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Conserved domains on  [gi|19743565|ref|NP_000765|]
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cytochrome P450 2F1 precursor [Homo sapiens]

Protein Classification

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 ...
62-486 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  Cd Length: 425  Bit Score: 857.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20669   1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20669  81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20669 161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20669 241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20669 321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
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 ...
62-486 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  Cd Length: 425  Bit Score: 857.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20669   1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20669  81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20669 161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20669 241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20669 321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20669 401 LGAPEDIDLTPLSSGLGNVPRPFQL 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
31-488 2.62e-173

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: 495.26  E-value: 2.62e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565    31 PPGPRPLSILGNLLLLCSQDMLTS-LTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFT- 108
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSvFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   109 --KGNGIAFSSGDRWKVLRQFSIQILRNFGmgKRSIEERILEEGSFLLAELRKTEGEP--FDPTFVLSRSVSNIICSVLF 184
Cdd:pfam00067  81 pfLGKGIVFANGPRWRQLRRFLTPTFTSFG--KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   185 GSRFD-YDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLdWVPGPHQRIFQN-FKCLRDLIAHSVHDHQASLDPR--S 260
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILK-YFPGPHGRKLKRaRKKIKDLLDKLIEERRETLDSAkkS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   261 PRDFIQCFLTKMAEEKEdplSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPAL 340
Cdd:pfam00067 238 PRDFLDALLLAKEEEDG---SKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   341 KDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSF 420
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   421 KKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSL--QPLGAPEDIDLTPlssGLGNLPRPFQLCL 488
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVelPPGTDPPDIDETP---GLLLPPKPYKLKF 461
PTZ00404 PTZ00404
cytochrome P450; Provisional
55-491 1.07e-56

cytochrome P450; Provisional


Pssm-ID: 173595  Cd Length: 482  Bit Score: 195.71  E-value: 1.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   55 LTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRN 134
Cdd:PTZ00404  54 LTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTSSGEYWKRNREIVGKAMRK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  135 FGMgkRSIEERILEEGSFLLAELRKTE--GEPFDPTFVLSRSVSNIICSVLFGSRFDYDDE----RLLTIIRLINDNFQI 208
Cdd:PTZ00404 134 TNL--KHIYDLLDDQVDVLIESMKKIEssGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDihngKLAELMGPMEQVFKD 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  209 MSSpwGELYDIF----PSLLDWVpgphQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDplshfH 284
Cdd:PTZ00404 212 LGS--GSLFDVIeitqPLYYQYL----EHTDKNFKKIKKFIKEKYHEHLKTIDPEVPRDLLDLLIKEYGTNTDD-----D 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  285 MDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIP 364
Cdd:PTZ00404 281 ILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSP 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  365 MNLPHRVTRD-TAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQsfkkSPAFMPFSAGRRLCLGESLAR 443
Cdd:PTZ00404 361 FGLPRSTSNDiIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDS----NDAFMPFSIGPRNCVGQQFAQ 436
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19743565  444 MELFLYLTAILQSFSLQplgapeDIDLTPLS----SGLGNLPRPFQLCLRPR 491
Cdd:PTZ00404 437 DELYLAFSNIILNFKLK------SIDGKKIDeteeYGLTLKPNKFKVLLEKR 482
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
31-485 1.40e-36

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 139.49  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  31 PPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPR--RVVVLSGYQAVKEALVD-------QGEEFSGRGDY 101
Cdd:COG2124   4 PPAPKLLGSPFALPRLLEFAPRFFLERAEDPYGDYFTLRLPGPgdGFWVVSRPADVREVLRDprffssaLGAGLRPRLLR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 102 PAFFNFTkgngIAFSSGDRWKVLRQFSIQILRNFGMgkRSIEERILEEGSFLLAELRkteGEPFDPTFVLSRSVSNIICS 181
Cdd:COG2124  84 PVLGDGS----LLTLDGPEHTRLRKLLAPAFTPRAL--RGYRPLIREIADRLLDDLW---QGGADLVLDFAAELTLRVIA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 182 VLFGSRFDyDDERLLtiirlindnfqimssPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQAslDPRSP 261
Cdd:COG2124 155 ELLGVPLE-DRPQLL---------------RWSDALLLRLDPDLGPEEPWRRARAARRELDAYLRALIAERRA--APRDD 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 262 rdfiqcFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLvvgrarlpalk 341
Cdd:COG2124 217 ------LLSLLLSAEDDGGGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR----------- 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 342 draamPYTDAVIHEVQRFADIIPMnLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDanqsfk 421
Cdd:COG2124 280 -----PLLEAVVEETLRLYPPVPL-ARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN------ 347
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19743565 422 kspAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDID--LTPLSSGLGNLPRPFQ 485
Cdd:COG2124 348 ---AHLPFGGGPHRCLGAALARLELKVALAELLRRFPLLLLAEPPPLVrrPTLVPRGGERLPVRRR 410
 
Name Accession Description Interval E-value
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
62-486 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  Cd Length: 425  Bit Score: 857.14  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20669   1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20669  81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20669 161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20669 241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20669 321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20669 401 LGAPEDIDLTPLSSGLGNVPRPFQL 425
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
62-486 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  Cd Length: 425  Bit Score: 752.86  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd11026   1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKRS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd11026  81 IEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd11026 161 PLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd11026 241 TTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYT 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd11026 321 IPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSS 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd11026 401 PVGPKDPDLTPRFSGFTNSPRPYQL 425
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
62-486 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  Cd Length: 425  Bit Score: 669.74  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20665   1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKRS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20665  81 IEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20665 161 ALLDYLPGSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQEKHNQQSEFTLENLAVTVTDLFGAGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20665 241 TTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20665 321 IPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKS 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20665 401 LVDPKDIDTTPVVNGFASVPPPYQL 425
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
62-486 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  Cd Length: 425  Bit Score: 590.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20670   1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALANGERWRILRRFSLTILRNFGMGKRS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20670  81 IEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMYS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20670 161 GIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLDPQNPRDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFAGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20670 241 TVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRGYL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20670 321 LPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRS 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20670 401 LVPPADIDITPKISGFGNIPPTYEL 425
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
62-486 0e+00

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  Cd Length: 425  Bit Score: 587.15  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20668   1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRDFGVGKRG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20668  81 IEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20668 161 SVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEKKNPNTEFYMKNLVMTTLNLFFAGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20668 241 TVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRDFF 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20668 321 LPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKS 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20668 401 PQSPEDIDVSPKHVGFATIPRNYTM 425
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
62-486 0e+00

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  Cd Length: 425  Bit Score: 545.53  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20672   1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFANGERWKTLRRFSLATMRDFGMGKRS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20672  81 VEERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELFS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20672 161 GFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHQNLMISVLSLFFAGTE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20672 241 TTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRGYL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20672 321 LPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVAS 400
                       410       420
                ....*....|....*....|....*
gi 19743565 462 LGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20672 401 PVAPEDIDLTPKESGVGKIPPTYQI 425
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
62-486 3.09e-174

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: 496.25  E-value: 3.09e-174
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20664   1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNGENWKEMRRFTLTTLRDFGMGKKT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20664  81 SEDKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWvPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20664 161 WLGPF-PGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFLVKQQEEEESSDSFFHDDNLTCSVGNLFGAGTD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGrARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20664 240 TTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIG-SRQPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRGYF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20664 319 IPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQP 398
                       410       420
                ....*....|....*....|....*..
gi 19743565 462 L--GAPEDIDLTPLsSGLGNLPRPFQL 486
Cdd:cd20664 399 PpgVSEDDLDLTPG-LGFTLNPLPHQL 424
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
31-488 2.62e-173

