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Conserved domains on  [gi|1109516678|ref|NP_001334179|]
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aromatase [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
72-485 0e+00

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


:

Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 889.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  72 SACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKA 151
Cdd:cd20616     1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 152 LSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKP 231
Cdd:cd20616    81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 DIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTM 311
Cdd:cd20616   161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 312 SVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKG 391
Cdd:cd20616   241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 392 TNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESI 471
Cdd:cd20616   321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                         410
                  ....*....|....
gi 1109516678 472 QKIHDLSLHPDETK 485
Cdd:cd20616   401 QKTNDLSLHPDETQ 414
 
Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
72-485 0e+00

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 889.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  72 SACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKA 151
Cdd:cd20616     1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 152 LSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKP 231
Cdd:cd20616    81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 DIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTM 311
Cdd:cd20616   161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 312 SVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKG 391
Cdd:cd20616   241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 392 TNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESI 471
Cdd:cd20616   321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                         410
                  ....*....|....
gi 1109516678 472 QKIHDLSLHPDETK 485
Cdd:cd20616   401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
48-485 1.41e-115

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: 348.50  E-value: 1.41e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  48 PGPGYCMGIGPLISHgrflWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHY--SSRFGSKLGLQCI 125
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 126 GMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLR 205
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 206 IPLD------ESAIVVKIQGYFD-----AWQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKleE 274
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 275 CMDFATELILA---EKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDI 350
Cdd:pfam00067 238 PRDFLDALLLAkeeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 351 QKLKVMENFIYESMRYQPVVD-LVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENF----AKNVPY 424
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109516678 425 RYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETK 485
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYK 458
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-459 9.96e-40

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: 148.12  E-value: 9.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  79 RVYGEFMRVWISGEETLIISKSSSMFHIMKHN-HYSSRFGSKLGLQCIGMHEKGIIFNNnPELWKTTRPFFMKALSGPGL 157
Cdd:COG2124    29 REYGPVFRVRLPGGGAWLVTRYEDVREVLRDPrTFSSDGGLPEVLRPLPLLGDSLLTLD-GPEHTRLRRLVQPAFTPRRV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 158 VRMVTVCAESLKTHLDRLEEvtneSGYVDVLTLLRRVMLDTSNTLFLRIPLDESAivvKIQGYFDAWQALLIKPDIffki 237
Cdd:COG2124   108 AALRPRIREIADELLDRLAA----RGPVDLVEEFARPLPVIVICELLGVPEEDRD---RLRRWSDALLDALGPLPP---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 238 sWLYKKYEKSVKDLKDAIEVLIAEKRRRISTeekleecmDFATELILAEKRGD-LTRENV-NQCILeMLIAAPDTMSVSL 315
Cdd:COG2124   177 -ERRRRARRARAELDAYLRELIAERRAEPGD--------DLLSALLAARDDGErLSDEELrDELLL-LLLAGHETTANAL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEiqtvigerdikiddiqkLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNII 395
Cdd:COG2124   247 AWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVL 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109516678 396 LNIGRMHRLE-FFPKPNEFTLEnfakNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:COG2124   310 LSLAAANRDPrVFPDPDRFDPD----RPPNAHL-PFGGGPHRCLGAALARLEARIALATLLRRFP 369
PLN02738 PLN02738
carotene beta-ring hydroxylase
80-465 4.07e-28

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 118.09  E-value: 4.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  80 VYGEFMRVWISGEETLIISKSSSMFHIMKHNH--YSSRFGSKLGLQCIGmheKGIIFNNNpELWKTTRPFFMKALSGPGL 157
Cdd:PLN02738  163 TYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSkaYSKGILAEILEFVMG---KGLIPADG-EIWRVRRRAIVPALHQKYV 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 158 VRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLD----ESAIVVKIQGYFDAWQALLIKP-- 231
Cdd:PLN02738  239 AAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDslsnDTGIVEAVYTVLREAEDRSVSPip 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 ----DIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRIStEEKL---EECMDFATELIL---AEKRGDLTRENVNQCIL 301
Cdd:PLN02738  319 vweiPIWKDISPRQRKVAEALKLINDTLDDLIAICKRMVE-EEELqfhEEYMNERDPSILhflLASGDDVSSKQLRDDLM 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 EMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDD 381
Cdd:PLN02738  398 TMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLEND 477
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 382 VIDGYPVKKGTNIILNIGRMHR-------LEFF---------PKPNEfTLENFAknvpyryFQPFGFGPRGCAGKYIAMV 445
Cdd:PLN02738  478 MLGGYPIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNFS-------YLPFGGGPRKCVGDMFASF 549
                         410       420
                  ....*....|....*....|
gi 1109516678 446 MMKAILVTLLRRFHVKTLQG 465
Cdd:PLN02738  550 ENVVATAMLVRRFDFQLAPG 569
 
Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
72-485 0e+00

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 889.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  72 SACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKA 151
Cdd:cd20616     1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 152 LSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKP 231
Cdd:cd20616    81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 DIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTM 311
Cdd:cd20616   161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 312 SVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKG 391
Cdd:cd20616   241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 392 TNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESI 471
Cdd:cd20616   321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                         410
                  ....*....|....
gi 1109516678 472 QKIHDLSLHPDETK 485
Cdd:cd20616   401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
48-485 1.41e-115

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: 348.50  E-value: 1.41e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  48 PGPGYCMGIGPLISHgrflWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHY--SSRFGSKLGLQCI 125
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 126 GMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLR 205
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 206 IPLD------ESAIVVKIQGYFD-----AWQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKleE 274
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 275 CMDFATELILA---EKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDI 350
Cdd:pfam00067 238 PRDFLDALLLAkeeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 351 QKLKVMENFIYESMRYQPVVD-LVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENF----AKNVPY 424
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109516678 425 RYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETK 485
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYK 458
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
82-482 2.07e-67

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


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 222.00  E-value: 2.07e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  82 GEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQcIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMV 161
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPA-LGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 162 TVCAESLKTHLDRLEEvtNESGYVDVLTLLRRVMLDT-SNTLFLRiplDESAIVVKIQGYFDAWQALLIKPDIFFKISWL 240
Cdd:cd00302    80 PVIREIARELLDRLAA--GGEVGDDVADLAQPLALDViARLLGGP---DLGEDLEELAELLEALLKLLGPRLLRPLPSPR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 241 YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEEcmdfateLILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLF 320
Cdd:cd00302   155 LRRLRRARARLRDYLEELIARRRAEPADDLDLLL-------LADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 321 LIAKHPNVEEAIIKEIQTVIGERDIkiDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGR 400
Cdd:cd00302   228 LLARHPEVQERLRAEIDAVLGDGTP--EDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 401 MHRLE-FFPKPNEFTLENF---AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVEsiQKIHD 476
Cdd:cd00302   306 AHRDPeVFPDPDEFDPERFlpeREEPRYAHL-PFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELE--WRPSL 382

                  ....*.
gi 1109516678 477 LSLHPD 482
Cdd:cd00302   383 GTLGPA 388
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
82-485 5.30e-48

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: 171.24  E-value: 5.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  82 GEFMRVWISGEETLIISKSSSM--FHIMKHNHYSSRFGSKLGLqcIGMHEKGIIFNNNpELWKTTRPFFMKALSGPGLVR 159
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIkeAFVKNGDNFSDRPLLPSFE--IISGGKGILFSNG-DYWKELRRFALSSLTKTKLKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 160 --------MVTVCAESLKTHLDRLEEVtNESGYVDVLTLlrRVMLdtsNTLF-LRIPLDESAIVVKIQGYFDA--WQALL 228
Cdd:cd20617    78 kmeelieeEVNKLIESLKKHSKSGEPF-DPRPYFKKFVL--NIIN---QFLFgKRFPDEDDGEFLKLVKPIEEifKELGS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 229 IKPDIFFKI-----SWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEklEECMDFAtELILAEKRGD---LTRENVNQCI 300
Cdd:cd20617   152 GNPSDFIPIllpfyFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNN--PRDLIDD-ELLLLLKEGDsglFDDDSIISTC 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 301 LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKAL 378
Cdd:cd20617   229 LDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGnDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLgLPRVTT 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 379 EDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF---AKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTL 454
Cdd:cd20617   309 EDTEIGGYFIPKGTQIIINIYSLHRDEkYFEDPEEFNPERFlenDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANL 388
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1109516678 455 LRRFHVKTLQGQcvESIQKIHD-LSLHPDETK 485
Cdd:cd20617   389 LLNFKFKSSDGL--PIDEKEVFgLTLKPKPFK 418
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
82-483 2.92e-46

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: 166.54  E-value: 2.92e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  82 GEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQC-IGmheKGIIFNNnPELWKTTRpffmKALSgPG---- 156
Cdd:cd20628     1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPwLG---DGLLTST-GEKWRKRR----KLLT-PAfhfk 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 157 -LVRMVTVCAESLKTHLDRLEEVTNEsGYVDVLTLLRR----VMLDTSntlfLRIPLDesAIVVKIQGYFDAWQAL---- 227
Cdd:cd20628    72 iLESFVEVFNENSKILVEKLKKKAGG-GEFDIFPYISLctldIICETA----MGVKLN--AQSNEDSEYVKAVKRIleii 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 228 -------LIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRR-RISTEEKLEECMDFATE--------LILAEKRGD- 290
Cdd:cd20628   145 lkrifspWLRFDFIFRLTSLGKEQRKALKVLHDFTNKVIKERREeLKAEKRNSEEDDEFGKKkrkafldlLLEAHEDGGp 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 291 LTRENvnqcILE----MLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE--RDIKIDDIQKLKVMENFIYESM 364
Cdd:cd20628   225 LTDED----IREevdtFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVIKETL 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 365 RYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRL-EFFPKPNEF-----TLENFAKNVPYRYFqPFGFGPRGCA 438
Cdd:cd20628   301 RLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNpEYFPDPEKFdpdrfLPENSAKRHPYAYI-PFSAGPRNCI 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1109516678 439 G-KYiAMVMMKAILVTLLRRFHVKTLQGQcvESIQKIHDLSLHPDE 483
Cdd:cd20628   380 GqKF-AMLEMKTLLAKILRNFRVLPVPPG--EDLKLIAEIVLRSKN 422
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
128-462 4.43e-45

