370
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 154146204 440 PFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSP 477
Cdd:cd11076  371 PFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDAK 408
PLN02687 PLN02687
flavonoid 3'-monooxygenase
65-482 2.72e-24

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 106.05  E-value: 2.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  65 RVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGR----GA--MAVfdrftCGNGIVFSN-GPRWHSLR 137
Cdd:PLN02687  57 HTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRppnsGAehMAY-----NYQDLVFAPyGPRWRALR 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 138 N------FALGVLRELGVGRStiedrilEEAACVLDEFQATMG-APFDPQQLLDSAVSNVICTVVFGKRY-----DYGDP 205
Cdd:PLN02687 132 KicavhlFSAKALDDFRHVRE-------EEVALLVRELARQHGtAPVNLGQLVNVCTTNALGRAMVGRRVfagdgDEKAR 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 206 EFRRLLnlfsdnfcIMSSRWAEIYNM--FPSFMDW-----IPGPHNRIFKNFQElrlFISEQIQWHWQSRQTG--EPRDF 276
Cdd:PLN02687 205 EFKEMV--------VELMQLAGVFNVgdFVPALRWldlqgVVGKMKRLHRRFDA---MMNGIIEEHKAAGQTGseEHKDL 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 277 IDCFLDQMDKEQQDLE-SHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDR 355
Cdd:PLN02687 274 LSTLLALKREQQADGEgGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDL 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 356 ARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFL--DDHGEFQ 433
Cdd:PLN02687 354 PQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpgGEHAGVD 433
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 154146204 434 ---NNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVG-SPANINL 482
Cdd:PLN02687 434 vkgSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWeLADGqTPDKLNM 487
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
253-469 3.61e-24

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: 104.59  E-value: 3.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 253 LRLFIS----EQIQWHWQ----------SRQTGEPrDFIDCFLDQMDKEQ----QDLESHFqdeTLVMTthdlffGGTET 314
Cdd:cd11058  163 LRLLIPkslrKKRKEHFQytrekvdrrlAKGTDRP-DFMSYILRNKDEKKgltrEELEANA---SLLII------AGSET 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 315 TSTTLRyGLLIML-KYPEVAAKVQEELdatvgRTWAPRIED-----RARLPYTNAVLHEIQRFISVLPLGLPRALTRD-V 387
Cdd:cd11058  233 TATALS-GLTYYLlKNPEVLRKLVDEI-----RSAFSSEDDitldsLAQLPYLNAVIQEALRLYPPVPAGLPRVVPAGgA 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 388 NLKNHFLHKGTFV-IPLLvSAHRDPTQFKDPDHFNPTNFLDDHGEFQNND---AFMPFALGKRMCLGAGLARSEIFLFLT 463
Cdd:cd11058  307 TIDGQFVPGGTSVsVSQW-AAYRSPRNFHDPDEFIPERWLGDPRFEFDNDkkeAFQPFSVGPRNCIGKNLAYAEMRLILA 385

                 ....*.
gi 154146204 464 AILQKF 469
Cdd:cd11058  386 KLLWNF 391
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
122-482 7.17e-24

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: 104.04  E-value: 7.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 122 GNGIVFSN-GPRWHSLRN------FALGVLRELGVGRSTiedrileEAACVLDEF--QATMGAPFDPQQLLDSAVSNVIC 192
Cdd:cd20657   49 AQDMVFAPyGPRWRLLRKlcnlhlFGGKALEDWAHVREN-------EVGHMLKSMaeASRKGEPVVLGEMLNVCMANMLG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 193 TVVFGKR-----YDYGDPEFR-------RLLNLFSDNFCIMSSRWaeiynmfpsfMDW--IPGPHNRIFKNFQElrlFIS 258
Cdd:cd20657  122 RVMLSKRvfaakAGAKANEFKemvvelmTVAGVFNIGDFIPSLAW----------MDLqgVEKKMKRLHKRFDA---LLT 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 259 EQIQWHwqsRQTGEPRDFIDCFLDQMDKEQQDlesHFQDETLVMTT-----HDLFFGGTETTSTTLRYGLLIMLKYPEVA 333
Cdd:cd20657  189 KILEEH---KATAQERKGKPDFLDFVLLENDD---NGEGERLTDTNikallLNLFTAGTDTSSSTVEWALAELIRHPDIL 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 334 AKVQEELDATVGRTwAPRIE-DRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPT 412
Cdd:cd20657  263 KKAQEEMDQVIGRD-RRLLEsDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPD 341
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154146204 413 QFKDPDHFNPTNFL-------DDHGefqNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVG-SPANINL 482
Cdd:cd20657  342 VWENPLEFKPERFLpgrnakvDVRG---NDFELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWkLPAGqTPEELNM 417
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
67-481 1.19e-23

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 103.78  E-value: 1.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  67 LMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGR--GAMAVFDRFTCGNGIVFSNGPRWHSLRNfaLGVL 144
Cdd:PLN00110  56 LAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRppNAGATHLAYGAQDMVFADYGPRWKLLRK--LSNL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 145 RELGvGRStIED----RILE-----EAACVLDEfqatMGAPFDPQQLLDSAVSNVICTVVFGKR-YDYGDPEfrrlLNLF 214
Cdd:PLN00110 134 HMLG-GKA-LEDwsqvRTVElghmlRAMLELSQ----RGEPVVVPEMLTFSMANMIGQVILSRRvFETKGSE----SNEF 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 215 SDnFCIMSSRWAEIYNM--FPSFMDW-----IPGPHNRIFKNFQELrlfISEQIQWHWQS--RQTGEPRdfidcFLDQMD 285
Cdd:PLN00110 204 KD-MVVELMTTAGYFNIgdFIPSIAWmdiqgIERGMKHLHKKFDKL---LTRMIEEHTASahERKGNPD-----FLDVVM 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 286 KEQQDLEShfqdETLVMTT-----HDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPY 360
Cdd:PLN00110 275 ANQENSTG----EKLTLTNikallLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPY 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 361 TNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEF---QNND- 436
Cdd:PLN00110 351 LQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKidpRGNDf 430
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 154146204 437 AFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVGSPANIN 481
Cdd:PLN00110 431 ELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWkLPDGVELNMD 476
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
81-474 1.83e-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: 102.67  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  81 WLGPLPAVVLCGYEALRDALVLQADAFSG--RGAMAVFDRFtcGNGIVFSNGPRW-------------HSLRNFALGVLR 145
Cdd:cd11064    7 WPGGPDGIVTADPANVEHILKTNFDNYPKgpEFRDLFFDLL--GDGIFNVDGELWkfqrktashefssRALREFMESVVR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 146 ELgvgrstiedriLEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRllNLFSDNFCIMSSRW 225
Cdd:cd11064   85 EK-----------VEKLLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPE--VPFAKAFDDASEAV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 226 AEIYNMFPSF---MDWI-PGPHNRIFKNFQELRLFISEQIQwhwQSRQT--------GEPRDFIDCFLDQMDKEQQDLES 293
Cdd:cd11064  152 AKRFIVPPWLwklKRWLnIGSEKKLREAIRVIDDFVYEVIS---RRREElnsreeenNVREDLLSRFLASEEEEGEPVSD 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 294 HFQDETLVMtthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDA-----TVGRTWAPRIEDRARLPYTNAVLHEI 368
Cdd:cd11064  229 KFLRDIVLN----FILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSklpklTTDESRVPTYEELKKLVYLHAALSES 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 369 QRFISVLPLGlPRALTRDVNLKN-HFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDDHGEFQNNDA--FMPFALG 444
Cdd:cd11064  305 LRLYPPVPFD-SKEAVNDDVLPDgTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLRPESPykFPAFNAG 383
                        410       420       430
                 ....*....|....*....|....*....|
gi 154146204 445 KRMCLGAGLARSEIFLFLTAILQKFSLLPV 474
Cdd:cd11064  384 PRICLGKDLAYLQMKIVAAAILRRFDFKVV 413
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
62-473 2.90e-23

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221  Cd Length: 503  Bit Score: 102.50  E-value: 2.90e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  62 DLD-RVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTcGNG--IVFSN-GPRWHSLR 137
Cdd:PLN02394  50 DLNhRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFT-GKGqdMVFTVyGDHWRKMR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 138 N------FALGVLRELGVGRStiedrilEEAACVLDEFQA---TMGAPFDPQQLLDSAVSNVICTVVFGKRYD-YGDPEF 207
Cdd:PLN02394 129 RimtvpfFTNKVVQQYRYGWE-------EEADLVVEDVRAnpeAATEGVVIRRRLQLMMYNIMYRMMFDRRFEsEDDPLF 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 208 RRLLNLFSDNfcimsSRWAEI--YNmfpsFMDWIP--GPHNR----IFKNFQELRL------FISEQIQWHWQSRQTGEP 273
Cdd:PLN02394 202 LKLKALNGER-----SRLAQSfeYN----YGDFIPilRPFLRgylkICQDVKERRLalfkdyFVDERKKLMSAKGMDKEG 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 274 rdfIDCFLDQMDKEQQDLEshFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIE 353
Cdd:PLN02394 273 ---LKCAIDHILEAQKKGE--INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEP 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 354 DRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLknhflhkGTFVIP----LLVSA---HRDPTQFKDPDHFNPTNFL 426
Cdd:PLN02394 348 DTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKL-------GGYDIPaeskILVNAwwlANNPELWKNPEEFRPERFL 420
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 154146204 427 DDHG--EFQNND-AFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:PLN02394 421 EEEAkvEANGNDfRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLP 470
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
74-473 2.89e-22

