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Conserved domains on  [gi|1050373214|gb|OCT75413|]
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hypothetical protein XELAEV_18030592mg [Xenopus laevis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
76-524 0e+00

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


:

Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 880.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  76 LQKMHKKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPKANVDFEEFATELVLRVFGYQSFTHDHKMLEKSSTKHMTGDGL 155
Cdd:cd20633     1 LQKMQKKHGDIFTVQIGGHYFTFVMDPLSFGAIVKESKSKLDFGKFASELVLRVFGYQPTENDHKMLQTLSTKHLMGDGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 156 VVMTHAMMENLQNLMVHNIGSEKGEREWHQDGLFNYSYNIVFRAGYLALYGNEPAKNKGSKEKAKEFDRKHSDELFYEFR 235
Cdd:cd20633    81 VVLNQAMMENLQNLMLHSKGSGDGGREWQQDGLFHYSYNIVFRAGYLALFGNEPDKEAGNKEKAKEQDLLHSEELFEEFR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 236 KYDQLFPRLAYAVLPPKDKIEAERLKRLFWNMLSIKKTLQKENISGWISEQHQQRAEHGMPEHMQDRFMFMLLWASQGNT 315
Cdd:cd20633   161 KFDQLFPRLAYSVLPPKDKLEAERLKRLFWDMLSVSKMSQKENISGWISEQQRQLAEHGMPEYMQDRFMFLLLWASQGNT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 316 GPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPGGPLINLTRDMLLKTPVMDSALEETLRLTAAPVLIRAVKQNM 395
Cdd:cd20633   241 GPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEVKPGGPLINLTRDMLLKTPVLDSAVEETLRLTAAPVLIRAVVQDM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 396 KVKMASGNDFSLRGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNGKKVKYYLMPWGAGSSICPGRF 475
Cdd:cd20633   321 TLKMANGREYALRKGDRLALFPYLAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFYKNGKKLKYYNMPWGAGVSICPGRF 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1050373214 476 FAANELKQFVFLMLTYFEFQLVNPNEEIPSIDPNRWGFGVMQPIHDIQF 524
Cdd:cd20633   401 FAVNEMKQFVFLMLTYFDLELVNPDEEIPSIDPSRWGFGTMQPTHDIQF 449
 
Name Accession Description Interval E-value
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
76-524 0e+00

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 880.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  76 LQKMHKKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPKANVDFEEFATELVLRVFGYQSFTHDHKMLEKSSTKHMTGDGL 155
Cdd:cd20633     1 LQKMQKKHGDIFTVQIGGHYFTFVMDPLSFGAIVKESKSKLDFGKFASELVLRVFGYQPTENDHKMLQTLSTKHLMGDGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 156 VVMTHAMMENLQNLMVHNIGSEKGEREWHQDGLFNYSYNIVFRAGYLALYGNEPAKNKGSKEKAKEFDRKHSDELFYEFR 235
Cdd:cd20633    81 VVLNQAMMENLQNLMLHSKGSGDGGREWQQDGLFHYSYNIVFRAGYLALFGNEPDKEAGNKEKAKEQDLLHSEELFEEFR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 236 KYDQLFPRLAYAVLPPKDKIEAERLKRLFWNMLSIKKTLQKENISGWISEQHQQRAEHGMPEHMQDRFMFMLLWASQGNT 315
Cdd:cd20633   161 KFDQLFPRLAYSVLPPKDKLEAERLKRLFWDMLSVSKMSQKENISGWISEQQRQLAEHGMPEYMQDRFMFLLLWASQGNT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 316 GPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPGGPLINLTRDMLLKTPVMDSALEETLRLTAAPVLIRAVKQNM 395
Cdd:cd20633   241 GPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEVKPGGPLINLTRDMLLKTPVLDSAVEETLRLTAAPVLIRAVVQDM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 396 KVKMASGNDFSLRGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNGKKVKYYLMPWGAGSSICPGRF 475
Cdd:cd20633   321 TLKMANGREYALRKGDRLALFPYLAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFYKNGKKLKYYNMPWGAGVSICPGRF 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1050373214 476 FAANELKQFVFLMLTYFEFQLVNPNEEIPSIDPNRWGFGVMQPIHDIQF 524
Cdd:cd20633   401 FAVNEMKQFVFLMLTYFDLELVNPDEEIPSIDPSRWGFGTMQPTHDIQF 449
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
59-524 1.18e-38

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: 147.04  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  59 IPWLGYALDFR--KNTLTFLQKMHKKHGDIFTVQIAGYYFTFVMDPlsfgPIIKEpkA-NVDFEEFATELVLRVFGYQSF 135
Cdd:pfam00067   7 LPLFGNLLQLGrkGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGP----EAVKE--VlIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 136 TH-----------DHKMLEKSSTKHMTGDGLVVMThAMMENLQNLMVHNIGSEKGE------REWHQDGLFNYSYNIVFR 198
Cdd:pfam00067  81 PFlgkgivfangpRWRQLRRFLTPTFTSFGKLSFE-PRVEEEARDLVEKLRKTAGEpgvidiTDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 199 AGYLALYGNEPaknkgskEKAKEFDRKHSDELFYEFRKYDQLFPRLAYavLPPKDKIEAERLKRLFWNMLSIKKTLQKEN 278
Cdd:pfam00067 160 ERFGSLEDPKF-------LELVKAVQELSSLLSSPSPQLLDLFPILKY--FPGPHGRKLKRARKKIKDLLDKLIEERRET 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 279 ISgwiSEQHQQRA---------EHGMPEHMQDR----FMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLk 345
Cdd:pfam00067 231 LD---SAKKSPRDfldalllakEEEDGSKLTDEelraTVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVI- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 346 etgqevkpgGPLINLTRDMLLKTPVMDSALEETLRL-TAAPVLI-RAVKQNMKVkmasgNDFSLRGGDRIAFFPYiAVQM 423
Cdd:pfam00067 307 ---------GDKRSPTYDDLQNMPYLDAVIKETLRLhPVVPLLLpREVTKDTVI-----PGYLIPKGTLVIVNLY-ALHR 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 424 DPGVHPEPEKYKYNRFLNEDGTKKtdffkngkkVKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQlVNPNEEI 503
Cdd:pfam00067 372 DPEVFPNPEEFDPERFLDENGKFR---------KSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVE-LPPGTDP 441
                         490       500
                  ....*....|....*....|.
gi 1050373214 504 PSIDpNRWGFGVMQPIHDIQF 524
Cdd:pfam00067 442 PDID-ETPGLLLPPKPYKLKF 461
PLN02302 PLN02302
ent-kaurenoic acid oxidase
259-500 7.93e-14

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 73.59  E-value: 7.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 259 RLKRLFWNMLSIKKTLQKENISG-------WISEQHQQRAEHGMPEHMQDrFMFMLLWASQGNTGPASFWFLLYLLKHPE 331
Cdd:PLN02302  241 KLVALFQSIVDERRNSRKQNISPrkkdmldLLLDAEDENGRKLDDEEIID-LLLMYLNAGHESSGHLTMWATIFLQEHPE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 332 AMQAVREEVEAVLKEtgqeVKPGGPLINL--TRDMLLKTPVMDsaleETLRL-TAAPVLIRAVKQNMKVkmasgNDFSLR 408
Cdd:PLN02302  320 VLQKAKAEQEEIAKK----RPPGQKGLTLkdVRKMEYLSQVID----ETLRLiNISLTVFREAKTDVEV-----NGYTIP 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 409 GGDRIAFFpYIAVQMDPGVHPEPEKYKYNRFLNEdgTKKTDFFkngkkvkyylMPWGAGSSICPGRFFAANELKQFVFLM 488
Cdd:PLN02302  387 KGWKVLAW-FRQVHMDPEVYPNPKEFDPSRWDNY--TPKAGTF----------LPFGLGSRLCPGNDLAKLEISIFLHHF 453
                         250
                  ....*....|..
gi 1050373214 489 LTYFEFQLVNPN 500
Cdd:PLN02302  454 LLGYRLERLNPG 465
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
303-501 2.33e-09

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 59.52  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 303 FMFMLLWASQGNTgpASF--WFLLYLLKHPEAMQAVREEVeavlketgqevkpggplinltrdmllktPVMDSALEETLR 380
Cdd:COG2124   230 ELLLLLLAGHETT--ANAlaWALYALLRHPEQLARLRAEP----------------------------ELLPAAVEETLR 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 L-TAAPVLIRAVKQnmkvkmasgnDFSLRG-----GDRIAFFPYiAVQMDPGVHPEPEKYKYNRflnedgtkktdffkng 454
Cdd:COG2124   280 LyPPVPLLPRTATE----------DVELGGvtipaGDRVLLSLA-AANRDPRVFPDPDRFDPDR---------------- 332
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1050373214 455 kkVKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFE-FQLVNPNE 501
Cdd:COG2124   333 --PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLAPPEE 378
 
Name Accession Description Interval E-value
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
76-524 0e+00

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 880.55  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  76 LQKMHKKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPKANVDFEEFATELVLRVFGYQSFTHDHKMLEKSSTKHMTGDGL 155
Cdd:cd20633     1 LQKMQKKHGDIFTVQIGGHYFTFVMDPLSFGAIVKESKSKLDFGKFASELVLRVFGYQPTENDHKMLQTLSTKHLMGDGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 156 VVMTHAMMENLQNLMVHNIGSEKGEREWHQDGLFNYSYNIVFRAGYLALYGNEPAKNKGSKEKAKEFDRKHSDELFYEFR 235
Cdd:cd20633    81 VVLNQAMMENLQNLMLHSKGSGDGGREWQQDGLFHYSYNIVFRAGYLALFGNEPDKEAGNKEKAKEQDLLHSEELFEEFR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 236 KYDQLFPRLAYAVLPPKDKIEAERLKRLFWNMLSIKKTLQKENISGWISEQHQQRAEHGMPEHMQDRFMFMLLWASQGNT 315
Cdd:cd20633   161 KFDQLFPRLAYSVLPPKDKLEAERLKRLFWDMLSVSKMSQKENISGWISEQQRQLAEHGMPEYMQDRFMFLLLWASQGNT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 316 GPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPGGPLINLTRDMLLKTPVMDSALEETLRLTAAPVLIRAVKQNM 395
Cdd:cd20633   241 GPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEVKPGGPLINLTRDMLLKTPVLDSAVEETLRLTAAPVLIRAVVQDM 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 396 KVKMASGNDFSLRGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNGKKVKYYLMPWGAGSSICPGRF 475
Cdd:cd20633   321 TLKMANGREYALRKGDRLALFPYLAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFYKNGKKLKYYNMPWGAGVSICPGRF 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1050373214 476 FAANELKQFVFLMLTYFEFQLVNPNEEIPSIDPNRWGFGVMQPIHDIQF 524
Cdd:cd20633   401 FAVNEMKQFVFLMLTYFDLELVNPDEEIPSIDPSRWGFGTMQPTHDIQF 449
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
74-523 1.17e-175

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 502.37  E-value: 1.17e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  74 TFLQKMHKKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPKANVDFEEFATELVLRVFGYQSFTHDHKMLEKSSTKHMTGD 153
Cdd:cd20634     1 KFLTRMKEKHGDIFTVQVAGRYVTVLLDPHSYDAVVWEPSTSLDFTSYARLLMDRIFDVQLPSYDPTEEKKRMESHFQGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 154 GLVVMTHAMMENLQNLMvhnIGSEKG-EREWHQDGLFNYSYNIVFRAGYLALYGNEpakNKGSKEKAKEFDRKHSDELFY 232
Cdd:cd20634    81 NLTQLTQAMFNNLQLLL---LGDAMGlSTEWKKDGLFNFCYSLLFRAGYLTLFGNE---NENSTHESQNKDRAHSAEVYH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 233 EFRKYDQLFPRLAYAVLPPKDKIEAERLKRLFWNMLSIKKTLQKENISGWISEQHQQRAEHGMPEHMQDRFMFMLLWASQ 312
Cdd:cd20634   155 EFRKLDQLLPKLARGTLSKEEKQEAASVKERLWKLLSPKRLNRKANRSSWLESYLLHLEEEGVDEEMQARAMLLQLWATQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 313 GNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPggpLINLTRDMLLKTPVMDSALEETLRLTAAPVLIRAVK 392
Cdd:cd20634   235 GNAGPAAFWLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVSQ---TLTINQELLDNTPVFDSVLSETLRLTAAPFITREVL 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 393 QNMKVKMASGNDFSLRGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNGKKVKYYLMPWGAGSSICP 472
Cdd:cd20634   312 QDMKLRLADGQEYNLRRGDRLCLFPFLSPQMDPEIHQEPEVFKYDRFLNADGTEKKDFYKNGKRLKYYNMPWGAGDNVCI 391
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1050373214 473 GRFFAANELKQFVFLMLTYFEFQLVNPNEEIPSIDPNRWGFGVMQPIHDIQ 523
Cdd:cd20634   392 GRHFAVNSIKQFVFLILTHFDVELKDPEAEIPEFDPSRYGFGLLQPEGDII 442
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
75-524 2.06e-139

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 410.23  E-value: 2.06e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  75 FLQKMHKKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPKaNVDFEEFATELVLRVFGYQSFT----HDHKMLEKSSTKHM 150
Cdd:cd20631     1 FLRSRQKKYGHIFTCKIAGKYVHFITDPFSYHSVIRHGK-HLDWKKFHFATSAKAFGHVSFDpsdgNTTENIHDTFIKTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 151 TGDGLVVMTHAMMENLQNLMVHNIGSEKGEREWHQDGLFNYSYNIVFRAGYLALYGNEPAKNKGSKEKAkEFDRKHSDEL 230
Cdd:cd20631    80 QGSALDSLTESMMENLQYVMLQDKSSSSSTKAWVTEGLYSFCYRVMFEAGYLTLFGKELTAREDKNARL-EAQRALILNA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 231 FYEFRKYDQLFPRLAyAVLPpkdkieAERLKRLFWNMLSIKKTLQKENISGW--ISEQHQQRAE-----HGMPEHMQDRF 303
Cdd:cd20631   159 LENFKEFDKVFPALV-AGLP------IHMFKTAKSAREALAERLLHENLQKRenISELISLRMLlndtlSTLDEMEKART 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 304 MFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPGGPLINLTRDMLLKTPVMDSALEETLRLTA 383
Cdd:cd20631   232 HVAMLWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQKVSDGGNPIVLTREQLDDMPVLGSIIKEALRLSS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 384 APVLIRAVKQNMKVKMASGNDFSLRGGDRIAFFPYIaVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNGKKVKYYLMP 463
Cdd:cd20631   312 ASLNIRVAKEDFTLHLDSGESYAIRKDDIIALYPQL-LHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKNGRKLKYYYMP 390
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1050373214 464 WGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEEIPSIDPNRWGFGVMQPIHDIQF 524
Cdd:cd20631   391 FGSGTSKCPGRFFAINEIKQFLSLMLCYFDMELLDGNAKCPPLDQSRAGLGILPPTHDVDF 451
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
75-526 5.56e-124