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: 163.47  E-value: 4.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 128 HEKGIIFNNNPElWKTTRpffmKALSgPGLVRMVTVcaeslKTHLDRLEEVTNE-------------SGYVDVLTLLRR- 193
Cdd:cd11054    54 KPLGLLNSNGEE-WHRLR----SAVQ-KPLLRPKSV-----ASYLPAINEVADDfverirrlrdedgEEVPDLEDELYKw 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 194 -------VMLDTSNTLFLRIPLDESAIVVK-IQGYFDAWQALLIKPDIFFKISW-LYKKYEKSVKDLKDAIEVLIAEKRR 264
Cdd:cd11054   123 slesigtVLFGKRLGCLDDNPDSDAQKLIEaVKDIFESSAKLMFGPPLWKYFPTpAWKKFVKAWDTIFDIASKYVDEALE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 265 RI-STEEKLEECMDFATELIlaeKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGER 343
Cdd:cd11054   203 ELkKKDEEDEEEDSLLEYLL---SKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDG 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 344 D-IKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLE----- 416
Cdd:cd11054   280 EpITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEeYFPDPEEFIPErwlrd 359
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1109516678 417 --NFAKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKT 462
Cdd:cd11054   360 dsENKNIHPFASL-PFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEY 406
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
133-490 8.87e-44

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: 159.28  E-value: 8.87e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 133 IFNNNPELWKTTR----PFF-MKALSGPGlVRMVTVCAEslktHLDRLEEvTNESGYVDVLTLLRRVMLDT-SNTLF--- 203
Cdd:cd20620    50 LLTSEGDLWRRQRrlaqPAFhRRRIAAYA-DAMVEATAA----LLDRWEA-GARRGPVDVHAEMMRLTLRIvAKTLFgtd 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 204 -------LRIPLDE--SAIVVKIQGYFDAWQALLIKPDiffkiswlyKKYEKSVKDLKDAIEVLIAEKRRRISTEEklee 274
Cdd:cd20620   124 vegeadeIGDALDValEYAARRMLSPFLLPLWLPTPAN---------RRFRRARRRLDEVIYRLIAERRAAPADGG---- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 275 cmDFATELILAEKRGDLTRENVNQC---ILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQ 351
Cdd:cd20620   191 --DLLSMLLAARDEETGEPMSDQQLrdeVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTAEDLP 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 352 KLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFAKNVP-----YR 425
Cdd:cd20620   269 QLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPrFWPDPEAFDPERFTPEREaarprYA 348
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109516678 426 YFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIhdlSLHPdetKNMLEM 490
Cdd:cd20620   349 YF-PFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPVEPEPLI---TLRP---KNGVRM 406
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
133-462 1.25e-41

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: 153.91  E-value: 1.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 133 IFNNNPELWKTTR-----PFFMKALSGpgLVRMVTVCAESLkthLDRLEEVTNESGyVDVLTLLRRVMLDT--SNTL--- 202
Cdd:cd11057    47 LFSAPYPIWKLQRkalnpSFNPKILLS--FLPIFNEEAQKL---VQRLDTYVGGGE-FDILPDLSRCTLEMicQTTLgsd 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 203 FLRIPLDESAIVVKIQGYFDawqaLLIK--------PDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKL-- 272
Cdd:cd11057   121 VNDESDGNEEYLESYERLFE----LIAKrvlnpwlhPEFIYRLTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLds 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 273 -EECMDFATELI-------LAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD 344
Cdd:cd11057   197 eEDEENGRKPQIfidqlleLARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDG 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 345 --IKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVID-GYPVKKGTNIILNIGRMHRLEFF--PKPNEFTLENF- 418
Cdd:cd11057   277 qfITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIwgPDADQFDPDNFl 356
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1109516678 419 ----AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKT 462
Cdd:cd11057   357 persAQRHPYAFI-PFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKT 403
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
81-474 3.85e-40

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: 149.98  E-value: 3.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  81 YGEFMRVWISGEETLIISKSSSMFHIM------KHNHYSSRFGSKLGLQCIGmheKGIIFNNNPELWKTTRPFFMKALSG 154
Cdd:cd20613    11 YGPVFVFWILHRPIVVVSDPEAVKEVLitlnlpKPPRVYSRLAFLFGERFLG---NGLVTEVDHEKWKKRRAILNPAFHR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 155 PGLVRMVTV---CAESLkthLDRLEEVTNESGYVDVLTLLRRVMLD-TSNTLF---LRIPLDE-SAIVVKIQGYFDAWQA 226
Cdd:cd20613    88 KYLKNLMDEfneSADLL---VEKLSKKADGKTEVNMLDEFNRVTLDvIAKVAFgmdLNSIEDPdSPFPKAISLVLEGIQE 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 227 LLIKPDIFFKIS-WLY-KKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEEcmDFATELI-LAEKRGDLTRENVNQCILEM 303
Cdd:cd20613   165 SFRNPLLKYNPSkRKYrREVREAIKFLRETGRECIEERLEALKRGEEVPN--DILTHILkASEEEPDFDMEELLDDFVTF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 304 LIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGER-DIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDV 382
Cdd:cd20613   243 FIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKqYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIE 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 383 IDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFAKNVP-----YRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLR 456
Cdd:cd20613   323 LGGYKIPAGTTVLVSTYVMGRMEeYFEDPLKFDPERFSPEAPekipsYAYF-PFSLGPRSCIGQQFAQIEAKVILAKLLQ 401
                         410
                  ....*....|....*...
gi 1109516678 457 RFHVKTLQGQCVESIQKI 474
Cdd:cd20613   402 NFKFELVPGQSFGILEEV 419
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-459 9.96e-40

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: 148.12  E-value: 9.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  79 RVYGEFMRVWISGEETLIISKSSSMFHIMKHN-HYSSRFGSKLGLQCIGMHEKGIIFNNnPELWKTTRPFFMKALSGPGL 157
Cdd:COG2124    29 REYGPVFRVRLPGGGAWLVTRYEDVREVLRDPrTFSSDGGLPEVLRPLPLLGDSLLTLD-GPEHTRLRRLVQPAFTPRRV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 158 VRMVTVCAESLKTHLDRLEEvtneSGYVDVLTLLRRVMLDTSNTLFLRIPLDESAivvKIQGYFDAWQALLIKPDIffki 237
Cdd:COG2124   108 AALRPRIREIADELLDRLAA----RGPVDLVEEFARPLPVIVICELLGVPEEDRD---RLRRWSDALLDALGPLPP---- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 238 sWLYKKYEKSVKDLKDAIEVLIAEKRRRISTeekleecmDFATELILAEKRGD-LTRENV-NQCILeMLIAAPDTMSVSL 315
Cdd:COG2124   177 -ERRRRARRARAELDAYLRELIAERRAEPGD--------DLLSALLAARDDGErLSDEELrDELLL-LLLAGHETTANAL 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEiqtvigerdikiddiqkLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNII 395
Cdd:COG2124   247 AWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVL 309
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1109516678 396 LNIGRMHRLE-FFPKPNEFTLEnfakNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:COG2124   310 LSLAAANRDPrVFPDPDRFDPD----RPPNAHL-PFGGGPHRCLGAALARLEARIALATLLRRFP 369
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
83-469 1.10e-37

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: 143.11  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  83 EFMRVWISGEETLIISKSSSMFHIMKHN--------HYSSRFGSKLGlqcigmheKGIiFNNNPELWKTTRPFFMKALSG 154
Cdd:cd11064     2 TFRGPWPGGPDGIVTADPANVEHILKTNfdnypkgpEFRDLFFDLLG--------DGI-FNVDGELWKFQRKTASHEFSS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 155 PGLvR--MVTVCAESLKTHLDR-LEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAI---VVKIQGYFDAWQALL 228
Cdd:cd11064    73 RAL-RefMESVVREKVEKLLVPlLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPslpEVPFAKAFDDASEAV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 229 IKPDIFFKISWLYKK-----YEKSvkdLKDAIEVL-------IAEKR-RRISTEEKLEECMDFATELILA--EKRGDLTR 293
Cdd:cd11064   152 AKRFIVPPWLWKLKRwlnigSEKK---LREAIRVIddfvyevISRRReELNSREEENNVREDLLSRFLASeeEEGEPVSD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILEMLIAAPDTMSVSL--FFmlFLIAKHPNVEEAIIKEIQTVI------GERDIKIDDIQKLKVMENFIYESMR 365
Cdd:cd11064   229 KFLRDIVLNFILAGRDTTAAALtwFF--WLLSKNPRVEEKIREELKSKLpklttdESRVPTYEELKKLVYLHAALSESLR 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 366 YQPVVDLVMRKALEDDVI-DGYPVKKGTNIILNI---GRMHR------LEFfpKPNEF-TLENFAKNVPYRYFQPFGFGP 434
Cdd:cd11064   307 LYPPVPFDSKEAVNDDVLpDGTFVKKGTRIVYSIyamGRMESiwgedaLEF--KPERWlDEDGGLRPESPYKFPAFNAGP 384
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1109516678 435 RGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVE 469
Cdd:cd11064   385 RICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVE 419
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
81-459 3.72e-37