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 99.08  E-value: 2.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTcGNG--IVFS-NGPRWHSLRN------FALGVL 144
Cdd:cd11074    3 FGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFT-GKGqdMVFTvYGEHWRKMRRimtvpfFTNKVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 145 RELGVGRStiedrilEEAACVLDEFQATMGAPFDP---QQLLDSAVSNVICTVVFGKRYDY-GDPEFRRLLNLFSDNfci 220
Cdd:cd11074   82 QQYRYGWE-------EEAARVVEDVKKNPEAATEGiviRRRLQLMMYNNMYRIMFDRRFESeDDPLFVKLKALNGER--- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 221 msSRWAEIYNMfpSFMDWIP--GPHNR----IFKNFQELRL------FISEQIQWhwqSRQTGEPRDFIDCFLDQMDKEQ 288
Cdd:cd11074  152 --SRLAQSFEY--NYGDFIPilRPFLRgylkICKEVKERRLqlfkdyFVDERKKL---GSTKSTKNEGLKCAIDHILDAQ 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 289 QDLEshFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEI 368
Cdd:cd11074  225 KKGE--INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKET 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 369 QRFISVLPLGLPRALTRDVNLknhflhkGTFVIP----LLVSA---HRDPTQFKDPDHFNPTNFLDD--HGEFQNND-AF 438
Cdd:cd11074  303 LRLRMAIPLLVPHMNLHDAKL-------GGYDIPaeskILVNAwwlANNPAHWKKPEEFRPERFLEEesKVEANGNDfRY 375
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 154146204 439 MPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd11074  376 LPFGVGRRSCPGIILALPILGITIGRLVQNFELLP 410
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
189-469 3.63e-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: 3.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 189 NVICTVVFGKRYDY-GDPEFRRLLNLFSDNFCIMS----SRWaeiynMFPSFMDWIPGPhnRIFKNFQELRLFISEQIQW 263
Cdd:cd11061  112 DVMGDLAFGKSFGMlESGKDRYILDLLEKSMVRLGvlghAPW-----LRPLLLDLPLFP--GATKARKRFLDFVRAQLKE 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 264 HwQSRQTGEPRDFIDCFLDQMDKEQQDLESH--FQDETLVmtthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELD 341
Cdd:cd11061  185 R-LKAEEEKRPDIFSYLLEAKDPETGEGLDLeeLVGEARL-----LIVAGSDTTATALSAIFYYLARNPEAYEKLRAELD 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 342 ATVGRTWAPRIEDR-ARLPYTNAVLHEIQRFISVLPLGLPRALTRD-VNLKNHFLHKGTFV-IPLLvSAHRDPTQFKDPD 418
Cdd:cd11061  259 STFPSDDEIRLGPKlKSLPYLRACIDEALRLSPPVPSGLPRETPPGgLTIDGEYIPGGTTVsVPIY-SIHRDERYFPDPF 337
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154146204 419 HFNPTNFLDDHGEFQNN-DAFMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd11061  338 EFIPERWLSRPEELVRArSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRY 389
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
110-470 4.88e-22

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: 98.01  E-value: 4.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 110 RGAMAVFdrftCGNGIVFSNGPRWHSLR-----NFAlgvlrelgvgRSTIEDRILEEaacvlDEFQATM------GAPFD 178
Cdd:cd11063   41 RDAFKPL----LGDGIFTSDGEEWKHSRallrpQFS----------RDQISDLELFE-----RHVQNLIkllprdGSTVD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 179 PQQL-----LDSAvsnvicT-VVFGKRYD-----YGDPEFRRLLNLFSD--NFCIMSSRWAEIYNMFPS--FMDwipgpH 243
Cdd:cd11063  102 LQDLffrltLDSA------TeFLFGESVDslkpgGDSPPAARFAEAFDYaqKYLAKRLRLGKLLWLLRDkkFRE-----A 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 244 NRIFKNFqeLRLFISEQIQWHWQSRQTGEPRDFIdcFLDQMDKEQQDLEsHFQDETLvmtthDLFFGGTETTSTTLRYGL 323
Cdd:cd11063  171 CKVVHRF--VDPYVDKALARKEESKDEESSDRYV--FLDELAKETRDPK-ELRDQLL-----NILLAGRDTTASLLSFLF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 324 LIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALtRDVNL-----KNH----FL 394
Cdd:cd11063  241 YELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAV-RDTTLprgggPDGkspiFV 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154146204 395 HKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDdhgEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFS 470
Cdd:cd11063  320 PKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWED---LKRPGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFD 393
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
112-469 7.52e-22

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: 97.32  E-value: 7.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 112 AMAVFDRFTCGNGIVFSNGPRWHSLRN-----FALGVLRELgvgrstiEDRILEEA---ACVLDEFqATMGAPFDPQQLL 183
Cdd:cd11051   36 LRKFLTPLTGGSSLISMEGEEWKRLRKrfnpgFSPQHLMTL-------VPTILDEVeifAAILREL-AESGEVFSLEELT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 184 DSAVSNVICTVVFGKRYDY--GDPEFRRLLNLFSDNfcimssrWAEIYNMFPSFMDWipgphnRIFKnfqelrlfiseqi 261
Cdd:cd11051  108 TNLTFDVIGRVTLDIDLHAqtGDNSLLTALRLLLAL-------YRSLLNPFKRLNPL------RPLR------------- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 262 qwHWQSRQTgeprdfIDCFLDQMDKEQQDLEshfqdetlvMTTHDL---FFGGTETTSTTLRYGLLIMLKYPEVAAKVQE 338
Cdd:cd11051  162 --RWRNGRR------LDRYLKPEVRKRFELE---------RAIDQIktfLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRA 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 339 ELDATVGRTWAPRIEDRA-------RLPYTNAVLHEIQRFISvlPLGLPRALTRDVNL----KNHFLHKGTFVIPLLVSA 407
Cdd:cd11051  225 EHDEVFGPDPSAAAELLRegpellnQLPYTTAVIKETLRLFP--PAGTARRGPPGVGLtdrdGKEYPTDGCIVYVCHHAI 302
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154146204 408 HRDPTQFKDPDHFNPTNFL--DDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd11051  303 HRDPEYWPRPDEFIPERWLvdEGHELYPPKSAWRPFERGPRNCIGQELAMLELKIILAMTVRRF 366
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
272-484 1.07e-21

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: 97.38  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 272 EPRDFID--CFLDQM--DKEQQDLESHFQDETLVMTThdlffGGTETTSTTLRY--GLLIMLKYPEVAAKVQEEL-DATV 344
Cdd:cd11066  202 EIEDGTDkpCIVGNIlkDKESKLTDAELQSICLTMVS-----AGLDTVPLNLNHliGHLSHPPGQEIQEKAYEEIlEAYG 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 345 GRTWAP-RIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPT 423
Cdd:cd11066  277 NDEDAWeDCAAEEKCPYVVALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPE 356
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154146204 424 NFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPANINLNP 484
Cdd:cd11066  357 RWLDASGDLIPGPPHFSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEEPMELDP 417
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
306-474 2.31e-21

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: 96.36  E-value: 2.31e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 306 DLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPlGLPRALT- 384
Cdd:cd20648  241 ELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIP-GNARVIPd 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 385 RDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLdDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTA 464
Cdd:cd20648  320 RDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWL-GKGDTHHPYASLPFGFGKRSCIGRRIAELEVYLALAR 398
                        170
                 ....*....|
gi 154146204 465 ILQKFSLLPV 474
Cdd:cd20648  399 ILTHFEVRPE 408
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
295-473 5.41e-21

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 95.43  E-value: 5.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 295 FQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELD---ATVGRTWAPRIEDRARLPYTNAVLHEIQRF 371
Cdd:PLN02987 263 FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEkirAMKSDSYSLEWSDYKSMPFTQCVVNETLRV 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 372 ISVLPlGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGA 451
Cdd:PLN02987 343 ANIIG-GIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPGY 421
                        170       180
                 ....*....|....*....|..
gi 154146204 452 GLARSEIFLFLTAILQKFSLLP 473
Cdd:PLN02987 422 ELARVALSVFLHRLVTRFSWVP 443
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
75-483 5.68e-21

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: 94.98  E-value: 5.68e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRdaLVLQA--DAFSGRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLReLGVGRS 152
Cdd:cd11042    6 GDVFTFNLLGKKVTVLLGPEANE--FFFNGkdEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFGLNILR-RGKLRG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 153 TIeDRILEEAacvlDEFQATMGApFDPQQLLDSAVSNVICTVV---FGKrydygdpEFRRLLN-----LFSDnfciMSSR 224
Cdd:cd11042   83 YV-PLIVEEV----EKYFAKWGE-SGEVDLFEEMSELTILTASrclLGK-------EVRELLDdefaqLYHD----LDGG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 225 WAEIYNMFPsfmdWIPGPHNRIFKNFQ-ELRLFISEQIQwhwQSRQTG--EPRDFIDCFLDqmdkeqqdleSHFQDETlV 301
Cdd:cd11042  146 FTPIAFFFP----PLPLPSFRRRDRARaKLKEIFSEIIQ---KRRKSPdkDEDDMLQTLMD----------AKYKDGR-P 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 302 MTTHD-------LFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAP-RIEDRARLPYTNAVLHEIQRFIS 373
Cdd:cd11042  208 LTDDEiaglliaLLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDPlTYDVLKEMPLLHACIKETLRLHP 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 374 VLPLgLPRALTRDVNLknhflHKGTFVIP----LLVSA---HRDPTQFKDPDHFNPTNFLDDHGEFQNND--AFMPFALG 444
Cdd:cd11042  288 PIHS-LMRKARKPFEV-----EGGGYVIPkghiVLASPavsHRDPEIFKNPDEFDPERFLKGRAEDSKGGkfAYLPFGAG 361
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 154146204 445 KRMCLGAGLARSEIFLFLTAILQKFSL-LPVGSPANINLN 483
Cdd:cd11042  362 RHRCIGENFAYLQIKTILSTLLRNFDFeLVDSPFPEPDYT 401
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
275-473 5.80e-21

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: 95.17  E-value: 5.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 275 DFIDCFLDQMDKEQQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIED 354
Cdd:cd20650  204 DFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDT 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 355 RARLPYTNAVLHEIQRfisVLPLG--LPRALTRDVNLKNHFLHKGTFV-IPLLVsAHRDPTQFKDPDHFNPTNFLDDHGE 431
Cdd:cd20650  284 VMQMEYLDMVVNETLR---LFPIAgrLERVCKKDVEINGVFIPKGTVVmIPTYA-LHRDPQYWPEPEEFRPERFSKKNKD 359
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 154146204 432 FQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20650  360 NIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKP 401
PLN02290 PLN02290
cytokinin trans-hydroxylase
71-471 1.40e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 94.50  E-value: 1.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  71 SSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAfSGR------GAmavfdRFTCGNGIVFSNGPRWHSLRNF-ALGV 143
Cdd:PLN02290  90 SKQYGKRFIYWNGTEPRLCLTETELIKELLTKYNTV-TGKswlqqqGT-----KHFIGRGLLMANGADWYHQRHIaAPAF 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 144 LRELGVGRSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLfsDNFCIMSS 223
Cdd:PLN02290 164 MGDRLKGYAGHMVECTKQMLQSLQKAVESGQTEVEIGEYMTRLTADIISRTEFDSSYEKGKQIFHLLTVL--QRLCAQAT 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 224 RwaeiYNMFPSfMDWIPGPHNRIFKNFQ-ELRLFISEQIQWHWQSRQTGEP----RDFIDCFLDQMDKEQQDLESHfqDE 298
Cdd:PLN02290 242 R----HLCFPG-SRFFPSKYNREIKSLKgEVERLLMEIIQSRRDCVEIGRSssygDDLLGMLLNEMEKKRSNGFNL--NL 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 299 TLVM-TTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEIQRFISVLPL 377
Cdd:PLN02290 315 QLIMdECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGE-TPSVDHLSKLTLLNMVINESLRLYPPATL 393
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 378 gLPRALTRDVNLKNHFLHKGTFV-IPLLVSAHRDPTQFKDPDHFNPTNFLDDhgEFQNNDAFMPFALGKRMCLGAGLARS 456
Cdd:PLN02290 394 -LPRMAFEDIKLGDLHIPKGLSIwIPVLAIHHSEELWGKDANEFNPDRFAGR--PFAPGRHFIPFAAGPRNCIGQAFAMM 470
                        410
                 ....*....|....*
gi 154146204 457 EIFLFLTAILQKFSL 471
Cdd:PLN02290 471 EAKIILAMLISKFSF 485
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
297-490 2.52e-20