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 370.48  E-value: 5.56e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  75 FLQKMHKKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPKaNVDFEEFATELVLRVFGYQSFTHD--HKMLEK--SSTKHM 150
Cdd:cd20632     1 FLLALQKKHGDVFTVLIAGKYITFIMDPFLYPYVIKHGK-QLDFHEFSDRLASKTFGYPPLRSPkfPGLNEQihRSYQYL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 151 TGDGLVVMTHAMMENLQNLMVHNIgseKGEREWHQDGLFNYSYNIVFRAGYLALYGNEPAKNKgskekakefdRKHSDEL 230
Cdd:cd20632    80 QGENLDILTESMMGNLQLVLRQQF---LGETDWETEELYEFCSRIMFEATFLTLYGKPPDDDR----------HKVISEL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 231 FYEFRKYDQLFPRLAyAVLPpkdkIEaerlkrLFWNMLSIKKTLQK----ENISGW--ISEQHQQRAE-----HGMPEHM 299
Cdd:cd20632   147 RKKFRKFDAMFPYLV-ANIP----IE------LLGATKSIREKLIKyflpQKMAKWsnPSEVIQARQElleqyDVLQDYD 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 300 QDRFMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPGGPlINLTRDMLLKTPVMDSALEETL 379
Cdd:cd20632   216 KAAHHFAFLWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQSTGQELGPDFD-IHLTREQLDSLVYLESAINESL 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 380 RLTAAPVLIRAVKQNMKVKMASGNDFSLRGGDRIAFFPYIaVQMDPGVHPEPEKYKYNRFLnEDGTKKTDFFKNGKKVKY 459
Cdd:cd20632   295 RLSSASMNIRVVQEDFTLKLESDGSVNLRKGDIVALYPQS-LHMDPEIYEDPEVFKFDRFV-EDGKKKTTFYKRGQKLKY 372
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050373214 460 YLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVnPNEEIPSIDPNRWGFGVMQPIHDIQFRY 526
Cdd:cd20632   373 YLMPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDLELL-EEQKPPGLDNSRAGLGILPPNSDVRFRY 438
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
76-523 1.12e-85

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 271.55  E-value: 1.12e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  76 LQKMHKKH---GDIFTVQIAGYYFTFVMDPLSFGPIIKEPKaNVDFEEFATELVLRVFGYQSF----------THDHKML 142
Cdd:cd11040     1 LLRNGKKYfsgGPIFTIRLGGQKIYVITDPELISAVFRNPK-TLSFDPIVIVVVGRVFGSPESakkkegepggKGLIRLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 143 EKSSTKHMTG-DGLVVMTHAMMENLQNLMvhNIGSEKGEREWHQDGLFNYSYNIVFRAGYLALYGNEPAKNkgskekake 221
Cdd:cd11040    80 HDLHKKALSGgEGLDRLNEAMLENLSKLL--DELSLSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPEL--------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 222 fdrkhSDELFYEFRKYDQLFPRLAYAVLPP--KDKIEA-ERLKRLFWNMLSiKKTLQKENISGWISEQHQQRAEHGMPEH 298
Cdd:cd11040   149 -----DPDLVEDFWTFDRGLPKLLLGLPRLlaRKAYAArDRLLKALEKYYQ-AAREERDDGSELIRARAKVLREAGLSEE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 299 MQDRFMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVKpggplINLTRDMLLKTPVMDSALEET 378
Cdd:cd11040   223 DIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNA-----ILDLTDLLTSCPLLDSTYLET 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 379 LRLTAAPVLIRAVKQNMKvkmaSGNDFSLRGGDRIaFFPYIAVQMDPGVH-PEPEKYKYNRFLNEDGTKKtdffknGKKV 457
Cdd:cd11040   298 LRLHSSSTSVRLVTEDTV----LGGGYLLRKGSLV-MIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKK------GRGL 366
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050373214 458 KYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVN-PNEEIPSIDPnRWGFGVMQPIHDIQ 523
Cdd:cd11040   367 PGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGgGDWKVPGMDE-SPGLGILPPKRDVR 432
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
59-524 1.18e-38

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: 147.04  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  59 IPWLGYALDFR--KNTLTFLQKMHKKHGDIFTVQIAGYYFTFVMDPlsfgPIIKEpkA-NVDFEEFATELVLRVFGYQSF 135
Cdd:pfam00067   7 LPLFGNLLQLGrkGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGP----EAVKE--VlIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 136 TH-----------DHKMLEKSSTKHMTGDGLVVMThAMMENLQNLMVHNIGSEKGE------REWHQDGLFNYSYNIVFR 198
Cdd:pfam00067  81 PFlgkgivfangpRWRQLRRFLTPTFTSFGKLSFE-PRVEEEARDLVEKLRKTAGEpgvidiTDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 199 AGYLALYGNEPaknkgskEKAKEFDRKHSDELFYEFRKYDQLFPRLAYavLPPKDKIEAERLKRLFWNMLSIKKTLQKEN 278
Cdd:pfam00067 160 ERFGSLEDPKF-------LELVKAVQELSSLLSSPSPQLLDLFPILKY--FPGPHGRKLKRARKKIKDLLDKLIEERRET 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 279 ISgwiSEQHQQRA---------EHGMPEHMQDR----FMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLk 345
Cdd:pfam00067 231 LD---SAKKSPRDfldalllakEEEDGSKLTDEelraTVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVI- 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 346 etgqevkpgGPLINLTRDMLLKTPVMDSALEETLRL-TAAPVLI-RAVKQNMKVkmasgNDFSLRGGDRIAFFPYiAVQM 423
Cdd:pfam00067 307 ---------GDKRSPTYDDLQNMPYLDAVIKETLRLhPVVPLLLpREVTKDTVI-----PGYLIPKGTLVIVNLY-ALHR 371
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 424 DPGVHPEPEKYKYNRFLNEDGTKKtdffkngkkVKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQlVNPNEEI 503
Cdd:pfam00067 372 DPEVFPNPEEFDPERFLDENGKFR---------KSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVE-LPPGTDP 441
                         490       500
                  ....*....|....*....|.
gi 1050373214 504 PSIDpNRWGFGVMQPIHDIQF 524
Cdd:pfam00067 442 PDID-ETPGLLLPPKPYKLKF 461
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
73-518 9.73e-37

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 140.52  E-value: 9.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  73 LTFLQKMHKKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPkaNVDFEEFATELVLRVFG------YQSFTHDHKMLE--- 143
Cdd:cd20635     2 LEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSK--DVDFQKAVQDPVQNTASiskesfFEYHTKIHDMMKgkl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 144 KSSTKHMTGDGLVVMTHAMMENLqnlmvhniGSEKGEREwhqdglfnysYNIVFRAGYLALYGNEPAKN--KGSKEKAKE 221
Cdd:cd20635    80 ASSNLAPLSDKLCEEFKEQLELL--------GSEGTGDL----------NDLVRHVMYPAVVNNLFGKGllPTSEEEIKE 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 222 FDrKHsdelfyeFRKYDQLFprlAYAVLPPKDKIEA-----ERLKRLFWNMLS-IKKTLQKENISgwiseqhQQRAEHGM 295
Cdd:cd20635   142 FE-EH-------FVKFDEQF---EYGSQLPEFFLRDwssskQWLLSLFEKVVPdAEKTKPLENNS-------KTLLQHLL 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 296 P---EHMQDRFMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVkpggplINLTRDMLLKTPVMD 372
Cdd:cd20635   204 DtvdKENAPNYSLLLLWASLANAIPITFWTLAFILSHPSVYKKVMEEISSVLGKAGKDK------IKISEDDLKKMPYIK 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 373 SALEETLRLTAAPVLIRAVKQNMKVKmasgnDFSLRGGDRIAFFPYIAvQMDPGVHPEPEKYKYNRFLNEDgTKKTDFFK 452
Cdd:cd20635   278 RCVLEAIRLRSPGAITRKVVKPIKIK-----NYTIPAGDMLMLSPYWA-HRNPKYFPDPELFKPERWKKAD-LEKNVFLE 350
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050373214 453 ngkkvkyYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPneeIPSIDPNRWgFGVMQP 518
Cdd:cd20635   351 -------GFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLLDP---VPKPSPLHL-VGTQQP 405
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
78-527 9.26e-33

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


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 130.11  E-value: 9.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  78 KMHKKHGDIFtvQIAGYYFTFVMDPLSFGP-IIKEPKANVDFEEFATELVLRVFGYQSFTHDHKMLEKSSTKHMTgDGLV 156
Cdd:cd11041     5 EKYKKNGGPF--QLPTPDGPLVVLPPKYLDeLRNLPESVLSFLEALEEHLAGFGTGGSVVLDSPLHVDVVRKDLT-PNLP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 157 VMTHAMMENLQNLMVHNIGSEKgerEWHQDGLFNYSYNIVFRAGYLALYGNEPAKNKGSKEKAKEFdrkhSDELF---YE 233
Cdd:cd11041    82 KLLPDLQEELRAALDEELGSCT---EWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEWLDLTINY----TIDVFaaaAA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 234 FRKYDQLFPRLAYAVLPPKDKIEA--ERLKRLFWNMLSIKKTLQKENISG-------WISEQHQQRAEHGmPEHMQDRFM 304
Cdd:cd11041   155 LRLFPPFLRPLVAPFLPEPRRLRRllRRARPLIIPEIERRRKLKKGPKEDkpndllqWLIEAAKGEGERT-PYDLADRQL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 305 FMLLwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQevkpggplinLTRDMLLKTPVMDSALEETLRLTAA 384
Cdd:cd11041   234 ALSF-AAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGG----------WTKAALNKLKKLDSFMKESQRLNPL 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 385 PVLI--RAVKQNMKVKmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGT----KKTDFFKNGKKVk 458
Cdd:cd11041   303 SLVSlrRKVLKDVTLS----DGLTLPKGTRIAVPAH-AIHRDPDIYPDPETFDGFRFYRLREQpgqeKKHQFVSTSPDF- 376
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1050373214 459 yylMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVnPNEEIPsidPNRW-GFGVMQPIH-DIQFRYR 527
Cdd:cd11041   377 ---LGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLP-EGGERP---KNIWfGEFIMPDPNaKVLVRRR 440
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
81-527 4.88e-31

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 124.64  E-value: 4.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  81 KKHGDIFTVQIAGYYFTFVMDPLSFGPIIKEPKANVDFEE---FATELVLRVFGYQSFTHDHKMLEKSstkhmtgdGLVV 157
Cdd:cd11042     3 KKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEvygFLTPPFGGGVVYYAPFAEQKEQLKF--------GLNI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 158 MTHAMMENLQNLMVHNIgsEKGEREWHQDGLFNysyniVFRA-GYL-------ALYGnepaknkgskekaKEFDRKHSDE 229
Cdd:cd11042    75 LRRGKLRGYVPLIVEEV--EKYFAKWGESGEVD-----LFEEmSELtiltasrCLLG-------------KEVRELLDDE 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 230 LFYEFRKYDQ-------LFPrlaYAVLPP---KDKIEAeRLKRLFWNMLSIKKTLQKENISGWISEQHQQRAEHG--MPE 297
Cdd:cd11042   135 FAQLYHDLDGgftpiafFFP---PLPLPSfrrRDRARA-KLKEIFSEIIQKRRKSPDKDEDDMLQTLMDAKYKDGrpLTD 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 298 HMQDRFMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEveavlketgQEVKPGGPLINLTRDMLLKTPVMDSALEE 377
Cdd:cd11042   211 DEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREE---------QKEVLGDGDDPLTYDVLKEMPLLHACIKE 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 378 TLRLT-AAPVLIRAVKQNMKVkmaSGNDFSLRGGDRIAFFPYIAvQMDPGVHPEPEKYKYNRFLNEDGTKKtdffkngKK 456
Cdd:cd11042   282 TLRLHpPIHSLMRKARKPFEV---EGGGYVIPKGHIVLASPAVS-HRDPEIFKNPDEFDPERFLKGRAEDS-------KG 350
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1050373214 457 VKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPneEIPSIDPNrwgFGVMQPIHDIQFRYR 527
Cdd:cd11042   351 GKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDS--PFPEPDYT---TMVVWPKGPARVRYK 416
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
84-504 8.01e-30

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: 120.70  E-value: 8.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  84 GDIFTVQIAGYYFTFVMDPLSFGPIIKEPKANVDFEEFATELVLRVFGYQSFTHD---HKMLEKSSTKHMTGDGLVVMTH 160
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDgpeHRRLRRLLAPAFTPRALAALRP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 161 AMMENLQNLMvhnigsekgeREWHQDG-----LFNYSYNIVFRAGYLALYGNEPAKnkgskekakefdrkHSDELFYEFR 235
Cdd:cd00302    81 VIREIARELL----------DRLAAGGevgddVADLAQPLALDVIARLLGGPDLGE--------------DLEELAELLE 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 236 KYDQLFPRLAYAVLPPKDKIEAERLKRLFWNML--SIKKTLQKENISGWISEQHQQRAEHGMPEHMQDRFMFMLLWASQG 313
Cdd:cd00302   137 ALLKLLGPRLLRPLPSPRLRRLRRARARLRDYLeeLIARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHE 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 314 NTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETgqevkpggplinlTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVK 392
Cdd:cd00302   217 TTASLLAWALYLLARHPEVQERLRAEIDAVLGDG-------------TPEDLSKLPYLEAVVEETLRLyPPVPLLPRVAT 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 393 QNMKVkmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFfkngkkvkyylMPWGAGSSICP 472
Cdd:cd00302   284 EDVEL-----GGYTIPAGTLVLLSLY-AAHRDPEVFPDPDEFDPERFLPEREEPRYAH-----------LPFGAGPHRCL 346
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1050373214 473 GRFFAANELKQFVFLMLTYFEFQLVnPNEEIP 504
Cdd:cd00302   347 GARLARLELKLALATLLRRFDFELV-PDEELE 377
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
322-522 9.69e-20

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: 91.45  E-value: 9.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLL-KHPEAMQAVREEVEAVLKETGQEvkpggplinLTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVKm 399
Cdd:cd11056   251 FALYELaKNPEIQEKLREEIDEVLEKHGGE---------LTYEALQEMKYLDQVVNETLRKyPPLPFLDRVCTKDYTLP- 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asGNDFSLRGGDRIaFFPYIAVQMDPGVHPEPEKYKYNRFLNEdgtkktdffkNGKKVKYYL-MPWGAGSSICPGRFFAA 478
Cdd:cd11056   321 --GTDVVIEKGTPV-IIPVYALHHDPKYYPEPEKFDPERFSPE----------NKKKRHPYTyLPFGDGPRNCIGMRFGL 387
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1050373214 479 NELKQFVFLMLTYFEFQLVNPNEEIPSIDPNRWgfgVMQPIHDI 522
Cdd:cd11056   388 LQVKLGLVHLLSNFRVEPSSKTKIPLKLSPKSF---VLSPKGGI 428
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
84-508 3.92e-17

