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Conserved domains on  [gi|124001560|ref|NP_031843|]
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cytochrome P450 2F2 precursor [Mus musculus]

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: 865.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20669   81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20669  161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20669  241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20669  321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 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: 865.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20669   81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20669  161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20669  241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20669  321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20669  401 LGAPEDIDLTPLSSGLGNVPRPFQL 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
31-488 0e+00

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: 515.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560   31 PPGPKPLPILGNLLQLRSQDLLTS-LTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFT- 108
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSvFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  109 --RGNGIAFSDGERWKILRRFSVQILRNFGmgKRSIEERILEEGSFLLEVLRKM--EGKPFDPVFILSRSVSNIICSVVF 184
Cdd:pfam00067  81 pfLGKGIVFANGPRWRQLRRFLTPTFTSFG--KLSFEPRVEEEARDLVEKLRKTagEPGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  185 GSRFD-YDDERLLTIIHFINDNFKIMSSPWGEMYNIFPSvLDWIPGPHKRLFRNFGGM-KDLIARSVREHQDSLDP--NS 260
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPI-LKYFPGPHGRKLKRARKKiKDLLDKLIEERRETLDSakKS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  261 PRDFIDCFLTKMAQEKQdplSHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTL 340
Cdd:pfam00067 238 PRDFLDALLLAKEEEDG---SKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  341 EDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSF 420
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  421 KKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTL--QPLVDPEDIDLTPlssGLGNLPRPFQLCM 488
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVelPPGTDPPDIDETP---GLLLPPKPYKLKF 461
PTZ00404 PTZ00404
cytochrome P450; Provisional
32-491 8.76e-66

cytochrome P450; Provisional


Pssm-ID: 173595  Cd Length: 482  Bit Score: 219.98  E-value: 8.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  32 PGPKPLPILGNLLQLRSQDLLTsLTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGN 111
Cdd:PTZ00404  32 KGPIPIPILGNLHQLGNLPHRD-LTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 112 GIAFSDGERWKILRRFSVQILRNFGMgkRSIEERILEEGSFLLEVLRKME--GKPFDPVFILSRSVSNIICSVVFGSRFD 189
Cdd:PTZ00404 111 GIVTSSGEYWKRNREIVGKAMRKTNL--KHIYDLLDDQVDVLIESMKKIEssGETFEPRYYLTKFTMSAMFKYIFNEDIS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 190 YDDE----RLLTIIHFINDNFKIMSSpwGEMYNIF----PSVLDWIpgphKRLFRNFGGMKDLIARSVREHQDSLDPNSP 261
Cdd:PTZ00404 189 FDEDihngKLAELMGPMEQVFKDLGS--GSLFDVIeitqPLYYQYL----EHTDKNFKKIKKFIKEKYHEHLKTIDPEVP 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 262 RDFIDCFLTKMAQEKQDplshfNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLE 341
Cdd:PTZ00404 263 RDLLDLLIKEYGTNTDD-----DILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLS 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 342 DRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRD-TPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNhsf 420
Cdd:PTZ00404 338 DRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDiIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD--- 414
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124001560 421 kKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQPlVDPEDIDLTPlSSGLGNLPRPFQLCMHIR 491
Cdd:PTZ00404 415 -SNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKS-IDGKKIDETE-EYGLTLKPNKFKVLLEKR 482
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
31-485 1.91e-45

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 163.75  E-value: 1.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  31 PPGPKPLPILGNLLQLRSQDLLTSLTKLSKEYGSVFTVYLGSR--PVIVLSGYQTVKEALVDKGEEFSGRGA---YPVFF 105
Cdd:COG2124    4 PPAPKLLGSPFALPRLLEFAPRFFLERAEDPYGDYFTLRLPGPgdGFWVVSRPADVREVLRDPRFFSSALGAglrPRLLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 106 NFTRGNGIAFSDGERWKILRRFSVQILRNFGMgkRSIEERILEEGSfllEVLRKMEGKPFDPVFILSRSVSNIICSVVFG 185
Cdd:COG2124   84 PVLGDGSLLTLDGPEHTRLRKLLAPAFTPRAL--RGYRPLIREIAD---RLLDDLWQGGADLVLDFAAELTLRVIAELLG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 186 SRFDyDDERLLtiihfindnfkimssPWGEMYNIFPSVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSldpnsPRDfi 265
Cdd:COG2124  159 VPLE-DRPQLL---------------RWSDALLLRLDPDLGPEEPWRRARAARRELDAYLRALIAERRAA-----PRD-- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 266 DcFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRvvgrsrmptledrts 345
Cdd:COG2124  216 D-LLSLLLSAEDDGGGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR--------------- 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 346 mPYTDAVIHEVQRFADVIPMnLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDdnhsfkkspA 425
Cdd:COG2124  280 -PLLEAVVEETLRLYPPVPL-ARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN---------A 348
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124001560 426 FMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQPLVDPEDID--LTPLSSGLGNLPRPFQ 485
Cdd:COG2124  349 HLPFGGGPHRCLGAALARLELKVALAELLRRFPLLLLAEPPPLVrrPTLVPRGGERLPVRRR 410
CYP450_TxtE TIGR04458
4-nitrotryptophan synthase; Members of this family are cytochrome P450 enzymes that convert ...
370-466 8.48e-03

4-nitrotryptophan synthase; Members of this family are cytochrome P450 enzymes that convert L-tryptophan into L-4-nitrotryptophan. In thaxtomin gene clusters, this enzyme (TxtE) uses nitric acid (NO) derived from arginine by the nitric oxide synthase TxtD, and O2, to perform the tryptophan nitration. L-4-nitrotryptophan is then used as a non-proteinogenic amino acid by non-ribosomal peptide synthases (NRPS).


Pssm-ID: 275251  Cd Length: 403  Bit Score: 38.31  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  370 RV-TRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNpehfLDDNHSFKKspafMPFSAGRRLCLGEPLARMELFI 448
Cdd:TIGR04458 295 RVaTTDVDMGGVRIKAGQAVALFLGAANRDPEVFERPNDFD----LDRPNSGRH----LSFGQGVHACLGRQIASLQLKW 366
                          90
                  ....*....|....*....
gi 124001560  449 YFTSILQNF-TLQPLVDPE 466
Cdd:TIGR04458 367 FFVALLGRFpGIRPAGEPL 385
 
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: 865.61  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20669   81 IEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20669  161 SVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20669  241 TVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20669  321 IPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 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: 750.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd11026    1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd11026   81 IEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd11026  161 PLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd11026  241 TTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd11026  321 IPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSS 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 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: 697.09  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20665    1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20665   81 IEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20665  161 ALLDYLPGSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQEKHNQQSEFTLENLAVTVTDLFGAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20665  241 TTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20665  321 IPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKS 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 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: 592.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALANGERWRILRRFSLTILRNFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20670   81 IEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMYS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20670  161 GIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLDPQNPRDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20670  241 TVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRGYL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20670  321 LPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRS 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 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: 579.45  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20668    1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRDFGVGKRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20668   81 IEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20668  161 SVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEKKNPNTEFYMKNLVMTTLNLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20668  241 TVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRDFF 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20668  321 LPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKS 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 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: 550.15  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFANGERWKTLRRFSLATMRDFGMGKRS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20672   81 VEERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20672  161 GFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHQNLMISVLSLFFAGTE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20672  241 TTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRGYL 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20672  321 LPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVAS 400
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20672  401 PVAPEDIDLTPKESGVGKIPPTYQI 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
31-488 0e+00