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: 495.26  E-value: 2.62e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565    31 PPGPRPLSILGNLLLLCSQDMLTS-LTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFT- 108
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSvFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   109 --KGNGIAFSSGDRWKVLRQFSIQILRNFGmgKRSIEERILEEGSFLLAELRKTEGEP--FDPTFVLSRSVSNIICSVLF 184
Cdd:pfam00067  81 pfLGKGIVFANGPRWRQLRRFLTPTFTSFG--KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   185 GSRFD-YDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLdWVPGPHQRIFQN-FKCLRDLIAHSVHDHQASLDPR--S 260
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILK-YFPGPHGRKLKRaRKKIKDLLDKLIEERRETLDSAkkS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   261 PRDFIQCFLTKMAEEKEdplSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPAL 340
Cdd:pfam00067 238 PRDFLDALLLAKEEEDG---SKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   341 KDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSF 420
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   421 KKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSL--QPLGAPEDIDLTPlssGLGNLPRPFQLCL 488
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVelPPGTDPPDIDETP---GLLLPPKPYKLKF 461
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
62-486 5.70e-166

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  Cd Length: 421  Bit Score: 475.06  E-value: 5.70e-166
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20662   1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKKS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20662  81 LEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKeDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20662 161 WIMKYLPGSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYLKEMAKYP-DPTTSFNEENLICSTLDLFFAGTE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20662 240 TTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLAGFH 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQsFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd20662 320 LPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQ-FKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKP 398
                       410       420
                ....*....|....*....|....*
gi 19743565 462 lgAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20662 399 --PPNEKLSLKFRMGITLSPVPHRI 421
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
62-486 2.78e-142

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  Cd Length: 428  Bit Score: 415.25  E-value: 2.78e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNF---TKGNGIAFSS-GDRWKVLRQFSIQILRNFGM 137
Cdd:cd20663   1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLgfgPKSQGVVLARyGPAWREQRRFSVSTLRNFGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 138 GKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELY 217
Cdd:cd20663  81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 218 DIFPSLLDwVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDP-RSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLL 296
Cdd:cd20663 161 NAFPVLLR-IPGLAGKVFPGQKAFLALLDELLTEHRTTWDPaQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLF 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 297 FGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTA 376
Cdd:cd20663 240 SAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIE 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 377 FRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQS 456
Cdd:cd20663 320 VQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQR 399
                       410       420       430
                ....*....|....*....|....*....|.
gi 19743565 457 FSLQ-PLGAPEDIDLTPLssGLGNLPRPFQL 486
Cdd:cd20663 400 FSFSvPAGQPRPSDHGVF--AFLVSPSPYQL 428
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
63-486 2.16e-135

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: 397.35  E-value: 2.16e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMgKRSI 142
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNGDYWKELRRFALSSLTKTKL-KKKM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 143 EERILEEGSFLLAELRKTE--GEPFDPTFVLSRSVSNIICSVLFGSRFD-YDDERLLTIIRLINDNFQIMSSPWgeLYDI 219
Cdd:cd20617  80 EELIEEEVNKLIESLKKHSksGEPFDPRPYFKKFVLNIINQFLFGKRFPdEDDGEFLKLVKPIEEIFKELGSGN--PSDF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 220 FPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDplSHFHMDTLLMTTHNLLFGG 299
Cdd:cd20617 158 IPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDS--GLFDDDSIISTCLDLFLAG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 300 TKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRG 379
Cdd:cd20617 236 TDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEIGG 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 380 FLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSfKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSL 459
Cdd:cd20617 316 YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGN-KLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKF 394
                       410       420
                ....*....|....*....|....*...
gi 19743565 460 QP-LGAPEDIDLTPlssGLGNLPRPFQL 486
Cdd:cd20617 395 KSsDGLPIDEKEVF---GLTLKPKPFKV 419
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
62-472 2.72e-131

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  Cd Length: 422  Bit Score: 386.85  E-value: 2.72e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20671   1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKRT 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFdPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20671  81 IEDKILEELQFLNGQIDSFNGKPF-PLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLYP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 sLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPlSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20671 160 -VLGAFLKLHKPILDKVEEVCMILRTLIEARRPTIDGNPLHSYIEALIQKQEEDDPKE-TLFHDANVLACTLDLVMAGTE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPmNLPHRVTRDTAFRGFL 381
Cdd:cd20671 238 TTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRCTAADTQFKGYL 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQ- 460
Cdd:cd20671 317 IPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLp 396
                       410
                ....*....|...
gi 19743565 461 -PLGAPEDIDLTP 472
Cdd:cd20671 397 pPGVSPADLDATP 409
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
62-466 6.30e-130

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: 383.42  E-value: 6.30e-130
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS 141
Cdd:cd20667   1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLRELGLGKQA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIFP 221
Cdd:cd20667  81 LESQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAFP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 SLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASlDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTK 301
Cdd:cd20667 161 WLMRYLPGPHQKIFAYHDAVRSFIKKEVIRHELR-TNEAPQDFIDCYLAQITKTKDDPVSTFSEENMIQVVIDLFLGGTE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRGFL 381
Cdd:cd20667 240 TTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHGYY 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQ- 460
Cdd:cd20667 320 VEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQl 399

                ....*.
gi 19743565 461 PLGAPE 466
Cdd:cd20667 400 PEGVQE 405
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
63-486 3.87e-129

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: 381.57  E-value: 3.87e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKEALvdQGEEFSGRGDYPAF--FNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKR 140
Cdd:cd20651   1 GDVVGLKLGKDKVVVVSGYEAVREVL--SREEFDGRPDGFFFrlRTFGKRLGITFTDGPFWKEQRRFVLRHLRDFGFGRR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 141 SIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDnFQIMSSPWGELYDIF 220
Cdd:cd20651  79 SMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVHL-LFRNFDMSGGLLNQF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 221 PSLLDWVPG--PHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMaEEKEDPLSHFHMDTLLMTTHNLLFG 298
Cdd:cd20651 158 PWLRFIAPEfsGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNPRDLIDAYLREM-KKKEPPSSSFTDDQLVMICLDLFIA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 299 GTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFR 378
Cdd:cd20651 237 GSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTTLG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 379 GFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFS 458
Cdd:cd20651 317 GYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFT 396
                       410       420
                ....*....|....*....|....*...
gi 19743565 459 LQPLGaPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20651 397 FSPPN-GSLPDLEGIPGGITLSPKPFRV 423
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
62-485 1.06e-128

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: 380.40  E-value: 1.06e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGN-GIAFSS-GDRWKVLRQFSIQILRNFGMGK 139
Cdd:cd11027   1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGkDIAFGDySPTWKLHRKLAHSALRLYASGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 140 RSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSpwGELYDI 219
Cdd:cd11027  81 PRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELLGA--GSLLDI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 220 FPsLLDWVPGPHQRIFQNFKCLRDLIAHSVHD-HQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHM---DTLLMTTHNL 295
Cdd:cd11027 159 FP-FLKYFPNKALRELKELMKERDEILRKKLEeHKETFDPGNIRDLTDALIKAKKEAEDEGDEDSGLltdDHLVMTISDI 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 296 LFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDT 375
Cdd:cd11027 238 FGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTCDT 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 376 AFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDAN-QSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAIL 454
Cdd:cd11027 318 TLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENgKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLL 397
                       410       420       430
                ....*....|....*....|....*....|..
gi 19743565 455 QSFSL-QPLGAPEDiDLTPlSSGLGNLPRPFQ 485
Cdd:cd11027 398 QKFRFsPPEGEPPP-ELEG-IPGLVLYPLPYK 427
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
62-486 2.58e-124