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: 92.28  E-value: 2.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 297 DETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEeldatvgrtwaprieDRARLPytnAVLHEIQRFISVLP 376
Cdd:cd11032  196 DEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRA---------------DPSLIP---GAIEEVLRYRPPVQ 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 377 LgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTnflddhgefQNNDAFMPFALGKRMCLGAGLARS 456
Cdd:cd11032  258 R-TARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDID---------RNPNPHLSFGHGIHFCLGAPLARL 327
                        170       180       190
                 ....*....|....*....|....*....|....
gi 154146204 457 EIFLFLTAILQKFSLLPVGSPANINLNPQCTGLG 490
Cdd:cd11032  328 EARIALEALLDRFPRIRVDPDVPLELIDSPVVFG 361
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
73-471 5.17e-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: 92.13  E-value: 5.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  73 HW----GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTcGNGIVFSNGPRWHSLRN-----FALGV 143
Cdd:cd20639    6 HWrkiyGKTFLYWFGPTPRLTVADPELIREILLTRADHFDRYEAHPLVRQLE-GDGLVSLRGEKWAHHRRvitpaFHMEN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 144 LREL--GVGRSTI------EDRILEEAAC---VLDEFQATmgapfdpqqlldsaVSNVICTVVFGKRYDYGDPEFR---R 209
Cdd:cd20639   85 LKRLvpHVVKSVAdmldkwEAMAEAGGEGevdVAEWFQNL--------------TEDVISRTAFGSSYEDGKAVFRlqaQ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 210 LLNLFSDnfcIMSSRWAEIYNMFPSfmdwipgPHNR-IFKNFQELRLFISEQIQwhwQSRQTGEPRDFIDCFLDQMdkeQ 288
Cdd:cd20639  151 QMLLAAE---AFRKVYIPGYRFLPT-------KKNRkSWRLDKEIRKSLLKLIE---RRQTAADDEKDDEDSKDLL---G 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 289 QDLESHFQDETLVMTTHDL-------FFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYT 361
Cdd:cd20639  215 LMISAKNARNGEKMTVEEIieecktfFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTL 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 362 NAVLHEIQRfisVLP--LGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDD-HGEFQNNDA 437
Cdd:cd20639  295 GMILNETLR---LYPpaVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGvARAAKHPLA 371
                        410       420       430
                 ....*....|....*....|....*....|....
gi 154146204 438 FMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd20639  372 FIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEF 405
PLN02655 PLN02655
ent-kaurene oxidase
65-470 1.23e-19

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 91.34  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  65 RVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGR---GAMAVFDRFTCGngIVFSNGPRWHSL--RNF 139
Cdd:PLN02655  23 RTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRklsKALTVLTRDKSM--VATSDYGDFHKMvkRYV 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 140 ALGVL-----RELGVGRSTIEDRILEEaacVLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKrydygDPEfrrllNLF 214
Cdd:PLN02655 101 MNNLLganaqKRFRDTRDMLIENMLSG---LHALVKDDPHSPVNFRDVFENELFGLSLIQALGE-----DVE-----SVY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 215 SDNFCIMSSRWaEIYNM-----------------FPsFMDWIPgphNRIFknfqELRLFISEQ---------IQWHWQSR 268
Cdd:PLN02655 168 VEELGTEISKE-EIFDVlvhdmmmcaievdwrdfFP-YLSWIP---NKSF----ETRVQTTEFrrtavmkalIKQQKKRI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 269 QTGEPRDfidCFLDQMDKEqqdlESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGrTW 348
Cdd:PLN02655 239 ARGEERD---CYLDFLLSE----ATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCG-DE 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 349 APRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDD 428
Cdd:PLN02655 311 RVTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGE 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 154146204 429 HGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFS 470
Cdd:PLN02655 391 KYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFE 432
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
158-494 2.63e-19

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: 90.04  E-value: 2.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 158 ILEEAACVLDEF--QATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYgDPEFRRLLNLFSDNFCIMssrwAEIYNMFPSF 235
Cdd:cd11041   87 LQEELRAALDEElgSCTEWTEVNLYDTVLRIVARVSARVFVGPPLCR-NEEWLDLTINYTIDVFAA----AAALRLFPPF 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 236 M----DWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQ---TGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTthdlf 308
Cdd:cd11041  162 LrplvAPFLPEPRRLRRLLRRARPLIIPEIERRRKLKKgpkEDKPNDLLQWLIEAAKGEGERTPYDLADRQLALS----- 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 309 FGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVN 388
Cdd:cd11041  237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVT 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 389 LKN-HFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDA---------FMPFALGKRMCLGAGLARSEI 458
Cdd:cd11041  317 LSDgLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKhqfvstspdFLGFGHGRHACPGRFFASNEI 396
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 154146204 459 FLFLTAILQK--FSLLPVGS-PANInlnpqCTGLGNVPP 494
Cdd:cd11041  397 KLILAHLLLNydFKLPEGGErPKNI-----WFGEFIMPD 430
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
76-474 3.59e-19

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 90.05  E-value: 3.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  76 PVFTVWLGPL--PAVVLCGYEALRDALVLQADAFSGrgAMAVFDRFTC---GNGIVFSNGPRWHSLRNFalgvLREL--- 147
Cdd:cd20622    2 PIIQLFIRPFgkPWVIVADFREAQDILMRRTKEFDR--SDFTIDVFGGigpHHHLVKSTGPAFRKHRSL----VQDLmtp 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 148 ----GVGRSTIEDRILEeaacVLDEFQATM----GAPFDPQQLLDSAVSNVICTVVFGKRYDygDPEFRRLLNLFSDN-- 217
Cdd:cd20622   76 sflhNVAAPAIHSKFLD----LIDLWEAKArlakGRPFSAKEDIHHAALDAIWAFAFGINFD--ASQTRPQLELLEAEds 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 218 --------------------FCIMSSRWAEIYNM-----FPSFMDWIPGPHNRIFKNFQELRLFISEQIQWHWQSRQTGE 272
Cdd:cd20622  150 tilpagldepvefpeaplpdELEAVLDLADSVEKsikspFPKLSHWFYRNQPSYRRAAKIKDDFLQREIQAIARSLERKG 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 273 PRDFIDCFLDQM--------DKEQQDLESHFQdetlVMttHDLFFG----GTETTSTTLRYGLLIMLKYPEVAAKVQEEL 340
Cdd:cd20622  230 DEGEVRSAVDHMvrrelaaaEKEGRKPDYYSQ----VI--HDELFGyliaGHDTTSTALSWGLKYLTANQDVQSKLRKAL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 341 DATVGRTWA----PRIED--RARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLL---------- 404
Cdd:cd20622  304 YSAHPEAVAegrlPTAQEiaQARIPYLDAVIEEILRCANTAPI-LSREATVDTQVLGYSIPKGTNVFLLNngpsylsppi 382
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 405 -------VSAHRDPTQF------KDPDHFNPTNFL-----DDHGEFQ-NNDAFMPFALGKRMCLGAGLARSEIFLFLTAI 465
Cdd:cd20622  383 eidesrrSSSSAAKGKKagvwdsKDIADFDPERWLvtdeeTGETVFDpSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLL 462

                 ....*....
gi 154146204 466 LQKFSLLPV 474
Cdd:cd20622  463 VWNFELLPL 471
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
256-482 6.44e-19

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  Cd Length: 444  Bit Score: 88.96  E-value: 6.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 256 FISEQIQwHWQSRQTGEPRDFIDCFLDQMDKEQQDLeshFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAK 335
Cdd:cd20658  198 IIDERIK-QWREGKKKEEEDWLDVFITLKDENGNPL---LTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRK 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 336 VQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFViplLVSAH---RDPT 412
Cdd:cd20658  274 ATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHV---LLSRYglgRNPK 350
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 154146204 413 QFKDPDHFNPTNFLDDHGEF---QNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPANINL 482
Cdd:cd20658  351 VWDDPLKFKPERHLNEDSEVtltEPDLRFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPNVSSVDL 423
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
298-489 1.15e-18

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: 88.05  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 298 ETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPl 377
Cdd:cd20647  236 EEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLP- 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 378 GLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFL-DDHGEFQNNDAFMPFALGKRMCLGAGLARS 456
Cdd:cd20647  315 GNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLrKDALDRVDNFGSIPFGYGIRSCIGRRIAEL 394
                        170       180       190
                 ....*....|....*....|....*....|...
gi 154146204 457 EIFLFLTAILQKFSLLPvgSPANINLNPQCTGL 489
Cdd:cd20647  395 EIHLALIQLLQNFEIKV--SPQTTEVHAKTHGL 425
PLN02738 PLN02738
carotene beta-ring hydroxylase
67-477 1.77e-18

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 88.43  E-value: 1.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  67 LMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSgRGAMAVFDRFTCGNGIVFSNGPRWHSLRNFALGVLRE 146
Cdd:PLN02738 157 LYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSKAYS-KGILAEILEFVMGKGLIPADGEIWRVRRRAIVPALHQ 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 147 LGV-------GRSTieDRILEEaacvLDEfQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDygdpefrrllNLFSDNFC 219
Cdd:PLN02738 236 KYVaamislfGQAS--DRLCQK----LDA-AASDGEDVEMESLFSRLTLDIIGKAVFNYDFD----------SLSNDTGI 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 220 I----MSSRWAEIYNMFPsFMDW-IP-----GPHNR--------IFKNFQEL-----RLFISEQIQWHWQSRQTGEPRdf 276
Cdd:PLN02738 299 VeavyTVLREAEDRSVSP-IPVWeIPiwkdiSPRQRkvaealklINDTLDDLiaickRMVEEEELQFHEEYMNERDPS-- 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 277 IDCFL----DQMDKEQqdleshFQDEtlVMTthdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWaPRI 352
Cdd:PLN02738 376 ILHFLlasgDDVSSKQ------LRDD--LMT---MLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRF-PTI 443
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 353 EDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVnLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNF-LD--DH 429
Cdd:PLN02738 444 EDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDM-LGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpLDgpNP 522
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 154146204 430 GEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL-LPVGSP 477
Cdd:PLN02738 523 NETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFqLAPGAP 571
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
271-472 1.96e-18