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: 142.02  E-value: 3.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  81 YGEFMRVW-ISGEETLIISKSSSMFHIMKHNHYS---SRFGSKLGLQCIGmheKGIIFNNNpELWKTTRPFFMKALSGPG 156
Cdd:cd11069     1 YGGLIRYRgLFGSERLLVTDPKALKHILVTNSYDfekPPAFRRLLRRILG---DGLLAAEG-EEHKRQRKILNPAFSYRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 157 LVRMVTV---CAESLKTHLDR-LEEVTNESGYVDVLTLLRRVMLDT-SNTLFLRiplDESAIVVKIQGYFDAWQALL--- 228
Cdd:cd11069    77 VKELYPIfwsKAEELVDKLEEeIEESGDESISIDVLEWLSRATLDIiGLAGFGY---DFDSLENPDNELAEAYRRLFept 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 229 -IKPDIFFKISWLYKKYE-----KSVKDLKDAIEVL-------IAEKRRRISTEEKLEEcMDFATELILAEKRGDLTR-- 293
Cdd:cd11069   154 lLGSLLFILLLFLPRWLVrilpwKANREIRRAKDVLrrlareiIREKKAALLEGKDDSG-KDILSILLRANDFADDERls 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 --ENVNQcILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVI---GERDIKIDDIQKLKVMENFIYESMRYQP 368
Cdd:cd11069   233 deELIDQ-ILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdpPDGDLSYDDLDRLPYLNAVCRETLRLYP 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 369 VVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFF--PKPNEF-------TLENFAKNVP--YRYFQPFGFGPRGC 437
Cdd:cd11069   312 PVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIwgPDAEEFnperwlePDGAASPGGAgsNYALLTFLHGPRSC 391
                         410       420
                  ....*....|....*....|..
gi 1109516678 438 AGKYIAMVMMKAILVTLLRRFH 459
Cdd:cd11069   392 IGKKFALAEMKVLLAALVSRFE 413
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
77-462 6.21e-37

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: 141.18  E-value: 6.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  77 YNRVYGEFM----RVWISGEETL--IISKSSSMFHIMKHnhySSRFGSKLGlqcigmheKGIIFNNnPELWKTTRPFFMK 150
Cdd:cd11055     2 YGKVFGLYFgtipVIVVSDPEMIkeILVKEFSNFTNRPL---FILLDEPFD--------SSLLFLK-GERWKRLRTTLSP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 151 ALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDES-----AIVVKIQGYFDAWQ 225
Cdd:cd11055    70 TFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQnnpddPFLKAAKKIFRNSI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 226 -----ALLIKPDIFFKISWLYK-KYEKSVKDLKDAIEVLIAEKRRRISTEEKleecmDFATELILAEKRGD------LT- 292
Cdd:cd11055   150 irlflLLLLFPLRLFLFLLFPFvFGFKSFSFLEDVVKKIIEQRRKNKSSRRK-----DLLQLMLDAQDSDEdvskkkLTd 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 293 RENVNQCILeMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQPVVD 371
Cdd:cd11055   225 DEIVAQSFI-FLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGsPTYDTVSKLKYLDMVINETLRLYPPAF 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 372 LVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEF-----TLENFAKNVPYRYfQPFGFGPRGCAGKYIAMV 445
Cdd:cd11055   304 FISRECKEDCTINGVFIPKGVDVVIPVYAIHHdPEFWPDPEKFdperfSPENKAKRHPYAY-LPFGAGPRNCIGMRFALL 382
                         410
                  ....*....|....*..
gi 1109516678 446 MMKAILVTLLRRFHVKT 462
Cdd:cd11055   383 EVKLALVKILQKFRFVP 399
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
77-458 3.09e-36

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: 139.42  E-value: 3.09e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  77 YNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLG--LQCI-GmheKGIIfNNNPELWKTTRPFFMKALS 153
Cdd:cd11046     6 WFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAeiLEPImG---KGLI-PADGEIWKKRRRALVPALH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 154 GPGLVRMVTV---CAESLkthLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLD----ESAIVVKIQG-YFDA-- 223
Cdd:cd11046    82 KDYLEMMVRVfgrCSERL---MEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGsvteESPVIKAVYLpLVEAeh 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 224 ---WQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATEL-------ILAEKRGDLTR 293
Cdd:cd11046   159 rsvWEPPYWDIPAALFIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLNEDdpsllrfLVDMRDEDVDS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGER-DIKIDDIQKLKVMENFIYESMRYQPVVDL 372
Cdd:cd11046   239 KQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRlPPTYEDLKKLKYTRRVLNESLRLYPQPPV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 373 VMRKALEDDVIDG--YPVKKGTNIILNIGRMHRL-EFFPKPNEFTLENF---------AKNVPYRYFqPFGFGPRGCAGK 440
Cdd:cd11046   319 LIRRAVEDDKLPGggVKVPAGTDIFISVYNLHRSpELWEDPEEFDPERFldpfinppnEVIDDFAFL-PFGGGPRKCLGD 397
                         410
                  ....*....|....*...
gi 1109516678 441 YIAMVMMKAILVTLLRRF 458
Cdd:cd11046   398 QFALLEATVALAMLLRRF 415
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
82-464 3.22e-35

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: 136.30  E-value: 3.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  82 GEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKL--GLQCIGMHEkgiIFNNNPELWKTTRPFFMKALSGPGLVR 159
Cdd:cd11083     1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFRRISSLesVFREMGING---VFSAEGDAWRRQRRLVMPAFSPKHLRY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 160 MVTvcaeSLKTHLDRL----EEVTNESGYVDVLTLLRRVMLD-TSNTLFLR----IPLDESAIVVKIQGYFdawqallik 230
Cdd:cd11083    78 FFP----TLRQITERLrerwERAAAEGEAVDVHKDLMRYTVDvTTSLAFGYdlntLERGGDPLQEHLERVF--------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 231 PDIFFKIS-----WLY------KKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILA--EKRGDLTRENVN 297
Cdd:cd11083   145 PMLNRRVNapfpyWRYlrlpadRALDRALVEVRALVLDIIAAARARLAANPALAEAPETLLAMMLAedDPDARLTDDEIY 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 298 QCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKID--DIQKLKVMENFIYESMRYQPVVDLVMR 375
Cdd:cd11083   225 ANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLleALDRLPYLEAVARETLRLKPVAPLLFL 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 376 KALEDDVIDGYPVKKGTNIILnigrMHRL-----EFFPKPNEFT----LENFAKNVPY--RYFQPFGFGPRGCAGKYIAM 444
Cdd:cd11083   305 EPNEDTVVGDIALPAGTPVFL----LTRAagldaEHFPDPEEFDperwLDGARAAEPHdpSSLLPFGAGPRLCPGRSLAL 380
                         410       420
                  ....*....|....*....|
gi 1109516678 445 VMMKAILVTLLRRFHVKTLQ 464
Cdd:cd11083   381 MEMKLVFAMLCRNFDIELPE 400
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
231-496 1.22e-34

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: 134.70  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 231 PDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKR--RRISTEEKlEECMDFAT----------ELILAEKRGD--LT---- 292
Cdd:cd20660   155 PDFIYSLTPDGREHKKCLKILHGFTNKVIQERKaeLQKSLEEE-EEDDEDADigkrkrlaflDLLLEASEEGtkLSdedi 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 293 RENVNQCILEmliaAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG--ERDIKIDDIQKLKVMENFIYESMRYQPVV 370
Cdd:cd20660   234 REEVDTFMFE----GHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGdsDRPATMDDLKEMKYLECVIKEALRLFPSV 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 371 DLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNE-----FTLENFAKNVPYRYFqPFGFGPRGCAGKYIAM 444
Cdd:cd20660   310 PMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRdPRQFPDPEKfdpdrFLPENSAGRHPYAYI-PFSAGPRNCIGQKFAL 388
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1109516678 445 VMMKAILVTLLRRFHvktlqgqcVESIQKIHDLslhpdetKNMLEMIFTPRN 496
Cdd:cd20660   389 MEEKVVLSSILRNFR--------IESVQKREDL-------KPAGELILRPVD 425
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
93-466 5.71e-33

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: 129.71  E-value: 5.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  93 ETLIISKSSSMFHIMKHNHYSSRFGSKL-GLQCI---GMHEKGIIFNNNPELWKTTRPFFMKALSGPG-----------L 157
Cdd:cd11044     2 ETLEFLRDPEDFIQSRYQKYGPVFKTHLlGRPTVfviGAEAVRFILSGEGKLVRYGWPRSVRRLLGENslslqdgeehrR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 158 VRMVTVCA---ESLKTHLDRLEEVTNE-------SGYVDVLTLLRRVMLDTSNTLFLRipLDESAIVVKIQGYFDAW-QA 226
Cdd:cd11044    82 RRKLLAPAfsrEALESYVPTIQAIVQSylrkwlkAGEVALYPELRRLTFDVAARLLLG--LDPEVEAEALSQDFETWtDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 227 LL-IKPDIFFKiswLYKKYEKSVKDLKDAIEVLIAEKRrristEEKLEECMDfATELILAEKRGD---LTRENVNQCILE 302
Cdd:cd11044   160 LFsLPVPLPFT---PFGRAIRARNKLLARLEQAIRERQ-----EEENAEAKD-ALGLLLEAKDEDgepLSMDELKDQALL 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 303 MLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDV 382
Cdd:cd11044   231 LLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 383 IDGYPVKKGTNIILNIGRMHRL-EFFPKPNEFTLENFA------KNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLL 455
Cdd:cd11044   311 LGGYQIPKGWLVYYSIRDTHRDpELYPDPERFDPERFSparsedKKKPFSLI-PFGGGPRECLGKEFAQLEMKILASELL 389
                         410
                  ....*....|.
gi 1109516678 456 RRFHVKTLQGQ 466
Cdd:cd11044   390 RNYDWELLPNQ 400
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
230-460 1.76e-31