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: 515.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560   31 PPGPKPLPILGNLLQLRSQDLLTS-LTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFT- 108
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSvFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  109 --RGNGIAFSDGERWKILRRFSVQILRNFGmgKRSIEERILEEGSFLLEVLRKM--EGKPFDPVFILSRSVSNIICSVVF 184
Cdd:pfam00067  81 pfLGKGIVFANGPRWRQLRRFLTPTFTSFG--KLSFEPRVEEEARDLVEKLRKTagEPGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  185 GSRFD-YDDERLLTIIHFINDNFKIMSSPWGEMYNIFPSvLDWIPGPHKRLFRNFGGM-KDLIARSVREHQDSLDP--NS 260
Cdd:pfam00067 159 GERFGsLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPI-LKYFPGPHGRKLKRARKKiKDLLDKLIEERRETLDSakKS 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  261 PRDFIDCFLTKMAQEKQdplSHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTL 340
Cdd:pfam00067 238 PRDFLDALLLAKEEEDG---SKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  341 EDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSF 420
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  421 KKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTL--QPLVDPEDIDLTPlssGLGNLPRPFQLCM 488
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVelPPGTDPPDIDETP---GLLLPPKPYKLKF 461
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
62-486 0e+00

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: 515.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNGENWKEMRRFTLTTLRDFGMGKKT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20664   81 SEDKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWiPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20664  161 WLGPF-PGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFLVKQQEEEESSDSFFHDDNLTCSVGNLFGAGTD 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGrSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20664  240 TTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIG-SRQPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRGYF 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20664  319 IPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQP 398
                        410       420
                 ....*....|....*....|....*..
gi 124001560 462 LVDP--EDIDLTPLsSGLGNLPRPFQL 486
Cdd:cd20664  399 PPGVseDDLDLTPG-LGFTLNPLPHQL 424
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
62-486 3.37e-172

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: 491.23  E-value: 3.37e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKKS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20662   81 LEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKqDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20662  161 WIMKYLPGSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYLKEMAKYP-DPTTSFNEENLICSTLDLFFAGTE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20662  240 TTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLAGFH 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHsFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd20662  320 LPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQ-FKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKP 398
                        410       420
                 ....*....|....*....|....*
gi 124001560 462 LVDpEDIDLTpLSSGLGNLPRPFQL 486
Cdd:cd20662  399 PPN-EKLSLK-FRMGITLSPVPHRI 421
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
62-486 7.31e-148

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: 429.50  E-value: 7.31e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNF---TRGNGIAFSD-GERWKILRRFSVQILRNFGM 137
Cdd:cd20663    1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLgfgPKSQGVVLARyGPAWREQRRFSVSTLRNFGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 138 GKRSIEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMY 217
Cdd:cd20663   81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 218 NIFPsVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNS-PRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLL 296
Cdd:cd20663  161 NAFP-VLLRIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQpPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 297 FGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTP 376
Cdd:cd20663  240 SAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 377 FRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQN 456
Cdd:cd20663  320 VQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQR 399
                        410       420       430
                 ....*....|....*....|....*....|.
gi 124001560 457 FTLQ-PLVDPEDIDLTPLssGLGNLPRPFQL 486
Cdd:cd20663  400 FSFSvPAGQPRPSDHGVF--AFLVSPSPYQL 428
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
62-485 3.12e-141

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: 412.37  E-value: 3.12e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGN-GIAFSD-GERWKILRRFSVQILRNFGMGK 139
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGkDIAFGDySPTWKLHRKLAHSALRLYASGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 140 RSIEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSpwGEMYNI 219
Cdd:cd11027   81 PRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELLGA--GSLLDI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 220 FPSvLDWIPGPHKRLFRNFGG-MKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNM---DTLLMTTHNL 295
Cdd:cd11027  159 FPF-LKYFPNKALRELKELMKeRDEILRKKLEEHKETFDPGNIRDLTDALIKAKKEAEDEGDEDSGLltdDHLVMTISDI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 296 LFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDT 375
Cdd:cd11027  238 FGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTCDT 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 376 PFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSF-KKSPAFMPFSAGRRLCLGEPLARMELFIYFTSIL 454
Cdd:cd11027  318 TLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLvPKPESFLPFSAGRRVCLGESLAKAELFLFLARLL 397
                        410       420       430
                 ....*....|....*....|....*....|.
gi 124001560 455 QNFTLQPLVDPEDIDLTPlSSGLGNLPRPFQ 485
Cdd:cd11027  398 QKFRFSPPEGEPPPELEG-IPGLVLYPLPYK 427
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
63-486 2.18e-140

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: 410.07  E-value: 2.18e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMgKRSI 142
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNGDYWKELRRFALSSLTKTKL-KKKM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 143 EERILEEGSFLLEVLRKME--GKPFDPVFILSRSVSNIICSVVFGSRFD-YDDERLLTIIHFINDNFKIMSSPWgeMYNI 219
Cdd:cd20617   80 EELIEEEVNKLIESLKKHSksGEPFDPRPYFKKFVLNIINQFLFGKRFPdEDDGEFLKLVKPIEEIFKELGSGN--PSDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 220 FPSVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDplSHFNMDTLLMTTHNLLFGG 299
Cdd:cd20617  158 IPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDS--GLFDDDSIISTCLDLFLAG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 300 TETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRG 379
Cdd:cd20617  236 TDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEIGG 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 380 FLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSfKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTL 459
Cdd:cd20617  316 YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGN-KLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKF 394
                        410       420
                 ....*....|....*....|....*..
gi 124001560 460 QPlVDPEDIDlTPLSSGLGNLPRPFQL 486
Cdd:cd20617  395 KS-SDGLPID-EKEVFGLTLKPKPFKV 419
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
63-486 2.37e-137

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: 402.37  E-value: 2.37e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEALVDkgEEFSGRgayPVFFNF---TRGN--GIAFSDGERWKILRRFSVQILRNFGM 137
Cdd:cd20651    1 GDVVGLKLGKDKVVVVSGYEAVREVLSR--EEFDGR---PDGFFFrlrTFGKrlGITFTDGPFWKEQRRFVLRHLRDFGF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 138 GKRSIEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFK--IMSspwGE 215
Cdd:cd20651   76 GRRSMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVHLLFRnfDMS---GG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 216 MYNIFPSVLDWIPG--PHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMaQEKQDPLSHFNMDTLLMTTH 293
Cdd:cd20651  153 LLNQFPWLRFIAPEfsGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNPRDLIDAYLREM-KKKEPPSSSFTDDQLVMICL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 294 NLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTR 373
Cdd:cd20651  232 DLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALK 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 374 DTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSI 453
Cdd:cd20651  312 DTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGL 391
                        410       420       430
                 ....*....|....*....|....*....|...
gi 124001560 454 LQNFTLQPLVDPEdIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20651  392 LQNFTFSPPNGSL-PDLEGIPGGITLSPKPFRV 423
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
62-472 3.45e-136

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: 399.56  E-value: 3.45e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKRT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFdPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20671   81 IEDKILEELQFLNGQIDSFNGKPF-PLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLYP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 sVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKmaQEKQDPLSH-FNMDTLLMTTHNLLFGGT 300
Cdd:cd20671  160 -VLGAFLKLHKPILDKVEEVCMILRTLIEARRPTIDGNPLHSYIEALIQK--QEEDDPKETlFHDANVLACTLDLVMAGT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 301 ETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPmNLPHRVTRDTPFRGF 380
Cdd:cd20671  237 ETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRCTAADTQFKGY 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 381 LIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQ 460
Cdd:cd20671  316 LIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFL 395
                        410
                 ....*....|....
gi 124001560 461 --PLVDPEDIDLTP 472
Cdd:cd20671  396 ppPGVSPADLDATP 409
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
62-460 1.54e-131

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: 387.66  E-value: 1.54e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS 141
Cdd:cd20667    1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLRELGLGKQA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYNIFP 221
Cdd:cd20667   81 LESQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAFP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSlDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTE 301
Cdd:cd20667  161 WLMRYLPGPHQKIFAYHDAVRSFIKKEVIRHELR-TNEAPQDFIDCYLAQITKTKDDPVSTFSEENMIQVVIDLFLGGTE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFL 381
Cdd:cd20667  240 TTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHGYY 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQ 460
Cdd:cd20667  320 VEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQ 398
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
62-486 6.16e-129