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: 87.30  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 271 GEPRDFIDCFLDQMDKEQQDLE-------SHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEEldat 343
Cdd:cd11082  185 EEPTCLLDFWTHEILEEIKEAEeegepppPHSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREE---- 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 344 VGRTWAPRI-----EDRARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNL-KNHFLHKGTFVIPLLVSAHRDPtqFKDP 417
Cdd:cd11082  261 QARLRPNDEppltlDLLEEMKYTRQVVKEVLRYRPPAPM-VPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEP 337
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 154146204 418 DHFNPTNFLDDHGE----FQNndaFMPFALGKRMCLGAGLARSEIFLFLTailqKFSLL 472
Cdd:cd11082  338 DKFDPDRFSPERQEdrkyKKN---FLVFGAGPHQCVGQEYAINHLMLFLA----LFSTL 389
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
193-499 6.70e-18

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: 85.88  E-value: 6.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 193 TVVFGKRYDYGDPEFRRLLNLFSDNFCIMSSRwaeiynmFPSFMdwIPGPHN---RIFKNFQelrlfiseqiQWHwqsRQ 269
Cdd:cd11040  138 EALFGPKLPELDPDLVEDFWTFDRGLPKLLLG-------LPRLL--ARKAYAardRLLKALE----------KYY---QA 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 270 TGEPRDFIDCFLDQMDKEQQDLESHFQDetlvMTTHDL--FFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDA--TVG 345
Cdd:cd11040  196 AREERDDGSELIRARAKVLREAGLSEED----IARAELalLWAINANTIPAAFWLLAHILSDPELLERIREEIEPavTPD 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 346 RTWAPRI---EDRARLPYTNAVLHEIQRFISVLPLglPRALTRDVNLKN-HFLHKGTFV-IPLLVsAHRDPTQF-KDPDH 419
Cdd:cd11040  272 SGTNAILdltDLLTSCPLLDSTYLETLRLHSSSTS--VRLVTEDTVLGGgYLLRKGSLVmIPPRL-LHMDPEIWgPDPEE 348
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 420 FNPTNFLDDHGEFQNND---AFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPANINLNP-QCTGLGNVPPA 495
Cdd:cd11040  349 FDPERFLKKDGDKKGRGlpgAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGMdESPGLGILPPK 428

                 ....
gi 154146204 496 FQLR 499
Cdd:cd11040  429 RDVR 432
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
306-473 7.38e-18

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: 85.48  E-value: 7.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 306 DLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPlGLPRALT- 384
Cdd:cd20646  240 ELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVP-GNARVIVe 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 385 RDVNLKNHFLHKGT-FVIPLLVSAHrDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLT 463
Cdd:cd20646  319 KEVVVGDYLFPKNTlFHLCHYAVSH-DETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALS 397
                        170
                 ....*....|
gi 154146204 464 AILQKFSLLP 473
Cdd:cd20646  398 RLIKRFEVRP 407
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
292-471 1.17e-17

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: 84.86  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 292 ESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRF 371
Cdd:cd20645  219 DNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRL 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 372 ISVLPLgLPRALTRDVNLKNHFLHKGTFvipLLVSAHR---DPTQFKDPDHFNPTNFLDDHGEFqNNDAFMPFALGKRMC 448
Cdd:cd20645  299 TPSVPF-TSRTLDKDTVLGDYLLPKGTV---LMINSQAlgsSEEYFEDGRQFKPERWLQEKHSI-NPFAHVPFGIGKRMC 373
                        170       180
                 ....*....|....*....|...
gi 154146204 449 LGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd20645  374 IGRRLAELQLQLALCWIIQKYQI 396
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
300-479 1.66e-17

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: 84.29  E-value: 1.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 300 LVMTTHDLffggTETTSTTLRYGLLimlKYPEVAAKVQEELDATVGRTwaPRIEDRARLPYTNAVLHEIQRFISVLPLgL 379
Cdd:cd11045  219 LMMAAHDT----TTSTLTSMAYFLA---RHPEWQERLREESLALGKGT--LDYEDLGQLEVTDWVFKEALRLVPPVPT-L 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 380 PRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNND-AFMPFALGKRMCLGAGLARSEI 458
Cdd:cd11045  289 PRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRyAWAPFGGGAHKCIGLHFAGMEV 368
                        170       180
                 ....*....|....*....|...
gi 154146204 459 FLFLTAILQKF--SLLPVGSPAN 479
Cdd:cd11045  369 KAILHQMLRRFrwWSVPGYYPPW 391
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
306-469 2.32e-17

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: 84.00  E-value: 2.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 306 DLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVlPLGLPRALTR 385
Cdd:cd20643  241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPV-AVSLQRYITE 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 386 DVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLD-DHGEFQNndafMPFALGKRMCLGAGLARSEIFLFLTA 464
Cdd:cd20643  320 DLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSkDITHFRN----LGFGFGPRQCLGRRIAETEMQLFLIH 395

                 ....*
gi 154146204 465 ILQKF 469
Cdd:cd20643  396 MLENF 400
PLN02302 PLN02302
ent-kaurenoic acid oxidase
270-486 2.39e-17

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 84.38  E-value: 2.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 270 TGEPRDFIDCFLDQMDKEQQDLEshfqDETLVmtthDLFF----GGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVG 345
Cdd:PLN02302 262 SPRKKDMLDLLLDAEDENGRKLD----DEEII----DLLLmylnAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAK 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 346 RTWAPR----IEDRARLPYTNAVLHEIQRFISVLPLGLPRALTrDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFN 421
Cdd:PLN02302 334 KRPPGQkgltLKDVRKMEYLSQVIDETLRLINISLTVFREAKT-DVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFD 412
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 154146204 422 PTNFlDDHGEfqNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPvgspaninLNPQC 486
Cdd:PLN02302 413 PSRW-DNYTP--KAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLER--------LNPGC 466
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
261-471 2.46e-17

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 84.12  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 261 IQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVMTthdlffGGTETTSTTLRYGLLIMLKYPEVaakvQEEL 340
Cdd:cd20644  200 IQKIYQELAFGRPQHYTGIVAELLLQAELSLEAIKANITELTA------GGVDTTAFPLLFTLFELARNPDV----QQIL 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 341 DATVGRTWAPRIEDRAR----LPYTNAVLHEIQRFISVlPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKD 416
Cdd:cd20644  270 RQESLAAAAQISEHPQKalteLPLLKAALKETLRLYPV-GITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPR 348
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 154146204 417 PDHFNPTNFLDDHGEFQNNDAfMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:cd20644  349 PERYDPQRWLDIRGSGRNFKH-LAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLV 402
PLN02971 PLN02971
tryptophan N-hydroxylase
257-482 5.78e-17

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 83.55  E-value: 5.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 257 ISEQIQWhWQSRQTGEPRDFIDCFLDQMDKEQQDLEShfQDEtLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKV 336
Cdd:PLN02971 289 IDERIKM-WREGKRTQIEDFLDIFISIKDEAGQPLLT--ADE-IKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKA 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 337 QEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKD 416
Cdd:PLN02971 365 MEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSD 444
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154146204 417 PDHFNPTNFLDDHGEF---QNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPANINL 482
Cdd:PLN02971 445 PLSFKPERHLNECSEVtltENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETRVEL 513
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
90-469 6.51e-17

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: 81.96  E-value: 6.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  90 LCGYEALRDALVLQA----DAFSGRGAMAVFDRFTCGNGIVFSNGP---RWHSL--RNFALGVLRELG------VGRSTI 154
Cdd:cd20629    9 RGVYVLLRHDDVMAVlrdpRTFSSETYDATLGGPFLGHSILAMDGEehrRRRRLlqPAFAPRAVARWEepivrpIAEELV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 155 EDRILEEAACVLDEFqaTMGAPFdpqqlldsavsNVICTVVFGKRYDYgdPEFRRLlnlfsdnfcimssrwaeIYNMFPS 234
Cdd:cd20629   89 DDLADLGRADLVEDF--ALELPA-----------RVIYALLGLPEEDL--PEFTRL-----------------ALAMLRG 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 235 FMDWIPGPHNRIFKNFQELRLFISEQIQwhwqsRQTGEPR-DFIDCFLdQMDKEQQDLEshfqDETLVMTTHDLFFGGTE 313
Cdd:cd20629  137 LSDPPDPDVPAAEAAAAELYDYVLPLIA-----ERRRAPGdDLISRLL-RAEVEGEKLD----DEEIISFLRLLLPAGSD 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 314 TTSTTLRYGLLIMLKYPEVAAKVQEeldatvgrtwaprieDRARLPytnAVLHEIQRFISVLpLGLPRALTRDVNLKNHF 393
Cdd:cd20629  207 TTYRALANLLTLLLQHPEQLERVRR---------------DRSLIP---AAIEEGLRWEPPV-ASVPRMALRDVELDGVT 267
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 154146204 394 LHKGTFVIPLLVSAHRDPTQFKDPDHFNPtnFLDDHGEFQnndafmpFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd20629  268 IPAGSLLDLSVGSANRDEDVYPDPDVFDI--DRKPKPHLV-------FGGGAHRCLGEHLARVELREALNALLDRL 334
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
73-478 2.32e-16

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


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 80.92  E-value: 2.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  73 HW----GPVFTVWLGPLPAVVLCGYEALRD-----ALVLQADAFSGRGAMAVFdrftcGNGIVFSNGPRWHSLRNFalgV 143
Cdd:cd20640    6 KWrkqyGPIFTYSTGNKQFLYVSRPEMVKEinlcvSLDLGKPSYLKKTLKPLF-----GGGILTSNGPHWAHQRKI---I 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 144 LRELGVGR-STIEDRILEEAACVLDEFQAT------MGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSd 216
Cdd:cd20640   78 APEFFLDKvKGMVDLMVDSAQPLLSSWEERidraggMAADIVVDEDLRAFSADVISRACFGSSYSKGKEIFSKLRELQK- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 217 nfcIMSSRwaeiyNMFPSFMDW--IPGPHNR-IFKNFQELRLFISEQIQwhwQSRQTGEP-RDFIDCFLDQMDKEQQDLE 292
Cdd:cd20640  157 ---AVSKQ-----SVLFSIPGLrhLPTKSNRkIWELEGEIRSLILEIVK---EREEECDHeKDLLQAILEGARSSCDKKA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 293 SHfqDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEE-LDATVGRtwAPRIEDRARLPYTNAVLHEIQRF 371
Cdd:cd20640  226 EA--EDFIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEvLEVCKGG--PPDADSLSRMKTVTMVIQETLRL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 372 ISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLDD-HGEFQNNDAFMPFALGKRMCL 449
Cdd:cd20640  302 YPPAAF-VSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGvAAACKPPHSYMPFGAGARTCL 380
                        410       420       430
                 ....*....|....*....|....*....|...
gi 154146204 450 GAGLARSEIFLFLTAILQKFSLLP----VGSPA 478
Cdd:cd20640  381 GQNFAMAELKVLVSLILSKFSFTLspeyQHSPA 413
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
74-472 2.89e-16