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  Cd Length: 426  Bit Score: 369.11  E-value: 2.58e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSS-GDRWKVLRQFSIQILRNFGMGKR 140
Cdd:cd20666   1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPyGPVWRQQRKFSHSTLRHFGLGKL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 141 SIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWGELYDIF 220
Cdd:cd20666  81 SLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAAILVNIC 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 221 PSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPL-SHFHMDTLLMTTHNLLFGG 299
Cdd:cd20666 161 PWLYYLPFGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLHIEEEQKNNAeSSFNEDYLFYIIGDLFIAG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 300 TKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRG 379
Cdd:cd20666 241 TDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 380 FLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSL 459
Cdd:cd20666 321 YTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTF 400
                       410       420
                ....*....|....*....|....*....
gi 19743565 460 QPlgaPEDIDLTPLSS--GLGNLPRPFQL 486
Cdd:cd20666 401 LL---PPNAPKPSMEGrfGLTLAPCPFNI 426
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
62-486 4.95e-113

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  Cd Length: 430  Bit Score: 340.43  E-value: 4.95e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRgdyPAFFNFTK---GNGIAFSS-GDRWKVLRQFSIQILRNFGM 137
Cdd:cd11028   1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGR---PDFYSFQFisnGKSMAFSDyGPRWKLHRKLAQNALRTFSN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 138 GKRS--IEERILEEGSFLLAELRKTEGE--PFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLiNDNF-QIMSSp 212
Cdd:cd11028  78 ARTHnpLEEHVTEEAEELVTELTENNGKpgPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVKS-NDDFgAFVGA- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 213 wGELYDIFPslldWVPGPHQRIFQNFK----CLRDLIAHSVHDHQASLDPRSPRDFIQCFLtKMAEEK---EDPLSHFHm 285
Cdd:cd11028 156 -GNPVDVMP----WLRYLTRRKLQKFKellnRLNSFILKKVKEHLDTYDKGHIRDITDALI-KASEEKpeeEKPEVGLT- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 286 DTLLMTTHNLLFG-GTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIP 364
Cdd:cd11028 229 DEHIISTVQDLFGaGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVP 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 365 MNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPA--FMPFSAGRRLCLGESLA 442
Cdd:cd11028 309 FTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTKVdkFLPFGAGRRRCLGEELA 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 19743565 443 RMELFLYLTAILQ--SFSLQPlGAPEdiDLTPlSSGLGNLPRPFQL 486
Cdd:cd11028 389 RMELFLFFATLLQqcEFSVKP-GEKL--DLTP-IYGLTMKPKPFKV 430
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
55-487 2.62e-112

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  Cd Length: 436  Bit Score: 339.10  E-value: 2.62e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  55 LTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSS-GDRWKVLRQFSIQILR 133
Cdd:cd20661   5 MKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKyGRGWTEHRKLAVNCFR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 134 NFGMGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPW 213
Cdd:cd20661  85 YFGYGQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAW 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 214 GELYDIFPsLLDWVP-GPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTLLMTT 292
Cdd:cd20661 165 VFLYNAFP-WIGILPfGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFSV 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 293 HNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVT 372
Cdd:cd20661 244 GELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATS 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 373 RDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTA 452
Cdd:cd20661 324 KDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTA 403
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 19743565 453 ILQSFSLQplgAPEDI--DLTPlSSGLGNLPRPFQLC 487
Cdd:cd20661 404 LLQRFHLH---FPHGLipDLKP-KLGMTLQPQPYLIC 436
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
62-486 2.57e-98

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  Cd Length: 435  Bit Score: 302.79  E-value: 2.57e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSS--GDRWKVLRQFSIQILRNFGMGK 139
Cdd:cd20677   1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSEkyGESWKLHKKIAKNALRTFSKEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 140 RS-------IEERILEEGSFLLAEL--RKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRlINDNFQIMS 210
Cdd:cd20677  81 AKsstcsclLEEHVCAEASELVKTLveLSKEKGSFDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVE-INNDLLKAS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 211 SPwGELYDIFPsLLDWVPGPHQRIFQNF-KCLRDLIAHSVHDHQASLDPRSPRD----FIQCFLTKMAEEKEDPLSHfhm 285
Cdd:cd20677 160 GA-GNLADFIP-ILRYLPSPSLKALRKFiSRLNNFIAKSVQDHYATYDKNHIRDitdaLIALCQERKAEDKSAVLSD--- 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 286 DTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPM 365
Cdd:cd20677 235 EQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPF 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 366 NLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPA--FMPFSAGRRLCLGESLAR 443
Cdd:cd20677 315 TIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVekVLIFGMGVRKCLGEDVAR 394
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19743565 444 MELFLYLTAILQSFSLQPLgaPED-IDLTPlSSGLGNLPRPFQL 486
Cdd:cd20677 395 NEIFVFLTTILQQLKLEKP--PGQkLDLTP-VYGLTMKPKPYRL 435
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
62-486 3.37e-95

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: 294.99  E-value: 3.37e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSS-GDRWKVLRQFSIQILRNFGMG-- 138
Cdd:cd20675   1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFGGySERWKAHRRVAHSTVRAFSTRnp 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 139 --KRSIEERILEEGSFLLAE-LRKTEGEP-FDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTII-RliNDNF-QIMSSp 212
Cdd:cd20675  81 rtRKAFERHVLGEARELVALfLRKSAGGAyFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLgR--NDQFgRTVGA- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 213 wGELYDIFPSLLdWVPGPHQRIFQNFKCLR----DLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTL 288
Cdd:cd20675 158 -GSLVDVMPWLQ-YFPNPVRTVFRNFKQLNrefyNFVLDKVLQHRETLRGGAPRDMMDAFILALEKGKSGDSGVGLDKEY 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 289 LMTTHNLLFGGTK-TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNL 367
Cdd:cd20675 236 VPSTVTDIFGASQdTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTI 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 368 PHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAF--MPFSAGRRLCLGESLARME 445
Cdd:cd20675 316 PHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLASsvMIFSVGKRRCIGEELSKMQ 395
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19743565 446 LFLYlTAILQ---SFSLQPlgaPEDIDLTpLSSGLGNLPRPFQL 486
Cdd:cd20675 396 LFLF-TSILAhqcNFTANP---NEPLTMD-FSYGLTLKPKPFTI 434
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
62-472 1.86e-92

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  Cd Length: 437  Bit Score: 287.68  E-value: 1.86e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFS--SGDRWKVLRQFSIQILRNFGM-- 137
Cdd:cd20676   1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLTFStdSGPVWRARRKLAQNALKTFSIas 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 138 GKRS-----IEERILEEGSFLLAELRKTEGEP--FDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMS 210
Cdd:cd20676  81 SPTSsssclLEEHVSKEAEYLVSKLQELMAEKgsFDPYRYIVVSVANVICAMCFGKRYSHDDQELLSLVNLSDEFGEVAG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 211 SpwGELYDIFPsLLDWVPGPHQRIFQNF-KCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHM-DTL 288
Cdd:cd20676 161 S--GNPADFIP-ILRYLPNPAMKRFKDInKRFNSFLQKIVKEHYQTFDKDNIRDITDSLIEHCQDKKLDENANIQLsDEK 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 289 LMTTHNLLFG-GTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNL 367
Cdd:cd20676 238 IVNIVNDLFGaGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFTI 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 368 PHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQ-SFKK--SPAFMPFSAGRRLCLGESLARM 444
Cdd:cd20676 318 PHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGtEINKteSEKVMLFGLGKRRCIGESIARW 397
                       410       420       430
                ....*....|....*....|....*....|
gi 19743565 445 ELFLYLTAILQ--SFSLQPlgaPEDIDLTP 472
Cdd:cd20676 398 EVFLFLAILLQqlEFSVPP---GVKVDMTP 424
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
63-486 1.72e-90