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: 381.05  E-value: 6.16e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSD-GERWKILRRFSVQILRNFGMGKR 140
Cdd:cd20666    1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPyGPVWRQQRKFSHSTLRHFGLGKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 141 SIEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKImsSPWGEMYNIF 220
Cdd:cd20666   81 SLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEI--SVNSAAILVN 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 221 P-SVLDWIP-GPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPL-SHFNMDTLLMTTHNLLF 297
Cdd:cd20666  159 IcPWLYYLPfGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLHIEEEQKNNAeSSFNEDYLFYIIGDLFI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 298 GGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPF 377
Cdd:cd20666  239 AGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVL 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 378 RGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNF 457
Cdd:cd20666  319 QGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSF 398
                        410       420       430
                 ....*....|....*....|....*....|.
gi 124001560 458 TLQPlvdPEDIDLTPLSS--GLGNLPRPFQL 486
Cdd:cd20666  399 TFLL---PPNAPKPSMEGrfGLTLAPCPFNI 426
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
55-487 2.42e-119

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: 356.82  E-value: 2.42e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  55 LTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSD-GERWKILRRFSVQILR 133
Cdd:cd20661    5 MKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKyGRGWTEHRKLAVNCFR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 134 NFGMGKRSIEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPW 213
Cdd:cd20661   85 YFGYGQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 214 GEMYNIFPsvldWIP----GPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTLL 289
Cdd:cd20661  165 VFLYNAFP----WIGilpfGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 290 MTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPH 369
Cdd:cd20661  241 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 370 RVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFIY 449
Cdd:cd20661  321 ATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLF 400
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 124001560 450 FTSILQNFTLQplVDPEDI-DLTPlSSGLGNLPRPFQLC 487
Cdd:cd20661  401 FTALLQRFHLH--FPHGLIpDLKP-KLGMTLQPQPYLIC 436
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
62-486 3.11e-117

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: 351.21  E-value: 3.11e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRgayPVFFNFT---RGNGIAFSD-GERWKILRRFSVQILRNFGM 137
Cdd:cd11028    1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGR---PDFYSFQfisNGKSMAFSDyGPRWKLHRKLAQNALRTFSN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 138 GKRS--IEERILEEGSFLLEVLRKMEGK--PFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHfINDNF-KIMSSp 212
Cdd:cd11028   78 ARTHnpLEEHVTEEAEELVTELTENNGKpgPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVK-SNDDFgAFVGA- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 213 wGEMYNIFPsvldWIPGPHKRLFRNF----GGMKDLIARSVREHQDSLDPNSPRDFIDCFLtKMAQEKQD---PLSHFNm 285
Cdd:cd11028  156 -GNPVDVMP----WLRYLTRRKLQKFkellNRLNSFILKKVKEHLDTYDKGHIRDITDALI-KASEEKPEeekPEVGLT- 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 286 DTLLMTTHNLLFG-GTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIP 364
Cdd:cd11028  229 DEHIISTVQDLFGaGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVP 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 365 MNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPA--FMPFSAGRRLCLGEPLA 442
Cdd:cd11028  309 FTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTKVdkFLPFGAGRRRCLGEELA 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 124001560 443 RMELFIYFTSILQNFTLQPlVDPEDIDLTPlSSGLGNLPRPFQL 486
Cdd:cd11028  389 RMELFLFFATLLQQCEFSV-KPGEKLDLTP-IYGLTMKPKPFKV 430
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
62-486 3.19e-104

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: 318.19  E-value: 3.19e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRgayPVFFNFT---RGNGIAFSD--GERWKILRRFSVQILRNFG 136
Cdd:cd20677    1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGR---PDFYTFSliaNGKSMTFSEkyGESWKLHKKIAKNALRTFS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 137 MGKRS-------IEERILEEGSFLLEVLRKMEGK--PFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFK 207
Cdd:cd20677   78 KEEAKsstcsclLEEHVCAEASELVKTLVELSKEkgSFDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVEINNDLLK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 208 IMSSpwGEMYNIFPsVLDWIPGPHKRLFRNF-GGMKDLIARSVREHQDSLDPNSPRDFIDCFL----TKMAQEKQDPLSH 282
Cdd:cd20677  158 ASGA--GNLADFIP-ILRYLPSPSLKALRKFiSRLNNFIAKSVQDHYATYDKNHIRDITDALIalcqERKAEDKSAVLSD 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 283 fnmDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADV 362
Cdd:cd20677  235 ---EQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSF 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 363 IPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPA--FMPFSAGRRLCLGEP 440
Cdd:cd20677  312 VPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVekVLIFGMGVRKCLGED 391
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 124001560 441 LARMELFIYFTSILQNFTLQPLVDPEdIDLTPlSSGLGNLPRPFQL 486
Cdd:cd20677  392 VARNEIFVFLTTILQQLKLEKPPGQK-LDLTP-VYGLTMKPKPYRL 435
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
63-486 8.79e-98

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: 301.25  E-value: 8.79e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEALvdKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFSVQILRNFGMGKRS- 141
Cdd:cd20652    1 GSIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGGNGIICAEGDLWRDQRRFVHDWLRQFGMTKFGn 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 ----IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMsspwGEMy 217
Cdd:cd20652   79 grakMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLI----GVA- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 218 nifpSVLDWIP---------GPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRD---FIDCFLTKMAQE--KQDPLSHF 283
Cdd:cd20652  154 ----GPVNFLPflrhlpsykKAIEFLVQGQAKTHAIYQKIIDEHKRRLKPENPRDaedFELCELEKAKKEgeDRDLFDGF 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 284 NMDTLLMTTHNLLFG-GTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADV 362
Cdd:cd20652  230 YTDEQLHHLLADLFGaGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSV 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 363 IPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLA 442
Cdd:cd20652  310 VPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELA 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 124001560 443 RMELFIYFTSILQNFTLQpLVDPEDIDLTPLSSGLGNLPRPFQL 486
Cdd:cd20652  390 RMILFLFTARILRKFRIA-LPDGQPVDSEGGNVGITLTPPPFKI 432
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
62-486 2.19e-96

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: 298.07  E-value: 2.19e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSD-GERWKILRRFSVQILRNFGMG-- 138
Cdd:cd20675    1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFGGySERWKAHRRVAHSTVRAFSTRnp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 139 --KRSIEERILEEGSFLLEVL--RKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFiNDNF-------- 206
Cdd:cd20675   81 rtRKAFERHVLGEARELVALFlrKSAGGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLGR-NDQFgrtvgags 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 207 --KIMssPWgemynifpsvLDWIPGPHKRLFRNFGGMK----DLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPL 280
Cdd:cd20675  160 lvDVM--PW----------LQYFPNPVRTVFRNFKQLNrefyNFVLDKVLQHRETLRGGAPRDMMDAFILALEKGKSGDS 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 281 SHFNMDTLLMTTHNLLFG-GTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRF 359
Cdd:cd20675  228 GVGLDKEYVPSTVTDIFGaSQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRF 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 360 ADVIPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAF--MPFSAGRRLCL 437
Cdd:cd20675  308 SSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLASsvMIFSVGKRRCI 387
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 124001560 438 GEPLARMELFIyFTSILQ---NFTLQPlVDPEDIDltpLSSGLGNLPRPFQL 486
Cdd:cd20675  388 GEELSKMQLFL-FTSILAhqcNFTANP-NEPLTMD---FSYGLTLKPKPFTI 434
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
62-460 2.36e-95