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: 125.76  E-value: 1.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 230 KPDIFFKISWLYK-KYEKSVKDLKDAIEVLIAEKRRRISTEEK-LEECMDFATELILAEKrgdLTRENV-NQCIlEMLIA 306
Cdd:cd11068   166 RPPILNKLRRRAKrQFREDIALMRDLVDEIIAERRANPDGSPDdLLNLMLNGKDPETGEK---LSDENIrYQMI-TFLIA 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 307 APDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDG- 385
Cdd:cd11068   242 GHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGk 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 386 YPVKKGTNIILNIGRMHR---------LEFfpKPNEFTLENFAKnVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLR 456
Cdd:cd11068   322 YPLKKGDPVLVLLPALHRdpsvwgedaEEF--RPERFLPEEFRK-LPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQ 398

                  ....
gi 1109516678 457 RFHV 460
Cdd:cd11068   399 RFDF 402
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
125-485 3.53e-30

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: 121.93  E-value: 3.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 125 IGMHEKGIIFNNNPELWKTTRPFFMKAL-----SGPGLVRMVTVCAESLkthLDRLEEVtnESGYVDVLTLLRRVMLDT- 198
Cdd:cd11027    46 FSRGGKDIAFGDYSPTWKLHRKLAHSALrlyasGGPRLEEKIAEEAEKL---LKRLASQ--EGQPFDPKDELFLAVLNVi 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 199 SNTLF-LRIPLDESA---IVVKIQGYFDAWQALLIKpDIFfkiSWL----YKKYEKSVKDLKDAIEVLiaekrrristEE 270
Cdd:cd11027   121 CSITFgKRYKLDDPEflrLLDLNDKFFELLGAGSLL-DIF---PFLkyfpNKALRELKELMKERDEIL----------RK 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 271 KLEE---------CMDFATELILA----EKRGD-----LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAI 332
Cdd:cd11027   187 KLEEhketfdpgnIRDLTDALIKAkkeaEDEGDedsglLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 333 IKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPK 409
Cdd:cd11027   267 HAELDDVIGrDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPkEWDD 346
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 410 PNEFTLENF----AKNVP-YRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDET 484
Cdd:cd11027   347 PDEFRPERFldenGKLVPkPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPELEGIPGLVLYPLPY 426

                  .
gi 1109516678 485 K 485
Cdd:cd11027   427 K 427
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
133-458 4.00e-30

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: 121.90  E-value: 4.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 133 IFNNNPELWKTTR----PFFMKAlsgpglvRMVTVcaESLKTHLDRLEEVTNESG-YVDVLTLLRRVMLDTS-------- 199
Cdd:cd11063    52 IFTSDGEEWKHSRallrPQFSRD-------QISDL--ELFERHVQNLIKLLPRDGsTVDLQDLFFRLTLDSAteflfges 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 200 -NTLFLRIPLDESAIVVKIqgyFDAWQALLIKPDIFFKISWLY--KKYEKSVKDLKDAIEVLIAE--KRRRISTEEKLEE 274
Cdd:cd11063   123 vDSLKPGGDSPPAARFAEA---FDYAQKYLAKRLRLGKLLWLLrdKKFREACKVVHRFVDPYVDKalARKEESKDEESSD 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 275 CMDFATELIlaeKRGDLTRENVNQcILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKL 353
Cdd:cd11063   200 RYVFLDELA---KETRDPKELRDQ-LLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGpEPTPTYEDLKNM 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 354 KVMENFIYESMRYQPVVDLVMRKALEDDVI------DGYP---VKKGTNIILNIGRMHRLE--FFPKPNEFTLENFAKNV 422
Cdd:cd11063   276 KYLRAVINETLRLYPPVPLNSRVAVRDTTLprgggpDGKSpifVPKGTRVLYSVYAMHRRKdiWGPDAEEFRPERWEDLK 355
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1109516678 423 PYRY-FQPFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11063   356 RPGWeYLPFNGGPRICLGQQFALTEASYVLVRLLQTF 392
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
75-458 9.88e-30

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


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 120.91  E-value: 9.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  75 NYYNRVYGEFMRVWISGEETLIISKSSSMFHIM-KHNHYSSRFGSKLGLQciGMHEKGIIFNNNPElWKTTRPFFMKALS 153
Cdd:cd11052     5 YHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLsKKEGYFGKSPLQPGLK--KLLGRGLVMSNGEK-WAKHRRIANPAFH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 154 GPGLVRMVTVCAESLKTHLDRLEEVTNESG-YVDVLTLLRRVMLDT-SNTLFLRIPLDESAIVVKIqgyfDAWQALLIKP 231
Cdd:cd11052    82 GEKLKGMVPAMVESVSDMLERWKKQMGEEGeEVDVFEEFKALTADIiSRTAFGSSYEEGKEVFKLL----RELQKICAQA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 --DIFFKISWLYK-KYEKSVKDLKDAIEVLIAE--KRRRISTEEKLEEcmDFATELI-----LAEKRGDLTRENVNQCIL 301
Cdd:cd11052   158 nrDVGIPGSRFLPtKGNKKIKKLDKEIEDSLLEiiKKREDSLKMGRGD--DYGDDLLgllleANQSDDQNKNMTVQEIVD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 E---MLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMR-YQPVVDLVmRKA 377
Cdd:cd11052   236 EcktFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLRlYPPAVFLT-RKA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 378 LEDDVIDGYPVKKGTNIILNIGRMHRLEFF--PKPNEFTLENFAKNVPY-----RYFQPFGFGPRGCAGKYIAMVMMKAI 450
Cdd:cd11052   315 KEDIKLGGLVIPKGTSIWIPVLALHHDEEIwgEDANEFNPERFADGVAKaakhpMAFLPFGLGPRNCIGQNFATMEAKIV 394

                  ....*...
gi 1109516678 451 LVTLLRRF 458
Cdd:cd11052   395 LAMILQRF 402
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
242-481 1.82e-29

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: 120.25  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 242 KKYEKSVKDLKDAIEVLIAEkrrRISTEEKLEECMDfatelilaEKRGDLTRENVNQCILEMLIAAP------------- 308
Cdd:cd20680   177 KEHNKNLKILHTFTDNVIAE---RAEEMKAEEDKTG--------DSDGESPSKKKRKAFLDMLLSVTdeegnklshedir 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 309 -----------DTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG--ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMR 375
Cdd:cd20680   246 eevdtfmfeghDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGksDRPVTMEDLKKLRYLECVIKESLRLFPSVPLFAR 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 376 KALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFT-----LENFAKNVPYRYFqPFGFGPRGCAGKYIAMVMMKA 449
Cdd:cd20680   326 SLCEDCEIRGFKVPKGVNAVIIPYALHRdPRYFPEPEEFRperffPENSSGRHPYAYI-PFSAGPRNCIGQRFALMEEKV 404
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1109516678 450 ILVTLLRRFHVKTlqGQCVESIQKIHDLSLHP 481
Cdd:cd20680   405 VLSCILRHFWVEA--NQKREELGLVGELILRP 434
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
225-496 3.51e-29

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: 119.28  E-value: 3.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 225 QALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRI---STEEKLEECMDFATELILAEKRGDLTRENVNQCIL 301
Cdd:cd20621   156 RLIFGRKSWKLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIkknKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFI 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 EMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVD-LVMRKALE 379
Cdd:cd20621   236 TFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGnDDDITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQ 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 380 DDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF-----AKNVPYrYFQPFGFGPRGCAGKYIAMVMMKAILVT 453
Cdd:cd20621   316 DHQIGDLKIKKGWIVNVGYIYNHFNPkYFENPDEFNPERWlnqnnIEDNPF-VFIPFSAGPRNCIGQHLALMEAKIILIY 394
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1109516678 454 LLRRFHVKtlqgqcvesIQKIHDLslhpdetKNMLEMIFTPRN 496
Cdd:cd20621   395 ILKNFEIE---------IIPNPKL-------KLIFKLLYEPVN 421
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
232-495 5.18e-29

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: 118.87  E-value: 5.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 DIFFKISWL-YKKYEKSVK----DLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDL----TRENV-NQCIL 301
Cdd:cd20654   168 DAIPFLGWLdFGGHEKAMKrtakELDSILEEWLEEHRQKRSSSGKSKNDEDDDDVMMLSILEDSQisgyDADTViKATCL 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 EMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMR-YQPVVDLVMRKALE 379
Cdd:cd20654   248 ELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGkDRWVEESDIKNLVYLQAIVKETLRlYPPGPLLGPREATE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 380 DDVIDGYPVKKGTNIILNIGRMHR--------LEFfpKPNEFTLENFAKNVPYRYFQ--PFGFGPRGCAGKYIAMVMMKA 449
Cdd:cd20654   328 DCTVGGYHVPKGTRLLVNVWKIQRdpnvwsdpLEF--KPERFLTTHKDIDVRGQNFEliPFGSGRRSCPGVSFGLQVMHL 405
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1109516678 450 ILVTLLRRFHVKTLQGQCVesiqkihDLSLHPDET---KNMLEMIFTPR 495
Cdd:cd20654   406 TLARLLHGFDIKTPSNEPV-------DMTEGPGLTnpkATPLEVLLTPR 447
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
304-462 8.19e-29