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: 81.04  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRfTCGNGIVFSNGPRWHSLRN-----FALGVLRELG 148
Cdd:cd20649    2 YGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLITK-PMSDSLLCLRDERWKRVRSiltpaFSAAKMKEMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 149 VGRSTIEDRILEEaacvLDEFqATMGAPFDPQQLLDSAVSNVICTVVFGKRYD-YGDPEfrrllnlfsDNFCIMSSRWAE 227
Cdd:cd20649   81 PLINQACDVLLRN----LKSY-AESGNAFNIQRCYGCFTMDVVASVAFGTQVDsQKNPD---------DPFVKNCKRFFE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 228 IYNMFP------SFmDWIPGPHNRIF--KNFQELRLFISEQIQWHWQSRQTGEP----RDFIDCFLD------------- 282
Cdd:cd20649  147 FSFFRPililflAF-PFIMIPLARILpnKSRDELNSFFTQCIRNMIAFRDQQSPeerrRDFLQLMLDartsakflsvehf 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 283 ----QMDKE-------QQDLESHFQDETLVMTTHDLFFG--------GTETTSTTLRYGLLIMLKYPEVAAKVQEELDAT 343
Cdd:cd20649  226 divnDADESaydghpnSPANEQTKPSKQKRMLTEDEIVGqafifliaGYETTTNTLSFATYLLATHPECQKKLLREVDEF 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 344 VGRTWAPRIEDRARLPYTNAVLHEIQRfisVLP--LGLPRALTRDVNLKNHFLHKGTfVIPLLVSA-HRDPTQFKDPDHF 420
Cdd:cd20649  306 FSKHEMVDYANVQELPYLDMVIAETLR---MYPpaFRFAREAAEDCVVLGQRIPAGA-VLEIPVGFlHHDPEHWPEPEKF 381
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154146204 421 NPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLL 472
Cdd:cd20649  382 IPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
74-484 3.47e-16

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 80.75  E-value: 3.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  74 WGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAmAVFDRFTCGNGIVFSNGPRWHSLRNFalgVLREL--GVGR 151
Cdd:PLN02196  68 YGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFP-ASKERMLGKQAIFFHQGDYHAKLRKL---VLRAFmpDAIR 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 152 STIEDriLEEAAcvLDEFQATMGAPFDPQQLLDSAVSNVICTVVFGKRYDYGDPEFRRLLNLFSDNfcimssrwaeiYNM 231
Cdd:PLN02196 144 NMVPD--IESIA--QESLNSWEGTQINTYQEMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKG-----------YNS 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 232 FPSFmdwIPGP-HNRIFKNFQELRLFISEQIQwhwQSRQTGEPR-DFIDCFLDqmDKEQqdleshFQDETLVMTTHDLFF 309
Cdd:PLN02196 209 MPIN---LPGTlFHKSMKARKELAQILAKILS---KRRQNGSSHnDLLGSFMG--DKEG------LTDEQIADNIIGVIF 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 310 GGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGR-------TWapriEDRARLPYTNAVLHEIQRFISVLPLGLpRA 382
Cdd:PLN02196 275 AARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDkeegeslTW----EDTKKMPLTSRVIQETLRVASILSFTF-RE 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 383 LTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFlddhgEFQ-NNDAFMPFALGKRMCLGAGLARSEIFLF 461
Cdd:PLN02196 350 AVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF-----EVApKPNTFMPFGNGTHSCPGNELAKLEISVL 424
                        410       420
                 ....*....|....*....|...
gi 154146204 462 LTAILQKFSLLPVGSPANINLNP 484
Cdd:PLN02196 425 IHHLTTKYRWSIVGTSNGIQYGP 447
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
86-469 5.83e-16

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: 79.53  E-value: 5.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  86 PAVVLCGYEALRDalVLQADAFSgRGAMAVFD--RFT---CGNGIVFSNGPRWHS-LRNFalgVLRELGVGR-STIEDRI 158
Cdd:cd11031   24 EAWLVTRYADVRQ--VLADPRFS-RAAAAPPDapRLTpepLLPGSLMSMDPPEHTrLRRL---VAKAFTARRvERLRPRI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 159 LEEAACVLDEFQATmGAPFDpqqlLDSAVSN-----VICTVvFGkrYDYGD-PEFRRLlnlfSDNFCIMSSRWAEiynmf 232
Cdd:cd11031   98 EEIADELLDAMEAQ-GPPAD----LVEALALplpvaVICEL-LG--VPYEDrERFRAW----SDALLSTSALTPE----- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 233 psfmdwipgphnRIFKNFQELRLFISEQIqwhWQSRQtgEPR-DFIDCFLDQMDKEqqdleSHFQDETLVMTTHDLFFGG 311
Cdd:cd11031  161 ------------EAEAARQELRGYMAELV---AARRA--EPGdDLLSALVAARDDD-----DRLSEEELVTLAVGLLVAG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 312 TETTSTTLRYGLLIMLKYPEvaakvqeeldatvgrTWAPRIEDRARLPytNAVlHEIQRFISVLPL-GLPRALTRDVNLK 390
Cdd:cd11031  219 HETTASQIGNGVLLLLRHPE---------------QLARLRADPELVP--AAV-EELLRYIPLGAGgGFPRYATEDVELG 280
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154146204 391 NHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd11031  281 GVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDREPNPH---------LAFGHGPHHCLGAPLARLELQVALGALLRRL 350
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
295-473 7.83e-16

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: 79.05  E-value: 7.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 295 FQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEeldatvgrtwaprieDRARLPytnAVLHEIQRFISV 374
Cdd:cd11080  189 LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA---------------DRSLVP---RAIAETLRYHPP 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 375 LPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPtnFLDDHGEFQnndAFMP------FALGKRMC 448
Cdd:cd11080  251 VQL-IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNI--HREDLGIRS---AFSGaadhlaFGSGRHFC 324
                        170       180
                 ....*....|....*....|....*
gi 154146204 449 LGAGLARSEIflfLTAILQKFSLLP 473
Cdd:cd11080  325 VGAALAKREI---EIVANQVLDALP 346
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
296-469 5.38e-15

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: 76.44  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 296 QDETLVMTTHdLFFGGTETTSTTLRYGLLIMLKYPEVAAKVqeeldatvgrtwapriedRARLPYTNAVLHEIQRFISvl 375
Cdd:cd20625  199 EDELVANCIL-LLVAGHETTVNLIGNGLLALLRHPEQLALL------------------RADPELIPAAVEELLRYDS-- 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 376 PLGL-PRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRMCLGAGLA 454
Cdd:cd20625  258 PVQLtARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITRAPNRH---------LAFGAGIHFCLGAPLA 328
                        170
                 ....*....|....*
gi 154146204 455 RSEIFLFLTAILQKF 469
Cdd:cd20625  329 RLEAEIALRALLRRF 343
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
275-473 6.06e-15

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: 76.93  E-value: 6.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 275 DFIDCFLDQMDKEQQDLeshfQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGR----TWap 350
Cdd:cd20678  219 DFLDILLFAKDENGKSL----SDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDgdsiTW-- 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 351 riEDRARLPYTNAVLHEIQRFISVLPlGLPRALTRDVNLKN-HFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDH 429
Cdd:cd20678  293 --EHLDQMPYTTMCIKEALRLYPPVP-GISRELSKPVTFPDgRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPEN 369
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 154146204 430 GEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20678  370 SSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLP 413
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
302-471 9.32e-15

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


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 76.16  E-value: 9.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 302 MTTHDL-------FFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEIQRFISV 374
Cdd:cd20642  230 MSTEDVieecklfYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNN-KPDFEGLNHLKVVTMILYEVLRLYPP 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 375 LpLGLPRALTRDVNLKNHFLHKGTFV-IPLLVsAHRDPTQF-KDPDHFNPTNFLDDHGEFQNND-AFMPFALGKRMCLGA 451
Cdd:cd20642  309 V-IQLTRAIHKDTKLGDLTLPAGVQVsLPILL-VHRDPELWgDDAKEFNPERFAEGISKATKGQvSYFPFGWGPRICIGQ 386
                        170       180
                 ....*....|....*....|
gi 154146204 452 GLARSEIFLFLTAILQKFSL 471
Cdd:cd20642  387 NFALLEAKMALALILQRFSF 406
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
307-484 1.40e-14

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: 75.15  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 307 LFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDAtvgrtwapriedrarlpYTNAvLHEIQRFISVLPLGLPRALTRD 386
Cdd:cd20630  211 LIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPEL-----------------LRNA-LEEVLRWDNFGKMGTARYATED 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 387 VNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNflddhgEFQNNDAfmpFALGKRMCLGAGLARSEIFLFLTAIL 466
Cdd:cd20630  273 VELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR------DPNANIA---FGYGPHFCIGAALARLELELAVSTLL 343
                        170
                 ....*....|....*...
gi 154146204 467 QKFSLLPVGSPANINLNP 484
Cdd:cd20630  344 RRFPEMELAEPPVFDPHP 361
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
288-469 1.43e-14

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: 75.25  E-value: 1.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 288 QQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEeldatvgrtwaprieDRARLPytNAVlHE 367
Cdd:cd11030  197 EHGAPGELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALRA---------------DPSLVP--GAV-EE 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 368 IQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRM 447
Cdd:cd11030  259 LLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITRPARRH---------LAFGHGVHQ 329
                        170       180
                 ....*....|....*....|..
gi 154146204 448 CLGAGLARSEIFLFLTAILQKF 469
Cdd:cd11030  330 CLGQNLARLELEIALPTLFRRF 351
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
65-473 1.64e-14

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: 75.50  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  65 RVLMELSSHWGPVFTVWLGP-LPAVVLCGYEALRDalVLQADAFSGRGAMaVFDRFT---CGNGIVFSNGPRWHSLRN-- 138
Cdd:cd20679    2 QVVTQLVATYPQGCLWWLGPfYPIIRLFHPDYIRP--VLLASAAVAPKDE-LFYGFLkpwLGDGLLLSSGDKWSRHRRll 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 139 ---FALGVLRE----LGVGRSTIED---RILEEAACVLDEFQ--ATMgapfdpqqLLDSAVSnviCTVVFG-----KRYD 201
Cdd:cd20679   79 tpaFHFNILKPyvkiFNQSTNIMHAkwrRLASEGSARLDMFEhiSLM--------TLDSLQK---CVFSFDsncqeKPSE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 202 YgdpeFRRLLNLfsdnfcimSSRWAEIYNMFPSFMDWI--PGPHNRIFK-------NF-----QELRLFISEQ-IQWHWQ 266
Cdd:cd20679  148 Y----IAAILEL--------SALVVKRQQQLLLHLDFLyyLTADGRRFRracrlvhDFtdaviQERRRTLPSQgVDDFLK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 267 SRQTGEPRDFIDCFLDQMDKEQQDLeshfQDETlVMTTHDLF-FGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVG 345
Cdd:cd20679  216 AKAKSKTLDFIDVLLLSKDEDGKEL----SDED-IRAEADTFmFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLK 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 346 RTWAPRIE--DRARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNLKN-HFLHKGTFVIPLLVSAHRDPTQFKDPDHFNP 422
Cdd:cd20679  291 DREPEEIEwdDLAQLPFLTMCIKESLRLHPPVTA-ISRCCTQDIVLPDgRVIPKGIICLISIYGTHHNPTVWPDPEVYDP 369
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 154146204 423 TNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLP 473
Cdd:cd20679  370 FRFDPENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVLP 420
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
252-469 1.25e-13