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: 295.00  E-value: 2.36e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTR-GNGIAFSD-GERWKILRRFSVQILRNFGMGK 139
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRnGKDIAFADySATWQLHRKLVHSAFALFGEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 140 RSIEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSpwGEMYNI 219
Cdd:cd20673   81 QKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILNYNEGIVDTVAK--DSLVDI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 220 FPsVLDWIPGPHKRLFRNFGGMKD-LIARSVREHQDSLDPNSPRDFIDCFLT-KM------AQEKQDPLShFNMDTLLMT 291
Cdd:cd20673  159 FP-WLQIFPNKDLEKLKQCVKIRDkLLQKKLEEHKEKFSSDSIRDLLDALLQaKMnaennnAGPDQDSVG-LSDDHILMT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 292 THNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRV 371
Cdd:cd20673  237 VGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPLLIPHVA 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 372 TRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDD--NHSFKKSPAFMPFSAGRRLCLGEPLARMELFIY 449
Cdd:cd20673  317 LQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPtgSQLISPSLSYLPFGAGPRVCLGEALARQELFLF 396
                        410
                 ....*....|.
gi 124001560 450 FTSILQNFTLQ 460
Cdd:cd20673  397 MAWLLQRFDLE 407
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
62-472 5.15e-94

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: 291.92  E-value: 5.15e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFS--DGERWKILRRFSVQILRNFGM-- 137
Cdd:cd20676    1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLTFStdSGPVWRARRKLAQNALKTFSIas 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 138 GKRS-----IEERILEEGSFLLEVLRK-MEGK-PFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMS 210
Cdd:cd20676   81 SPTSsssclLEEHVSKEAEYLVSKLQElMAEKgSFDPYRYIVVSVANVICAMCFGKRYSHDDQELLSLVNLSDEFGEVAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 211 SpwGEMYNIFPsVLDWIPGPHKRLFRNFGG-MKDLIARSVREHQDSLDPNSPRDFIDCfLTKMAQEKQ-DPLSHFNM-DT 287
Cdd:cd20676  161 S--GNPADFIP-ILRYLPNPAMKRFKDINKrFNSFLQKIVKEHYQTFDKDNIRDITDS-LIEHCQDKKlDENANIQLsDE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 288 LLMTTHNLLFG-GTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMN 366
Cdd:cd20676  237 KIVNIVNDLFGaGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 367 LPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFL-DDNHSFKK--SPAFMPFSAGRRLCLGEPLAR 443
Cdd:cd20676  317 IPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLtADGTEINKteSEKVMLFGLGKRRCIGESIAR 396
                        410       420       430
                 ....*....|....*....|....*....|.
gi 124001560 444 MELFIYFTSILQN--FTLQPlvdPEDIDLTP 472
Cdd:cd20676  397 WEVFLFLAILLQQleFSVPP---GVKVDMTP 424
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
62-488 3.82e-87

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: 273.91  E-value: 3.82e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRgayPVFFNFT----RGNGIAFSD-GERWKILRRFSVQILRNfG 136
Cdd:cd20674    1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGR---PHSYTGKlvsqGGQDLSLGDySLLWKAHRKLTRSALQL-G 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 137 MgKRSIEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDErLLTIIHFINDNFKIMSSPWGEM 216
Cdd:cd20674   77 I-RNSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKEDKDTL-VQAFHDCVQELLKTWGHWSIQA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 217 YNIFPSvLDWIPGPH-KRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQD-PLSHFNMDTLLMTTHN 294
Cdd:cd20674  155 LDSIPF-LRFFPNPGlRRLKQAVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQPRGEkGMGQLLEGHVHMAVVD 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 295 LLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRD 374
Cdd:cd20674  234 LFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTRD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 375 TPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSfkkSPAFMPFSAGRRLCLGEPLARMELFIYFTSIL 454
Cdd:cd20674  314 SSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAA---NRALLPFGCGARVCLGEPLARLELFVFLARLL 390
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 124001560 455 QNFTLQPLVDPEDIDLTPLSSglGNL-PRPFQLCM 488
Cdd:cd20674  391 QAFTLLPPSDGALPSLQPVAG--INLkVQPFQVRL 423
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
62-484 2.87e-85

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: 268.68  E-value: 2.87e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  62 YGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNF-TRGNGIAFSD-GERWKILRRFSVQILRNfgMGK 139
Cdd:cd11065    1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELmGWGMRLLLMPyGPRWRLHRRLFHQLLNP--SAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 140 RSIEERILEEG-SFLLEVLRKmegkPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMSSPWGEMYN 218
Cdd:cd11065   79 RKYRPLQELESkQLLRDLLES----PDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGAYLVD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 219 IFPsVLDWIPGP------------HKRLFRNFGGMKDLIARSVREHQDSldpnsprdfiDCFlTKMAQEKQDPLSHFNMD 286
Cdd:cd11065  155 FFP-FLRYLPSWlgapwkrkarelRELTRRLYEGPFEAAKERMASGTAT----------PSF-VKDLLEELDKEGGLSEE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 287 TLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMN 366
Cdd:cd11065  223 EIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLG 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 367 LPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDD--NHSFKKSPAFMPFSAGRRLCLGEPLARM 444
Cdd:cd11065  303 IPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDpkGTPDPPDPPHFAFGFGRRICPGRHLAEN 382
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 124001560 445 ELFIYFTSILQNFTLQPLVDPEDIDLTP---LSSGLGNLPRPF 484
Cdd:cd11065  383 SLFIAIARLLWAFDIKKPKDEGGKEIPDepeFTDGLVSHPLPF 425
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
63-481 4.55e-67

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: 220.46  E-value: 4.55e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRRFsvqILRNFGMGK-RS 141
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRL---LAPAFTPRAlAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 142 IEERILEEGSFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDnfkimsspwgemYNIFP 221
Cdd:cd00302   78 LRPVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLK------------LLGPR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 222 SVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIdcfltkMAQEKQDPLSHfnmDTLLMTTHNLLFGGTE 301
Cdd:cd00302  146 LLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLL------ADADDGGGLSD---EEIVAELLTLLLAGHE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 302 TVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRsrmPTLEDRTSMPYTDAVIHEVQRFADVIPMnLPHRVTRDTPFRGFL 381
Cdd:cd00302  217 TTASLLAWALYLLARHPEVQERLRAEIDAVLGD---GTPEDLSKLPYLEAVVEETLRLYPPVPL-LPRVATEDVELGGYT 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 382 IPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNhsFKKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQP 461
Cdd:cd00302  293 IPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPER--EEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFEL 370
                        410       420
                 ....*....|....*....|.
gi 124001560 462 LVDPE-DIDLTPLSSGLGNLP 481
Cdd:cd00302  371 VPDEElEWRPSLGTLGPASLP 391
PTZ00404 PTZ00404
cytochrome P450; Provisional
32-491 8.76e-66

cytochrome P450; Provisional


Pssm-ID: 173595  Cd Length: 482  Bit Score: 219.98  E-value: 8.76e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  32 PGPKPLPILGNLLQLRSQDLLTsLTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGN 111
Cdd:PTZ00404  32 KGPIPIPILGNLHQLGNLPHRD-LTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 112 GIAFSDGERWKILRRFSVQILRNFGMgkRSIEERILEEGSFLLEVLRKME--GKPFDPVFILSRSVSNIICSVVFGSRFD 189
Cdd:PTZ00404 111 GIVTSSGEYWKRNREIVGKAMRKTNL--KHIYDLLDDQVDVLIESMKKIEssGETFEPRYYLTKFTMSAMFKYIFNEDIS 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 190 YDDE----RLLTIIHFINDNFKIMSSpwGEMYNIF----PSVLDWIpgphKRLFRNFGGMKDLIARSVREHQDSLDPNSP 261
Cdd:PTZ00404 189 FDEDihngKLAELMGPMEQVFKDLGS--GSLFDVIeitqPLYYQYL----EHTDKNFKKIKKFIKEKYHEHLKTIDPEVP 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 262 RDFIDCFLTKMAQEKQDplshfNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLE 341
Cdd:PTZ00404 263 RDLLDLLIKEYGTNTDD-----DILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLS 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 342 DRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRD-TPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNhsf 420
Cdd:PTZ00404 338 DRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDiIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD--- 414
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124001560 421 kKSPAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQPlVDPEDIDLTPlSSGLGNLPRPFQLCMHIR 491
Cdd:PTZ00404 415 -SNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKS-IDGKKIDETE-EYGLTLKPNKFKVLLEKR 482
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
63-471 2.25e-60