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: 118.02  E-value: 8.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 304 LIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKI--DDIQKLKVMENFIYESMRYQPVVDLVMRKALEDD 381
Cdd:cd11056   238 FLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGELtyEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDY 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 382 VIDG--YPVKKGTNIILNIGRMHRL-EFFPKPNE-----FTLENFAKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVT 453
Cdd:cd11056   318 TLPGtdVVIEKGTPVIIPVYALHHDpKYYPEPEKfdperFSPENKKKRHPYTYL-PFGDGPRNCIGMRFGLLQVKLGLVH 396

                  ....*....
gi 1109516678 454 LLRRFHVKT 462
Cdd:cd11056   397 LLSNFRVEP 405
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
185-484 9.06e-29

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: 117.74  E-value: 9.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 185 VDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFfkiSWLYK-------KYEKSVKDLKDAIEV 257
Cdd:cd11049   110 VDVDAEMHRLTLRVVARTLFSTDLGPEAAAELRQALPVVLAGMLRRAVPP---KFLERlptpgnrRFDRALARLRELVDE 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 258 LIAEKRRRISTEEkleecmDFATELILAEKRGD--LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKE 335
Cdd:cd11049   187 IIAEYRASGTDRD------DLLSLLLAARDEEGrpLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAE 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 336 IQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRL-EFFPKPNEFT 414
Cdd:cd11049   261 LDAVLGGRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDpEVYPDPERFD 340
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109516678 415 ----LENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHdlsLHPDET 484
Cdd:cd11049   341 pdrwLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGRPVRPRPLAT---LRPRRL 411
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
82-459 3.39e-28

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: 116.50  E-value: 3.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  82 GEFMRVWISGEETLIISkSSSMFH-IMKHN--HYSSR----FGSKLGLQCigmheKGIIFNNNPELWKTTR-----PFF- 148
Cdd:cd20618     1 GPLMYLRLGSVPTVVVS-SPEMAKeVLKTQdaVFASRprtaAGKIFSYNG-----QDIVFAPYGPHWRHLRkictlELFs 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 149 ---MKALSGpglVRMvtvcaESLKTHLDRLEEVTNESGYVDvltlLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDA-- 223
Cdd:cd20618    75 akrLESFQG---VRK-----EELSHLVKSLLEESESGKPVN----LREHLSDLTLNNITRMLFGKRYFGESEKESEEAre 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 224 -------WQALLIKPDI--------FFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKR 288
Cdd:cd20618   143 fkelideAFELAGAFNIgdyipwlrWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 289 GDLTRENVNQCILEMLIAAPDTMSVSL-FFMLFLIaKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRY 366
Cdd:cd20618   223 GKLSDDNIKALLLDMLAAGTDTSAVTIeWAMAELL-RHPEVMRKAQEELDSVVGrERLVEESDLPKLPYLQAVVKETLRL 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 367 QPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHR--------LEFfpKPNEFtLENFAKNVPYRYFQ--PFGFGPR 435
Cdd:cd20618   302 HPPGPLlLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRdpkvwedpLEF--KPERF-LESDIDDVKGQDFEllPFGSGRR 378
                         410       420
                  ....*....|....*....|....
gi 1109516678 436 GCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:cd20618   379 MCPGMPLGLRMVQLTLANLLHGFD 402
PLN02738 PLN02738
carotene beta-ring hydroxylase
80-465 4.07e-28

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 118.09  E-value: 4.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  80 VYGEFMRVWISGEETLIISKSSSMFHIMKHNH--YSSRFGSKLGLQCIGmheKGIIFNNNpELWKTTRPFFMKALSGPGL 157
Cdd:PLN02738  163 TYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSkaYSKGILAEILEFVMG---KGLIPADG-EIWRVRRRAIVPALHQKYV 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 158 VRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLD----ESAIVVKIQGYFDAWQALLIKP-- 231
Cdd:PLN02738  239 AAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDslsnDTGIVEAVYTVLREAEDRSVSPip 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 ----DIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRIStEEKL---EECMDFATELIL---AEKRGDLTRENVNQCIL 301
Cdd:PLN02738  319 vweiPIWKDISPRQRKVAEALKLINDTLDDLIAICKRMVE-EEELqfhEEYMNERDPSILhflLASGDDVSSKQLRDDLM 397
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 EMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDD 381
Cdd:PLN02738  398 TMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLEND 477
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 382 VIDGYPVKKGTNIILNIGRMHR-------LEFF---------PKPNEfTLENFAknvpyryFQPFGFGPRGCAGKYIAMV 445
Cdd:PLN02738  478 MLGGYPIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNFS-------YLPFGGGPRKCVGDMFASF 549
                         410       420
                  ....*....|....*....|
gi 1109516678 446 MMKAILVTLLRRFHVKTLQG 465
Cdd:PLN02738  550 ENVVATAMLVRRFDFQLAPG 569
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
165-458 4.50e-28

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: 115.76  E-value: 4.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 165 AESLKTHLDRLEEVTNES-------GYVDVLTLLRRVMLD-TSNTLFlriPLDESAIVVKIQGYFDAWQALLIKPDIFFK 236
Cdd:cd11053    84 GERLRAYGELIAEITEREidrwppgQPFDLRELMQEITLEvILRVVF---GVDDGERLQELRRLLPRLLDLLSSPLASFP 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 237 ------ISWL-YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKleecmDFATELILA--EKRGDLTRENVNQCILEMLIAA 307
Cdd:cd11053   161 alqrdlGPWSpWGRFLRARRRIDALIYAEIAERRAEPDAERD-----DILSLLLSArdEDGQPLSDEELRDELMTLLFAG 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 308 PDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIkiDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYP 387
Cdd:cd11053   236 HETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP--EDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYT 313
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109516678 388 VKKGTNIILNIGRMHRLE-FFPKPNEFTLENFA--KNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11053   314 LPAGTTVAPSIYLTHHRPdLYPDPERFRPERFLgrKPSPYEYL-PFGGGVRRCIGAAFALLEMKVVLATLLRRF 386
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
227-460 4.94e-28

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: 115.73  E-value: 4.94e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 227 LLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLE----ECMDFATELILAeKRGD---LTRENV-NQ 298
Cdd:cd20659   153 PLLHFDWIYYLTPEGRRFKKACDYVHKFAEEIIKKRRKELEDNKDEAlskrKYLDFLDILLTA-RDEDgkgLTDEEIrDE 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 299 CIlEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGER-DIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKA 377
Cdd:cd20659   232 VD-TFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTL 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 378 LEDDVIDGYPVKKGTNIILNIGRMHR--------LEFfpKPNEFTLENFAKNVPYRYFqPFGFGPRGCAGKYIAMVMMKA 449
Cdd:cd20659   311 TKPITIDGVTLPAGTLIAINIYALHHnptvwedpEEF--DPERFLPENIKKRDPFAFI-PFSAGPRNCIGQNFAMNEMKV 387
                         250
                  ....*....|.
gi 1109516678 450 ILVTLLRRFHV 460
Cdd:cd20659   388 VLARILRRFEL 398
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
185-460 1.91e-27

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: 113.95  E-value: 1.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 185 VDVLTLLRRVMLDTSNTLFLRIPLDESAivVKIQGYF-DAWQA--LLIKPDIFFKiswLYKKYEKSVKDLKDAIEVLIAE 261
Cdd:cd11045   109 FQFYPAIKELTLDLATRVFLGVDLGPEA--DKVNKAFiDTVRAstAIIRTPIPGT---RWWRGLRGRRYLEEYFRRRIPE 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 262 KRRRISTeekleecmDFATELILAE-KRGDL--TRENVNQCILeMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQT 338
Cdd:cd11045   184 RRAGGGD--------DLFSALCRAEdEDGDRfsDDDIVNHMIF-LMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLA 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 339 vIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRL-EFFPKPNEFTLEN 417
Cdd:cd11045   255 -LGKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMpEYWPNPERFDPER 333
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1109516678 418 FAKNVP----YRY-FQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHV 460
Cdd:cd11045   334 FSPERAedkvHRYaWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRW 381
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
166-465 1.97e-27