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: 83.42  E-value: 3.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  84 GDIFTVQIAGYYFTFVMDPlsfgPIIKEpkANV-DFEEFA----TELVLRVFGYQSFTHD----HKMLEKSSTKHMTGDG 154
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDP----EIIKE--AFVkNGDNFSdrplLPSFEIISGGKGILFSngdyWKELRRFALSSLTKTK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 155 L------VVMTHA--MMENLQNLmvhnigSEKGEREWHQDGLFNYSYNIVFRagYLAlygnepaknkgskekAKEFDRKH 226
Cdd:cd20617    75 LkkkmeeLIEEEVnkLIESLKKH------SKSGEPFDPRPYFKKFVLNIINQ--FLF---------------GKRFPDED 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 227 SDELFYEFRKYDQLFPRLA----YAVLPPKDKIEAERLKRLFWNMLSIKKTLQKENisgwisEQHQQRAEHGMPEHMQDR 302
Cdd:cd20617   132 DGEFLKLVKPIEEIFKELGsgnpSDFIPILLPFYFLYLKKLKKSYDKIKDFIEKII------EEHLKTIDPNNPRDLIDD 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 303 FMFML--------------------LW-ASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKetgqevkpGGPLINLT 361
Cdd:cd20617   206 ELLLLlkegdsglfdddsiistcldLFlAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVG--------NDRRVTLS 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 362 rDMLlKTPVMDSALEETLRL-TAAPV-LIRAVKQNMKVkmasgNDFSLRGGDRIaFFPYIAVQMDPGVHPEPEKYKYNRF 439
Cdd:cd20617   278 -DRS-KLPYLNAVIKEVLRLrPILPLgLPRVTTEDTEI-----GGYFIPKGTQI-IINIYSLHRDEKYFEDPEEFNPERF 349
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1050373214 440 LNEDGTKKTDFFkngkkvkyylMPWGAGSSICPGRFFAANELkqfvFLMLT----YFEFQLVNPNeeiPSIDP 508
Cdd:cd20617   350 LENDGNKLSEQF----------IPFGIGKRNCVGENLARDEL----FLFFAnlllNFKFKSSDGL---PIDEK 405
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
216-501 7.90e-17

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


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 82.73  E-value: 7.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 216 KEKAKEFDRKHSDELFYEFRKYDQLFPRLAyavLPPKDKIEAERLKRLF-WNMLSIKKTLQ-------KENISGWISEQH 287
Cdd:cd11059   133 DSRERELLRRLLASLAPWLRWLPRYLPLAT---SRLIIGIYFRAFDEIEeWALDLCARAESslaessdSESLTVLLLEKL 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 288 QQRAEHGMPEHMQDRFMFMLLWASQGNTGpASFWFLLY-LLKHPEAMQAVREEVEAVlketgqevkPGGPLINLTRDMLL 366
Cdd:cd11059   210 KGLKKQGLDDLEIASEALDHIVAGHDTTA-VTLTYLIWeLSRPPNLQEKLREELAGL---------PGPFRGPPDLEDLD 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 367 KTPVMDSALEETLRL-TAAPV-LIRAVKQNMKVkmasGNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDG 444
Cdd:cd11059   280 KLPYLNAVIRETLRLyPPIPGsLPRVVPEGGAT----IGGYYIPGGTIVSTQAY-SLHRDPEVFPDPEEFDPERWLDPSG 354
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1050373214 445 TKKtdffkngKKVKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNE 501
Cdd:cd11059   355 ETA-------REMKRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTSTTTDDD 404
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
304-518 1.31e-16

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


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 81.98  E-value: 1.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 304 MFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevkpGGPLINLTRDMLLKTPVMDSALEETLRL-T 382
Cdd:cd11083   227 VLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVL---------GGARVPPLLEALDRLPYLEAVARETLRLkP 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 383 AAPVLirAVKQNMKVKMAsgnDFSLRGGDRIaFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNgkkvkyyLM 462
Cdd:cd11083   298 VAPLL--FLEPNEDTVVG---DIALPAGTPV-FLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEPHDPSS-------LL 364
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1050373214 463 PWGAGSSICPGRFFAANELKqFVFLMLT-YFEFQLVNPNEEIPSidpnRWGFgVMQP 518
Cdd:cd11083   365 PFGAGPRLCPGRSLALMEMK-LVFAMLCrNFDIELPEPAPAVGE----EFAF-TMSP 415
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
322-522 1.02e-15

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: 79.17  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLL-KHPEAMQAVREEVEAVLKETGqevkpggpliNLTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVkm 399
Cdd:cd11055   248 FASYLLaTNPDVQEKLIEEIDEVLPDDG----------SPTYDTVSKLKYLDMVINETLRLyPPAFFISRECKEDCTI-- 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDgtkktdffkNGKKVKYYLMPWGAGSSICPGRFFAAN 479
Cdd:cd11055   316 ---NGVFIPKGVDVVIPVY-AIHHDPEFWPDPEKFDPERFSPEN---------KAKRHPYAYLPFGAGPRNCIGMRFALL 382
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1050373214 480 ELKQFVFLMLTYFEFqLVNPNEEIP-SIDPNrwgfGVMQPIHDI 522
Cdd:cd11055   383 EVKLALVKILQKFRF-VPCKETEIPlKLVGG----ATLSPKNGI 421
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
288-504 6.71e-15

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: 76.85  E-value: 6.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 288 QQRAEHGMPehMQDRF----MFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevkPGGPLinltrD 363
Cdd:cd11053   210 SARDEDGQP--LSDEElrdeLMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALG--------GDPDP-----E 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 364 MLLKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVkmasgNDFSLRGGDRIAFFPYIaVQMDPGVHPEPEKYKYNRFLne 442
Cdd:cd11053   275 DIAKLPYLDAVIKETLRLyPVAPLVPRRVKEPVEL-----GGYTLPAGTTVAPSIYL-THHRPDLYPDPERFRPERFL-- 346
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1050373214 443 dgtkktdffknGKKVK-YYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEEIP 504
Cdd:cd11053   347 -----------GRKPSpYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPERP 398
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
322-503 8.84e-15

Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; Fusarium verticillioides cytochrome P450 monooxygenase FUM15, is also called fumonisin biosynthesis cluster protein 15. The FUM15 gene is part of the gene cluster that mediates the biosynthesis of fumonisins B1, B2, B3, and B4, which are carcinogenic mycotoxins. This FUM15-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410692 [Multi-domain]  Cd Length: 437  Bit Score: 76.54  E-value: 8.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLL-KHPEAMQAVREEVeavlketgQEVKPGGPLINLTRDMLLKTPVMDSALEETLRLTAA-PVLIRAVKQNMKVKm 399
Cdd:cd11069   257 WALYLLaKHPDVQERLREEI--------RAALPDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPvPLTSREATKDTVIK- 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgndfslrgGDRIA-----FFPYIAVQMDPGVH-PEPEKYKYNRFLNEDGTKKTdffkNGKKVKYYLMPWGAGSSICPG 473
Cdd:cd11069   328 ----------GVPIPkgtvvLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASP----GGAGSNYALLTFLHGPRSCIG 393
                         170       180       190
                  ....*....|....*....|....*....|
gi 1050373214 474 RFFAANELKQFVFLMLTYFEFQLVNPNEEI 503
Cdd:cd11069   394 KKFALAEMKVLLAALVSRFEFELDPDAEVE 423
PLN02302 PLN02302
ent-kaurenoic acid oxidase
259-500 7.93e-14

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 73.59  E-value: 7.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 259 RLKRLFWNMLSIKKTLQKENISG-------WISEQHQQRAEHGMPEHMQDrFMFMLLWASQGNTGPASFWFLLYLLKHPE 331
Cdd:PLN02302  241 KLVALFQSIVDERRNSRKQNISPrkkdmldLLLDAEDENGRKLDDEEIID-LLLMYLNAGHESSGHLTMWATIFLQEHPE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 332 AMQAVREEVEAVLKEtgqeVKPGGPLINL--TRDMLLKTPVMDsaleETLRL-TAAPVLIRAVKQNMKVkmasgNDFSLR 408
Cdd:PLN02302  320 VLQKAKAEQEEIAKK----RPPGQKGLTLkdVRKMEYLSQVID----ETLRLiNISLTVFREAKTDVEV-----NGYTIP 386
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 409 GGDRIAFFpYIAVQMDPGVHPEPEKYKYNRFLNEdgTKKTDFFkngkkvkyylMPWGAGSSICPGRFFAANELKQFVFLM 488
Cdd:PLN02302  387 KGWKVLAW-FRQVHMDPEVYPNPKEFDPSRWDNY--TPKAGTF----------LPFGLGSRLCPGNDLAKLEISIFLHHF 453
                         250
                  ....*....|..
gi 1050373214 489 LTYFEFQLVNPN 500
Cdd:PLN02302  454 LLGYRLERLNPG 465
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
303-508 1.55e-13

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 72.21  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 303 FMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKEtgqevKPGGPLINL--TRDMLLKTPVMDsaleETLR 380
Cdd:cd11043   214 NILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKR-----KEEGEGLTWedYKSMKYTWQVIN----ETLR 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 L-TAAPVLIRAVKQNMKVKmasgnDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNedgtkktdffkNGKKVKY 459
Cdd:cd11043   285 LaPIVPGVFRKALQDVEYK-----GYTIPKGWKVLWSAR-ATHLDPEYFPDPLKFNPWRWEG-----------KGKGVPY 347
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1050373214 460 YLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQlVNPNEEIpSIDP 508
Cdd:cd11043   348 TFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWE-VVPDEKI-SRFP 394
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
321-494 2.93e-13

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: 71.86  E-value: 2.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketGQEVKPggplinlTRDMLLKTPVMDSALEETLRL-TAAPVLI--RAVKqnmkv 397
Cdd:cd11027   251 WAIAYLVNYPEVQAKLHAELDDVI---GRDRLP-------TLSDRKRLPYLEATIAEVLRLsSVVPLALphKTTC----- 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 398 kmasgnDFSLRG----GDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGtKKTDFFKNgkkvkyyLMPWGAGSSICPG 473
Cdd:cd11027   316 ------DTTLRGytipKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENG-KLVPKPES-------FLPFSAGRRVCLG 381
                         170       180
                  ....*....|....*....|...
gi 1050373214 474 RFFAANELkqFVFL--MLTYFEF 494
Cdd:cd11027   382 ESLAKAEL--FLFLarLLQKFRF 402
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
286-503 3.55e-13

cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). Members of the CYP97 clan include Arabidopsis thaliana cytochrome P450s 97A3 (CYP97A3), CYP97B3, and CYP97C1. CYP97A3 is also called protein LUTEIN DEFICIENT 5 (LUT5) and CYP97C1 is also called carotene epsilon-monooxygenase or protein LUTEIN DEFICIENT 1 (LUT1). These cytochromes function as beta- and epsilon-ring carotenoid hydroxylases and are involved in the biosynthesis of xanthophylls. CYP97 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 71.63  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 286 QHQQRAEHGMPEHMQDRFMFMLLwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevkpgGPLINLTRDML 365
Cdd:cd11046   228 LVDMRDEDVDSKQLRDDLMTMLI-AGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVL----------GDRLPPTYEDL 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 366 LKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVkmaSGNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDG 444
Cdd:cd11046   297 KKLKYTRRVLNESLRLyPQPPVLIRRAVEDDKL---PGGGVKVPAGTDIFISVY-NLHRSPELWEDPEEFDPERFLDPFI 372
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1050373214 445 TKKTDFFKNgkkvkYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEEI 503
Cdd:cd11046   373 NPPNEVIDD-----FAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHV 426
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
321-522 4.63e-13

cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is composed of family 4 cytochrome P450s from vertebrate subfamilies A (CYP4A), B (CYP4B), F (CYP4F), T (CYP4T), X (CYP4X), and Z (CYP4Z). Also included are similar proteins from lancelets, tunicates, hemichordates, echinoderms, mollusks, annelid worms, sponges, and choanoflagellates, among others. The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B and CYP4F are conserved among vertebrates. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4F enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4B_4F-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 71.05  E-value: 4.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketgqevkpgGPLINLTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQnmkvkm 399
Cdd:cd20659   249 WTLYSLAKHPEHQQKCREEVDEVL----------GDRDDIEWDDLSKLPYLTMCIKESLRLyPPVPFIARTLTK------ 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgnDFSLRG-----GDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDgTKKTDffkngkkvKYYLMPWGAGSSICPGR 474
Cdd:cd20659   313 ----PITIDGvtlpaGTLIAINIY-ALHHNPTVWEDPEEFDPERFLPEN-IKKRD--------PFAFIPFSAGPRNCIGQ 378
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1050373214 475 FFAANELKQFVFLMLTYFEFqLVNPNEEIPSIDPnrwgfGVMQPIHDI 522
Cdd:cd20659   379 NFAMNEMKVVLARILRRFEL-SVDPNHPVEPKPG-----LVLRSKNGI 420
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
279-502 6.04e-13

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 70.72  E-value: 6.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 279 ISGWISEQHQQRAEHGMPEHMQDRFMFMLLWASQGNTGPAS-------------------------FWFLLYLLKHPEAM 333
Cdd:cd20654   196 LEEWLEEHRQKRSSSGKSKNDEDDDDVMMLSILEDSQISGYdadtvikatclelilggsdttavtlTWALSLLLNNPHVL 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 334 QAVREEVEA-VLKETGQEVKPggplINltrdmllKTPVMDSALEETLRL--TAAPVLIRAVKQNMKVkmasgNDFSLRGG 410
Cdd:cd20654   276 KKAQEELDThVGKDRWVEESD----IK-------NLVYLQAIVKETLRLypPGPLLGPREATEDCTV-----GGYHVPKG 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 411 DRIaffpYIAV---QMDPGVHPEPEKYKYNRFLNEDgtKKTDFfkngKKVKYYLMPWGAGSSICPGRFFAAnelkQFVFL 487
Cdd:cd20654   340 TRL----LVNVwkiQRDPNVWSDPLEFKPERFLTTH--KDIDV----RGQNFELIPFGSGRRSCPGVSFGL----QVMHL 405
                         250
                  ....*....|....*..
gi 1050373214 488 MLTYF--EFQLVNPNEE 502
Cdd:cd20654   406 TLARLlhGFDIKTPSNE 422
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
304-504 7.62e-13

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


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 70.39  E-value: 7.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 304 MFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETgqevkpggpliNLTRDMLLKTPVMDSALEETLRLTa 383
Cdd:cd11044   228 ALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEE-----------PLTLESLKKMPYLDQVIKEVLRLV- 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 384 APV---LIRAVKqnmkvkmasgnDFSLrGGDRI-----AFFPYIAVQMDPGVHPEPEKYKYNRFLNEDgtkktdffKNGK 455
Cdd:cd11044   296 PPVgggFRKVLE-----------DFEL-GGYQIpkgwlVYYSIRDTHRDPELYPDPERFDPERFSPAR--------SEDK 355
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1050373214 456 KVKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVnPNEEIP 504
Cdd:cd11044   356 KKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELL-PNQDLE 403
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
301-503 3.22e-12