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: 72.25  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 252 ELRLFISEQIQWhwqsRQTgEPRDfiDCFLDQMDKEQQDLEShFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPE 331
Cdd:cd11078  170 ELWAYFADLVAE----RRR-EPRD--DLISDLLAAADGDGER-LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPD 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 332 VaakvQEELDAtvgrtwaprieDRARLPytNAVlHEIQRFISVLPlGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDP 411
Cdd:cd11078  242 Q----WRRLRA-----------DPSLIP--NAV-EETLRYDSPVQ-GLRRTATRDVEIGGVTIPAGARVLLLFGSANRDE 302
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 154146204 412 TQFKDPDHFNPTNflddhgefQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd11078  303 RVFPDPDRFDIDR--------PNARKHLTFGHGIHFCLGAALARMEARIALEELLRRL 352
PLN02500 PLN02500
cytochrome P450 90B1
285-470 1.26e-13

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 72.97  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 285 DKEQQDL------ESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGR---------TWa 349
Cdd:PLN02500 259 SVEEDDLlgwvlkHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAkkqsgeselNW- 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 350 priEDRARLPYTNAVLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDH 429
Cdd:PLN02500 338 ---EDYKKMEFTQCVINETLRLGNVVRF-LHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNN 413
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 154146204 430 -------GEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFS 470
Cdd:PLN02500 414 nrggssgSSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFN 461
PLN02936 PLN02936
epsilon-ring hydroxylase
307-471 1.65e-13

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 72.52  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 307 LFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGrTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRD 386
Cdd:PLN02936 286 MLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVED 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 387 VNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHG---EFQNNDAFMPFALGKRMCLGAGLARSEIFLFLT 463
Cdd:PLN02936 365 VLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPvpnETNTDFRYIPFSGGPRKCVGDQFALLEAIVALA 444

                 ....*...
gi 154146204 464 AILQKFSL 471
Cdd:PLN02936 445 VLLQRLDL 452
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
254-496 1.78e-13

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: 72.15  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 254 RLFISEQIQWHWQSRQTGEP-----RDFIDCFLDQMDK--EQQDLESHFQDETlvmtthDLFFGGTETTSTTLRYGLLIM 326
Cdd:cd20638  184 RNLIHAKIEENIRAKIQREDteqqcKDALQLLIEHSRRngEPLNLQALKESAT------ELLFGGHETTASAATSLIMFL 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 327 LKYPEVAAKVQEELDATVGRTWAPR------IEDRARLPYTNAVLHEIQRFISVLPLGLPRALtRDVNLKNHFLHKGTFV 400
Cdd:cd20638  258 GLHPEVLQKVRKELQEKGLLSTKPNenkelsMEVLEQLKYTGCVIKETLRLSPPVPGGFRVAL-KTFELNGYQIPKGWNV 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 401 IPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPANI 480
Cdd:cd20638  337 IYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNGPPTM 416
                        250
                 ....*....|....*.
gi 154146204 481 NLNPQCTGLGNVPPAF 496
Cdd:cd20638  417 KTSPTVYPVDNLPAKF 432
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
297-477 1.99e-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: 71.79  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 297 DETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEeldatvgrtwaprieDRARLPytNAVlHEIQRFISvlp 376
Cdd:cd11033  207 DEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRA---------------DPSLLP--TAV-EEILRWAS--- 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 377 lglP-----RALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRMCLGA 451
Cdd:cd11033  266 ---PvihfrRTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITRSPNPH---------LAFGGGPHFCLGA 333
                        170       180
                 ....*....|....*....|....*..
gi 154146204 452 GLARSEIFLFLTAILQKF-SLLPVGSP 477
Cdd:cd11033  334 HLARLELRVLFEELLDRVpDIELAGEP 360
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
323-482 3.06e-13

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: 71.19  E-value: 3.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 323 LLIMLKYPEVAAKVQEELDATVGRTWAPRI----EDRARLPYT-NAVLHEIqRFISvlPLGLPRALTRDVNLKNhflhkg 397
Cdd:cd20635  234 LAFILSHPSVYKKVMEEISSVLGKAGKDKIkiseDDLKKMPYIkRCVLEAI-RLRS--PGAITRKVVKPIKIKN------ 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 398 tFVIP----LLVS---AHRDPTQFKDPDHFNPTNFLD-DHGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQK- 468
Cdd:cd20635  305 -YTIPagdmLMLSpywAHRNPKYFPDPELFKPERWKKaDLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKy 383
                        170
                 ....*....|....*.
gi 154146204 469 -FSLL-PVGSPANINL 482
Cdd:cd20635  384 dFTLLdPVPKPSPLHL 399
PLN00168 PLN00168
Cytochrome P450; Provisional
49-469 5.19e-13

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 71.13  E-value: 5.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  49 LPLLGNLLQLQSGDLDRVLMELSSHWGPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGRGAMAVFDRFTCGNGIVF- 127
Cdd:PLN00168  45 LLGSLVWLTNSSADVEPLLRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTITr 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 128 -SNGPRWHSL-RNFalgVLRELGVGRSTIEDRILEEAACVLDEFQATMGAPFDPQQLLDSAVSNVICTVV---FGKRYD- 201
Cdd:PLN00168 125 sSYGPVWRLLrRNL---VAETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVlmcFGERLDe 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 202 -----YGDPEfRRLLNLFSDNFCIMSSRWAEIYNMFPSFMDWIPGPHNRIFKNFQELrlfISEQIQWHWQSRQTGEP--- 273
Cdd:PLN00168 202 pavraIAAAQ-RDWLLYVSKKMSVFAFFPAVTKHLFRGRLQKALALRRRQKELFVPL---IDARREYKNHLGQGGEPpkk 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 274 -----RDFIDCFLDQmdKEQQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTw 348
Cdd:PLN00168 278 ettfeHSYVDTLLDI--RLPEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDD- 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 349 APRI--EDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFL 426
Cdd:PLN00168 355 QEEVseEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFL 434
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 154146204 427 DDhGEFQNNDA-------FMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:PLN00168 435 AG-GDGEGVDVtgsreirMMPFGVGRRICAGLGIAMLHLEYFVANMVREF 483
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
233-469 9.78e-13

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


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 69.29  E-value: 9.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 233 PSFMDWIpgpHNRIFKNFQELRL----FISEQIQWHWQSRQTGEPRDFIDCFLDQ-MDKEQqdleshFQDETLVMTTHDL 307
Cdd:cd11034  128 ERLRDWV---HAILHDEDPEEGAaafaELFGHLRDLIAERRANPRDDLISRLIEGeIDGKP------LSDGEVIGFLTLL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 308 FFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDAtvgrtwapriedrarLPytNAVlHEIQRFISVLpLGLPRALTRDV 387
Cdd:cd11034  199 LLGGTDTTSSALSGALLWLAQHPEDRRRLIADPSL---------------IP--NAV-EEFLRFYSPV-AGLARTVTQEV 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 388 NLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRMCLGAGLARSEIFLFLTAILQ 467
Cdd:cd11034  260 EVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTPNRH---------LAFGSGVHRCLGSHLARVEARVALTEVLK 330

                 ..
gi 154146204 468 KF 469
Cdd:cd11034  331 RI 332
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
313-477 4.75e-12

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: 67.77  E-value: 4.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 313 ETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTwAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVnLKNH 392
Cdd:cd20616  238 DTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGER-DIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDV-IDGY 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 393 FLHKGTFVIPLLVSAHRDPTqFKDPDHFNPTNFlddhgefQNN---DAFMPFALGKRMCLGAGLARSEIFLFLTAILQKF 469
Cdd:cd20616  316 PVKKGTNIILNIGRMHRLEF-FPKPNEFTLENF-------EKNvpsRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRF 387

                 ....*...
gi 154146204 470 SLLPVGSP 477
Cdd:cd20616  388 QVCTLQGR 395
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
270-470 7.86e-12

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


Pssm-ID: 215600  Cd Length: 452  Bit Score: 67.07  E-value: 7.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 270 TGEPRDFIDCFLdqmdkeqQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEE------LDAT 343
Cdd:PLN03141 229 TGIPKDVVDVLL-------RDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLTEEnmklkrLKAD 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 344 VGRT--WAprieDRARLPYTNAVLHEIQRFISVLpLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFN 421
Cdd:PLN03141 302 TGEPlyWT----DYMSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFN 376
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 154146204 422 PTNFLDDHGefqNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFS 470
Cdd:PLN03141 377 PWRWQEKDM---NNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFR 422
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
245-478 1.90e-11

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: 65.46  E-value: 1.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 245 RIFKNFQELRLFISEQIQwhwqsRQTGEPRDfiDcFLDQMDKEQQDlESHFQDETLVMTTHDLFFGGTETTSTTLRYGLL 324
Cdd:cd11038  169 RIEAAVEELYDYADALIE-----ARRAEPGD--D-LISTLVAAEQD-GDRLSDEELRNLIVALLFAGVDTTRNQLGLAML 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 325 IMLKYPEVAAKVQEEldatvgrtwaPRIEDRArlpytnavLHEIQRFISVLPLgLPRALTRDVNLKNHFLHKGTFVIPLL 404
Cdd:cd11038  240 TFAEHPDQWRALRED----------PELAPAA--------VEEVLRWCPTTTW-ATREAVEDVEYNGVTIPAGTVVHLCS 300
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 154146204 405 VSAHRDPTQFkDPDHFNPTnflddhgefQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPA 478
Cdd:cd11038  301 HAANRDPRVF-DADRFDIT---------AKRAPHLGFGGGVHHCLGAFLARAELAEALTVLARRLPTPAIAGEP 364
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
75-493 2.55e-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: 65.30  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVftVWLGPLPAVVLCGYEALRDALVlQADAF-SGRG-AMAVFDRFTCGNGIVFSNGPRWHSLRnfalGVL-RELGVGR 151
Cdd:cd11037   13 GPV--VYLEKYDVYALARYDEVRAALR-DHETFsSARGvGLNDFLNWRLPGSILASDPPEHDRLR----AVLsRPLSPRA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 152 -STIEDRILEEAACVLDEFQAtmGAPFDpqqlldsAVSNVICTV---VFGKRYDYGDPEFRRLLnlfsdnfcimssRWAE 227
Cdd:cd11037   86 lRKLRDRIEEAADELVDELVA--RGEFD-------AVTDLAEAFplrVVPDLVGLPEEGRENLL------------PWAA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 228 I-YNMFpsfmdwipGPHNRIFKN----FQELRLFISEQIQwhwqsRQTGEPRDFIDCFLDQMDkeqqdlESHFQDETLVM 302
Cdd:cd11037  145 AtFNAF--------GPLNERTRAalprLKELRDWVAEQCA-----RERLRPGGWGAAIFEAAD------RGEITEDEAPL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 303 TTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEeldatvgrtwaprieDRARLPytNAVLhEIQRFISVLPlGLPRA 382
Cdd:cd11037  206 LMRDYLSAGLDTTISAIGNALWLLARHPDQWERLRA---------------DPSLAP--NAFE-EAVRLESPVQ-TFSRT 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 383 LTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRMCLGAGLARSEIFLFL 462
Cdd:cd11037  267 TTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITRNPSGH---------VGFGHGVHACVGQHLARLEGEALL 337
                        410       420       430
                 ....*....|....*....|....*....|.
gi 154146204 463 TAILQKFSLLPVGSPANINLNPQCTGLGNVP 493
Cdd:cd11037  338 TALARRVDRIELAGPPVRALNNTLRGLASLP 368
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
289-469 4.28e-11