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: 113.81  E-value: 1.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 166 ESLKTH-LDRLEEVTN-------ESGYVDVLTLLRRVMLDTSNTLFLRIplDESAIVVKIQGYFDAW-QALLIKPdiffk 236
Cdd:cd11043    77 EALKDRlLGDIDELVRqhldswwRGKSVVVLELAKKMTFELICKLLLGI--DPEEVVEELRKEFQAFlEGLLSFP----- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 237 ISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGD--LTRENVNQCILEMLIAAPDTMSVS 314
Cdd:cd11043   150 LNLPGTTFHRALKARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDEDGdsLTDEEILDNILTLLFAGHETTSTT 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 315 LFFMLFLIAKHPNVEEAIIKE----IQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKK 390
Cdd:cd11043   230 LTLAVKFLAENPKVLQELLEEheeiAKRKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPK 309
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109516678 391 GTNIILNIGRMHR-LEFFPKPNEFT---LENFAKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQG 465
Cdd:cd11043   310 GWKVLWSARATHLdPEYFPDPLKFNpwrWEGKGKGVPYTFL-PFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPD 387
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
82-461 1.10e-26

cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 111.61  E-value: 1.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  82 GEFMRVWISGEETLIISKSSSM--FHIMKHNHYSSR-------FGSKLGlQCIGmhekgiiFNNNPElWKTTRPFFMKAL 152
Cdd:cd20615     1 GPIYRIWSGPTPEIVLTTPEHVkeFYRDSNKHHKAPnnnsgwlFGQLLG-QCVG-------LLSGTD-WKRVRKVFDPAF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 153 SGPGLVRMVTVCAESLKTHLDRLEEV--TNESGYVDVLTLLRRVMLDTSNTLFL-RIPLDESAIVVKI-----QGYFDAW 224
Cdd:cd20615    72 SHSAAVYYIPQFSREARKWVQNLPTNsgDGRRFVIDPAQALKFLPFRVIAEILYgELSPEEKEELWDLaplreELFKYVI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 225 QALLIKpdifFKIS-WLYKKYEKSVKD-LKDAIEVL--IAEKRRristeEKLEECMdfATELILAEKRGDLTRENVNQCI 300
Cdd:cd20615   152 KGGLYR----FKISrYLPTAANRRLREfQTRWRAFNlkIYNRAR-----QRGQSTP--IVKLYEAVEKGDITFEELLQTL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 301 LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDD-IQKLKVMENF-IYESMRYQPVVDL-VMRKA 377
Cdd:cd20615   221 DEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDyILSTDTLLAYcVLESLRLRPLLAFsVPESS 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 378 LEDDVIDGYPVKKGTNIILNIGRM-HRLEFF-PKPNEFTLENFAKNVP--YRY-FQPFGFGPRGCAGKYIAMVMMKAILV 452
Cdd:cd20615   301 PTDKIIGGYRIPANTPVVVDTYALnINNPFWgPDGEAYRPERFLGISPtdLRYnFWRFGFGPRKCLGQHVADVILKALLA 380

                  ....*....
gi 1109516678 453 TLLRRFHVK 461
Cdd:cd20615   381 HLLEQYELK 389
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
122-461 9.45e-26

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: 109.23  E-value: 9.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 122 LQCIGMHeKGIIFNNNPeLWKTTRPFFMKALS--GPGLVRMVTVCAESLKTHLDRLEEvtNESGYVDVLTLLRRVMLdts 199
Cdd:cd20651    42 LRTFGKR-LGITFTDGP-FWKEQRRFVLRHLRdfGFGRRSMEEVIQEEAEELIDLLKK--GEKGPIQMPDLFNVSVL--- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 200 NTLFL-----RIPLDES------AIVVKIQGYFDAWQALLikpDIFFkisWL---------YKKYEKSVKDLKDAIEVLI 259
Cdd:cd20651   115 NVLWAmvageRYSLEDQklrkllELVHLLFRNFDMSGGLL---NQFP---WLrfiapefsgYNLLVELNQKLIEFLKEEI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 260 aeKRRRISTEEKLEEC-MD-FATELILAEKRGD-LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEI 336
Cdd:cd20651   189 --KEHKKTYDEDNPRDlIDaYLREMKKKEPPSSsFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEI 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 337 QTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEF 413
Cdd:cd20651   267 DEVVGrDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIgIPHRALKDTTLGGYRIPKDTTILASLYSVHMdPEYWGDPEEF 346
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1109516678 414 TLENF----AKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVK 461
Cdd:cd20651   347 RPERFldedGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFS 398
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
185-461 1.34e-25

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: 108.92  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 185 VDVLTLLRRVMLDTSNTLFLRIPL-DESAIVVKIQGY----FDAWQALLIKPDIFFKI-SWLYKKYEKSVKDLKDAIEVL 258
Cdd:cd11041   108 VNLYDTVLRIVARVSARVFVGPPLcRNEEWLDLTINYtidvFAAAAALRLFPPFLRPLvAPFLPEPRRLRRLLRRARPLI 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 259 IAEKRRRISTEEKL--EECMDFATELI-LAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKE 335
Cdd:cd11041   188 IPEIERRRKLKKGPkeDKPNDLLQWLIeAAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREE 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 336 IQTVIGERD-IKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVI-DGYPVKKGTNIILNIGRMHRLE-FFPKPN 411
Cdd:cd11041   268 IRSVLAEHGgWTKAALNKLKKLDSFMKESQRLNPLSLVSLrRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPdIYPDPE 347
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109516678 412 EFtlenfaknVPYRY---------------------FQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVK 461
Cdd:cd11041   348 TF--------DGFRFyrlreqpgqekkhqfvstspdFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFK 410
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
176-461 2.69e-25

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: 108.19  E-value: 2.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 176 EEVTNESGYVDVLTLLRR--------VMLDTSntlFLRIPLDESAIVVkiqgYFDAWQALLIKPDIF-FKI-SWLYKKYE 245
Cdd:cd11070    95 EQPSAKGGGVDVRDLLQRlalnvigeVGFGFD---LPALDEEESSLHD----TLNAIKLAIFPPLFLnFPFlDRLPWVLF 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 246 KSVKDLKDAIE------VLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRE----NVNqcIleMLIAAPDTMSVSL 315
Cdd:cd11070   168 PSRKRAFKDVDeflselLDEVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKellgNLF--I--FFIAGHETTANTL 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEIQTVIGERDIKID---DIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVI-----DGYP 387
Cdd:cd11070   244 SFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDyeeDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVitglgQEIV 323
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 388 VKKGTNIILNIGRMHR---------LEFFPK-----PNEFTLENFAKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVT 453
Cdd:cd11070   324 IPKGTYVGYNAYATHRdptiwgpdaDEFDPErwgstSGEIGAATRFTPARGAFI-PFSAGPRACLGRKFALVEFVAALAE 402

                  ....*...
gi 1109516678 454 LLRRFHVK 461
Cdd:cd11070   403 LFRQYEWR 410
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
234-458 1.68e-24

cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome P450 family 71 (CYP71) proteins, as well as some CYPs designated as belonging to a different family including CYP99A1, CYP83B1, and CYP84A1, among others. Characterized CYP71 enzymes include: parsnip (Pastinaca sativa) CYP71AJ4, also called angelicin synthase, that converts (+)-columbianetin to angelicin, an angular furanocumarin; periwinkle (Catharanthus roseus) CYP71D351, also called tabersonine 16-hydroxylase 2, that is involved in the foliar biosynthesis of vindoline; sorghum CYP71E1, also called 4-hydroxyphenylacetaldehyde oxime monooxygenase, that catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile; as well as maize CYP71C1, CYP71C2, and CYP71C4, which are monooxygenases catalyzing the oxidation of 3-hydroxyindolin-2-one, indolin-2-one, and indole, respectively. CYPs within a single CYP71 subfamily, such as the C subfamily, usually metabolize similar/related compounds. The CYP71-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410695 [Multi-domain]  Cd Length: 428  Bit Score: 105.62  E-value: 1.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 234 FFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGD--LTRENVNQCILEMLIAAPDTM 311
Cdd:cd11072   165 IDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEfpLTRDNIKAIILDMFLAGTDTS 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 312 SVSL-FFMLFLIaKHPNVEEAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQPVVD-LVMRKALEDDVIDGYPV 388
Cdd:cd11072   245 ATTLeWAMTELI-RNPRVMKKAQEEVREVVGGKGkVTEEDLEKLKYLKAVIKETLRLHPPAPlLLPRECREDCKINGYDI 323
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109516678 389 KKGTNIILN---IGRMHrlEFFPKPNEFTLENFA-KNVPYR--YFQ--PFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11072   324 PAKTRVIVNawaIGRDP--KYWEDPEEFRPERFLdSSIDFKgqDFEliPFGAGRRICPGITFGLANVELALANLLYHF 399
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
208-460 3.64e-24

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: 104.59  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 208 LDESAIVVKIQGYFDAWQALLIKPDIFFKiswlyKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEEcmDFATELILAEK 287
Cdd:cd11060   140 IDKLLPYFAVVGQIPWLDRLLLKNPLGPK-----RKDKTGFGPLMRFALEAVAERLAEDAESAKGRK--DMLDSFLEAGL 212
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 288 RG--DLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE----RDIKIDDIQKLKVMENFIY 361
Cdd:cd11060   213 KDpeKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEgklsSPITFAEAQKLPYLQAVIK 292
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 362 ESMRYQPVVDLVM-RKALED-DVIDGYPVKKGTNIILNIGRMHRLE--FFPKPNEFT----LENFAKNVPY--RYFQPFG 431
Cdd:cd11060   293 EALRLHPPVGLPLeRVVPPGgATICGRFIPGGTIVGVNPWVIHRDKevFGEDADVFRperwLEADEEQRRMmdRADLTFG 372
                         250       260
                  ....*....|....*....|....*....
gi 1109516678 432 FGPRGCAGKYIAMVMMKAILVTLLRRFHV 460
Cdd:cd11060   373 AGSRTCLGKNIALLELYKVIPELLRRFDF 401
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
294-465 3.98e-24

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: 104.56  E-value: 3.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPVVDL 372
Cdd:cd11026   225 ENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRnRTPSLEDRAKMPYTDAVIHEVQRFGDIVPL 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 373 -VMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF-------AKNvpyRYFQPFGFGPRGCAGKYIA 443
Cdd:cd11026   305 gVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPkQWETPEEFNPGHFldeqgkfKKN---EAFMPFSAGKRVCLGEGLA 381
                         170       180
                  ....*....|....*....|..
gi 1109516678 444 MVMMKAILVTLLRRFHVKTLQG 465
Cdd:cd11026   382 RMELFLFFTSLLQRFSLSSPVG 403
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
262-477 6.37e-24