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: 203.94  E-value: 2.25e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFT-RGNGIAFSD-GERWKILRR-FSVQILRNfgmgK 139
Cdd:cd20618    1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSyNGQDIVFAPyGPHWRHLRKiCTLELFSA----K 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 140 RsIEE----RILEEGSFLLEVLRKME-GKPFDPVFILSRSVSNIICSVVFGSRF----DYDDERLLTIIHFINDNFKIMS 210
Cdd:cd20618   77 R-LESfqgvRKEELSHLVKSLLEESEsGKPVNLREHLSDLTLNNITRMLFGKRYfgesEKESEEAREFKELIDEAFELAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 211 SP-WGEmYNIFPSVLDWiPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKM-AQEKQDPLSHFNMDTL 288
Cdd:cd20618  156 AFnIGD-YIPWLRWLDL-QGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLlDLDGEGKLSDDNIKAL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 289 LMtthNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLP 368
Cdd:cd20618  234 LL---DMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLP 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 369 HRVTRDTPFRGFLIPKGTdvITLLNT--VHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAF--MPFSAGRRLCLGEPLA-R 443
Cdd:cd20618  311 HESTEDCKVAGYDIPAGT--RVLVNVwaIGRDPKVWEDPLEFKPERFLESDIDDVKGQDFelLPFGSGRRMCPGMPLGlR 388
                        410       420
                 ....*....|....*....|....*....
gi 124001560 444 MeLFIYFTSILQNFTLQ-PLVDPEDIDLT 471
Cdd:cd20618  389 M-VQLTLANLLHGFDWSlPGPKPEDIDME 416
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
63-472 2.70e-60

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: 203.52  E-value: 2.70e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKE-----ALVDKGEEfsgrgaYPVFFNFTrGNGIAFSDGERWKILRR-----FSVQIL 132
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVilsssKLITKSFL------YDFLKPWL-GDGLLTSTGEKWRKRRKlltpaFHFKIL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 133 RNFgmgkrsiEERILEEGSFLLEVLRKMEGKP-FDPVFILSRSVSNIICSVVFGSRFDY---DDERLLTIIHFINDNFKI 208
Cdd:cd20628   74 ESF-------VEVFNENSKILVEKLKKKAGGGeFDIFPYISLCTLDIICETAMGVKLNAqsnEDSEYVKAVKRILEIILK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 209 -MSSPWgeMYNIFpsvLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSL-------------DPNSPRDFIDCFLtkMAQ 274
Cdd:cd20628  147 rIFSPW--LRFDF---IFRLTSLGKEQRKALKVLHDFTNKVIKERREELkaekrnseeddefGKKKRKAFLDLLL--EAH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 275 EKQDPLSHFNM----DTLLmtthnllFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRS-RMPTLEDRTSMPYT 349
Cdd:cd20628  220 EDGGPLTDEDIreevDTFM-------FAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDdRRPTLEDLNKMKYL 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 350 DAVIHEVQRFADVIPMnLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSfKKSP-AFMP 428
Cdd:cd20628  293 ERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSA-KRHPyAYIP 370
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 124001560 429 FSAGRRLCLGEPLARMELFIYFTSILQNFTLQPLVDPEDIDLTP 472
Cdd:cd20628  371 FSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGEDLKLIA 414
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
61-471 9.40e-55

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: 189.21  E-value: 9.40e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  61 EYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGN-GIAFSD-GERWKILRRFSVQIL------ 132
Cdd:cd11072    1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGkDIAFAPyGEYWRQMRKICVLELlsakrv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 133 RNFgmgkRSIEErilEEGSFLLEVLRKMEGKPfdPVFILSRSV----SNIICSVVFGSRFDYDDERllTIIHFINDNFKI 208
Cdd:cd11072   81 QSF----RSIRE---EEVSLLVKKIRESASSS--SPVNLSELLfsltNDIVCRAAFGRKYEGKDQD--KFKELVKEALEL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 209 MSSPWGEmyNIFPSV--LDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQD---PLSHF 283
Cdd:cd11072  150 LGGFSVG--DYFPSLgwIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDlefPLTRD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 284 NMDTLLMtthNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVI 363
Cdd:cd11072  228 NIKAIIL---DMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPA 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 364 PMNLPHRVTRDTPFRGFLIPKGTDVITllNT--VHYDSDQFKTPQEFNPEHFLDDN-----HSFKkspaFMPFSAGRRLC 436
Cdd:cd11072  305 PLLLPRECREDCKINGYDIPAKTRVIV--NAwaIGRDPKYWEDPEEFRPERFLDSSidfkgQDFE----LIPFGAGRRIC 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 124001560 437 LG--------E-PLARMeLFiYFtsilqNFTLQPLVDPEDIDLT 471
Cdd:cd11072  379 PGitfglanvElALANL-LY-HF-----DWKLPDGMKPEDLDME 415
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
59-471 6.44e-54

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: 186.97  E-value: 6.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  59 SKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNG-IAFSD-GERWKILRR------FSVQ 130
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSsIVWPPyGPRWRMLRKicttelFSPK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 131 ILRNFgmgkRSIEERILEEgsfLLEVLRKMEGKPfDPVFI---LSRSVSNIICSVVFGSR-FDYDDERLLTIIHFINDNF 206
Cdd:cd11073   81 RLDAT----QPLRRRKVRE---LVRYVREKAGSG-EAVDIgraAFLTSLNLISNTLFSVDlVDPDSESGSEFKELVREIM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 207 KIMSSPwgemyNI---FPSV--LDWiPGPHKRLFRNFGGMKDLIARSVREH--QDSLDPNSPRDFIDCFLTKMAQEKQDP 279
Cdd:cd11073  153 ELAGKP-----NVadfFPFLkfLDL-QGLRRRMAEHFGKLFDIFDGFIDERlaEREAGGDKKKDDDLLLLLDLELDSESE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 280 LSHFNMDTLLMtthNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRF 359
Cdd:cd11073  227 LTRNHIKALLL---DLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 360 ADVIPMNLPHRVTRDTPFRGFLIPKGTDVitLLNT--VHYDSDQFKTPQEFNPEHFLDDNHSFK-KSPAFMPFSAGRRLC 436
Cdd:cd11073  304 HPPAPLLLPRKAEEDVEVMGYTIPKGTQV--LVNVwaIGRDPSVWEDPLEFKPERFLGSEIDFKgRDFELIPFGSGRRIC 381
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 124001560 437 LGEPLA-RMELFIyFTSILQNF--TLQPLVDPEDIDLT 471
Cdd:cd11073  382 PGLPLAeRMVHLV-LASLLHSFdwKLPDGMKPEDLDME 418
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
63-473 6.08e-50