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: 68.32  E-value: 3.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 301 DRFMFmllwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevkpGGPLINLTRDMLLKTPVMDSALEETLR 380
Cdd:cd20628   235 DTFMF----AGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIF---------GDDDRRPTLEDLNKMKYLERVIKETLR 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 L-TAAPVLIRAVKQNMKVkmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEdgtkktdffkNGKKVKY 459
Cdd:cd20628   302 LyPSVPFIGRRLTEDIKL-----DGYTIPKGTTVVISIY-ALHRNPEYFPDPEKFDPDRFLPE----------NSAKRHP 365
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050373214 460 YL-MPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEEI 503
Cdd:cd20628   366 YAyIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGEDL 410
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
287-497 4.87e-12

cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, and similar cytochrome P450s; CYP46A1 is also called cholesterol 24-hydroxylase (EC 1.14.14.25), CH24H, cholesterol 24-monooxygenase, or cholesterol 24S-hydroxylase. It catalyzes the conversion of cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. CYP46A1 is associated with high-order brain functions; increased expression improves cognition while a reduction leads to a poor cognitive performance. It also plays a role in the pathogenesis or progression of neurodegenerative disorders. CYP46A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410706 [Multi-domain]  Cd Length: 429  Bit Score: 67.93  E-value: 4.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 287 HQQRAEHGMpEHMQDRFM-FMLlwASQGNTGPA-SFWFLLyLLKHPEAMQAVREEVEAVLketgqevkpgGPLINLTRDM 364
Cdd:cd20613   224 SEEEPDFDM-EELLDDFVtFFI--AGQETTANLlSFTLLE-LGRHPEILKRLQAEVDEVL----------GSKQYVEYED 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 365 LLKTPVMDSALEETLRLTA-APVLIRAVKQNMKVkmasgNDFSLRGGDRIAFFPYIAVQMdPGVHPEPEKYKYNRFLNED 443
Cdd:cd20613   290 LGKLEYLSQVLKETLRLYPpVPGTSRELTKDIEL-----GGYKIPAGTTVLVSTYVMGRM-EEYFEDPLKFDPERFSPEA 363
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1050373214 444 GTKKTdffkngkkvKYYLMPWGAGSSICPGRFFAANELKqfVFL--MLTYFEFQLV 497
Cdd:cd20613   364 PEKIP---------SYAYFPFSLGPRSCIGQQFAQIEAK--VILakLLQNFKFELV 408
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
185-493 7.74e-12

cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces cerevisiae cytochrome P450 56, also called cytochrome P450-DIT2, and similar fungal proteins. CYP56 is involved in spore wall maturation and is thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine-containing precursors of the spore wall. The CYP56-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 67.35  E-value: 7.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 185 QDGLFNYSYNIVFRAGYlalygnepaknkGSKEKAKEFDRKHSDELFYEFrkYDQLFPRLAY--AVLPPKDKIEAERLKR 262
Cdd:cd11070   107 RDLLQRLALNVIGEVGF------------GFDLPALDEEESSLHDTLNAI--KLAIFPPLFLnfPFLDRLPWVLFPSRKR 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 263 LFWNMLSIKKTLQKENISGWISEQHQQRAEHGMPEHMQDRF--------------MFMLLWASQGNTGPAsFWFLLYLL- 327
Cdd:cd11070   173 AFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRArrsggltekellgnLFIFFIAGHETTANT-LSFALYLLa 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 328 KHPEAMQAVREEVEAVLketgqevkPGGPLINLTRDMLLKTPVMDSALEETLRLtAAPVLI--RAVKQNMKVKMASGNDF 405
Cdd:cd11070   252 KHPEVQDWLREEIDSVL--------GDEPDDWDYEEDFPKLPYLLAVIYETLRL-YPPVQLlnRKTTEPVVVITGLGQEI 322
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 406 SLRGGDRIaFFPYIAVQMDPGVH-PEPEKYKYNRFLNEDGTKKTDFFKNGKKVKYylMPWGAGSSICPGRFFAANELKQF 484
Cdd:cd11070   323 VIPKGTYV-GYNAYATHRDPTIWgPDADEFDPERWGSTSGEIGAATRFTPARGAF--IPFSAGPRACLGRKFALVEFVAA 399

                  ....*....
gi 1050373214 485 VFLMLTYFE 493
Cdd:cd11070   400 LAELFRQYE 408
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
321-500 8.18e-12

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


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 67.24  E-value: 8.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKETG--QEVKpggpLINLtrdmllktPVMDSALEETLRL-TAAPVLIRAVKQNMKV 397
Cdd:cd20655   250 WAMAELINNPEVLEKAREEIDSVVGKTRlvQESD----LPNL--------PYLQAVVKETLRLhPPGPLLVRESTEGCKI 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 398 kmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKnGKKVKYylMPWGAGSSICPGRFFA 477
Cdd:cd20655   318 -----NGYDIPEKTTLFVNVY-AIMRDPNYWEDPLEFKPERFLASSRSGQELDVR-GQHFKL--LPFGSGRRGCPGASLA 388
                         170       180
                  ....*....|....*....|...
gi 1050373214 478 ANELKQFVFLMLTYFEFQLVNPN 500
Cdd:cd20655   389 YQVVGTAIAAMVQCFDWKVGDGE 411
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
321-496 8.27e-12

cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including insect cytochrome P450 306A1 (CYP306A1 or Cyp306a1) and CYP18A1. CYP306A1 functions as a carbon 25-hydroxylase and has an essential role in ecdysteroid biosynthesis during insect development. CYP18A1 is a 26-hydroxylase and plays a key role in steroid hormone inactivation. The CYP306A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 67.05  E-value: 8.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKEtgqevkPGGPLINLTRDMllktPVMDSALEETLRL-TAAPVLI-RAVKQNMKVk 398
Cdd:cd20652   256 WFLLYMALFPKEQRRIQRELDEVVGR------PDLVTLEDLSSL----PYLQACISESQRIrSVVPLGIpHGCTEDAVL- 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 399 masgNDFSLRGGDRIafFPYI-AVQMDPGVHPEPEKYKYNRFLNEDGT-KKTDFFkngkkvkyylMPWGAGSSICPGRFF 476
Cdd:cd20652   325 ----AGYRIPKGSMI--IPLLwAVHMDPNLWEEPEEFRPERFLDTDGKyLKPEAF----------IPFQTGKRMCLGDEL 388
                         170       180
                  ....*....|....*....|
gi 1050373214 477 AANELKQFVFLMLTYFEFQL 496
Cdd:cd20652   389 ARMILFLFTARILRKFRIAL 408
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
322-496 9.26e-12

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


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 66.82  E-value: 9.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLY-LLKHPEAMQAVREEVEAVLketgqevkPGGPlinLTRDMLLKTPVMDSALEETLRLTA-APVLIRAVKQNMKVkm 399
Cdd:cd11068   252 FALYyLLKNPEVLAKARAEVDEVL--------GDDP---PPYEQVAKLRYIRRVLDETLRLWPtAPAFARKPKEDTVL-- 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asGNDFSLRGGDRIaFFPYIAVQMDPGVH-PEPEKYKYNRFLNEDGTKktdFFKNGKKvkyylmPWGAGSSICPGRFFAA 478
Cdd:cd11068   319 --GGKYPLKKGDPV-LVLLPALHRDPSVWgEDAEEFRPERFLPEEFRK---LPPNAWK------PFGNGQRACIGRQFAL 386
                         170
                  ....*....|....*...
gi 1050373214 479 NELKQFVFLMLTYFEFQL 496
Cdd:cd11068   387 QEATLVLAMLLQRFDFED 404
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
322-502 1.74e-11

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 66.07  E-value: 1.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLLKHPEAMQAVREEVEAVLKEtgqevkpgGPLINLTRDMLLKT-PVMDSALEETLRL---TAAPvLIRAVkqnmkv 397
Cdd:cd11060   245 ILYYLLKNPRVYAKLRAEIDAAVAE--------GKLSSPITFAEAQKlPYLQAVIKEALRLhppVGLP-LERVV------ 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 398 kmasgndfsLRGGDRIA--FFP--------YIAVQMDPGVH-PEPEKYKYNRFLNEDGTKKtdffkngKKVKYYLMPWGA 466
Cdd:cd11060   310 ---------PPGGATICgrFIPggtivgvnPWVIHRDKEVFgEDADVFRPERWLEADEEQR-------RMMDRADLTFGA 373
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1050373214 467 GSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEE 502
Cdd:cd11060   374 GSRTCLGKNIALLELYKVIPELLRRFDFELVDPEKE 409
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
304-503 2.10e-11

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: 65.73  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 304 MFMLLW----ASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQevkpggplinLTRDMLLKTPVMDSALEETL 379
Cdd:cd11075   232 LVSLCSeflnAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAV----------VTEEDLPKMPYLKAVVLETL 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 380 RL--TAAPVLIRAVKQNMKVkmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTkkTDFFKNGKKV 457
Cdd:cd11075   302 RRhpPGHFLLPHAVTEDTVL-----GGYDIPAGAEVNFNVA-AIGRDPKVWEDPEEFKPERFLAGGEA--ADIDTGSKEI 373
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1050373214 458 KyyLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVnPNEEI 503
Cdd:cd11075   374 K--MMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLV-EGEEV 416
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
321-509 2.22e-11

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: 65.70  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketgqevkPGGPLINLT-RDMLlktPVMDSALEETLRL-TAAPVLI--RAVKqnmk 396
Cdd:cd20651   247 FAFLYLLLNPEVQRKVQEEIDEVV--------GRDRLPTLDdRSKL---PYTEAVILEVLRIfTLVPIGIphRALK---- 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 397 vkmasgnDFSLRG----GDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDffkngkkvkYYLMPWGAGSSICP 472
Cdd:cd20651   312 -------DTTLGGyripKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKD---------EWFLPFGAGKRRCL 375
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1050373214 473 GRFFAANELkqfvFLMLTYF--EFQLVNPNEEIPSIDPN 509
Cdd:cd20651   376 GESLARNEL----FLFFTGLlqNFTFSPPNGSLPDLEGI 410
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
306-481 3.10e-11

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


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 65.36  E-value: 3.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 306 MLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevkPGGPlinLTRDMLLKTPVMDSALEETLRLTaAP 385
Cdd:cd11049   227 TLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVL--------GGRP---ATFEDLPRLTYTRRVVTEALRLY-PP 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 386 VLI---RAVKQnmkVKMAsgnDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEdgtkktdffKNGKKVKYYLM 462
Cdd:cd11049   295 VWLltrRTTAD---VELG---GHRLPAGTEVAFSPY-ALHRDPEVYPDPERFDPDRWLPG---------RAAAVPRGAFI 358
                         170
                  ....*....|....*....
gi 1050373214 463 PWGAGSSICPGRFFAANEL 481
Cdd:cd11049   359 PFGAGARKCIGDTFALTEL 377
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
321-522 3.92e-11

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


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 64.89  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketGQEVKPggplinlTRDMLLKTPVMDSALEETLRLTA-APV-LIRAVKQNMKVK 398
Cdd:cd11026   248 WALLLLMKYPHIQEKVQEEIDRVI---GRNRTP-------SLEDRAKMPYTDAVIHEVQRFGDiVPLgVPHAVTRDTKFR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 399 masgnDFSLRGGDRIafFPYI-AVQMDPGVHPEPEKYKYNRFLNEDGT-KKTDFFkngkkvkyylMPWGAGSSICPGRFF 476
Cdd:cd11026   318 -----GYTIPKGTTV--IPNLtSVLRDPKQWETPEEFNPGHFLDEQGKfKKNEAF----------MPFSAGKRVCLGEGL 380
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1050373214 477 AANELkqfvFLMLTYF--EFQLVNPN-EEIPSIDPNRWGFGVMQPIHDI 522
Cdd:cd11026   381 ARMEL----FLFFTSLlqRFSLSSPVgPKDPDLTPRFSGFTNSPRPYQL 425
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
17-503 1.02e-10

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 63.80  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  17 MSKMALFLQIILALLVSFIggLYLLGIFRKRRSDEPPLDKGSI--PWLGYALD-FRKNTLTFLQKMHKKHGDIFTVQIAG 93
Cdd:PLN02196    1 MDFSALFLTLFAGALFLCL--LRFLAGFRRSSSTKLPLPPGTMgwPYVGETFQlYSQDPNVFFASKQKRYGSVFKTHVLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  94 YYFTFVMDPLS--FGPIIKEPKANVDFEEFATelvlRVFGYQS-FTHD---HKMLEKSSTKHMTGDGLvvmtHAMMENLQ 167
Cdd:PLN02196   79 CPCVMISSPEAakFVLVTKSHLFKPTFPASKE----RMLGKQAiFFHQgdyHAKLRKLVLRAFMPDAI----RNMVPDIE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 168 NLMVHNIGSEKGEREWHQDGLFNYSYNIVFragyLALYGnepaknkgskeKAKEFDRKHSDELFYEFRKYDQLFPRLAYA 247
Cdd:PLN02196  151 SIAQESLNSWEGTQINTYQEMKTYTFNVAL----LSIFG-----------KDEVLYREDLKRCYYILEKGYNSMPINLPG 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 248 VLPPKDKIEAERLKRLFWNMLSIKKT--LQKENISGWISEQHQQRAEhgmpEHMQDRFMfMLLWASQGNTGPASFWFLLY 325
Cdd:PLN02196  216 TLFHKSMKARKELAQILAKILSKRRQngSSHNDLLGSFMGDKEGLTD----EQIADNII-GVIFAARDTTASVLTWILKY 290
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 326 LLKHPEAMQAVREEVEAVLKETGQEVkpggpliNLTRDMLLKTPVMDSALEETLRltAAPVLIRAVKQNMKVKMASGNDF 405
Cdd:PLN02196  291 LAENPSVLEAVTEEQMAIRKDKEEGE-------SLTWEDTKKMPLTSRVIQETLR--VASILSFTFREAVEDVEYEGYLI 361
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 406 SlRGGDRIAFFPYIavQMDPGVHPEPEKYKYNRFlnEDGTKKTDFfkngkkvkyylMPWGAGSSICPGRFFAANELKQFV 485
Cdd:PLN02196  362 P-KGWKVLPLFRNI--HHSADIFSDPGKFDPSRF--EVAPKPNTF-----------MPFGNGTHSCPGNELAKLEISVLI 425
                         490
                  ....*....|....*...
gi 1050373214 486 FLMLTYFEFQLVNPNEEI 503
Cdd:PLN02196  426 HHLTTKYRWSIVGTSNGI 443
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
321-496 1.23e-10

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


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 63.58  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVeavlketgQEVKPGGPLINltrDML--LKTPVMdsALEETLRL-TAAPVLIRAVKQNMKV 397
Cdd:cd20640   252 WCLMLLALHPEWQDRVRAEV--------LEVCKGGPPDA---DSLsrMKTVTM--VIQETLRLyPPAAFVSREALRDMKL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 398 kmasGNDFSLRGgdRIAFFPYIAVQMDPGV-HPEPEKYKYNRFlnEDGTKKtdffknGKKVKYYLMPWGAGSSICPGRFF 476
Cdd:cd20640   319 ----GGLVVPKG--VNIWVPVSTLHLDPEIwGPDANEFNPERF--SNGVAA------ACKPPHSYMPFGAGARTCLGQNF 384
                         170       180
                  ....*....|....*....|
gi 1050373214 477 AANELKQFVFLMLTYFEFQL 496
Cdd:cd20640   385 AMAELKVLVSLILSKFSFTL 404
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
322-506 1.65e-10

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: 62.98  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLL-KHPEAMQAVREEVEAVLKetgqevkpGGPLinlTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVkm 399
Cdd:cd20620   234 WTWYLLaQHPEVAARLRAEVDRVLG--------GRPP---TAEDLPQLPYTEMVLQESLRLyPPAWIIGREAVEDDEI-- 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDgtkktdffkNGKKVKYYLMPWGAGSSICPGRFFAAN 479
Cdd:cd20620   301 ---GGYRIPAGSTVLISPY-VTHRDPRFWPDPEAFDPERFTPER---------EAARPRYAYFPFGGGPRICIGNHFAMM 367
                         170       180       190
                  ....*....|....*....|....*....|
gi 1050373214 480 ELKQFVFLMLTYFEFQLVnPNEEI---PSI 506
Cdd:cd20620   368 EAVLLLATIAQRFRLRLV-PGQPVepePLI 396
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
325-504 5.24e-10