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  Cd Length: 432  Bit Score: 282.76  E-value: 1.72e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKEALvdQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRNFGMGKRS- 141
Cdd:cd20652   1 GSIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGGNGIICAEGDLWRDQRRFVHDWLRQFGMTKFGn 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 ----IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMsspwGELY 217
Cdd:cd20652  79 grakMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLI----GVAG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 218 DI-FPSLLDWVPGphqrIFQNFKCLRDLIAHS-------VHDHQASLDPRSPRD---FIQCFLTKMAEEKE--DPLSHFH 284
Cdd:cd20652 155 PVnFLPFLRHLPS----YKKAIEFLVQGQAKThaiyqkiIDEHKRRLKPENPRDaedFELCELEKAKKEGEdrDLFDGFY 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 285 MDTLLMTTHNLLFG-GTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADII 363
Cdd:cd20652 231 TDEQLHHLLADLFGaGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVV 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 364 PMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLAR 443
Cdd:cd20652 311 PLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELAR 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 19743565 444 MELFLYLTAILQSFSLQpLGAPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20652 391 MILFLFTARILRKFRIA-LPDGQPVDSEGGNVGITLTPPPFKI 432
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
62-465 1.90e-89

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: 279.98  E-value: 1.90e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRgdyPAFFNFT----KGNGIAF-SSGDRWKVLRQFSIQILRNFG 136
Cdd:cd20673   1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGR---PRMVTTDllsrNGKDIAFaDYSATWQLHRKLVHSAFALFG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 137 MGKRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSpwGEL 216
Cdd:cd20673  78 EGSQKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILNYNEGIVDTVAK--DSL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 217 YDIFPSLldwvpgphqRIFQNfKCLRDLIAH-SVHD---------HQASLDPRSPRDFIQCFLT-KMAEE--------KE 277
Cdd:cd20673 156 VDIFPWL---------QIFPN-KDLEKLKQCvKIRDkllqkkleeHKEKFSSDSIRDLLDALLQaKMNAEnnnagpdqDS 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 278 DPLSHFHMdtlLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQ 357
Cdd:cd20673 226 VGLSDDHI---LMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVL 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 358 RFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDA--NQSFKKSPAFMPFSAGRRL 435
Cdd:cd20673 303 RIRPVAPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPtgSQLISPSLSYLPFGAGPRV 382
                       410       420       430
                ....*....|....*....|....*....|.
gi 19743565 436 CLGESLARMELFLYLTAILQSFSLQ-PLGAP 465
Cdd:cd20673 383 CLGEALARQELFLFMAWLLQRFDLEvPDGGQ 413
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
62-489 1.19e-83

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: 264.66  E-value: 1.19e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFfNFTKGNGIAFSSGD---RWKVLRQFSIQILRNfGMg 138
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTG-KLVSQGGQDLSLGDyslLWKAHRKLTRSALQL-GI- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 139 KRSIEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDErLLTIIRLINDNFQIMSSPWGELYD 218
Cdd:cd20674  78 RNSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKEDKDTL-VQAFHDCVQELLKTWGHWSIQALD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 219 IFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEK-EDPLSHFHMDTLLMTTHNLLF 297
Cdd:cd20674 157 SIPFLRFFPNPGLRRLKQAVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQPRgEKGMGQLLEGHVHMAVVDLFI 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 298 GGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAF 377
Cdd:cd20674 237 GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRDSSI 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 378 RGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSfkkSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSF 457
Cdd:cd20674 317 AGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAA---NRALLPFGCGARVCLGEPLARLELFVFLARLLQAF 393
                       410       420       430
                ....*....|....*....|....*....|..
gi 19743565 458 SLQPLGAPEDIDLTPLsSGLGNLPRPFQLCLR 489
Cdd:cd20674 394 TLLPPSDGALPSLQPV-AGINLKVQPFQVRLQ 424
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
62-484 5.29e-77

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: 247.49  E-value: 5.29e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNF-TKGNGIAF-SSGDRWKVLR-----QFSIQILRN 134
Cdd:cd11065   1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELmGWGMRLLLmPYGPRWRLHRrlfhqLLNPSAVRK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 135 FgmgkRSIEErilEEGSFLLAELRKTEGEPFDptfVLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDNFQIMSSPWG 214
Cdd:cd11065  81 Y----RPLQE---LESKQLLRDLLESPDDFLD---HIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 215 ELYDIFPsLLDWVPGphqRIFQNFK----CLRDLIAHSVHDH-QASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHmDTLL 289
Cdd:cd11065 151 YLVDFFP-FLRYLPS---WLGAPWKrkarELRELTRRLYEGPfEAAKERMASGTATPSFVKDLLEELDKEGGLSE-EEIK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 290 MTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLPH 369
Cdd:cd11065 226 YLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPH 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 370 RVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQS--FKKSPAFMPFSAGRRLCLGESLARMELF 447
Cdd:cd11065 306 ALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGtpDPPDPPHFAFGFGRRICPGRHLAENSLF 385
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 19743565 448 LYLTAILQSFSLQP--LGAPEDIDLTP-LSSGLGNLPRPF 484
Cdd:cd11065 386 IAIARLLWAFDIKKpkDEGGKEIPDEPeFTDGLVSHPLPF 425
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
63-481 8.95e-61

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


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 203.90  E-value: 8.95e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFsiqILRNFGMGK-RS 141
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRL---LAPAFTPRAlAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 142 IEERILEEGSFLLAELRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFDYDDERLltiIRLINDNFQIMSSPWgelydifp 221
Cdd:cd00302  78 LRPVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEEL---AELLEALLKLLGPRL-------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 222 sLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIqcfltkMAEEKEDPLSHfhmDTLLMTTHNLLFGGTK 301
Cdd:cd00302 147 -LRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLL------ADADDGGGLSD---EEIVAELLTLLLAGHE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 302 TVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDraaMPYTDAVIHEVQRFADIIPMnLPHRVTRDTAFRGFL 381
Cdd:cd00302 217 TTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTPEDLSK---LPYLEAVVEETLRLYPPVPL-LPRVATEDVELGGYT 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 382 IPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANqsFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQP 461
Cdd:cd00302 293 IPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPER--EEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFEL 370
                       410       420
                ....*....|....*....|.
gi 19743565 462 LGAPE-DIDLTPLSSGLGNLP 481
Cdd:cd00302 371 VPDEElEWRPSLGTLGPASLP 391
PTZ00404 PTZ00404
cytochrome P450; Provisional
55-491 1.07e-56

cytochrome P450; Provisional


Pssm-ID: 173595  Cd Length: 482  Bit Score: 195.71  E-value: 1.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565   55 LTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQFSIQILRN 134
Cdd:PTZ00404  54 LTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTSSGEYWKRNREIVGKAMRK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  135 FGMgkRSIEERILEEGSFLLAELRKTE--GEPFDPTFVLSRSVSNIICSVLFGSRFDYDDE----RLLTIIRLINDNFQI 208
Cdd:PTZ00404 134 TNL--KHIYDLLDDQVDVLIESMKKIEssGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDihngKLAELMGPMEQVFKD 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  209 MSSpwGELYDIF----PSLLDWVpgphQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDplshfH 284
Cdd:PTZ00404 212 LGS--GSLFDVIeitqPLYYQYL----EHTDKNFKKIKKFIKEKYHEHLKTIDPEVPRDLLDLLIKEYGTNTDD-----D 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  285 MDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIP 364
Cdd:PTZ00404 281 ILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSP 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  365 MNLPHRVTRD-TAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQsfkkSPAFMPFSAGRRLCLGESLAR 443
Cdd:PTZ00404 361 FGLPRSTSNDiIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDS----NDAFMPFSIGPRNCVGQQFAQ 436
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19743565  444 MELFLYLTAILQSFSLQplgapeDIDLTPLS----SGLGNLPRPFQLCLRPR 491
Cdd:PTZ00404 437 DELYLAFSNIILNFKLK------SIDGKKIDeteeYGLTLKPNKFKVLLEKR 482
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
63-471 3.18e-55