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: 103.85  E-value: 6.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 262 KRRRISTEEKLEE---CMDFATEL-------ILAEKrgDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEA 331
Cdd:cd20647   196 KFSQIHVDNRLREiqkQMDRGEEVkgglltyLLVSK--ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQ 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 332 IIKEIQTVIGERDIKI-DDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIIL-NIGRMHRLEFFPK 409
Cdd:cd20647   274 VYEEIVRNLGKRVVPTaEDVPKLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALcHYSTSYDEENFPR 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 410 PNEFT------------LENFAKnvpyryfQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTlQGQCVESIQKIHDL 477
Cdd:cd20647   354 AEEFRperwlrkdaldrVDNFGS-------IPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKV-SPQTTEVHAKTHGL 425
PLN02936 PLN02936
epsilon-ring hydroxylase
230-468 9.14e-24

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 104.10  E-value: 9.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 230 KPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATE------LILAEKRGDLTRENVNQCILEM 303
Cdd:PLN02936  207 KVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIEGEEYVNDsdpsvlRFLLASREEVSSVQLRDDLLSM 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 304 LIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVI 383
Cdd:PLN02936  287 LVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVL 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 384 -DGYPVKKGTNIILNIGRMHRL-EFFPKPNEFTLENF--------AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVT 453
Cdd:PLN02936  367 pGGYKVNAGQDIMISVYNIHRSpEVWERAEEFVPERFdldgpvpnETNTDFRYI-PFSGGPRKCVGDQFALLEAIVALAV 445
                         250
                  ....*....|....*
gi 1109516678 454 LLRRFHVKTLQGQCV 468
Cdd:PLN02936  446 LLQRLDLELVPDQDI 460
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
79-458 2.22e-23

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: 102.23  E-value: 2.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  79 RVYGEFMRVWISGEETLIISKSSSMFHIMKHN--HYSSRFGSKLGLqcIGMHEKGIIFNNNP-ELWKTTRP-FFMKALSG 154
Cdd:cd11073     2 KKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHdrVLSGRDVPDAVR--ALGHHKSSIVWPPYgPRWRMLRKiCTTELFSP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 155 PGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVltllRRVMLDT-----SNTLFLRIPLDESAivVKIQGYFDA-WQALL 228
Cdd:cd11073    80 KRLDATQPLRRRKVRELVRYVREKAGSGEAVDI----GRAAFLTslnliSNTLFSVDLVDPDS--ESGSEFKELvREIME 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 229 I--KPDI--------FFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKR-GDLTRENVN 297
Cdd:cd11073   154 LagKPNVadffpflkFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSeSELTRNHIK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 298 QCILEMLIAAPDTMSVSL-FFMLFLIaKHPNVEEAIIKEIQTVIGER-DIKIDDIQKLKVMENFIYESMRYQPVVD-LVM 374
Cdd:cd11073   234 ALLLDLFVAGTDTTSSTIeWAMAELL-RNPEKMAKARAELDEVIGKDkIVEESDISKLPYLQAVVKETLRLHPPAPlLLP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 375 RKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENF-AKNVPYR----YFQPFGFGPRGCAGKYIAMVMMK 448
Cdd:cd11073   313 RKAEEDVEVMGYTIPKGTQVLVNVWAIGRdPSVWEDPLEFKPERFlGSEIDFKgrdfELIPFGSGRRICPGLPLAERMVH 392
                         410
                  ....*....|
gi 1109516678 449 AILVTLLRRF 458
Cdd:cd11073   393 LVLASLLHSF 402
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
133-461 4.24e-23

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: 101.33  E-value: 4.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 133 IFNNNPELWKTTR-----PFFMKALSGpglvrMVTVCAESLKTHLDRLEEVTNESG------YVDvlTLLRRVMLDT-SN 200
Cdd:cd20640    62 ILTSNGPHWAHQRkiiapEFFLDKVKG-----MVDLMVDSAQPLLSSWEERIDRAGgmaadiVVD--EDLRAFSADViSR 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 201 TLFLRIPLDESAIVVKIQgyfdAWQALLIKPDIFFKISWLY---KKYEKSVKDLKDAIEVLI---AEKRRRISTEEKlee 274
Cdd:cd20640   135 ACFGSSYSKGKEIFSKLR----ELQKAVSKQSVLFSIPGLRhlpTKSNRKIWELEGEIRSLIleiVKEREEECDHEK--- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 275 cmDFATELILAEKRGDLTRENVNQCILE----MLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDI 350
Cdd:cd20640   208 --DLLQAILEGARSSCDKKAEAEDFIVDncknIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDADSL 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 351 QKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFF-PKPNEFTLENFAKNV------ 422
Cdd:cd20640   286 SRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLdPEIWgPDANEFNPERFSNGVaaackp 365
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1109516678 423 PYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVK 461
Cdd:cd20640   366 PHSYM-PFGAGARTCLGQNFAMAELKVLVSLILSKFSFT 403
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
239-468 1.32e-22

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: 99.98  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 239 WLYKKYEKSVKDLKDAI-EVLIAEK--RRRISTEEKLEECMDfatelILAEKRGD------LTRENVNQCILEMLIAAPD 309
Cdd:cd20655   168 QGFGKRIMDVSNRFDELlERIIKEHeeKRKKRKEGGSKDLLD-----ILLDAYEDenaeykITRNHIKAFILDLFIAGTD 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 310 TMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPV 388
Cdd:cd20655   243 TSAATTEWAMAELINNPEVLEKAREEIDSVVGkTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDI 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 389 KKGTNIILNIGRMHR-LEFFPKPNEFTLENFAKN--------VPYRYFQ--PFGFGPRGCAGKYIAMVMMKAILVTLLRR 457
Cdd:cd20655   323 PEKTTLFVNVYAIMRdPNYWEDPLEFKPERFLASsrsgqeldVRGQHFKllPFGSGRRGCPGASLAYQVVGTAIAAMVQC 402
                         250
                  ....*....|.
gi 1109516678 458 FHVKTLQGQCV 468
Cdd:cd20655   403 FDWKVGDGEKV 413
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
195-470 1.72e-22

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


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 99.60  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 195 MLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWLYKKYEKSVKDLkdaievliAEKRRRISTEEKLee 274
Cdd:cd11061   125 MLESGKDRYILDLLEKSMVRLGVLGHAPWLRPLLLDLPLFPGATKARKRFLDFVRAQ--------LKERLKAEEEKRP-- 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 275 cmDFATELILA---EKRGDLTRENVN-QCILeMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD-IKI-D 348
Cdd:cd11061   195 --DIFSYLLEAkdpETGEGLDLEELVgEARL-LIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDeIRLgP 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 349 DIQKLKVMENFIYESMR-YQPVVDLVMRKALEDDV-IDGYPVKKGTNIILNIGRMHRLE-FFPKPNEF------TLENFA 419
Cdd:cd11061   272 KLKSLPYLRACIDEALRlSPPVPSGLPRETPPGGLtIDGEYIPGGTTVSVPIYSIHRDErYFPDPFEFiperwlSRPEEL 351
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1109516678 420 KNvPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVES 470
Cdd:cd11061   352 VR-ARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGEDGEA 401
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
81-444 3.83e-22

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: 98.42  E-value: 3.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  81 YGEFMRVWISGEETLIISKSSSMFHIM-KHNH-YSSRFGSKLGLQCIGMHeKGIIFNNNPELWKTTRPFFMKALSgpglv 158
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLeKRSAiYSSRPRMPMAGELMGWG-MRLLLMPYGPRWRLHRRLFHQLLN----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 159 rmvtvcAESLKTHLDRLEEvtnESgyvdvLTLLRRVMLD-----------TSNTLF-----LRIPLDESAIVVKIQgYFD 222
Cdd:cd11065    75 ------PSAVRKYRPLQEL---ES-----KQLLRDLLESpddfldhirryAASIILrlaygYRVPSYDDPLLRDAE-EAM 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 223 AWQALLIKP-----DIF---------FKISWlyKKYEKSVKDL-KDAIEVLIAEKRRRISTEEKlEECmdFATELILA-E 286
Cdd:cd11065   140 EGFSEAGSPgaylvDFFpflrylpswLGAPW--KRKARELRELtRRLYEGPFEAAKERMASGTA-TPS--FVKDLLEElD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 287 KRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDI-KIDDIQKLKVMENFIYESMR 365
Cdd:cd11065   215 KEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLpTFEDRPNLPYVNAIVKEVLR 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 366 YQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFAKNVPYRYFQP------FGFGPRGC 437
Cdd:cd11065   295 WRPVAPLgIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHdPEVYPDPEEFDPERYLDDPKGTPDPPdpphfaFGFGRRIC 374

                  ....*..
gi 1109516678 438 AGKYIAM 444
Cdd:cd11065   375 PGRHLAE 381
PLN02655 PLN02655
ent-kaurene oxidase
232-497 7.95e-22