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


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 61.57  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 325 YLLKHPEAMQAVREEVEAVLKETgqevkpggplinLTRDMLLKTPVMDSALEETLRL-TAAPVLIR-AVKqnmkvkmasg 402
Cdd:cd11045   237 FLARHPEWQERLREESLALGKGT------------LDYEDLGQLEVTDWVFKEALRLvPPVPTLPRrAVK---------- 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 403 nDFSLRG-----GDRIAFFPyIAVQMDPGVHPEPEKYKYNRFL---NEDgtkktdffkngKKVKYYLMPWGAGSSICPGR 474
Cdd:cd11045   295 -DTEVLGyripaGTLVAVSP-GVTHYMPEYWPNPERFDPERFSperAED-----------KVHRYAWAPFGGGAHKCIGL 361
                         170       180       190
                  ....*....|....*....|....*....|
gi 1050373214 475 FFAANELKQFVFLMLTYFEFQLVnPNEEIP 504
Cdd:cd11045   362 HFAGMEVKAILHQMLRRFRWWSV-PGYYPP 390
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
301-503 5.81e-10

cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4F subfamily show diverse specificities among its members: CYP4F2 and CYP4F3 metabolize pro- and anti-inflammatory leukotrienes; CYP4F8 and CYP4F12 metabolize prostaglandins, endoperoxides and arachidonic acid; CYP4F11 and CYP4F12 metabolize VLFA and are unique in the CYP4F subfamily since they also hydroxylate xenobiotics such as benzphetamine, ethylmorphine, erythromycin, and ebastine. CYP4F belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 61.25  E-value: 5.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 301 DRFMFmllwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEvkpggpliNLTRDMLLKTPVMDSALEETLR 380
Cdd:cd20679   250 DTFMF----EGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPE--------EIEWDDLAQLPFLTMCIKESLR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 L-TAAPVLIRAVKQNMKVK----MASGNdfslrggdrIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTdffkngk 455
Cdd:cd20679   318 LhPPVTAISRCCTQDIVLPdgrvIPKGI---------ICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRS------- 381
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1050373214 456 kvKYYLMPWGAGSSICPGRFFAANELKqfVFLMLTYFEFQLVNPNEEI 503
Cdd:cd20679   382 --PLAFIPFSAGPRNCIGQTFAMAEMK--VVLALTLLRFRVLPDDKEP 425
PLN02966 PLN02966
cytochrome P450 83A1
310-498 7.03e-10

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 61.30  E-value: 7.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 310 ASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGqevkpggpLINLTRDMLLKTPVMDSALEETLRLTAA-PVLI 388
Cdd:PLN02966  300 AGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKG--------STFVTEDDVKNLPYFRALVKETLRIEPViPLLI 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 389 -RAVKQNMKVKmasgnDFSLRGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNedgtKKTDFfkngKKVKYYLMPWGAG 467
Cdd:PLN02966  372 pRACIQDTKIA-----GYDIPAGTTVNVNAWAVSRDEKEWGPNPDEFRPERFLE----KEVDF----KGTDYEFIPFGSG 438
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1050373214 468 SSICPGRFFAANELKQFVFLMLTYFEFQLVN 498
Cdd:PLN02966  439 RRMCPGMRLGAAMLEVPYANLLLNFNFKLPN 469
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
322-495 7.54e-10

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 60.89  E-value: 7.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLLK-HPEAMQAVREEVEAVLKETGQevkpggplinLTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVkm 399
Cdd:cd20650   250 FLLYELAtHPDVQQKLQEEIDAVLPNKAP----------PTYDTVMQMEYLDMVVNETLRLfPIAGRLERVCKKDVEI-- 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEdgtkktdffKNGKKVKYYLMPWGAGSSICPGRFFAAN 479
Cdd:cd20650   318 ---NGVFIPKGTVVMIPTY-ALHRDPQYWPEPEEFRPERFSKK---------NKDNIDPYIYLPFGSGPRNCIGMRFALM 384
                         170
                  ....*....|....*.
gi 1050373214 480 ELKQFVFLMLTYFEFQ 495
Cdd:cd20650   385 NMKLALVRVLQNFSFK 400
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
240-518 7.89e-10

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: 61.05  E-value: 7.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 240 LFPRLAYavLPP----KDKIEAERLKRLFWNML-----SIKKTLQKENISG-WISE-QHQQRAEHGMPEHmQDRFMFMLL 308
Cdd:cd11065   155 FFPFLRY--LPSwlgaPWKRKARELRELTRRLYegpfeAAKERMASGTATPsFVKDlLEELDKEGGLSEE-EIKYLAGSL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 309 WASQGNTGPASF-WFLLYLLKHPEAMQAVREEVEAVLKETGQevkpggPLINLtRDMLlktPVMDSALEETLRL-TAAPV 386
Cdd:cd11065   232 YEAGSDTTASTLqTFILAMALHPEVQKKAQEELDRVVGPDRL------PTFED-RPNL---PYVNAIVKEVLRWrPVAPL 301
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 387 -LIRAVKQnmkvkmasgnDFSLRGgdriAFFP--------YIAVQMDPGVHPEPEKYKYNRFLNEDGtkktdffKNGKKV 457
Cdd:cd11065   302 gIPHALTE----------DDEYEG----YFIPkgttvipnAWAIHHDPEVYPDPEEFDPERYLDDPK-------GTPDPP 360
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050373214 458 KYYLMPWGAGSSICPGRFFAANELkqfvFL----MLTYFEFQLVNPNEEIPSIDPNRWGFG-VMQP 518
Cdd:cd11065   361 DPPHFAFGFGRRICPGRHLAENSL----FIaiarLLWAFDIKKPKDEGGKEIPDEPEFTDGlVSHP 422
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
321-502 8.45e-10

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: 60.73  E-value: 8.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKETGQevkpggplinLTRDMLLKTPVMDSALEETLRL--TAAPVLIRAVKQNMKVK 398
Cdd:cd20621   251 MCLYYLAKYPEIQEKLRQEIKSVVGNDDD----------ITFEDLQKLNYLNAFIKEVLRLynPAPFLFPRVATQDHQIG 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 399 masgnDFSLRGGDRIAFFpYIAVQMDPGVHPEPEKYKYNRFLNEdgtkktdffKNGKKVKYYLMPWGAGSSICPGRFFAA 478
Cdd:cd20621   321 -----DLKIKKGWIVNVG-YIYNHFNPKYFENPDEFNPERWLNQ---------NNIEDNPFVFIPFSAGPRNCIGQHLAL 385
                         170       180
                  ....*....|....*....|....
gi 1050373214 479 NELKQFVFLMLTYFEFQlVNPNEE 502
Cdd:cd20621   386 MEAKIILIYILKNFEIE-IIPNPK 408
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
301-503 2.12e-09

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 59.77  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 301 DRFMFmllwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKETGQEVkpggplinlTRDMLLKTPVMDSALEETLR 380
Cdd:cd20680   249 DTFMF----EGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPV---------TMEDLKKLRYLECVIKESLR 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 L-TAAPVLIRAVKQNMKVkmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTdffkngkkvKY 459
Cdd:cd20680   316 LfPSVPLFARSLCEDCEI-----RGFKVPKGVNAVIIPY-ALHRDPRYFPEPEEFRPERFFPENSSGRH---------PY 380
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1050373214 460 YLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEEI 503
Cdd:cd20680   381 AYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQKREEL 424
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
303-501 2.33e-09

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 59.52  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 303 FMFMLLWASQGNTgpASF--WFLLYLLKHPEAMQAVREEVeavlketgqevkpggplinltrdmllktPVMDSALEETLR 380
Cdd:COG2124   230 ELLLLLLAGHETT--ANAlaWALYALLRHPEQLARLRAEP----------------------------ELLPAAVEETLR 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 L-TAAPVLIRAVKQnmkvkmasgnDFSLRG-----GDRIAFFPYiAVQMDPGVHPEPEKYKYNRflnedgtkktdffkng 454
Cdd:COG2124   280 LyPPVPLLPRTATE----------DVELGGvtipaGDRVLLSLA-AANRDPRVFPDPDRFDPDR---------------- 332
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1050373214 455 kkVKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFE-FQLVNPNE 501
Cdd:COG2124   333 --PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLAPPEE 378
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
288-529 3.21e-09

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: 58.96  E-value: 3.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 288 QQRAEHGMPEHMQDRfMFM----LLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEavlketgQEVKPGGPLINLTRD 363
Cdd:cd20674   212 QPRGEKGMGQLLEGH-VHMavvdLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELD-------RVLGPGASPSYKDRA 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 364 MLlktPVMDSALEETLRLTaaPVLIRAVKQnmkvkmASGNDFSLRGGD---RIAFFPYI-AVQMDPGVHPEPEKYKYNRF 439
Cdd:cd20674   284 RL---PLLNATIAEVLRLR--PVVPLALPH------RTTRDSSIAGYDipkGTVVIPNLqGAHLDETVWEQPHEFRPERF 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 440 LneDGTKKTDffkngkkvkyYLMPWGAGSSICPGRFFAANELkqFVFLMLTYFEFQLVNPN-EEIPSIDPNrwgFGV--- 515
Cdd:cd20674   353 L--EPGAANR----------ALLPFGCGARVCLGEPLARLEL--FVFLARLLQAFTLLPPSdGALPSLQPV---AGInlk 415
                         250
                  ....*....|....
gi 1050373214 516 MQPihdiqFRYRLR 529
Cdd:cd20674   416 VQP-----FQVRLQ 424
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
253-499 4.36e-09

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 58.76  E-value: 4.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 253 DKIEAERLKRLfwNMLSIKKTLQKENISGWISEQHQQRAEHGmPEHMQDrFMFMLLWASQGNTGPASFWFLLYLLKHPEA 332
Cdd:cd11064   188 YEVISRRREEL--NSREEENNVREDLLSRFLASEEEEGEPVS-DKFLRD-IVLNFILAGRDTTAAALTWFFWLLSKNPRV 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 333 MQAVREEVEAVLKETGqevkpGGPLINLTRDMLLKTPVMDSALEETLRLTaaPvlirAVKQNMKVKMA-----SGndFSL 407
Cdd:cd11064   264 EEKIREELKSKLPKLT-----TDESRVPTYEELKKLVYLHAALSESLRLY--P----PVPFDSKEAVNddvlpDG--TFV 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 408 RGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGtkktdFFKNGKKVKYylMPWGAGSSICPGRFFAANELKQFVFL 487
Cdd:cd11064   331 KKGTRIVYSIYAMGRMESIWGEDALEFKPERWLDEDG-----GLRPESPYKF--PAFNAGPRICLGKDLAYLQMKIVAAA 403
                         250
                  ....*....|..
gi 1050373214 488 MLTYFEFQLVNP 499
Cdd:cd11064   404 ILRRFDFKVVPG 415
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
322-506 5.26e-09

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: 58.31  E-value: 5.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLL-KHPEAMQAVREEVEAVLKETGQevkpggplinLTRDMLLKTPVMDSALEETLRLT-AAPVLIRAVKQnmkvkm 399
Cdd:cd11054   253 FLLYHLaKNPEVQEKLYEEIRSVLPDGEP----------ITAEDLKKMPYLKACIKESLRLYpVAPGNGRILPK------ 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgnDFSLRG-----GDRIAFFPYIAvQMDPGVHPEPEKYKYNRFLNEDGTkktdffkNGKKVKYYLMPWGAGSSICPGR 474
Cdd:cd11054   317 ----DIVLSGyhipkGTLVVLSNYVM-GRDEEYFPDPEEFIPERWLRDDSE-------NKNIHPFASLPFGFGPRMCIGR 384
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1050373214 475 FFAANELKQFVFLMLTyfEFQLVNPNEEIPSI 506
Cdd:cd11054   385 RFAELEMYLLLAKLLQ--NFKVEYHHEELKVK 414
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
321-496 6.46e-09

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 58.23  E-value: 6.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketGQEVKPggplinlTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVkm 399
Cdd:cd20639   254 WTTVLLAMHPEWQERARREVLAVC---GKGDVP-------TKDHLPKLKTLGMILNETLRLyPPAVATIRRAKKDVKL-- 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgNDFSLRGGDRIaFFPYIAVQMDPGV-HPEPEKYKYNRFlnEDGTKKTdffkngKKVKYYLMPWGAGSSICPGRFFAA 478
Cdd:cd20639   322 ---GGLDIPAGTEL-LIPIMAIHHDAELwGNDAAEFNPARF--ADGVARA------AKHPLAFIPFGLGPRTCVGQNLAI 389
                         170
                  ....*....|....*...
gi 1050373214 479 NELKQFVFLMLTYFEFQL 496
Cdd:cd20639   390 LEAKLTLAVILQRFEFRL 407
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
301-504 1.10e-08

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: 57.27  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 301 DRFMFmllwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevkpGGPLINLTRDMLLKTPVMDSALEETLR 380
Cdd:cd20660   238 DTFMF----EGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIF---------GDSDRPATMDDLKEMKYLECVIKEALR 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 L-TAAPVLIRAVKQNMKVKmasgnDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEdgtkktdffkNGKKVK- 458
Cdd:cd20660   305 LfPSVPMFGRTLSEDIEIG-----GYTIPKGTTVLVLTY-ALHRDPRQFPDPEKFDPDRFLPE----------NSAGRHp 368
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1050373214 459 YYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEEIP 504
Cdd:cd20660   369 YAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQKREDLK 414
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
321-509 1.48e-08

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 57.09  E-value: 1.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketGQEVKPggpliNLTRDMLLktPVMDSALEETLRLTA-APVLIRavkqnmkvKM 399
Cdd:cd20666   250 WCLLYMSLYPEVQEKVQAEIDTVI---GPDRAP-----SLTDKAQM--PFTEATIMEVQRMTVvVPLSIP--------HM 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 ASGNDfSLRG----GDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDG--TKKTDFfkngkkvkyylMPWGAGSSICPG 473
Cdd:cd20666   312 ASENT-VLQGytipKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGqlIKKEAF-----------IPFGIGRRVCMG 379
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1050373214 474 RFFAANELKQFVFLMLTYFEFQLVnPNEEIPSIDPN 509
Cdd:cd20666   380 EQLAKMELFLMFVSLMQSFTFLLP-PNAPKPSMEGR 414
PLN02655 PLN02655
ent-kaurene oxidase
298-473 1.93e-08

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 56.67  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 298 HMQDRFMFMLLW----ASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVlkeTGQEvkpggpliNLTRDMLLKTPVMDS 373
Cdd:PLN02655  257 HLTDEQLMMLVWepiiEAADTTLVTTEWAMYELAKNPDKQERLYREIREV---CGDE--------RVTEEDLPNLPYLNA 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 374 ALEETLRL-TAAPVL-IRAVKQNMKVkmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGtKKTDFF 451
Cdd:PLN02655  326 VFHETLRKySPVPLLpPRFVHEDTTL-----GGYDIPAGTQIAINIY-GCNMDKKRWENPEEWDPERFLGEKY-ESADMY 398
                         170       180
                  ....*....|....*....|..
gi 1050373214 452 KngkkvkyyLMPWGAGSSICPG 473
Cdd:PLN02655  399 K--------TMAFGAGKRVCAG 412
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
310-496 2.24e-08

Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP72 clan is associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. This clan includes: CYP734 enzymes that are involved in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis; CYP714 enzymes that are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels; and CYP72 family enzymes, among others. The CYP72 clan belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 56.19  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 310 ASQGNTGPASFWFLLYLLKHPEAMQAVREEVeavLKETGQEvkpggpliNLTRDMLLKTPVMDSALEETLRL-TAAPVLI 388
Cdd:cd11052   243 AGHETTALLLTWTTMLLAIHPEWQEKAREEV---LEVCGKD--------KPPSDSLSKLKTVSMVINESLRLyPPAVFLT 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 389 RAVKQNMKVkmasgNDFSLRGGDRIaFFPYIAVQMDPGVHPE-PEKYKYNRFlnEDGTKKtdffknGKKVKYYLMPWGAG 467
Cdd:cd11052   312 RKAKEDIKL-----GGLVIPKGTSI-WIPVLALHHDEEIWGEdANEFNPERF--ADGVAK------AAKHPMAFLPFGLG 377
                         170       180
                  ....*....|....*....|....*....
gi 1050373214 468 SSICPGRFFAANELKQFVFLMLTYFEFQL 496
Cdd:cd11052   378 PRNCIGQNFATMEAKIVLAMILQRFSFTL 406
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
323-522 2.78e-08

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 56.09  E-value: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 323 LLYLLKHPEAMQAVREEVEAVLketgqevkpgGPLINLTRDMLLKTPVMDSALEETLRLTaaPVLIRAVKQNMKVKMASG 402
Cdd:cd20670   250 FLLLMKYPEVEAKIHEEINQVI----------GPHRLPSVDDRVKMPYTDAVIHEIQRLT--DIVPLGVPHNVIRDTQFR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 403 NDFSLRGGDriaFFPYI-AVQMDPGVHPEPEKYKYNRFLNEDGT-KKTDFFkngkkvkyylMPWGAGSSICPGRFFAANE 480
Cdd:cd20670   318 GYLLPKGTD---VFPLLgSVLKDPKYFRYPEAFYPQHFLDEQGRfKKNEAF----------VPFSSGKRVCLGEAMARME 384
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1050373214 481 LKQFVFLMLTYFEFQLVNPNEEIpSIDPNRWGFGVMQPIHDI 522
Cdd:cd20670   385 LFLYFTSILQNFSLRSLVPPADI-DITPKISGFGNIPPTYEL 425
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
282-495 3.10e-08

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 55.72  E-value: 3.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 282 WISEQHQQRAEHG-----MPEHMQDRFM----FMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevk 352
Cdd:cd11082   194 WTHEILEEIKEAEeegepPPPHSSDEEIagtlLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLR-------- 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 353 pGGPLINLTRDMLLKTPVMDSALEETLRLTaAPVLIravkqnmkVKMASGNDFSLRGGDRIA----FFPYI-AVQMDPgv 427
Cdd:cd11082   266 -PNDEPPLTLDLLEEMKYTRQVVKEVLRYR-PPAPM--------VPHIAKKDFPLTEDYTVPkgtiVIPSIyDSCFQG-- 333
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1050373214 428 HPEPEKYKYNRFLNEDGTKKTdFFKNgkkvkyyLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQ 495
Cdd:cd11082   334 FPEPDKFDPDRFSPERQEDRK-YKKN-------FLVFGAGPHQCVGQEYAINHLMLFLALFSTLVDWK 393
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
281-502 5.33e-08

cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 55.31  E-value: 5.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 281 GWISEQHQQRAEHGMPEHmQDrFMFMLLWASQGNTGP------------------------ASFWFLLYLLKHPEAMQAV 336
Cdd:cd11061   176 DFVRAQLKERLKAEEEKR-PD-IFSYLLEAKDPETGEgldleelvgearllivagsdttatALSAIFYYLARNPEAYEKL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 337 REEVEAVLkETGQEVKPGgplinltrDMLLKTPVMDSALEETLRLT-AAP-VLIRAVkqnmkvkmasgndfsLRGGDRIA 414
Cdd:cd11061   254 RAELDSTF-PSDDEIRLG--------PKLKSLPYLRACIDEALRLSpPVPsGLPRET---------------PPGGLTID 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 415 --FFP---------YiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDffkngkkvKYYLMPWGAGSSICPGRFFAANELKQ 483
Cdd:cd11061   310 geYIPggttvsvpiY-SIHRDERYFPDPFEFIPERWLSRPEELVRA--------RSAFIPFSIGPRGCIGKNLAYMELRL 380
                         250
                  ....*....|....*....
gi 1050373214 484 FVFLMLTYFEFQLVNPNEE 502
Cdd:cd11061   381 VLARLLHRYDFRLAPGEDG 399
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
321-473 7.60e-08

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 54.85  E-value: 7.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVL--KETGQEvkpggplinltRDMLlKTPVMDSALEETLRL-TAAPVLI--RA----- 390
Cdd:cd11073   253 WAMAELLRNPEKMAKARAELDEVIgkDKIVEE-----------SDIS-KLPYLQAVVKETLRLhPPAPLLLprKAeedve 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 391 -----VKQNMKVkmasgndfslrggdriaFFPYIAVQMDPGVHPEPEKYKYNRFLNedgtKKTDFfkNGKKvkYYLMPWG 465
Cdd:cd11073   321 vmgytIPKGTQV-----------------LVNVWAIGRDPSVWEDPLEFKPERFLG----SEIDF--KGRD--FELIPFG 375

                  ....*...
gi 1050373214 466 AGSSICPG 473
Cdd:cd11073   376 SGRRICPG 383
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
321-473 1.00e-07

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 54.15  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKETGqevkpggpLINLTrDmLLKTPVMDSALEETLRL-TAAPVLiravkqnmkVKM 399
Cdd:cd20653   249 WAMSNLLNHPEVLKKAREEIDTQVGQDR--------LIEES-D-LPKLPYLQNIISETLRLyPAAPLL---------VPH 309
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1050373214 400 ASGNDFSLRGGD----RIAFFPYIAVQMDPGVHPEPEKYKYNRFLNEDgtkktdffKNGKKvkyyLMPWGAGSSICPG 473
Cdd:cd20653   310 ESSEDCKIGGYDiprgTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEE--------REGYK----LIPFGLGRRACPG 375
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
225-502 1.30e-07

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 53.84  E-value: 1.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 225 KHSDELFYEFRKYDQLFPRLAYA-----VLP-----PKDKIEA--ERLKRLFWNMLS----IKKTLQKENI----SGWIS 284
Cdd:cd11028   133 SRDDPEFLELVKSNDDFGAFVGAgnpvdVMPwlrylTRRKLQKfkELLNRLNSFILKkvkeHLDTYDKGHIrditDALIK 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 285 EQHQQRAEH----GMPEHMQDRFMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketGQEVKPggpliNL 360
Cdd:cd11028   213 ASEEKPEEEkpevGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVI---GRERLP-----RL 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 361 T-RDMLlktPVMDSALEETLRLTA-APVLIravkqnmkvKMASGNDFSLRG----GDRIAFFPYIAVQMDPGVHPEPEKY 434
Cdd:cd11028   285 SdRPNL---PYTEAFILETMRHSSfVPFTI---------PHATTRDTTLNGyfipKGTVVFVNLWSVNHDEKLWPDPSVF 352
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1050373214 435 KYNRFLNEDGT---KKTDFFkngkkvkyylMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQlVNPNEE 502
Cdd:cd11028   353 RPERFLDDNGLldkTKVDKF----------LPFGAGRRRCLGEELARMELFLFFATLLQQCEFS-VKPGEK 412
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
321-503 1.31e-07

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 54.15  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketGQEVKPGGPLINltrdmllKTPVMDSALEETLRLTaaPVLiravKQNMKVkma 400
Cdd:cd20647   259 WATYLLARHPEVQQQVYEEIVRNL---GKRVVPTAEDVP-------KLPLIRALLKETLRLF--PVL----PGNGRV--- 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 401 SGNDFSLRG-----GDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNgkkvkyylMPWGAGSSICPGRF 475
Cdd:cd20647   320 TQDDLIVGGylipkGTQLALCHY-STSYDEENFPRAEEFRPERWLRKDALDRVDNFGS--------IPFGYGIRSCIGRR 390
                         170       180
                  ....*....|....*....|....*...
gi 1050373214 476 FAANELKQFVFLMLTYFEFQLVNPNEEI 503
Cdd:cd20647   391 IAELEIHLALIQLLQNFEIKVSPQTTEV 418
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
323-518 2.43e-07

cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group includes CYP2C, and similar CYPs including mammalian CYP2E1, also called 4-nitrophenol 2-hydroxylase, as well as chicken CYP2H1 and CYP2H2. The CYP2C subfamily is composed of four human members (CYP2C8, CYP2C9, CYP2C18, CYP2C19) that metabolize approximately 20% of clinically used drugs, and all four exhibit genetic polymorphisms that results in toxicity or altered efficacy of some drugs in affected individuals. CYP2E1 participates in the metabolism of endogenous substrates, including acetone and fatty acids, and exogenous compounds such as anesthetics, ethanol, nicotine, acetaminophen, aspartame, and chlorzoxazone, among others. The CYP2C-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 53.03  E-value: 2.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 323 LLYLLKHPEAMQAVREEVEAVLketGQEVKPGgplinltrdML--LKTPVMDSALEETLR-LTAAPV-LIRAVKQNMKVK 398
Cdd:cd20665   250 LLLLLKHPEVTAKVQEEIDRVI---GRHRSPC---------MQdrSHMPYTDAVIHEIQRyIDLVPNnLPHAVTCDTKFR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 399 masgNDFSLRGGDRIAFFPyiAVQMDPGVHPEPEKYKYNRFLNEDGT-KKTDFFkngkkvkyylMPWGAGSSICPGRFFA 477
Cdd:cd20665   318 ----NYLIPKGTTVITSLT--SVLHDDKEFPNPEKFDPGHFLDENGNfKKSDYF----------MPFSAGKRICAGEGLA 381
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1050373214 478 ANELkqFVFL--MLTYFEFQ-LVNPNEeipsID--PNRWGFGVMQP 518
Cdd:cd20665   382 RMEL--FLFLttILQNFNLKsLVDPKD----IDttPVVNGFASVPP 421
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
280-526 2.77e-07

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 52.83  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 280 SGWISEQHQQRAEHGMPEHMQDRF--MFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVlketgqevkPGGPL 357
Cdd:cd20614   187 TGLVAALIRARDDNGAGLSEQELVdnLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA---------GDVPR 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 358 inlTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQnmkvkmasgnDFSLrGGDRIA-----FFPYIAVQMDPGVHPEP 431
Cdd:cd20614   258 ---TPAELRRFPLAEALFRETLRLhPPVPFVFRRVLE----------EIEL-GGRRIPagthlGIPLLLFSRDPELYPDP 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 432 EKYKYNRFLNEDGTKKtdffkngkkvKYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPneEIPSIDPNRW 511
Cdd:cd20614   324 DRFRPERWLGRDRAPN----------PVELLQFGGGPHFCLGYHVACVELVQFIVALARELGAAGIRP--LLVGVLPGRR 391
                         250
                  ....*....|....*
gi 1050373214 512 GFGVMQPIHDIQFRY 526
Cdd:cd20614   392 YFPTLHPSNKTRVAF 406
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
301-494 3.40e-07

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 52.66  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 301 DRFMFmllwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKEtGQevkpggpliNLTRDMLLKTPVMDSALEETLR 380
Cdd:cd20678   245 DTFMF----EGHDTTASGISWILYCLALHPEHQQRCREEIREILGD-GD---------SITWEHLDQMPYTTMCIKEALR 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 381 LTAaPVLIRAVKQNMKVKMASGNdfSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTdffkngkkvKYY 460
Cdd:cd20678   311 LYP-PVPGISRELSKPVTFPDGR--SLPAGITVSLSIY-GLHHNPAVWPNPEVFDPLRFSPENSSKRH---------SHA 377
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1050373214 461 LMPWGAGSSICPGRFFAANELKQFVFLMLTYFEF 494
Cdd:cd20678   378 FLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFEL 411
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
307-503 3.52e-07

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 52.53  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 307 LLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLkETGQevkpggPLINLTRDMLlktPVMDSALEETLRLTAApV 386
Cdd:cd20667   233 LFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVL-GASQ------LICYEDRKRL---PYTNAVIHEVQRLSNV-V 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 387 LIRAVKQNmkVKMASGNDFSLRGGDRIafFPYIA-VQMDPGVHPEPEKYKYNRFLNEDGtkktDFFKNGKkvkyyLMPWG 465
Cdd:cd20667   302 SVGAVRQC--VTSTTMHGYYVEKGTII--LPNLAsVLYDPECWETPHKFNPGHFLDKDG----NFVMNEA-----FLPFS 368
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1050373214 466 AGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEEI 503
Cdd:cd20667   369 AGHRVCLGEQLARMELFIFFTTLLRTFNFQLPEGVQEL 406
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
310-496 1.26e-06

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


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 50.74  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 310 ASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketGQEvKPggplinlTRDMLLKTPVMDSALEETLRL-TAAPVLI 388
Cdd:cd20642   245 AGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVF---GNN-KP-------DFEGLNHLKVVTMILYEVLRLyPPVIQLT 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 389 RAVKQNMKVkmasgNDFSLRGGDRIaFFPYIAVQMDPGVHPEPEK-YKYNRFlnEDG-TKKTdffKNgkKVKYYlmPWGA 466
Cdd:cd20642   314 RAIHKDTKL-----GDLTLPAGVQV-SLPILLVHRDPELWGDDAKeFNPERF--AEGiSKAT---KG--QVSYF--PFGW 378
                         170       180       190
                  ....*....|....*....|....*....|
gi 1050373214 467 GSSICPGRFFAANELKQFVFLMLTYFEFQL 496
Cdd:cd20642   379 GPRICIGQNFALLEAKMALALILQRFSFEL 408
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
321-518 2.06e-06

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: 50.01  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAvlketgqevKPGG---PLINlTRDMLlktPVMDSALEETLRL-TAAPVLI--RAVKQn 394
Cdd:cd20673   254 WIIAFLLHNPEVQKKIQEEIDQ---------NIGFsrtPTLS-DRNHL---PLLEATIREVLRIrPVAPLLIphVALQD- 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 395 mkvkmASGNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTdffkngKKVKYYLmPWGAGSSICPGR 474
Cdd:cd20673   320 -----SSIGEFTIPKGTRVVINLW-ALHHDEKEWDQPDQFMPERFLDPTGSQLI------SPSLSYL-PFGAGPRVCLGE 386
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050373214 475 FFAANELKQFVFLMLTYFEFQlVNPNEEIPSIDPNrwgFG-VMQP 518
Cdd:cd20673   387 ALARQELFLFMAWLLQRFDLE-VPDGGQLPSLEGK---FGvVLQI 427
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
322-518 2.23e-06

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 50.18  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLyLLKHPEAMQAVREEVEAVLketGQEVKPggplinlTRDMLLKTPVMDSALEETLRLT-AAPV-LIRAVKQNMKVKm 399
Cdd:cd20668   250 FLL-LMKHPEVEAKVHEEIDRVI---GRNRQP-------KFEDRAKMPYTEAVIHEIQRFGdVIPMgLARRVTKDTKFR- 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgnDFSLRGGDRIafFPYI-AVQMDPGVHPEPEKYKYNRFLNEDGT-KKTDFFkngkkvkyylMPWGAGSSICPGRFFA 477
Cdd:cd20668   318 ----DFFLPKGTEV--FPMLgSVLKDPKFFSNPKDFNPQHFLDDKGQfKKSDAF----------VPFSIGKRYCFGEGLA 381
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1050373214 478 ANELKQFVFLMLTYFEFQLVNPNEEIpSIDPNRWGFGVMQP 518
Cdd:cd20668   382 RMELFLFFTTIMQNFRFKSPQSPEDI-DVSPKHVGFATIPR 421
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
321-477 2.78e-06