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: 190.46  E-value: 3.18e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFT-KGNGIAFSS-GDRWKVLRQ------FSIQILRN 134
Cdd:cd20618   1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSyNGQDIVFAPyGPHWRHLRKictlelFSAKRLES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 135 FgmgkRSIEErilEEGSFLLAELRK--TEGEPFDPTFVLSRSVSNIICSVLFGSRF----DYDDERLLTIIRLINDNFQI 208
Cdd:cd20618  81 F----QGVRK---EELSHLVKSLLEesESGKPVNLREHLSDLTLNNITRMLFGKRYfgesEKESEEAREFKELIDEAFEL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 209 MsspwGELY--DIFPSLlDWV-PGPHQRIFQNFKCLRDLIAHSV---HDHQASLDPRSPRDFIQCFLTKMAEEKEDpLSH 282
Cdd:cd20618 154 A----GAFNigDYIPWL-RWLdLQGYEKRMKKLHAKLDRFLQKIieeHREKRGESKKGGDDDDDLLLLLDLDGEGK-LSD 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 283 fhmDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADI 362
Cdd:cd20618 228 ---DNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPP 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 363 IPMNLPHRVTRDTAFRGFLIPKGTdvITLLNT--VHYDPSQFLTPQEFNPEHFLDANQSFKKSPAF--MPFSAGRRLCLG 438
Cdd:cd20618 305 GPLLLPHESTEDCKVAGYDIPAGT--RVLVNVwaIGRDPKVWEDPLEFKPERFLESDIDDVKGQDFelLPFGSGRRMCPG 382
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 19743565 439 ESLA-RMeLFLYLTAILQSF--SLQPLGaPEDIDLT 471
Cdd:cd20618 383 MPLGlRM-VQLTLANLLHGFdwSLPGPK-PEDIDME 416
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
59-471 1.03e-47

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  Cd Length: 435  Bit Score: 170.41  E-value: 1.03e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  59 SKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAF--SSGDRWKVLRQ------FSIQ 130
Cdd:cd11073   1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVwpPYGPRWRMLRKicttelFSPK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 131 ILRNFgmgkRSIEERILEEgsfLLAELRK--TEGEPFDPTFVLSRSVSNIICSVLFGSR-FDYDDERLLTIIRLINDNFQ 207
Cdd:cd11073  81 RLDAT----QPLRRRKVRE---LVRYVREkaGSGEAVDIGRAAFLTSLNLISNTLFSVDlVDPDSESGSEFKELVREIME 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 208 IMSSPwgELYDIFPSL--LDWvPGPHQRIFQNFKCLRDLIAHSVHDHQA--SLDPRSPRDFIQCFLTKMAEEKEDPLSHF 283
Cdd:cd11073 154 LAGKP--NVADFFPFLkfLDL-QGLRRRMAEHFGKLFDIFDGFIDERLAerEAGGDKKKDDDLLLLLDLELDSESELTRN 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 284 HMDTLLMtthNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADII 363
Cdd:cd11073 231 HIKALLL---DLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPA 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 364 PMNLPHRVTRDTAFRGFLIPKGTDVitLLNT--VHYDPSQFLTPQEFNPEHFLDANQSFK-KSPAFMPFSAGRRLCLGES 440
Cdd:cd11073 308 PLLLPRKAEEDVEVMGYTIPKGTQV--LVNVwaIGRDPSVWEDPLEFKPERFLGSEIDFKgRDFELIPFGSGRRICPGLP 385
                       410       420       430
                ....*....|....*....|....*....|....
gi 19743565 441 LA-RMeLFLYLTAILQSF--SLQPLGAPEDIDLT 471
Cdd:cd11073 386 LAeRM-VHLVLASLLHSFdwKLPDGMKPEDLDME 418
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
61-471 1.63e-47

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: 169.57  E-value: 1.63e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  61 EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGN-GIAFSS-GDRWKVLRQFSIQIL------ 132
Cdd:cd11072   1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGkDIAFAPyGEYWRQMRKICVLELlsakrv 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 133 RNFgmgkRSIEErilEEGSFLLAELRKTEG--EPFDPTFVLSRSVSNIICSVLFGSRFDYDDERllTIIRLINDNFQIMS 210
Cdd:cd11072  81 QSF----RSIRE---EEVSLLVKKIRESASssSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQD--KFKELVKEALELLG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 211 SPWgeLYDIFPSL--LDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKED---PLSHFHM 285
Cdd:cd11072 152 GFS--VGDYFPSLgwIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDlefPLTRDNI 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 286 DTLLMtthNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPM 365
Cdd:cd11072 230 KAIIL---DMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPL 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 366 NLPHRVTRDTAFRGFLIPKGTDVITllNT--VHYDPSQFLTPQEFNPEHFLDAN-----QSFKkspaFMPFSAGRRLCLG 438
Cdd:cd11072 307 LLPRECREDCKINGYDIPAKTRVIV--NAwaIGRDPKYWEDPEEFRPERFLDSSidfkgQDFE----LIPFGAGRRICPG 380
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 19743565 439 ESLARMELFLYLTAILQSF--SLqPLGA-PEDIDLT 471
Cdd:cd11072 381 ITFGLANVELALANLLYHFdwKL-PDGMkPEDLDME 415
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
63-472 1.38e-45

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: 164.62  E-value: 1.38e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKE-----ALVDQGEEfsgrgdYPAFFNFTkGNGIAFSSGDRWKVLRQ-----FSIQIL 132
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEDIEVilsssKLITKSFL------YDFLKPWL-GDGLLTSTGEKWRKRRKlltpaFHFKIL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 133 RNFgmgkrsiEERILEEGSFLLAELRKTEGEP-FDPTFVLSRSVSNIICSVLFGSRFDY---DDERLLTIIRLINDNFQI 208
Cdd:cd20628  74 ESF-------VEVFNENSKILVEKLKKKAGGGeFDIFPYISLCTLDIICETAMGVKLNAqsnEDSEYVKAVKRILEIILK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 209 -MSSPWgelydIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASL-------------DPRSPRDFIQCFLtkMAE 274
Cdd:cd20628 147 rIFSPW-----LRFDFIFRLTSLGKEQRKALKVLHDFTNKVIKERREELkaekrnseeddefGKKKRKAFLDLLL--EAH 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 275 EKEDPLSHFHM----DTllmtthnLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRA-RLPALKDRAAMPYT 349
Cdd:cd20628 220 EDGGPLTDEDIreevDT-------FMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDdRRPTLEDLNKMKYL 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 350 DAVIHEVQRFADIIPMnLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSfKKSP-AFMP 428
Cdd:cd20628 293 ERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSA-KRHPyAYIP 370
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19743565 429 FSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTP 472
Cdd:cd20628 371 FSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGEDLKLIA 414
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
63-491 2.67e-45