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: 64.47  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 289 QDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEeldatvgrtwaprieDRARLPytNAVlHEI 368
Cdd:cd11029  201 RDEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRA---------------DPELWP--AAV-EEL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 369 QRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRMC 448
Cdd:cd11029  263 LRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITRDANGH---------LAFGHGIHYC 333
                        170       180
                 ....*....|....*....|.
gi 154146204 449 LGAGLARSEIFLFLTAILQKF 469
Cdd:cd11029  334 LGAPLARLEAEIALGALLTRF 354
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
307-473 1.92e-10

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: 62.22  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 307 LFFGGTETTSTTLRYGLLIMLKYPEVaakvQEELdatvgrtwaprIEDRARLPytnAVLHEIQRFISvlPLGLPRALTRD 386
Cdd:cd11035  198 LFLAGLDTVASALGFIFRHLARHPED----RRRL-----------REDPELIP---AAVEELLRRYP--LVNVARIVTRD 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 387 VNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHgefqnndafMPFALGKRMCLGAGLARSEIFLFLTAIL 466
Cdd:cd11035  258 VEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDRKPNRH---------LAFGAGPHRCLGSHLARLELRIALEEWL 328
                        170
                 ....*....|
gi 154146204 467 QK---FSLLP 473
Cdd:cd11035  329 KRipdFRLAP 338
PLN02774 PLN02774
brassinosteroid-6-oxidase
284-462 4.53e-10

brassinosteroid-6-oxidase


Pssm-ID: 178373  Cd Length: 463  Bit Score: 61.72  E-value: 4.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 284 MDKEQQdlESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGR-------TWapriEDRA 356
Cdd:PLN02774 251 MRKEGN--RYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEHLAIRERkrpedpiDW----NDYK 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 357 RLPYTNAVLHEIQRFISVLPlGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNd 436
Cdd:PLN02774 325 SMRFTRAVIFETSRLATIVN-GVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHNY- 402
                        170       180
                 ....*....|....*....|....*.
gi 154146204 437 aFMPFALGKRMCLGAGLARSEIFLFL 462
Cdd:PLN02774 403 -FFLFGGGTRLCPGKELGIVEISTFL 427
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
253-455 3.03e-09

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: 59.08  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 253 LRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLESHFQDETLVmtthDLFFGGTETTSTTLRYGLLIMLKYPEV 332
Cdd:cd20636  185 LHEYMEKAIEEKLQRQQAAEYCDALDYMIHSARENGKELTMQELKESAV----ELIFAAFSTTASASTSLVLLLLQHPSA 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 333 AAKVQEELDA---TVGRTWAP---RIEDRARLPYTNAVLHEIQRFISVLPLGLPRALtRDVNLKNHFLHKGTFVIPLLVS 406
Cdd:cd20636  261 IEKIRQELVShglIDQCQCCPgalSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTAL-QTFELDGYQIPKGWSVMYSIRD 339
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 154146204 407 AH------RDPTQFkDPDHFNPTNFLDDHGEFQnndaFMPFALGKRMCLGAGLAR 455
Cdd:cd20636  340 THetaavyQNPEGF-DPDRFGVEREESKSGRFN----YIPFGGGVRSCIGKELAQ 389
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
264-473 3.81e-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: 58.51  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 264 HWQSRQTGEprdfidcflDQMDKEQQDLESHFQDETLVMTTHdLFFGGTETTSTTLryGLLI--MLKYPEVAAkvqeeld 341
Cdd:cd20612  162 SFQLRRAAQ---------AAAARLGALLDAAVADEVRDNVLG-TAVGGVPTQSQAF--AQILdfYLRRPGAAH------- 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 342 atvgrtWAPRIEDRARLPYTNAVLH----EIQRFISVLPlGLPRALTRDVNLK-----NHFLHKGTFVIPLLVSAHRDPT 412
Cdd:cd20612  223 ------LAEIQALARENDEADATLRgyvlEALRLNPIAP-GLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPR 295
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 154146204 413 QFKDPDHFNPTnflddhgefQNNDAFMPFALGKRMCLGAGLARSeiflFLTAILQKFSLLP 473
Cdd:cd20612  296 AFPDPERFRLD---------RPLESYIHFGHGPHQCLGEEIARA----ALTEMLRVVLRLP 343
PLN03018 PLN03018
homomethionine N-hydroxylase
224-470 5.86e-09

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 58.48  E-value: 5.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 224 RWAEIYNmfpsfmdwIPGPHNRIFKNFQELRLF----ISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLEShfQDET 299
Cdd:PLN03018 246 RWLRGWN--------IDGQEERAKVNVNLVRSYnnpiIDERVELWREKGGKAAVEDWLDTFITLKDQNGKYLVT--PDEI 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 300 LVMTThDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGL 379
Cdd:PLN03018 316 KAQCV-EFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVP 394
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 380 PRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHG------EFQNNDAFMPFALGKRMCLGAGL 453
Cdd:PLN03018 395 PHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDGitkevtLVETEMRFVSFSTGRRGCVGVKV 474
                        250
                 ....*....|....*..
gi 154146204 454 ARSEIFLFLTAILQKFS 470
Cdd:PLN03018 475 GTIMMVMMLARFLQGFN 491
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
297-465 8.89e-09

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: 57.45  E-value: 8.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 297 DETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVGRTWAPRieDRARLPYTNAVLHEIQRFISVLP 376
Cdd:cd20614  206 EQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAGDVPRTPA--ELRRFPLAEALFRETLRLHPPVP 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 377 LgLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGEFQNNDaFMPFALGKRMCLGAGLARS 456
Cdd:cd20614  284 F-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPNPVE-LLQFGGGPHFCLGYHVACV 361

                 ....*....
gi 154146204 457 EIFLFLTAI 465
Cdd:cd20614  362 ELVQFIVAL 370
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
251-465 2.47e-08

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: 56.01  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 251 QELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLE-SHFQDETLvmtthDLFFGGTETTSTTLRYGLLIMLKY 329
Cdd:cd20637  182 DSLQKSLEKAIREKLQGTQGKDYADALDILIESAKEHGKELTmQELKDSTI-----ELIFAAFATTASASTSLIMQLLKH 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 330 PEVAAKVQEELDAT-VGRTWAP-----RIEDRARLPYTNAVLHEIQRFISVLPLGLpRALTRDVNLKNHFLHKGTFVIPL 403
Cdd:cd20637  257 PGVLEKLREELRSNgILHNGCLcegtlRLDTISSLKYLDCVIKEVLRLFTPVSGGY-RTALQTFELDGFQIPKGWSVLYS 335
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 154146204 404 LVSAHRDPTQFKDPDHFNPTNFLDDHGEfqNNDA---FMPFALGKRMCLGAGLARseIFLFLTAI 465
Cdd:cd20637  336 IRDTHDTAPVFKDVDAFDPDRFGQERSE--DKDGrfhYLPFGGGVRTCLGKQLAK--LFLKVLAV 396
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
321-499 2.47e-08

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: 56.15  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 321 YGLLimlKYPEVAAKVQEELDATVGRT-------WAPRI--EDRARLPYTNAVLHEIQRFISV------------LPLGL 379
Cdd:cd20632  240 YYLL---RHPEALAAVRDEIDHVLQSTgqelgpdFDIHLtrEQLDSLVYLESAINESLRLSSAsmnirvvqedftLKLES 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 380 pralTRDVNLKnhflhKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLDDHGE---FQNNDA-----FMPFALGKRMCLGA 451
Cdd:cd20632  317 ----DGSVNLR-----KGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKkttFYKRGQklkyyLMPFGSGSSKCPGR 387
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 154146204 452 GLARSEIFLFLTAILQKFSLLPVGSPANINLNPQCTGLGNVPPAFQLR 499
Cdd:cd20632  388 FFAVNEIKQFLSLLLLYFDLELLEEQKPPGLDNSRAGLGILPPNSDVR 435
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
289-473 4.42e-08

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 55.56  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 289 QDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDA-TVGRTWAPRIEDR------------ 355
Cdd:PLN03195 282 EDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKAlEKERAKEEDPEDSqsfnqrvtqfag 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 356 -------ARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPTNFLD 427
Cdd:PLN03195 362 lltydslGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIK 441
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 154146204 428 DhGEFQNND--AFMPFALGKRMCLGAGLARSEIFLFLtAILQ---KFSLLP 473
Cdd:PLN03195 442 D-GVFQNASpfKFTAFQAGPRICLGKDSAYLQMKMAL-ALLCrffKFQLVP 490
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
311-478 2.40e-07

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 53.16  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 311 GTETTSTTLRYGLLIMLKYPEVAAKVQEELDATVG-RTWAPRIEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNL 389
Cdd:PLN02426 305 GRDTVASALTSFFWLLSKHPEVASAIREEADRVMGpNQEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLP 384
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 390 KNHFLHKGTFVIPLLVSAHRDPtQFKDPDH--FNPTNFLDDhGEFQNNDAF-MP-FALGKRMCLGAGLARSEIFLFLTAI 465
Cdd:PLN02426 385 DGTFVAKGTRVTYHPYAMGRME-RIWGPDCleFKPERWLKN-GVFVPENPFkYPvFQAGLRVCLGKEMALMEMKSVAVAV 462
                        170
                 ....*....|...
gi 154146204 466 LQKFSLLPVGSPA 478
Cdd:PLN02426 463 VRRFDIEVVGRSN 475
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
363-478 2.56e-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: 2.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 363 AVLHEIQRFISVLPlGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTnflddhgefQNNDAFMPFA 442
Cdd:cd11079  229 AAIDEILRLDDPFV-ANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPD---------RHAADNLVYG 298
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 154146204 443 LGKRMCLGAGLARSEIFLFLTAILQKFS--LLPVGSPA 478
Cdd:cd11079  299 RGIHVCPGAPLARLELRILLEELLAQTEaiTLAAGGPP 336
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
267-471 3.05e-07