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 49.78  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketgqevkpgGPLINLTRDMLLKTPVMDSALEETLRL-TAAPVLIravkQNMKVKM 399
Cdd:cd11074   255 WGIAELVNHPEIQKKLRDELDTVL----------GPGVQITEPDLHKLPYLQAVVKETLRLrMAIPLLV----PHMNLHD 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 ASGNDFSLRGGDRI---AFFpyiaVQMDPGVHPEPEKYKYNRFLNEDGTKKtdffKNGKKVKYylMPWGAGSSICPGRFF 476
Cdd:cd11074   321 AKLGGYDIPAESKIlvnAWW----LANNPAHWKKPEEFRPERFLEEESKVE----ANGNDFRY--LPFGVGRRSCPGIIL 390

                  .
gi 1050373214 477 A 477
Cdd:cd11074   391 A 391
PTZ00404 PTZ00404
cytochrome P450; Provisional
23-481 3.13e-06

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 49.72  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  23 FLQIILALLVSFIgglYLLGIFRKRRSDEPPLdKG--SIPWLGYALDFRKNTLTFLQKMHKKHGDIFTVQIAGYYFTFVM 100
Cdd:PTZ00404    3 LFNIILFLFIFYI---IHNAYKKYKKIHKNEL-KGpiPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 101 DPLsfgpIIKEPKANvDFEEFATELVLRVFGYQSFTH-------DH---------KMLEKSSTKHmtgdglvvmTHAMME 164
Cdd:PTZ00404   79 DPI----LIREMFVD-NFDNFSDRPKIPSIKHGTFYHgivtssgEYwkrnreivgKAMRKTNLKH---------IYDLLD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 165 NLQNLMVHNIGS--EKGE--------REWHQDGLFNY------SYNIVFRAGYLA-LYG--NEPAKNKGSkekAKEFDR- 224
Cdd:PTZ00404  145 DQVDVLIESMKKieSSGEtfepryylTKFTMSAMFKYifnediSFDEDIHNGKLAeLMGpmEQVFKDLGS---GSLFDVi 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 225 KHSDELFYEFRKY-DQLFPRLAyavlppkdKIEAERLKRlfwNMLSIKKTLQKENISGWISEqHQQRAEHGMPEHMQDRF 303
Cdd:PTZ00404  222 EITQPLYYQYLEHtDKNFKKIK--------KFIKEKYHE---HLKTIDPEVPRDLLDLLIKE-YGTNTDDDILSILATIL 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 304 MFMLlwASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLKetgqevkpGGPLINLTRDMllKTPVMDSALEETLRLTA 383
Cdd:PTZ00404  290 DFFL--AGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVN--------GRNKVLLSDRQ--STPYTVAIIKETLRYKP 357
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 384 APVLiravkqnmKVKMASGNDFSLRGGDRI-----AFFPYIAVQMDPGVHPEPEKYKYNRFLNedgTKKTDFFkngkkvk 458
Cdd:PTZ00404  358 VSPF--------GLPRSTSNDIIIGGGHFIpkdaqILINYYSLGRNEKYFENPEQFDPSRFLN---PDSNDAF------- 419
                         490       500
                  ....*....|....*....|...
gi 1050373214 459 yylMPWGAGSSICPGRFFAANEL 481
Cdd:PTZ00404  420 ---MPFSIGPRNCVGQQFAQDEL 439
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
325-495 3.60e-06

cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 49.57  E-value: 3.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 325 YLLKHPEAMQA-VREEVEAVLKETGqevkpggpliNLTRDMLLKTPVMDSALEETLRLtAAPVLI---RAvKQNMKVKMA 400
Cdd:cd11071   251 RLGLAGEELHArLAEEIRSALGSEG----------GLTLAALEKMPLLKSVVYETLRL-HPPVPLqygRA-RKDFVIESH 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 401 SGNdFSLRGGDRIafFPYIA-VQMDPGVHPEPEKYKYNRFLNEDGtkktdffkngkKVKYYLMpWGAG---------SSI 470
Cdd:cd11071   319 DAS-YKIKKGELL--VGYQPlATRDPKVFDNPDEFVPDRFMGEEG-----------KLLKHLI-WSNGpeteeptpdNKQ 383
                         170       180
                  ....*....|....*....|....*.
gi 1050373214 471 CPGRFFAANELKQFV-FLMLTYFEFQ 495
Cdd:cd11071   384 CPGKDLVVLLARLFVaELFLRYDTFT 409
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
323-503 4.84e-06

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 48.99  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 323 LLYLLKHPEAMQAVREEVEAVLketGQEVKPggplinlTRDMLLKTPVMDSALEETLRLTAA-PV-LIRAVKQNMKVKma 400
Cdd:cd20669   250 FLILMKYPKVAARVQEEIDRVV---GRNRLP-------TLEDRARMPYTDAVIHEIQRFADIiPMsLPHAVTRDTNFR-- 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 401 sgNDFSLRGGDRIAFFpyIAVQMDPGVHPEPEKYKYNRFLNEDGT-KKTDFFkngkkvkyylMPWGAGSSICPGRFFAAN 479
Cdd:cd20669   318 --GFLIPKGTDVIPLL--NSVHYDPTQFKDPQEFNPEHFLDDNGSfKKNDAF----------MPFSAGKRICLGESLARM 383
                         170       180
                  ....*....|....*....|....
gi 1050373214 480 ELKQFVFLMLTYFEFQLVNPNEEI 503
Cdd:cd20669   384 ELFLYLTAILQNFSLQPLGAPEDI 407
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
307-502 5.02e-06

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: 49.03  E-value: 5.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 307 LLWASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketgqevkpGG--PLINLTRDMllktPVMDSALEETLRLT-A 383
Cdd:cd20664   233 LFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVI---------GSrqPQVEHRKNM----PYTDAVIHEIQRFAnI 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 384 APvliravkqnMKVKMASGNDFSLRG-----GDRIafFPYI-AVQMDPGVHPEPEKYKYNRFLNEDGtkktDFFKNGKkv 457
Cdd:cd20664   300 VP---------MNLPHATTRDVTFRGyfipkGTYV--IPLLtSVLQDKTEWEKPEEFNPEHFLDSQG----KFVKRDA-- 362
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1050373214 458 kyyLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVNPNEE 502
Cdd:cd20664   363 ---FMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPPGVSE 404
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
321-492 6.38e-06

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


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 48.56  E-value: 6.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKET-GQEVKpggplinltrdMLLKTPVMDSALEETLRLTAAPV-LIRAVKQNMKVK 398
Cdd:cd20643   256 WTLYELARNPNVQEMLRAEVLAARQEAqGDMVK-----------MLKSVPLLKAAIKETLRLHPVAVsLQRYITEDLVLQ 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 399 masgnDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTkktdFFKNgkkvkyylMPWGAGSSICPGRFFAA 478
Cdd:cd20643   325 -----NYHIPAGTLVQVGLY-AMGRDPTVFPKPEKYDPERWLSKDIT----HFRN--------LGFGFGPRQCLGRRIAE 386
                         170
                  ....*....|....
gi 1050373214 479 NELKQFVFLMLTYF 492
Cdd:cd20643   387 TEMQLFLIHMLENF 400
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
24-473 6.86e-06

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 48.53  E-value: 6.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214  24 LQIILALLVSfIGGLYLLGIFRKRRSDEPPLDKGsIPWLGYALDFRK-NTLTFLQKMHKKHGDIFTVQIAGYYFTFVmdp 102
Cdd:PLN03234    3 LFLIIAALVA-AAAFFFLRSTTKKSLRLPPGPKG-LPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVI--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 103 lSFGPIIKEPKANVDFEEFATELVL---------RVFGYQSFTHDHKMLEKSSTKHMTGDGLVVMTHAMMEN-LQNLM-- 170
Cdd:PLN03234   78 -SSAELAKELLKTQDLNFTARPLLKgqqtmsyqgRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEeCQRMMdk 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 171 VHNIGSEKGEREWhQDGLFNYSYNIVFRAGYLALYgnepakNKGSKEKAKEFDRKHSDELFYEFRKYDQLFPRLAYAvlp 250
Cdd:PLN03234  157 IYKAADQSGTVDL-SELLLSFTNCVVCRQAFGKRY------NEYGTEMKRFIDILYETQALLGTLFFSDLFPYFGFL--- 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 251 pkDKIE--AERLKRLFWNMLSIKKTLQKENISGWISEQHQQ-------RAEHGMP-----EHMQDRFMFMLLWASQGNTG 316
Cdd:PLN03234  227 --DNLTglSARLKKAFKELDTYLQELLDETLDPNRPKQETEsfidllmQIYKDQPfsikfTHENVKAMILDIVVPGTDTA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 317 PASF-WFLLYLLKHPEAMQAVREEVEAVLKETGQevkpggplinLTRDMLLKTPVMDSALEETLRLTAA-PVLIRavKQN 394
Cdd:PLN03234  305 AAVVvWAMTYLIKYPEAMKKAQDEVRNVIGDKGY----------VSEEDIPNLPYLKAVIKESLRLEPViPILLH--RET 372
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 395 MKVKMASGNDFSLRGGDRIAFFpyiAVQMDPGVHPE-PEKYKYNRFLNEDgtKKTDFfkngKKVKYYLMPWGAGSSICPG 473
Cdd:PLN03234  373 IADAKIGGYDIPAKTIIQVNAW---AVSRDTAAWGDnPNEFIPERFMKEH--KGVDF----KGQDFELLPFGSGRRMCPA 443
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
322-495 6.99e-06

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 48.40  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLL-KHPEAMQAVREEVEAVLketGQEVKPGGPLINLTRDMLLKTPVMDSALEETLRLTAAPVLIRAVKQNMKVKMA 400
Cdd:cd11051   207 WAFYLLsKHPEVLAKVRAEHDEVF---GPDPSAAAELLREGPELLNQLPYTTAVIKETLRLFPPAGTARRGPPGVGLTDR 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 401 SGNDFSLRGgdriaFFPYI---AVQMDPGVHPEPEKYKYNRFLNEDGTKKTDffkngkkVKYYLMPWGAGSSICPGRFFA 477
Cdd:cd11051   284 DGKEYPTDG-----CIVYVchhAIHRDPEYWPRPDEFIPERWLVDEGHELYP-------PKSAWRPFERGPRNCIGQELA 351
                         170
                  ....*....|....*...
gi 1050373214 478 ANELKQFVFLMLTYFEFQ 495
Cdd:cd11051   352 MLELKIILAMTVRRFDFE 369
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
269-498 8.48e-06

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 48.27  E-value: 8.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 269 SIKKTLQKENISGWISEQHQQRAEH----GMPEHMQD--RFMFMLLWASQGNTGPASFWFLLYLLKHPEAMQAVREEvea 342
Cdd:cd20638   194 NIRAKIQREDTEQQCKDALQLLIEHsrrnGEPLNLQAlkESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKE--- 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 343 vLKETGQEVKPGGPLINLTRDMLLKTPVMDSALEETLRLTaAPVliravkqnmkvkmasgndfslRGGDRIAF--FPYIA 420
Cdd:cd20638   271 -LQEKGLLSTKPNENKELSMEVLEQLKYTGCVIKETLRLS-PPV---------------------PGGFRVALktFELNG 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 421 VQMDPG---------------VHPEPEKYKYNRFLN---EDGTkktdffkngkkvKYYLMPWGAGSSICPGRFFAANELK 482
Cdd:cd20638   328 YQIPKGwnviysicdthdvadIFPNKDEFNPDRFMSplpEDSS------------RFSFIPFGGGSRSCVGKEFAKVLLK 395
                         250
                  ....*....|....*.
gi 1050373214 483 QFVFLMLTYFEFQLVN 498
Cdd:cd20638   396 IFTVELARHCDWQLLN 411
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
321-473 1.06e-05

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketgqevKPGGPlinLTRDMLLKTPVMDSALEETLRL-TAAPVLIravkQNMKVKM 399
Cdd:PLN02394  315 WGIAELVNHPEIQKKLRDELDTVL-------GPGNQ---VTEPDTHKLPYLQAVVKETLRLhMAIPLLV----PHMNLED 380
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1050373214 400 ASGNDFSLRGGDRI---AFFpyiaVQMDPGVHPEPEKYKYNRFLNEDGTKKTdffkNGKKVKYylMPWGAGSSICPG 473
Cdd:PLN02394  381 AKLGGYDIPAESKIlvnAWW----LANNPELWKNPEEFRPERFLEEEAKVEA----NGNDFRF--LPFGVGRRSCPG 447
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
321-495 1.18e-05

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 47.83  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKETGQevkpggPLINLTRDMllktPVMDSALEETLRLTaaPVliraVKQNMKVKma 400
Cdd:cd20648   256 WSLYELSRHPDVQTALHREITAALKDNSV------PSAADVARM----PLLKAVVKEVLRLY--PV----IPGNARVI-- 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 401 sgNDFSLRGGDRIafFP--------YIAVQMDPGVHPEPEKYKYNRFLNEDGTKKtdffkngkkvKYYLMPWGAGSSICP 472
Cdd:cd20648   318 --PDRDIQVGEYI--IPkktlitlcHYATSRDENQFPDPNSFRPERWLGKGDTHH----------PYASLPFGFGKRSCI 383
                         170       180
                  ....*....|....*....|...
gi 1050373214 473 GRFFAANELKQFVFLMLTYFEFQ 495
Cdd:cd20648   384 GRRIAELEVYLALARILTHFEVR 406
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
321-473 2.16e-05

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: 46.78  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketGQEVKpggplinLTRDMLLKTPVMDSALEETLRL-TAAPVLIRavKQNMKVKM 399
Cdd:cd20618   251 WAMAELLRHPEVMRKAQEELDSVV---GRERL-------VEESDLPKLPYLQAVVKETLRLhPPGPLLLP--HESTEDCK 318
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1050373214 400 ASGNDFSlrGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNE--DGTKKTDFfkngkkvkyYLMPWGAGSSICPG 473
Cdd:cd20618   319 VAGYDIP--AGTRVLVNVW-AIGRDPKVWEDPLEFKPERFLESdiDDVKGQDF---------ELLPFGSGRRMCPG 382
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
321-497 2.35e-05

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 47.08  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPGGP-LIN---------LTRDMLLKTPVMDSALEETLRLTAApvlira 390
Cdd:PLN03195  314 WFVYMIMMNPHVAEKLYSELKALEKERAKEEDPEDSqSFNqrvtqfaglLTYDSLGKLQYLHAVITETLRLYPA------ 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 391 VKQNMKVKMASG---NDFSLRGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLnEDGtkktdFFKNGKKVKYylMPWGAG 467
Cdd:PLN03195  388 VPQDPKGILEDDvlpDGTKVKAGGMVTYVPYSMGRMEYNWGPDAASFKPERWI-KDG-----VFQNASPFKF--TAFQAG 459
                         170       180       190
                  ....*....|....*....|....*....|
gi 1050373214 468 SSICPGRFFAANELKQFVFLMLTYFEFQLV 497
Cdd:PLN03195  460 PRICLGKDSAYLQMKMALALLCRFFKFQLV 489
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
307-473 2.45e-05