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: 163.13  E-value: 2.67e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTkGNGIAFSSGDRWkvLRQ-------FSIQILRNF 135
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYERLKLLL-GNGLLTSEGDLW--RRQrrlaqpaFHRRRIAAY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 136 GmgkrsieERILEEGSFLLAELRKTEGE-PFDPTFVLSRSVSNIICSVLFGSRfdyDDERLLTIIRLINDNFQIMSSPWG 214
Cdd:cd20620  78 A-------DAMVEATAALLDRWEAGARRgPVDVHAEMMRLTLRIVAKTLFGTD---VEGEADEIGDALDVALEYAARRML 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 215 elydIFPSLLDWVPGPHQRIFQ-NFKCLRDLIAHSVHDHQAslDPRSPRDFIQCFLTKMAEEKEDPLShfhmDTLL---- 289
Cdd:cd20620 148 ----SPFLLPLWLPTPANRRFRrARRRLDEVIYRLIAERRA--APADGGDLLSMLLAARDEETGEPMS----DQQLrdev 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 290 MTthnLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRaRLPALKDRAAMPYTDAVIHEVQRFADIIPMnLPH 369
Cdd:cd20620 218 MT---LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGG-RPPTAEDLPQLPYTEMVLQESLRLYPPAWI-IGR 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 370 RVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQsfKKSP--AFMPFSAGRRLCLGESLARMELF 447
Cdd:cd20620 293 EAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPERE--AARPryAYFPFGGGPRICIGNHFAMMEAV 370
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19743565 448 LYLTAILQSFSLQPLGApEDIDLTPLSSglgnlprpfqlcLRPR 491
Cdd:cd20620 371 LLLATIAQRFRLRLVPG-QPVEPEPLIT------------LRPK 401
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
55-465 2.82e-44

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: 160.83  E-value: 2.82e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  55 LTKLSKEYGSMYTVHL-GPRRVVVLSGYQAVKEALV-DQGEEFSGRGDYPAFFNFTKgNGIAFSSGDRWKVLRQ-----F 127
Cdd:cd11053   4 LERLRARYGDVFTLRVpGLGPVVVLSDPEAIKQIFTaDPDVLHPGEGNSLLEPLLGP-NSLLLLDGDRHRRRRKllmpaF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 128 SIQILRNFGmgkRSIEERILEEgsflLAELRktEGEPFDpTFVLSRSVS-NIICSVLFGSrfdYDDERLLTIIRLINDNF 206
Cdd:cd11053  83 HGERLRAYG---ELIAEITERE----IDRWP--PGQPFD-LRELMQEITlEVILRVVFGV---DDGERLQELRRLLPRLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 207 QIMSSPWGELYDIFPSLLDWvpGPHQRIFQNFKCLRDLIAHSVHDHQAslDPRSPRDFIqcfLTKM---AEEKEDPLSHF 283
Cdd:cd11053 150 DLLSSPLASFPALQRDLGPW--SPWGRFLRARRRIDALIYAEIAERRA--EPDAERDDI---LSLLlsaRDEDGQPLSDE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 284 HMDTLLMTthnLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALkdrAAMPYTDAVIHEVQRFADII 363
Cdd:cd11053 223 ELRDELMT---LLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDPEDI---AKLPYLDAVIKETLRLYPVA 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 364 PMnLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDAnqsfKKSP-AFMPFSAGRRLCLGESLA 442
Cdd:cd11053 297 PL-VPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGR----KPSPyEYLPFGGGVRRCIGAAFA 371
                       410       420
                ....*....|....*....|...
gi 19743565 443 RMELFLYLTAILQSFSLQPLGAP 465
Cdd:cd11053 372 LLEMKVVLATLLRRFRLELTDPR 394
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
61-469 3.37e-43

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: 158.18  E-value: 3.37e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  61 EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFN-FTKG-NGIAFSS-GDRWKVLRqfsiqilRNF-- 135
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVlFSSNkHMVNSSPyGPLWRTLR-------RNLvs 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 136 GM-------GKRSIEERILEEgsfLLAELRKTEGEpfDPTFVLSRSV-SNIICSVL----FGSRFDydDERLLTIIRLIN 203
Cdd:cd11075  74 EVlspsrlkQFRPARRRALDN---LVERLREEAKE--NPGPVNVRDHfRHALFSLLlymcFGERLD--EETVRELERVQR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 204 DnfQIMSSPWGELYDIFPSLLdWVPGPHQ-RIFQNFK-----CLRDLI-AHSVHDHQASLDPRSPRDFIQCFLTKMAEEK 276
Cdd:cd11075 147 E--LLLSFTDFDVRDFFPALT-WLLNRRRwKKVLELRrrqeeVLLPLIrARRKRRASGEADKDYTDFLLLDLLDLKEEGG 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 277 EDPLSHFHMDTLLMTThnlLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEV 356
Cdd:cd11075 224 ERKLTDEELVSLCSEF---LNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLET 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 357 QRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQ---------SFKkspaFM 427
Cdd:cd11075 301 LRRHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEaadidtgskEIK----MM 376
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 19743565 428 PFSAGRRLCLGESLARMELFLYLTAILQSFS-LQPLGAPEDID 469
Cdd:cd11075 377 PFGAGRRICPGLGLATLHLELFVARLVQEFEwKLVEGEEVDFS 419
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
61-461 2.86e-40

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: 150.04  E-value: 2.86e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  61 EYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRgdyPAFFNFTK--GNGIAFSSGDRWKVLRQ-----FSIQILR 133
Cdd:cd11055   1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNR---PLFILLDEpfDSSLLFLKGERWKRLRTtlsptFSSGKLK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 134 NfgmgkrsIEERILEEGSFLLAELRK--TEGEPFDPTFVLSRSVSNIICSVLFG----SRFDYDDErLLTIIR-----LI 202
Cdd:cd11055  78 L-------MVPIINDCCDELVEKLEKaaETGKPVDMKDLFQGFTLDVILSTAFGidvdSQNNPDDP-FLKAAKkifrnSI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 203 NDNFQIMSSPWGELYDIFpsLLDWVPGphqriFQNFKCLRDLIAHSVHDHQASLDPRsPRDFIQCFLTkmAEEKEDPLSH 282
Cdd:cd11055 150 IRLFLLLLLFPLRLFLFL--LFPFVFG-----FKSFSFLEDVVKKIIEQRRKNKSSR-RKDLLQLMLD--AQDSDEDVSK 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 283 FHMDTLLMTTHNLLF--GGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFA 360
Cdd:cd11055 220 KKLTDDEIVAQSFIFllAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLY 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 361 DIIPMNLpHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGES 440
Cdd:cd11055 300 PPAFFIS-RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMR 378
                       410       420
                ....*....|....*....|.
gi 19743565 441 LARMELFLYLTAILQSFSLQP 461
Cdd:cd11055 379 FALLEVKLALVKILQKFRFVP 399
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
60-471 2.81e-39