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: 175.85  E-value: 6.08e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAY----PVFfnftrGNGIAFSDGERWKILRR-----FSVQILR 133
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYerlkLLL-----GNGLLTSEGDLWRRQRRlaqpaFHRRRIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 134 NFGmgkrsieERILEEGSFLLEVLRKMEG-KPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNF-KIMSS 211
Cdd:cd20620   76 AYA-------DAMVEATAALLDRWEAGARrGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGDALDVALEYAaRRMLS 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 212 PwgemyniFPSVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDslDPNSPRDFIDCFLtkMAQEKQD--PLShfnmDTLL 289
Cdd:cd20620  149 P-------FLLPLWLPTPANRRFRRARRRLDEVIYRLIAERRA--APADGGDLLSMLL--AARDEETgePMS----DQQL 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 290 ----MTthnLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRsRMPTLEDRTSMPYTDAVIHEVQRFADVIPM 365
Cdd:cd20620  214 rdevMT---LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGG-RPPTAEDLPQLPYTEMVLQESLRLYPPAWI 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 366 nLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDD----NHSFkkspAFMPFSAGRRLCLGEPL 441
Cdd:cd20620  290 -IGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEreaaRPRY----AYFPFGGGPRICIGNHF 364
                        410       420       430
                 ....*....|....*....|....*....|..
gi 124001560 442 ARMELFIYFTSILQNFTLQpLVDPEDIDLTPL 473
Cdd:cd20620  365 AMMEAVLLLATIAQRFRLR-LVPGQPVEPEPL 395
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
61-467 3.25e-48

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: 171.61  E-value: 3.25e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  61 EYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTrGNGIAFSDGERWKILRR-----FSVQILRNf 135
Cdd:cd11055    1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEPF-DSSLLFLKGERWKRLRTtlsptFSSGKLKL- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 136 gmgkrsIEERILEEGSFLLEVLRKM--EGKPFDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKimSSPW 213
Cdd:cd11055   79 ------MVPIINDCCDELVEKLEKAaeTGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFR--NSII 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 214 GEMYNIFPSVLDWIPgpHKRLFRNFGG-----MKDLIaRSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLSHFNMDTL 288
Cdd:cd11055  151 RLFLLLLLFPLRLFL--FLLFPFVFGFksfsfLEDVV-KKIIEQRRKNKSSRRKDLLQLMLDAQDSDEDVSKKKLTDDEI 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 289 LMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLp 368
Cdd:cd11055  228 VAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFIS- 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 369 HRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELFI 448
Cdd:cd11055  307 RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKL 386
                        410
                 ....*....|....*....
gi 124001560 449 YFTSILQNFTLQPLVDPED 467
Cdd:cd11055  387 ALVKILQKFRFVPCKETEI 405
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
61-471 3.28e-48

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: 171.66  E-value: 3.28e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  61 EYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFN-FTRG-NGIAFSD-GERWKILRR------FSVQI 131
Cdd:cd11075    1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVlFSSNkHMVNSSPyGPLWRTLRRnlvsevLSPSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 132 LRNFgmgkRSIEERILEEgsfLLEVLRKMEGKPFDPVFILS---RSVSNIICSVVFGSRFDydDERLLTIIHFINDNFKI 208
Cdd:cd11075   81 LKQF----RPARRRALDN---LVERLREEAKENPGPVNVRDhfrHALFSLLLYMCFGERLD--EETVRELERVQRELLLS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 209 MSSPwgEMYNIFPsVLDWIPGPHKR------LFRNFGGMKDLI-ARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLS 281
Cdd:cd11075  152 FTDF--DVRDFFP-ALTWLLNRRRWkkvlelRRRQEEVLLPLIrARRKRRASGEADKDYTDFLLLDLLDLKEEGGERKLT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 282 HFNMDTLLMTThnlLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFAD 361
Cdd:cd11075  229 DEELVSLCSEF---LNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 362 VIPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLD-----DNHSFKKSPAFMPFSAGRRLC 436
Cdd:cd11075  306 PGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAggeaaDIDTGSKEIKMMPFGAGRRIC 385
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 124001560 437 LGEPLARMELFIYFTSILQNFTLQPlVDPEDIDLT 471
Cdd:cd11075  386 PGLGLATLHLELFVARLVQEFEWKL-VEGEEVDFS 419
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
60-471 9.79e-46

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: 165.01  E-value: 9.79e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  60 KEYGSVFTVYLGSRPVIVLS---GYQTVkealvdkgeeFSGRGAYP--------VFFNFTRGN--GIAFSDGERWKILRR 126
Cdd:cd11054    2 KKYGPIVREKLGGRDIVHLFdpdDIEKV----------FRNEGKYPirpsleplEKYRKKRGKplGLLNSNGEEWHRLRS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 127 -FSVQILR-----NF--GMGK------RSIEERILEEGSF---LLEVLRK--MEGkpfdpvfilsrsvsniICSVVFGSR 187
Cdd:cd11054   72 aVQKPLLRpksvaSYlpAINEvaddfvERIRRLRDEDGEEvpdLEDELYKwsLES----------------IGTVLFGKR 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 188 F----DYDDERLLTIIHFINDNFKIMsspwGEMYNIFPSVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSLDPNSPRD 263
Cdd:cd11054  136 LgcldDNPDSDAQKLIEAVKDIFESS----AKLMFGPPLWKYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEED 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 264 FID-CFLTKMAQEKQdplshFNMDTLLMTTHNLLFGGTETVGTTLrhAFLI--LMKYPKVQARVQEEIDRVVGRSRMPTL 340
Cdd:cd11054  212 EEEdSLLEYLLSKPG-----LSKKEIVTMALDLLLAGVDTTSNTL--AFLLyhLAKNPEVQEKLYEEIRSVLPDGEPITA 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 341 EDRTSMPYTDAVIHEVQRFADVIPMNLphRVT-RDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHS 419
Cdd:cd11054  285 EDLKKMPYLKACIKESLRLYPVAPGNG--RILpKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSE 362
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 124001560 420 FKKSPAF--MPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQPlvDPEDIDLT 471
Cdd:cd11054  363 NKNIHPFasLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEY--HHEELKVK 414
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
31-485 1.91e-45

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 163.75  E-value: 1.91e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  31 PPGPKPLPILGNLLQLRSQDLLTSLTKLSKEYGSVFTVYLGSR--PVIVLSGYQTVKEALVDKGEEFSGRGA---YPVFF 105
Cdd:COG2124    4 PPAPKLLGSPFALPRLLEFAPRFFLERAEDPYGDYFTLRLPGPgdGFWVVSRPADVREVLRDPRFFSSALGAglrPRLLR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 106 NFTRGNGIAFSDGERWKILRRFSVQILRNFGMgkRSIEERILEEGSfllEVLRKMEGKPFDPVFILSRSVSNIICSVVFG 185
Cdd:COG2124   84 PVLGDGSLLTLDGPEHTRLRKLLAPAFTPRAL--RGYRPLIREIAD---RLLDDLWQGGADLVLDFAAELTLRVIAELLG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 186 SRFDyDDERLLtiihfindnfkimssPWGEMYNIFPSVLDWIPGPHKRLFRNFGGMKDLIARSVREHQDSldpnsPRDfi 265
Cdd:COG2124  159 VPLE-DRPQLL---------------RWSDALLLRLDPDLGPEEPWRRARAARRELDAYLRALIAERRAA-----PRD-- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 266 DcFLTKMAQEKQDPLSHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRvvgrsrmptledrts 345
Cdd:COG2124  216 D-LLSLLLSAEDDGGGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR--------------- 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 346 mPYTDAVIHEVQRFADVIPMnLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDdnhsfkkspA 425
Cdd:COG2124  280 -PLLEAVVEETLRLYPPVPL-ARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN---------A 348
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124001560 426 FMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQPLVDPEDID--LTPLSSGLGNLPRPFQ 485
Cdd:COG2124  349 HLPFGGGPHRCLGAALARLELKVALAELLRRFPLLLLAEPPPLVrrPTLVPRGGERLPVRRR 410
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
55-465 1.39e-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: 161.60  E-value: 1.39e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  55 LTKLSKEYGSVFTV-YLGSRPVIVLSGYQTVKEALVDKGEEFSGRGA----YPVFFNftrgNGIAFSDGERWKILRR--- 126
Cdd:cd11053    4 LERLRARYGDVFTLrVPGLGPVVVLSDPEAIKQIFTADPDVLHPGEGnsllEPLLGP----NSLLLLDGDRHRRRRKllm 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 127 --FSVQILRNFGmgkRSIEERILEEgsflLEVLRkmEGKPFDPVFILSRSVSNIICSVVFGSrfdYDDERLLTIIHFIND 204
Cdd:cd11053   80 paFHGERLRAYG---ELIAEITERE----IDRWP--PGQPFDLRELMQEITLEVILRVVFGV---DDGERLQELRRLLPR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 205 NFKIMSSPWgemyNIFPSVL-DWIP-GPHKRLFRNFGGMKDLIARSVREHQDslDPNSPRDFIdcfLTKMAQEKQDPLSH 282
Cdd:cd11053  148 LLDLLSSPL----ASFPALQrDLGPwSPWGRFLRARRRIDALIYAEIAERRA--EPDAERDDI---LSLLLSARDEDGQP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 283 FNMDTL---LMTthnLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRsrmPTLEDRTSMPYTDAVIHEVQRF 359
Cdd:cd11053  219 LSDEELrdeLMT---LLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGD---PDPEDIAKLPYLDAVIKETLRL 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 360 ADVIPMnLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDdnhsFKKSP-AFMPFSAGRRLCLG 438
Cdd:cd11053  293 YPVAPL-VPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLG----RKPSPyEYLPFGGGVRRCIG 367
                        410       420
                 ....*....|....*....|....*..
gi 124001560 439 EPLARMELFIYFTSILQNFTLQPLVDP 465
Cdd:cd11053  368 AAFALLEMKVVLATLLRRFRLELTDPR 394
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
70-466 9.99e-43