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 46.71  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 307 LLW----ASQGNTGPASFWFLLYLLKHPEAMQAVREEVEAVLketGQEVKpggplinLTRDMLLKTPVMDSALEETLRLT 382
Cdd:cd20656   234 LLWdmitAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVV---GSDRV-------MTEADFPQLPYLQCVVKEALRLH 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 383 AAPVLIRAVKQNMKVKMASgndFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDgtkkTDFfkngKKVKYYLM 462
Cdd:cd20656   304 PPTPLMLPHKASENVKIGG---YDIPKGANVHVNVW-AIARDPAVWKNPLEFRPERFLEED----VDI----KGHDFRLL 371
                         170
                  ....*....|.
gi 1050373214 463 PWGAGSSICPG 473
Cdd:cd20656   372 PFGAGRRVCPG 382
PLN02738 PLN02738
carotene beta-ring hydroxylase
297-496 2.58e-05

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 46.83  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 297 EHMQDRFMFMLLWASQgnTGPASFWFLLYLL-KHPEAMQAVREEVEAVLKEtgqevkpGGPLINLTRDMLLKTPVMDsal 375
Cdd:PLN02738  390 KQLRDDLMTMLIAGHE--TSAAVLTWTFYLLsKEPSVVAKLQEEVDSVLGD-------RFPTIEDMKKLKYTTRVIN--- 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 376 eETLRL-TAAPVLIRAVKQNmkvKMASGndFSLRGGDRIaFFPYIAVQMDPGVHPEPEKYKYNRFlNEDGTKKTDFFKNg 454
Cdd:PLN02738  458 -ESLRLyPQPPVLIRRSLEN---DMLGG--YPIKRGEDI-FISVWNLHRSPKHWDDAEKFNPERW-PLDGPNPNETNQN- 528
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1050373214 455 kkvkYYLMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQL 496
Cdd:PLN02738  529 ----FSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQL 566
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
325-502 2.99e-05

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 46.42  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 325 YLLKHPEAMQAVREEVEAVLKETGQevkpggplINLTRdmLLKTPVMDSALEETLRLTaAPV---LIRAVkqnmkvkmas 401
Cdd:cd11058   243 YLLKNPEVLRKLVDEIRSAFSSEDD--------ITLDS--LAQLPYLNAVIQEALRLY-PPVpagLPRVV---------- 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 402 gndfsLRGGDRIAFFpYIAVQMDPGVHP-----------EPEKYKYNRFLNEDGtkktdfFKNGKKVKYYLMPWGAGSSI 470
Cdd:cd11058   302 -----PAGGATIDGQ-FVPGGTSVSVSQwaayrsprnfhDPDEFIPERWLGDPR------FEFDNDKKEAFQPFSVGPRN 369
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1050373214 471 CPGRFFAANELKQFVFLMLTYFEFQLVNPNEE 502
Cdd:cd11058   370 CIGKNLAYAEMRLILAKLLWNFDLELDPESED 401
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
321-474 1.19e-04

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 44.63  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLketgqevkpgGPLINLTRDMLLKTPVMDSALEETLRL-TAAPVLIRAvkqnmkvKM 399
Cdd:cd11076   246 WIMARMVLHPDIQSKAQAEIDAAV----------GGSRRVADSDVAKLPYLQAVVKETLRLhPPGPLLSWA-------RL 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 ASgNDFSLrGGDRI-----AFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKNGKKvkyyLMPWGAGSSICPGR 474
Cdd:cd11076   309 AI-HDVTV-GGHVVpagttAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGADVSVLGSDLR----LAPFGAGRRVCPGK 382
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
322-508 1.52e-04

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 44.30  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLLKHPEAMQAVREEVEAVLketgqevkpGGPLINLTRDMLLKTPVMDSALEETLRLTaAPVliravkqNMKVKMAS 401
Cdd:PLN02426  316 FFWLLSKHPEVASAIREEADRVM---------GPNQEAASFEEMKEMHYLHAALYESMRLF-PPV-------QFDSKFAA 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 402 GNDF-----SLRGGDRIAFFPYIAVQMDPGVHPEPEKYKYNRFLNeDGTkktdfFKNGKKVKYYLmpWGAGSSICPGRFF 476
Cdd:PLN02426  379 EDDVlpdgtFVAKGTRVTYHPYAMGRMERIWGPDCLEFKPERWLK-NGV-----FVPENPFKYPV--FQAGLRVCLGKEM 450
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1050373214 477 AANELKQFVFLMLTYFEFQLVNPNEEIPSIDP 508
Cdd:PLN02426  451 ALMEMKSVAVAVVRRFDIEVVGRSNRAPRFAP 482
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
322-504 3.04e-04

cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 43.29  E-value: 3.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLLK-HPEAMQAVREEVEaVLKETGQEVKpggplINLTRDMllktPVMDSALEETLRL-TAAPVLIRAVKQNMKVkm 399
Cdd:cd20649   283 FATYLLAtHPECQKKLLREVD-EFFSKHEMVD-----YANVQEL----PYLDMVIAETLRMyPPAFRFAREAAEDCVV-- 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 400 asgNDFSLRGGDRIAFfPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFkngkkvkyYLmPWGAGSSICPGRFFAAN 479
Cdd:cd20649   351 ---LGQRIPAGAVLEI-PVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFV--------YL-PFGAGPRSCIGMRLALL 417
                         170       180
                  ....*....|....*....|....*
gi 1050373214 480 ELKQFVFLMLTYFEFQLVnPNEEIP 504
Cdd:cd20649   418 EIKVTLLHILRRFRFQAC-PETEIP 441
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
321-496 3.21e-04

cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; Cytochrome P450 27A1 (CYP27A1, EC 1.14.15.15) is also called CYP27, cholestanetriol 26-monooxygenase, sterol 26-hydroxylase, 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase, cytochrome P-450C27/25, sterol 27-hydroxylase, or vitamin D(3) 25-hydroxylase. It catalyzes the first step in the oxidation of the side chain of sterol intermediates, the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, and the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. It also hydroxylates vitamin D3 at the 25-position, as well as cholesterol at positions 24 and 25. CYP27A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 43.11  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKEtgqEVKPggplinlTRDMLLKTPVMDSALEETLRLTaaPVliraVKQNMKV--- 397
Cdd:cd20646   255 WALYHLARDPEIQERLYQEVISVCPG---DRIP-------TAEDIAKMPLLKAVIKETLRLY--PV----VPGNARVive 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 398 KMASGNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKngkkvkyylMPWGAGSSICPGRFFA 477
Cdd:cd20646   319 KEVVVGDYLFPKNTLFHLCHY-AVSHDETNFPEPERFKPERWLRDGGLKHHPFGS---------IPFGYGVRACVGRRIA 388
                         170       180
                  ....*....|....*....|.
gi 1050373214 478 anELKQFVFL--MLTYFEFQL 496
Cdd:cd20646   389 --ELEMYLALsrLIKRFEVRP 407
PLN02774 PLN02774
brassinosteroid-6-oxidase
325-501 3.31e-04

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 43.23  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 325 YLLKHPEAMQAVREEVEAVLKETgqevKPGGPL-------INLTRDMLLktpvmdsaleETLRL-TAAPVLIRAVKQNMK 396
Cdd:PLN02774  290 YLHDHPKALQELRKEHLAIRERK----RPEDPIdwndyksMRFTRAVIF----------ETSRLaTIVNGVLRKTTQDME 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 397 VkmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLnedgtkktdffKNGKKVKYYLMPWGAGSSICPGRFF 476
Cdd:PLN02774  356 L-----NGYVIPKGWRIYVYTR-EINYDPFLYPDPMTFNPWRWL-----------DKSLESHNYFFLFGGGTRLCPGKEL 418
                         170       180
                  ....*....|....*....|....*
gi 1050373214 477 AANELKQFVFLMLTYFEFQLVNPNE 501
Cdd:PLN02774  419 GIVEISTFLHYFVTRYRWEEVGGDK 443
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
310-496 4.08e-04

cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Arabidopsis thaliana CYP709B3 is involved in abscisic acid (ABA) and salt stress response. CYP709 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 42.82  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 310 ASQGNTGPASFWFLLYLLKHPEAMQAVREEveaVLKETGQEVKPGGplinltrDMLLKTPVMDSALEETLRLTAAPVLI- 388
Cdd:cd20641   246 AGHETTSNLLTWTMFLLSLHPDWQEKLREE---VFRECGKDKIPDA-------DTLSKLKLMNMVLMETLRLYGPVINIa 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 389 RAVKQNMKVKmasgnDFSLRGGDRIAfFPYIAVQMDPGV-HPEPEKYKYNRFLNEDGTKKTDffkngkkvKYYLMPWGAG 467
Cdd:cd20641   316 RRASEDMKLG-----GLEIPKGTTII-IPIAKLHRDKEVwGSDADEFNPLRFANGVSRAATH--------PNALLSFSLG 381
                         170       180
                  ....*....|....*....|....*....
gi 1050373214 468 SSICPGRFFAANELKQFVFLMLTYFEFQL 496
Cdd:cd20641   382 PRACIGQNFAMIEAKTVLAMILQRFSFSL 410
PLN02648 PLN02648
allene oxide synthase
322-446 6.94e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 42.23  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLYLLKH----PEAMQA-VREEVEAVLKETGQEVkpggplinlTRDMLLKTPVMDSALEETLRLTAaPVLI---RAvKQ 393
Cdd:PLN02648  291 FFPALLKWvgraGEELQArLAEEVRSAVKAGGGGV---------TFAALEKMPLVKSVVYEALRIEP-PVPFqygRA-RE 359
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1050373214 394 NMKVKmASGNDFSLRGGDRIAFFPYIAVQmDPGVHPEPEKYKYNRFLNEDGTK 446
Cdd:PLN02648  360 DFVIE-SHDAAFEIKKGEMLFGYQPLVTR-DPKVFDRPEEFVPDRFMGEEGEK 410
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
420-510 1.04e-03

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 41.53  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 420 AVQMDPGVHPEPEKYKYNRFLNEDGTKKTDFFKngkkvkyylMPWGAGSSICPGRFFAANELKQFVFLMLTYFEFQLVnP 499
Cdd:cd11066   339 AANHDPEHFGDPDEFIPERWLDASGDLIPGPPH---------FSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPK-D 408
                          90
                  ....*....|.
gi 1050373214 500 NEEIPSIDPNR 510
Cdd:cd11066   409 EEEPMELDPFE 419
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
377-474 1.42e-03

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 41.17  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 377 ETLRLT-AAPVLIRAVKQNMKVKMASGNDFSLRGGDRIaFFPYIAVQMDPGVHPEPEKYKYNRFLNEdgtkktdffkngk 455
Cdd:cd20612   246 EALRLNpIAPGLYRRATTDTTVADGGGRTVSIKAGDRV-FVSLASAMRDPRAFPDPERFRLDRPLES------------- 311
                          90
                  ....*....|....*....
gi 1050373214 456 kvkyYLMpWGAGSSICPGR 474
Cdd:cd20612   312 ----YIH-FGHGPHQCLGE 325
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
322-522 2.12e-03

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 40.53  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 322 FLLyLLKHPEAMQAVREEVEAVLketGQEVKPggplinlTRDMLLKTPVMDSALEETLRLT-AAPvliravkqnMKVKMA 400
Cdd:cd20672   250 FLL-MLKYPHVAEKVQKEIDQVI---GSHRLP-------TLDDRAKMPYTDAVIHEIQRFSdLIP---------IGVPHR 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 401 SGNDFSLRG---GDRIAFFPYIAVQM-DPGVHPEPEKYKYNRFLNEDGT-KKTDFFkngkkvkyylMPWGAGSSICPGRF 475
Cdd:cd20672   310 VTKDTLFRGyllPKNTEVYPILSSALhDPQYFEQPDTFNPDHFLDANGAlKKSEAF----------MPFSTGKRICLGEG 379
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1050373214 476 FAANELkqFVFLMLTYFEFQLVNP--NEEIpSIDPNRWGFGVMQPIHDI 522
Cdd:cd20672   380 IARNEL--FLFFTTILQNFSVASPvaPEDI-DLTPKESGVGKIPPTYQI 425
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
321-473 3.69e-03

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 39.84  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVLKETGQEVKPGGPlinltrdmllKTPVMDSALEETLRL-TAAPV-LIRAVKQNMKVk 398
Cdd:PLN00110  311 WSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLP----------KLPYLQAICKESFRKhPSTPLnLPRVSTQACEV- 379
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1050373214 399 masgNDFSLRGGDRIaFFPYIAVQMDPGVHPEPEKYKYNRFLNEDGTKktdffKNGKKVKYYLMPWGAGSSICPG 473
Cdd:PLN00110  380 ----NGYYIPKNTRL-SVNIWAIGRDPDVWENPEEFRPERFLSEKNAK-----IDPRGNDFELIPFGAGRRICAG 444
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
323-495 3.71e-03

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: 39.89  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 323 LLYLLKHPEAMQAVREEVEAVLKETGQEVkpggplinlTRDMLLKTPVMDSALEETLRL-TAAPVLIRAVKQNMKVkmas 401
Cdd:cd11057   251 LLLLAMHPEVQEKVYEEIMEVFPDDGQFI---------TYEDLQQLVYLEMVLKETMRLfPVGPLVGRETTADIQL---- 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 402 GNDFSLRGGDRIAFFPYiAVQMDPGVH-PEPEKYKYNRFLNEDGTKKTdffkngkkvKYYLMPWGAGSSICPGRFFAANE 480
Cdd:cd11057   318 SNGVVIPKGTTIVIDIF-NMHRRKDIWgPDADQFDPDNFLPERSAQRH---------PYAFIPFSAGPRNCIGWRYAMIS 387
                         170
                  ....*....|....*
gi 1050373214 481 LKQFVFLMLTYFEFQ 495
Cdd:cd11057   388 MKIMLAKILRNYRLK 402
PLN02183 PLN02183
ferulate 5-hydroxylase
321-473 4.51e-03

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 39.83  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 321 WFLLYLLKHPEAMQAVREEVEAVlketgqevkpggplINLTRDM----LLKTPVMDSALEETLRL-TAAPVLIRAVKQNM 395
Cdd:PLN02183  326 WAMAELMKSPEDLKRVQQELADV--------------VGLNRRVeesdLEKLTYLKCTLKETLRLhPPIPLLLHETAEDA 391
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1050373214 396 KVkmasgNDFSLRGGDRIAFFPYiAVQMDPGVHPEPEKYKYNRFLNEDGtkkTDFfkngKKVKYYLMPWGAGSSICPG 473
Cdd:PLN02183  392 EV-----AGYFIPKRSRVMINAW-AIGRDKNSWEDPDTFKPSRFLKPGV---PDF----KGSHFEFIPFGSGRRSCPG 456
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
296-480 5.66e-03

cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 39.08  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 296 PEHMQDRFMFMLLwASQGNTgpASF--WFLLYLLKHPEAMQAVREEVEAVlketgqevkpGGPLINLTRDMLLKTPVMDS 373
Cdd:cd11063   214 PKELRDQLLNILL-AGRDTT--ASLlsFLFYELARHPEVWAKLREEVLSL----------FGPEPTPTYEDLKNMKYLRA 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1050373214 374 ALEETLRLtaAPVliraVKQNMKVKM----------ASGND--FsLRGGDRIAFFPYiAVQMDPGVH-PEPEKYKYNRFL 440
Cdd:cd11063   281 VINETLRL--YPP----VPLNSRVAVrdttlprgggPDGKSpiF-VPKGTRVLYSVY-AMHRRKDIWgPDAEEFRPERWE 352
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1050373214 441 nedgtkktdffkNGKKVKYYLMPWGAGSSICPGRFFAANE 480
Cdd:cd11063   353 ------------DLKRPGWEYLPFNGGPRICLGQQFALTE 380
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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