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: 147.29  E-value: 2.81e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  60 KEYGSMYTVHLGPRRVVVLSGYQAVKEALvdQGEefsgrGDYPA--------FFNFTKGN--GIAFSSGDRWKVLRQ-FS 128
Cdd:cd11054   2 KKYGPIVREKLGGRDIVHLFDPDDIEKVF--RNE-----GKYPIrpslepleKYRKKRGKplGLLNSNGEEWHRLRSaVQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 129 IQILRNfgmgkRSIE------ERILEEgsFL--LAELRKTEGEPfdptfvlsrsVSNI-----------ICSVLFGSRFD 189
Cdd:cd11054  75 KPLLRP-----KSVAsylpaiNEVADD--FVerIRRLRDEDGEE----------VPDLedelykwslesIGTVLFGKRLG 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 190 YDDERLLTIIRLINDNFQIMSSPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQ-CF 268
Cdd:cd11054 138 CLDDNPDSDAQKLIEAVKDIFESSAKLMFGPPLWKYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDEEEdSL 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 269 LTKMAEEKEDPlshfhMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPY 348
Cdd:cd11054 218 LEYLLSKPGLS-----KKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPY 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 349 TDAVIHEVQRFADIIPMNLphRVT-RDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAF- 426
Cdd:cd11054 293 LKACIKESLRLYPVAPGNG--RILpKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNIHPFa 370
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 19743565 427 -MPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGapEDIDLT 471
Cdd:cd11054 371 sLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHH--EELKVK 414
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
31-485 1.40e-36

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 139.49  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  31 PPGPRPLSILGNLLLLCSQDMLTSLTKLSKEYGSMYTVHLGPR--RVVVLSGYQAVKEALVD-------QGEEFSGRGDY 101
Cdd:COG2124   4 PPAPKLLGSPFALPRLLEFAPRFFLERAEDPYGDYFTLRLPGPgdGFWVVSRPADVREVLRDprffssaLGAGLRPRLLR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 102 PAFFNFTkgngIAFSSGDRWKVLRQFSIQILRNFGMgkRSIEERILEEGSFLLAELRkteGEPFDPTFVLSRSVSNIICS 181
Cdd:COG2124  84 PVLGDGS----LLTLDGPEHTRLRKLLAPAFTPRAL--RGYRPLIREIADRLLDDLW---QGGADLVLDFAAELTLRVIA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 182 VLFGSRFDyDDERLLtiirlindnfqimssPWGELYDIFPSLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQAslDPRSP 261
Cdd:COG2124 155 ELLGVPLE-DRPQLL---------------RWSDALLLRLDPDLGPEEPWRRARAARRELDAYLRALIAERRA--APRDD 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 262 rdfiqcFLTKMAEEKEDPLSHFHMDTLLMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLvvgrarlpalk 341
Cdd:COG2124 217 ------LLSLLLSAEDDGGGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR----------- 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 342 draamPYTDAVIHEVQRFADIIPMnLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDanqsfk 421
Cdd:COG2124 280 -----PLLEAVVEETLRLYPPVPL-ARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN------ 347
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19743565 422 kspAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDID--LTPLSSGLGNLPRPFQ 485
Cdd:COG2124 348 ---AHLPFGGGPHRCLGAALARLELKVALAELLRRFPLLLLAEPPPLVrrPTLVPRGGERLPVRRR 410
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
54-472 2.40e-35

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: 136.73  E-value: 2.40e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  54 SLTKLSKEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTKGNGIAFSSGDRWKVLRQ-----FS 128
Cdd:cd11046   2 DLYKWFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADGEIWKKRRRalvpaLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 129 IQILRNF-GMGKRSIEerileegsFLLAELRK--TEGEPFDptfvLSRSVSNIICSVLFGSRFDYDDERLLTIIRLINDN 205
Cdd:cd11046  82 KDYLEMMvRVFGRCSE--------RLMEKLDAaaETGESVD----MEEEFSSLTLDIIGLAVFNYDFGSVTEESPVIKAV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 206 FQIM-----SSPWGELYDIFPSLLDWVPGphQRIFQ-NFK----CLRDLIAHSVHDHQASLDPRSPRDFIQcfltkmaeE 275
Cdd:cd11046 150 YLPLveaehRSVWEPPYWDIPAALFIVPR--QRKFLrDLKllndTLDDLIRKRKEMRQEEDIELQQEDYLN--------E 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 276 KEDPLSHFHMDTL------------LMTthnLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDR 343
Cdd:cd11046 220 DDPSLLRFLVDMRdedvdskqlrddLMT---MLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDL 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 344 AAMPYTDAVIHEVQRFADIIPMNLPHRVTRDTAFRG-FLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDanqSFKK 422
Cdd:cd11046 297 KKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGgVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLD---PFIN 373
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 19743565 423 SP-------AFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQPLGAPEDIDLTP 472
Cdd:cd11046 374 PPneviddfAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGMTT 430
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
84-461 4.30e-35

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: 135.74  E-value: 4.30e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  84 VKEALVDQGEEFSGRGdypAFFNFTK---GNGIAFSSGDRWKVLRQfsiQILRNFGMGK-RSIEERILEEGSFLLAELRK 159
Cdd:cd11056  24 IKQILVKDFAHFHDRG---LYSDEKDdplSANLFSLDGEKWKELRQ---KLTPAFTSGKlKNMFPLMVEVGDELVDYLKK 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 160 T--EGEPFDPTFVLSRSVSNIICSVLFG---SRFDYDDERLLTIIRLINDNFQIMSSPWGeLYDIFPSLLDW-----VPG 229
Cdd:cd11056  98 QaeKGKELEIKDLMARYTTDVIASCAFGldaNSLNDPENEFREMGRRLFEPSRLRGLKFM-LLFFFPKLARLlrlkfFPK 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 230 PHQRIFqnfkclRDLIAHSVHDHQASLDPRSprDFIQCFL-TKMAEEKEDPLSHFHMDTLLMTTHNLLF--GGTKTVSTT 306
Cdd:cd11056 177 EVEDFF------RKLVRDTIEYREKNNIVRN--DFIDLLLeLKKKGKIEDDKSEKELTDEELAAQAFVFflAGFETSSST 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 307 LHHAFLALMKYPKVQARVQEEIDLVV----GRARLPALKDraaMPYTDAVIHEVQRFADIIPMnLPHRVTRDTAFRG--F 380
Cdd:cd11056 249 LSFALYELAKNPEIQEKLREEIDEVLekhgGELTYEALQE---MKYLDQVVNETLRKYPPLPF-LDRVCTKDYTLPGtdV 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 381 LIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFLYLTAILQSFSLQ 460
Cdd:cd11056 325 VIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVE 404

                .
gi 19743565 461 P 461
Cdd:cd11056 405 P 405
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
63-491 5.08e-35

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  Cd Length: 447  Bit Score: 135.82  E-value: 5.08e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  63 GSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPA----FFNFtkgNGIAFSS-GDRWKVLRQFS-IQILRNfg 136
Cdd:cd20654   1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAaklmGYNY---AMFGFAPyGPYWRELRKIAtLELLSN-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 137 mgkRSIEE----RILEEGSFL--LAELRKTEGEPFDPTFV-----LSRSVSNIICSVLFGSRF-----DYDDERLLTIIR 200
Cdd:cd20654  76 ---RRLEKlkhvRVSEVDTSIkeLYSLWSNNKKGGGGVLVemkqwFADLTFNVILRMVVGKRYfggtaVEDDEEAERYKK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 201 LINDNFQIMsspwGELY--DIFPSL--LDWVpGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKM--AE 274
Cdd:cd20654 153 AIREFMRLA----GTFVvsDAIPFLgwLDFG-GHEKAMKRTAKELDSILEEWLEEHRQKRSSSGKSKNDEDDDDVMmlSI 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 275 EKEDPLSHFHMDTLL-MTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVI 353
Cdd:cd20654 228 LEDSQISGYDADTVIkATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIV 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 354 HEVQRFADIIPMNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDAN-------QSFKkspaF 426
Cdd:cd20654 308 KETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHkdidvrgQNFE----L 383
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19743565 427 MPFSAGRRLCLGESLARMELFLYLTAILQSFSL-QPLGAPedIDLTPlSSGLgNLPR--PFQLCLRPR 491
Cdd:cd20654 384 IPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIkTPSNEP--VDMTE-GPGL-TNPKatPLEVLLTPR 447
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
69-462 5.72e-35