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: 156.65  E-value: 9.99e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  70 LGSRPVIVLSGYQTVKEALVDKGEEFSGrgAYPVFFNFTRGNGIAFSDGERWKILRR-----FSVQILRnfgmgkrSIEE 144
Cdd:cd20621   10 LGSKPLISLVDPEYIKEFLQNHHYYKKK--FGPLGIDRLFGKGLLFSEGEEWKKQRKllsnsFHFEKLK-------SRLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 145 RILEegsFLLEVLRKMEGKPFDPVFILSRSVSNIICSVVFGSRFD---YDDERLLTIIHFINDNF--KIMSSPWgemYNI 219
Cdd:cd20621   81 MINE---ITKEKIKKLDNQNVNIIQFLQKITGEVVIRSFFGEEAKdlkINGKEIQVELVEILIESflYRFSSPY---FQL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 220 FPSVL-----DWIPGPHKR-------LFRNFggMKDLIARSVREHQDSLDPNSPRDFIDCFLTKMAQEKQDPLShfnMDT 287
Cdd:cd20621  155 KRLIFgrkswKLFPTKKEKklqkrvkELRQF--IEKIIQNRIKQIKKNKDEIKDIIIDLDLYLLQKKKLEQEIT---KEE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 288 LLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNL 367
Cdd:cd20621  230 IIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLF 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 368 PHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKSPAFMPFSAGRRLCLGEPLARMELF 447
Cdd:cd20621  310 PRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAK 389
                        410
                 ....*....|....*....
gi 124001560 448 IYFTSILQNFTLQPLVDPE 466
Cdd:cd20621  390 IILIYILKNFEIEIIPNPK 408
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
23-471 1.23e-42

cytochrome P450 family protein; Provisional


Pssm-ID: 215583  Cd Length: 514  Bit Score: 158.45  E-value: 1.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  23 SSRGKGQLPPGPKPLPILGNLLQLRSQDLLTsLTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYP 102
Cdd:PLN03112  26 SMRKSLRLPPGPPRWPIVGNLLQLGPLPHRD-LASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 103 VFFNFTRGNG-IAFSD-GERWKILRRFSVQILRNFGMGKRSIEERILEEGSFLLEVLRKME-GKPFDPVFILSRSVSNII 179
Cdd:PLN03112 105 AAVHLAYGCGdVALAPlGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHLIQDVWEAAQtGKPVNLREVLGAFSMNNV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 180 CSVVFGSRF----DYDDERLLTIIHFINDNFKIMsspwGEMY-NIFPSVLDWIP--GPHKRLFRNFGGMKDLIARSVREH 252
Cdd:PLN03112 185 TRMLLGKQYfgaeSAGPKEAMEFMHITHELFRLL----GVIYlGDYLPAWRWLDpyGCEKKMREVEKRVDEFHDKIIDEH 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 253 QDS----LDPNSPRDFIDCFLTKMAQEKQDplsHFNMDTLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEI 328
Cdd:PLN03112 261 RRArsgkLPGGKDMDFVDVLLSLPGENGKE---HMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEEL 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 329 DRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEF 408
Cdd:PLN03112 338 DSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEF 417
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 409 NPE-HFLDDNHSFKKS--PAF--MPFSAGRRLCLGEPLARMELFIYFTSILQNF--TLQPLVDPEDIDLT 471
Cdd:PLN03112 418 RPErHWPAEGSRVEIShgPDFkiLPFSAGKRKCPGAPLGVTMVLMALARLFHCFdwSPPDGLRPEDIDTQ 487
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
22-470 1.42e-41

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 155.40  E-value: 1.42e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  22 FSSRGKGQLPPGPKPLPILGNLLQLRSQDLLTsLTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGR--- 98
Cdd:PLN00110  24 LLPKPSRKLPPGPRGWPLLGALPLLGNMPHVA-LAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRppn 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  99 -GAYPVFFNftrGNGIAFSD-GERWKILRRFSvqilrNFGM-GKRSIEERILEEGSFLLEVLRKM-----EGKPFDPVFI 170
Cdd:PLN00110 103 aGATHLAYG---AQDMVFADyGPRWKLLRKLS-----NLHMlGGKALEDWSQVRTVELGHMLRAMlelsqRGEPVVVPEM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 171 LSRSVSNIICSVVFgSRfdyddeRLLTIIHFINDNFKIM---SSPWGEMYNI---FPSV----LDWIPGPHKRLFRNFgg 240
Cdd:PLN00110 175 LTFSMANMIGQVIL-SR------RVFETKGSESNEFKDMvveLMTTAGYFNIgdfIPSIawmdIQGIERGMKHLHKKF-- 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 241 mKDLIARSVREHQDSLDPNSPR-DFIDCFLTKMAQEKQDPLSHFNMDTLLMtthNLLFGGTETVGTTLRHAFLILMKYPK 319
Cdd:PLN00110 246 -DKLLTRMIEEHTASAHERKGNpDFLDVVMANQENSTGEKLTLTNIKALLL---NLFTAGTDTSSSVIEWSLAEMLKNPS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 320 VQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDS 399
Cdd:PLN00110 322 ILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDP 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 400 DQFKTPQEFNPEHFLDDNHSfKKSP-----AFMPFSAGRRLCLGeplARMELfiyftsILQNFTLQPLVD------PEDI 468
Cdd:PLN00110 402 DVWENPEEFRPERFLSEKNA-KIDPrgndfELIPFGAGRRICAG---TRMGI------VLVEYILGTLVHsfdwklPDGV 471