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 52.70  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 267 SRQTGEP--RDFIDCFLDqMDKEQQDLESHFQDETLVMTTHDLFFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDATV 344
Cdd:PLN02169 268 SRAETEPysKDALTYYMN-VDTSKYKLLKPKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKF 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 345 GRtwapriEDRARLPYTNAVLHEIQRFISVLPLGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQF-KDPDHFNPT 423
Cdd:PLN02169 347 DN------EDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPE 420
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 154146204 424 NFLDDHGEFQNNDA--FMPFALGKRMCLGAGLARSEIFLFLTAILQKFSL 471
Cdd:PLN02169 421 RWISDNGGLRHEPSykFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDF 470
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
298-493 4.98e-07

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 51.66  E-value: 4.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 298 ETLVMTTHDLFFG-GTETTSTTLRYGLLIMLKYPEVAakvqeELDATvgrtwapRIEDRarlpytNAVLHEIQRFISVlP 376
Cdd:cd20619  188 ESEAIATILVFYAvGHMAIGYLIASGIELFARRPEVF-----TAFRN-------DESAR------AAIINEMVRMDPP-Q 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 377 LGLPRALTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNptnflddHGEFQNNDAFMPFALGKRMCLGAGLARS 456
Cdd:cd20619  249 LSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFD-------HTRPPAASRNLSFGLGPHSCAGQIISRA 321
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 154146204 457 EIFLFLTAILQKFSLLPVGSPANINLNPQCTGLGNVP 493
Cdd:cd20619  322 EATTVFAVLAERYERIELAEEPTVAHNDFARRYRKLP 358
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
75-480 7.14e-07

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: 51.52  E-value: 7.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  75 GPVFTVWLGPLPAVVLCGYEALRDALVLQADAFSGR--GAMAVFDRFTcGNGIVFSNGPRWHSLR-------------NF 139
Cdd:cd20615    1 GPIYRIWSGPTPEIVLTTPEHVKEFYRDSNKHHKAPnnNSGWLFGQLL-GQCVGLLSGTDWKRVRkvfdpafshsaavYY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 140 ALGVLRElgvGRSTIEDriLEEAACVLDEFQatmgapFDPQQLLDSAVSNVICTVVFGKrydYGDPEFRRLLNLFSDNFC 219
Cdd:cd20615   80 IPQFSRE---ARKWVQN--LPTNSGDGRRFV------IDPAQALKFLPFRVIAEILYGE---LSPEEKEELWDLAPLREE 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 220 IMSSRWAEIYNMFpSFMDWIPGPHNRIFKNFQ-ELRLFISEQIQWHWQSRQTGEPRDFIDCFLDQMDKEQQDLesHFQDE 298
Cdd:cd20615  146 LFKYVIKGGLYRF-KISRYLPTAANRRLREFQtRWRAFNLKIYNRARQRGQSTPIVKLYEAVEKGDITFEELL--QTLDE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 299 TLvmtthdlfFGGTETTSTTLRYGLLIMLKYPEVAAKVQEELDAtvgRTWAPRIEDRARLPYTNAVLH----EIQRFISV 374
Cdd:cd20615  223 ML--------FANLDVTTGVLSWNLVFLAANPAVQEKLREEISA---AREQSGYPMEDYILSTDTLLAycvlESLRLRPL 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 375 LPLGLPRALTRDVNLKNHFLHKGTFVIpllVSA----HRDPTQFKDPDHFNPTNFLD-DHGEFQNNdaFMPFALGKRMCL 449
Cdd:cd20615  292 LAFSVPESSPTDKIIGGYRIPANTPVV---VDTyalnINNPFWGPDGEAYRPERFLGiSPTDLRYN--FWRFGFGPRKCL 366
                        410       420       430
                 ....*....|....*....|....*....|.
gi 154146204 450 GAGLARSEIFLFLTAILQKFSLLPVGSPANI 480
Cdd:cd20615  367 GQHVADVILKALLAHLLEQYELKLPDQGENE 397
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
330-478 1.16e-06

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: 50.54  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 330 PEVAAKVQEELDAtvgrtwAPRIEDRarlPYTNAVLHEIQRFISVLPLGLpRALTRDVNLKNHFLHKGTFVIPLLVSAHR 409
Cdd:cd20624  222 PEQAARAREEAAV------PPGPLAR---PYLRACVLDAVRLWPTTPAVL-RESTEDTVWGGRTVPAGTGFLIFAPFFHR 291
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 154146204 410 DPTQFKDPDHFNPTNFLDdhGEFQNNDAFMPFALGKRMCLGAGLARSEIFLFLTAILQKFSLLPVGSPA 478
Cdd:cd20624  292 DDEALPFADRFVPEIWLD--GRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLESPR 358
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
77-431 1.39e-06

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: 50.34  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204  77 VFTVWLGPLP-------AVVLC---GYEALRD-ALVLQADAFSGrgAMAVFDRFTCGNGIV---FSNGPRWHSLRNFALG 142
Cdd:cd11071   11 VFRVNMPPGPpissdprVVALLdakSFPVLFDnSKVEKEDVFGG--TYMPSTSFTGGYRVLpylDTSEPKHAKLKAFLFE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 143 VLRELGvgrstieDRILEEAACVLDEFQATM------GAPFDPQQLLDSAVSNVICTVVFGKRYDYGDpefrrllnlFSD 216
Cdd:cd11071   89 LLKSRS-------SRFIPEFRSALSELFDKWeaelakKGKASFNDDLEKLAFDFLFRLLFGADPSETK---------LGS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 217 NFCIMSSRWAeIYNMFPSFmdWIPGPHnriFKNFQELRLFI--SEQIQWHWQsrqtgEPRDFIDCF-LDQMDKEQQDLES 293
Cdd:cd11071  153 DGPDALDKWL-ALQLAPTL--SLGLPK---ILEELLLHTFPlpFFLVKPDYQ-----KLYKFFANAgLEVLDEAEKLGLS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 294 HfqDETLvmttHDLFF-------GGTettSTTLRygllIMLKY-----PEVAAKVQEELDATVGRTWAPRIEDRARLPYT 361
Cdd:cd11071  222 R--EEAV----HNLLFmlgfnafGGF---SALLP----SLLARlglagEELHARLAEEIRSALGSEGGLTLAALEKMPLL 288
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 154146204 362 NAVLHEIQRFISVLPLGLPRAlTRDVNLKNH---FL-HKGTFV---IPLlvsAHRDPTQFKDPDHFNPTNFLDDHGE 431
Cdd:cd11071  289 KSVVYETLRLHPPVPLQYGRA-RKDFVIESHdasYKiKKGELLvgyQPL---ATRDPKVFDNPDEFVPDRFMGEEGK 361
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
323-496 1.16e-05

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: 47.76  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 323 LLIMLKYPEVAAKVQEELDATVGRT-WAPRI---------EDRARLPYTNAVLHEIQRFISVlPLGLpRALTRDVNLknH 392
Cdd:cd20631  251 LFYLLRCPEAMKAATKEVKRTLEKTgQKVSDggnpivltrEQLDDMPVLGSIIKEALRLSSA-SLNI-RVAKEDFTL--H 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 393 FLHKGTFVI---------PLLVsaHRDPTQFKDPDHFNPTNFLDDHGE----FQNNDA-----FMPFALGKRMCLGAGLA 454
Cdd:cd20631  327 LDSGESYAIrkddiialyPQLL--HLDPEIYEDPLTFKYDRYLDENGKekttFYKNGRklkyyYMPFGSGTSKCPGRFFA 404
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 154146204 455 RSEIFLFLTAILQKFSL-LPVGSPANINLNPQCTGLGNVPPAF 496
Cdd:cd20631  405 INEIKQFLSLMLCYFDMeLLDGNAKCPPLDQSRAGLGILPPTH 447
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
397-455 2.20e-04

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 43.25  E-value: 2.20e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 154146204 397 GTFVIPLLVSAHRDPTQFKDPDHFNPTnflddhgefQNNDAFMPFALGKRMCLGAGLAR 455
Cdd:cd11036  256 GDHVVVLLAAANRDPEAFPDPDRFDLG---------RPTARSAHFGLGRHACLGAALAR 305
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
336-458 6.15e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 42.10  E-value: 6.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 336 VQEELDATVGRTWA----PriEDRARLPYTNA----VLHEIQRFISvlPLGL-PRALTRDVNLKNHFLHKGTFVIPLLVS 406
Cdd:cd11039  215 LNEPRDAIAGTCWGllsnP--EQLAEVMAGDVhwlrAFEEGLRWIS--PIGMsPRRVAEDFEIRGVTLPAGDRVFLMFGS 290
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 154146204 407 AHRDPTQFKDPDHFNptnflddhgEFQNNDAFMPFALGKRMCLGAGLARSEI 458
Cdd:cd11039  291 ANRDEARFENPDRFD---------VFRPKSPHVSFGAGPHFCAGAWASRQMV 333
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
323-471 6.51e-04

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  Cd Length: 449  Bit Score: 41.97  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 323 LLIMLKYPEVAAKVQEELDATVGRT-------WAPRIEDRARL---PYTNAVLHEIQRfISVLPLgLPRALTRDVNLK-- 390
Cdd:cd20633  248 LLYLLKHPEAMKAVREEVEQVLKETgqevkpgGPLINLTRDMLlktPVLDSAVEETLR-LTAAPV-LIRAVVQDMTLKma 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 391 ---NHFLHKGTFV--IPLLvSAHRDPTQFKDPDHFNPTNFLDDHG----EFQNNDA-----FMPFALGKRMCLGAGLARS 456
Cdd:cd20633  326 ngrEYALRKGDRLalFPYL-AVQMDPEIHPEPHTFKYDRFLNPDGgkkkDFYKNGKklkyyNMPWGAGVSICPGRFFAVN 404
                        170
                 ....*....|....*
gi 154146204 457 EIFLFLTAILQKFSL 471
Cdd:cd20633  405 EMKQFVFLMLTYFDL 419
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
348-427 4.49e-03

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 39.43  E-value: 4.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 154146204 348 WAPRIEDRARlPYTNAVLHEIQRFISVLPLGLPRAlTRDVNLKNHFLHKGTFVIPLLVSAHRDPTQFKDPDHFNPTNFLD 427
Cdd:cd11067  253 WRERLRSGDE-DYAEAFVQEVRRFYPFFPFVGARA-RRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLG 330
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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