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: 135.46  E-value: 5.72e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  69 HLGPRRVVVLSGYQAVKEALVDQGEEFSGrgDYPAFFNFTKGNGIAFSSGDRWKVLRQ-----FSIQILRNFgmgKRSIE 143
Cdd:cd20621   9 NLGSKPLISLVDPEYIKEFLQNHHYYKKK--FGPLGIDRLFGKGLLFSEGEEWKKQRKllsnsFHFEKLKSR---LPMIN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 144 ERILEEgsfllaeLRKTEGEPFDPTFVLSRSVSNIICSVLFGSRFD----YDDERLLTIIRLINDNF-QIMSSPwgeLYD 218
Cdd:cd20621  84 EITKEK-------IKKLDNQNVNIIQFLQKITGEVVIRSFFGEEAKdlkiNGKEIQVELVEILIESFlYRFSSP---YFQ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 219 IFPSLL-----DWVPGPHQRIFQN-----FKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLShfhMDTL 288
Cdd:cd20621 154 LKRLIFgrkswKLFPTKKEKKLQKrvkelRQFIEKIIQNRIKQIKKNKDEIKDIIIDLDLYLLQKKKLEQEIT---KEEI 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 289 LMTTHNLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAMPYTDAVIHEVQRFADIIPMNLP 368
Cdd:cd20621 231 IQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFP 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 369 HRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARMELFL 448
Cdd:cd20621 311 RVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKI 390
                       410
                ....*....|....
gi 19743565 449 YLTAILQSFSLQPL 462
Cdd:cd20621 391 ILIYILKNFEIEII 404
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
50-462 8.27e-35

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: 134.69  E-value: 8.27e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  50 DMLTSLTKLSkEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRGDYPAFFNFTkGNGIAFSSGD---RWKVLRQ 126
Cdd:cd11049   1 DPLGFLSSLR-AHGDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKGGPLFDRARPLL-GNGLATCPGEdhrRQRRLMQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 127 --FSIQILRNFGmgkRSIEERILEegsflLAElRKTEGEPFDPTFVLSRSVSNIICSVLFGSrfDYDDERLLTI---IRL 201
Cdd:cd11049  79 paFHRSRIPAYA---EVMREEAEA-----LAG-SWRPGRVVDVDAEMHRLTLRVVARTLFST--DLGPEAAAELrqaLPV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 202 INDNFQIMSSPwgelydifPSLLDWVPGPHQRIFQN-FKCLRDLIAHSVHDHQASLDPRSprDFIQCFLTKMAEEKEdPL 280
Cdd:cd11049 148 VLAGMLRRAVP--------PKFLERLPTPGNRRFDRaLARLRELVDEIIAEYRASGTDRD--DLLSLLLAARDEEGR-PL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 281 SHFHMDTLLMTthnLLFGGTKTVSTTLHHAFLALMKYPKVQARVQEEIDLVVGrARLPALKDRAAMPYTDAVIHEVQRFA 360
Cdd:cd11049 217 SDEELRDQVIT---LLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLY 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 361 DIIPMnLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGES 440
Cdd:cd11049 293 PPVWL-LTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDT 371
                       410       420
                ....*....|....*....|..
gi 19743565 441 LARMELFLYLTAILQSFSLQPL 462
Cdd:cd11049 372 FALTELTLALATIASRWRLRPV 393
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
62-484 1.51e-33

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: 131.67  E-value: 1.51e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  62 YGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRgdyPAFFNF------TKGNGIAFS-SGDRWKVLRQFSIQIL-- 132
Cdd:cd11066   1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSR---PTFYTFhkvvssTQGFTIGTSpWDESCKRRRKAAASALnr 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 133 RNFgmgkRSIEERILEEGSFLLAELRKTEGE---PFDPTFVLSRSVSNIICSVLFGSRFD-YDDERLLTIIRLINDNFQI 208
Cdd:cd11066  78 PAV----QSYAPIIDLESKSFIRELLRDSAEgkgDIDPLIYFQRFSLNLSLTLNYGIRLDcVDDDSLLLEIIEVESAISK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 209 MSSPWGELYDIFPsLLDWVPGPHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPRDFIQCFLTKMAEEKEDPLSHFHMDTL 288
Cdd:cd11066 154 FRSTSSNLQDYIP-ILRYFPKMSKFRERADEYRNRRDKYLKKLLAKLKEEIEDGTDKPCIVGNILKDKESKLTDAELQSI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 289 LMTthnLLFGGTKTVSTTLHH--AFLALMKYPKVQARVQEEIDLVVGRARLPALKDRAAM--PYTDAVIHEVQRFADIIP 364
Cdd:cd11066 233 CLT---MVSAGLDTVPLNLNHliGHLSHPPGQEIQEKAYEEILEAYGNDEDAWEDCAAEEkcPYVVALVKETLRYFTVLP 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 365 MNLPHRVTRDTAFRGFLIPKGTDVITLLNTVHYDPSQFLTPQEFNPEHFLDANQSFKKSPAFMPFSAGRRLCLGESLARM 444
Cdd:cd11066 310 LGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANR 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 19743565 445 ELFLYLTAILQSFSLQPLGAPEDIDLTPLS-----SGLGNLPRPF 484
Cdd:cd11066 390 ELYTAICRLILLFRIGPKDEEEPMELDPFEynacpTALVAEPKPF 434
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
60-448 1.13e-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: 128.45  E-value: 1.13e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565  60 KEYGSMYTVHLGPRRVVVLSGYQAVKEALVDQGEEFSGRgdYP-AFFNFTKGNGIAFSSGDRWKVLRQFSIQILrnfgmG 138
Cdd:cd11043   3 KRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSW--YPkSVRKLLGKSSLLTVSGEEHKRLRGLLLSFL-----G 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 139 KRSIEERILEE-GSFLLAELRKTEGEPFDPTFVLSRSVS-NIICSVLFGsrfdYDDERLLTIIRLindNFQIMSSPWGEl 216
Cdd:cd11043  76 PEALKDRLLGDiDELVRQHLDSWWRGKSVVVLELAKKMTfELICKLLLG----IDPEEVVEELRK---EFQAFLEGLLS- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 217 ydiFPslLDWvPG-PHQRIFQNFKCLRDLIAHSVHDHQASLDPRSPR-DFIQCFLTKMAEEkEDPLSHFHMDTLLMTthn 294
Cdd:cd11043 148 ---FP--LNL-PGtTFHRALKARKRIRKELKKIIEERRAELEKASPKgDLLDVLLEEKDED-GDSLTDEEILDNILT--- 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743565 295 LLFGGTKTVSTTLhhafLALMKY----PKVQARVQEE-IDLVVGRARLPAL--KDRAAMPYTDAVIHEVQRFADIIPmNL 367
Cdd:cd11043 218 LLFAGHETTSTTL----TLAVKFlaenPKVLQELLEEhEEIAKRKEEGEGLtwEDYKSMK