                 ..
gi 124001560 469 DL 470
Cdd:PLN00110 472 EL 473
PLN02687 PLN02687
flavonoid 3'-monooxygenase
23-438 1.90e-41

flavonoid 3'-monooxygenase


Pssm-ID: 215371  Cd Length: 517  Bit Score: 154.97  E-value: 1.90e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  23 SSRGKGQLPPGPKPLPILGNLLQLRSQDLLTsLTKLSKEYGSVFTVYLGSRPVIVLSGYQTVKEALVDKGEEFSGR---- 98
Cdd:PLN02687  28 SGKHKRPLPPGPRGWPVLGNLPQLGPKPHHT-MAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRppns 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  99 GAYPVFFNFtrgNGIAFSD-GERWKILRR------FSVQILRNFgmgkRSIEERilEEGSFLLEVLRKMEGKPFDPVFIL 171
Cdd:PLN02687 107 GAEHMAYNY---QDLVFAPyGPRWRALRKicavhlFSAKALDDF----RHVREE--EVALLVRELARQHGTAPVNLGQLV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 172 SRSVSNIICSVVFGSR-FDYD-DERLltiihfinDNFKIMSSPWGEM---YNI--FPSVLDW-----IPGPHKRLFRNFG 239
Cdd:PLN02687 178 NVCTTNALGRAMVGRRvFAGDgDEKA--------REFKEMVVELMQLagvFNVgdFVPALRWldlqgVVGKMKRLHRRFD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 240 GMKDLIarsVREHQDSLDPNSPR--DFIDCFLTKMAQEKQD----PLSHFNMDTLLMtthNLLFGGTETVGTTLRHAFLI 313
Cdd:PLN02687 250 AMMNGI---IEEHKAAGQTGSEEhkDLLSTLLALKREQQADgeggRITDTEIKALLL---NLFTAGTDTTSSTVEWAIAE 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 314 LMKYPKVQARVQEEIDRVVGRSRMPTLEDRTSMPYTDAVIHEVQRFADVIPMNLPHRVTRDTPFRGFLIPKGTDVITLLN 393
Cdd:PLN02687 324 LIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVW 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 124001560 394 TVHYDSDQFKTPQEFNPEHFL-DDNHS---FKKSP-AFMPFSAGRRLCLG 438
Cdd:PLN02687 404 AIARDPEQWPDPLEFRPDRFLpGGEHAgvdVKGSDfELIPFGAGRRICAG 453
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
63-460 1.53e-40

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 150.83  E-value: 1.53e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEALVDkgEEFSGRGAYPVFFNFtrGNGIAFSDGERWKILRR-----FSVQILRNFgm 137
Cdd:cd11057    1 GSPFRAWLGPRPFVITSDPEIVQVVLNS--PHCLNKSFFYDFFRL--GRGLFSAPYPIWKLQRKalnpsFNPKILLSF-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 138 gkrsiEERILEEGSFLLEVLRKMEGKP-FDPVFILSRSVSNIICSVVFGSRFDYDDERLLTIIHFINDNFKIMS----SP 212
Cdd:cd11057   75 -----LPIFNEEAQKLVQRLDTYVGGGeFDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFELIAkrvlNP 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 213 WgemynIFPSVLDWIPGPHKR------LFRNFGG--MKDLIAR-----SVREHQDSLDPNSPRDFIDCFLTKMAQEK--- 276
Cdd:cd11057  150 W-----LHPEFIYRLTGDYKEeqkarkILRAFSEkiIEKKLQEvelesNLDSEEDEENGRKPQIFIDQLLELARNGEeft 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 277 -QDPLSHFNMdtllmtthnLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVG-RSRMPTLEDRTSMPYTDAVIH 354
Cdd:cd11057  225 dEEIMDEIDT---------MIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPdDGQFITYEDLQQLVYLEMVLK 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 355 EVQRFADVIPMNLphRVTrDTPFR---GFLIPKGTDVITLLNTVHYDSDQFKT-PQEFNPEHFLDDNhSFKKSP-AFMPF 429
Cdd:cd11057  296 ETMRLFPVGPLVG--RET-TADIQlsnGVVIPKGTTIVIDIFNMHRRKDIWGPdADQFDPDNFLPER-SAQRHPyAFIPF 371
                        410       420       430
                 ....*....|....*....|....*....|.
gi 124001560 430 SAGRRLCLGEPLARMELFIYFTSILQNFTLQ 460
Cdd:cd11057  372 SAGPRNCIGWRYAMISMKIMLAKILRNYRLK 402
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
63-472 8.04e-40

cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of vertebrate cytochrome P450 family 4, subfamily V (CYP4V) enzymes and similar proteins, including invertebrate subfamily C (CYP4C). Insect CYP4C enzymes may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. CYP4V2, the most characterized member of the CYP4V subfamily, is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 148.95  E-value: 8.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  63 GSVFTVYLGSRPVIVLSGYQTVKEAL-----VDKGEEFSgrgaypvFFNFTRGNGIAFSDGERWKILRR-----FSVQIL 132
Cdd:cd20660    1 GPIFRIWLGPKPIVVLYSAETVEVILssskhIDKSFEYD-------FLHPWLGTGLLTSTGEKWHSRRKmltptFHFKIL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 133 RNFgmgkrsIEErILEEGSFLLEVLRK-MEGKPFDPVFILSRSVSNIICSVVFGSRFDYDDE----------RLLTIIHf 201
Cdd:cd20660   74 EDF------LDV-FNEQSEILVKKLKKeVGKEEFDIFPYITLCALDIICETAMGKSVNAQQNsdseyvkavyRMSELVQ- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 202 indnfKIMSSPW---GEMYNIFPsvldwiPG-PHKRLFRNFGGMKD-LIARSVREHQDSLDPNSPRD------------F 264
Cdd:cd20660  146 -----KRQKNPWlwpDFIYSLTP------DGrEHKKCLKILHGFTNkVIQERKAELQKSLEEEEEDDedadigkrkrlaF 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 265 IDCFLTkmAQEKQDPLShfNMDtLLMTTHNLLFGGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRS-RMPTLEDR 343
Cdd:cd20660  215 LDLLLE--ASEEGTKLS--DED-IREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSdRPATMDDL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 344 TSMPYTDAVIHEVQRFADVIPMnLPHRVTRDTPFRGFLIPKGTDVITLLNTVHYDSDQFKTPQEFNPEHFLDDNHSFKKS 423
Cdd:cd20660  290 KEMKYLECVIKEALRLFPSVPM-FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHP 368
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 124001560 424 PAFMPFSAGRRLCLGEPLARMELFIYFTSILQNFTLQPLVDPEDIDLTP 472
Cdd:cd20660  369 YAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQKREDLKPAG 417
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
68-461 1.65e-39

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: 148.07  E-value: 1.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560  68 VYLGSRPVIVLSGYQTVKEALVDKGEEFSGRGAYPVFFNFTRGNGIAFSDGERWKILRrfsvQIL-RNFGMGK-RSIEER 145
Cdd:cd11056    8 IYLFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELR----QKLtPAFTSGKlKNMFPL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 146 ILEEGSFLLEVLRK--MEGKPFDPVFILSRSVSNIICSVVFG---SRFDYDDERLLTIIHFINDNFKIMSSPWGeMYNIF 220
Cdd:cd11056   84 MVEVGDELVDYLKKqaEKGKELEIKDLMARYTTDVIASCAFGldaNSLNDPENEFREMGRRLFEPSRLRGLKFM-LLFFF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 221 PSVLDWI-----PGPHKRLFRNFggMKDLIarSVREHQDSLDPnsprDFIDCFL-TKMAQEKQDPLSHFNMDTLLMTTHN 294
Cdd:cd11056  163 PKLARLLrlkffPKEVEDFFRKL--VRDTI--EYREKNNIVRN----DFIDLLLeLKKKGKIEDDKSEKELTDEELAAQA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124001560 295 LLF--GGTETVGTTLRHAFLILMKYPKVQARVQEEIDRVVGRSRMP-TLEDRTSMPYTDAVIHEVQRFADVIPMnLPHRV 371
Cdd:cd11056  235 FVFflAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGElTYEALQEMKYLDQVVNETLRKYPPLPF-LDRVC 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*...