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 98.28  E-value: 7.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 DIFFKISWL-YKKYEKSVKDL---KDAI-EVLIAEKRRRISTEEKLEECMDFAteliLAEKRgDLTRENVNQCILEMLIA 306
Cdd:PLN02655  199 DFFPYLSWIpNKSFETRVQTTefrRTAVmKALIKQQKKRIARGEERDCYLDFL----LSEAT-HLTDEQLMMLVWEPIIE 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 307 APDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMR-YQPVVDLVMRKALEDDVIDG 385
Cdd:PLN02655  274 AADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLPYLNAVFHETLRkYSPVPLLPPRFVHEDTTLGG 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 386 YPVKKGTNIILNI-GRMHRLEFFPKPNEFTLENFAkNVPYRYFQ-----PFGFGPRGCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:PLN02655  354 YDIPAGTQIAINIyGCNMDKKRWENPEEWDPERFL-GEKYESADmyktmAFGAGKRVCAGSLQAMLIACMAIARLVQEFE 432
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1109516678 460 VKTLQGQC--VESIQkIHDLSLHPdetknmLEMIFTPRNS 497
Cdd:PLN02655  433 WRLREGDEekEDTVQ-LTTQKLHP------LHAHLKPRGS 465
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
304-461 8.47e-22

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 98.22  E-value: 8.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 304 LIAAPDTMSVSL--FFMLflIAKHPNVEEAIIKEIQTVIGERD--IKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALE 379
Cdd:PLN02426  302 LLAGRDTVASALtsFFWL--LSKHPEVASAIREEADRVMGPNQeaASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAE 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 380 DDVI-DGYPVKKGTNIILN---IGRMHR------LEFFP----KPNEFTLENfaknvPYRY--FQPfgfGPRGCAGKYIA 443
Cdd:PLN02426  380 DDVLpDGTFVAKGTRVTYHpyaMGRMERiwgpdcLEFKPerwlKNGVFVPEN-----PFKYpvFQA---GLRVCLGKEMA 451
                         170
                  ....*....|....*...
gi 1109516678 444 MVMMKAILVTLLRRFHVK 461
Cdd:PLN02426  452 LMEMKSVAVAVVRRFDIE 469
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
300-465 1.79e-21

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


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 96.52  E-value: 1.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 300 ILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKI--DDIQKLKVMENFIYESMRYQPVVDLVMRKA 377
Cdd:cd11042   217 LIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDPLtyDVLKEMPLLHACIKETLRLHPPIHSLMRKA 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 378 LED--DVIDGYPVKKGTNIILNIGRMHRL-EFFPKPNEFTLENFAKNVPY------RYFQPFGFGPRGCAGKYIAMVMMK 448
Cdd:cd11042   297 RKPfeVEGGGYVIPKGHIVLASPAVSHRDpEIFKNPDEFDPERFLKGRAEdskggkFAYLPFGAGRHRCIGENFAYLQIK 376
                         170
                  ....*....|....*..
gi 1109516678 449 AILVTLLRRFHVKTLQG 465
Cdd:cd11042   377 TILSTLLRNFDFELVDS 393
PLN02290 PLN02290
cytokinin trans-hydroxylase
243-458 3.86e-21

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 96.42  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 243 KYEKSVKDLKDAIEVLIAE---KRRRISTEEKLEECMDFATELILAEKrgDLTRENVNQCILEMLI--------AAPDTM 311
Cdd:PLN02290  255 KYNREIKSLKGEVERLLMEiiqSRRDCVEIGRSSSYGDDLLGMLLNEM--EKKRSNGFNLNLQLIMdecktfffAGHETT 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 312 SVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKG 391
Cdd:PLN02290  333 ALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPKG 412
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109516678 392 TNIILNIGRMHRLE--FFPKPNEFTLENFAKN--VPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:PLN02290  413 LSIWIPVLAIHHSEelWGKDANEFNPDRFAGRpfAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKF 483
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
225-469 3.99e-21

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: 95.34  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 225 QALLIKPDIFFKISWLYKKyeKSVKDLKDAIEvLIAEK-RRRISTEEkleECMDFATELILA-EKRGDLTRENVN-QCIL 301
Cdd:cd11058   151 QALRRYPWLLRLLRLLIPK--SLRKKRKEHFQ-YTREKvDRRLAKGT---DRPDFMSYILRNkDEKKGLTREELEaNASL 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 eMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVI-GERDIKIDDIQKLKVMENFIYESMR-YQPVVDLVMRKALE 379
Cdd:cd11058   225 -LIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFsSEDDITLDSLAQLPYLNAVIQEALRlYPPVPAGLPRVVPA 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 380 D-DVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFAKNVPYRY-------FQPFGFGPRGCAGKYIAMVMMKAI 450
Cdd:cd11058   304 GgATIDGQFVPGGTSVSVSQWAAYRSPrNFHDPDEFIPERWLGDPRFEFdndkkeaFQPFSVGPRNCIGKNLAYAEMRLI 383
                         250
                  ....*....|....*....
gi 1109516678 451 LVTLLRRFHVKtLQGQCVE 469
Cdd:cd11058   384 LAKLLWNFDLE-LDPESED 401
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
139-465 4.07e-21

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: 95.77  E-value: 4.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 139 ELWKTTRPFFMKALSGPGLVRMVTVCAE-SLKTHLDRL-EEVTNESGYVDVLTLLRRVMLdtsnTLFLRI----PLDESA 212
Cdd:cd11075    62 PLWRTLRRNLVSEVLSPSRLKQFRPARRrALDNLVERLrEEAKENPGPVNVRDHFRHALF----SLLLYMcfgeRLDEET 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 213 I--VVKIQ----------GYFDAWQALLIkpdIFFKISWlyKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDF-- 278
Cdd:cd11075   138 VreLERVQrelllsftdfDVRDFFPALTW---LLNRRRW--KKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFll 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 279 --ATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKV 355
Cdd:cd11075   213 ldLLDLKEEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGdEAVVTEEDLPKMPY 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 356 MENFIYESMR-YQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR--------LEFfpKPNEFTLENFAKNVP--- 423
Cdd:cd11075   293 LKAVVLETLRrHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRdpkvwedpEEF--KPERFLAGGEAADIDtgs 370
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1109516678 424 --YRyFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQG 465
Cdd:cd11075   371 keIK-MMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEG 413
PTZ00404 PTZ00404
cytochrome P450; Provisional
77-489 5.09e-21

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 95.94  E-value: 5.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  77 YNRVYGEFMRVWISGEETLIISKS---SSMFhIMKHNHYSSRfgSKLGLQCIGMHEKGIIFNNNpELWKTTRPFFMKALS 153
Cdd:PTZ00404   57 MSKKYGGIFRIWFADLYTVVLSDPiliREMF-VDNFDNFSDR--PKIPSIKHGTFYHGIVTSSG-EYWKRNREIVGKAMR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 154 GPGLVRM-------VTVCAESLKTHldrleEVTNESgyVDVLTLLRRVMLDTSNTLFLR--IPLDESAIVVKIQ------ 218
Cdd:PTZ00404  133 KTNLKHIydllddqVDVLIESMKKI-----ESSGET--FEPRYYLTKFTMSAMFKYIFNedISFDEDIHNGKLAelmgpm 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 219 -------GYFDAWQALLIKPDIFFKisWLyKKYEKSVKDLKDAIEVLIAEKRRRISTEeKLEECMDfatelILAEKRGDL 291
Cdd:PTZ00404  206 eqvfkdlGSGSLFDVIEITQPLYYQ--YL-EHTDKNFKKIKKFIKEKYHEHLKTIDPE-VPRDLLD-----LLIKEYGTN 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 292 TRE---NVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQ 367
Cdd:PTZ00404  277 TDDdilSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNkVLLSDRQSTPYTVAIIKETLRYK 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 368 PVVDLVMRKALEDDVI--DGYPVKKGTNIILN---IGRMHrlEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYI 442
Cdd:PTZ00404  357 PVSPFGLPRSTSNDIIigGGHFIPKDAQILINyysLGRNE--KYFENPEQFDPSRFLNPDSNDAFMPFSIGPRNCVGQQF 434
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1109516678 443 AMVMMKAILVTLLRRFHVKTLQGQCVESIQkIHDLSLHPDETKNMLE 489
Cdd:PTZ00404  435 AQDELYLAFSNIILNFKLKSIDGKKIDETE-EYGLTLKPNKFKVLLE 480
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
259-481 3.96e-20

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: 92.47  E-value: 3.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 259 IAEKRRRISTEEKLEECMDFATELILAEKR---------GDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVE 329
Cdd:cd20652   189 IIDEHKRRLKPENPRDAEDFELCELEKAKKegedrdlfdGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQ 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 330 EAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMH-RLEF 406
Cdd:cd20652   269 RRIQRELDEVVGRPDlVTLEDLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHmDPNL 348
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1109516678 407 FPKPNEFTLENF----AKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHP 481
Cdd:cd20652   349 WEEPEEFRPERFldtdGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIALPDGQPVDSEGGNVGITLTP 427
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
172-501 5.37e-20

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: 91.98  E-value: 5.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 172 LDRLEEVTNESGYVDVLTLLRRVMLD-TSNTLF-LRIPLDESAIVVKIQGYFDAWQALLIKPDI-----FFKISWLY--- 241
Cdd:cd11059    88 IDRIAKEAGKSGSVDVYPLFTALAMDvVSHLLFgESFGTLLLGDKDSRERELLRRLLASLAPWLrwlprYLPLATSRlii 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 242 KKYEKSVKDLKD-AIEvLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLF 320
Cdd:cd11059   168 GIYFRAFDEIEEwALD-LCARAESSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIW 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 321 LIAKHPNVEEAIIKEIQTVIG--ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDD--VIDGYPVKKGTNI-I 395
Cdd:cd11059   247 ELSRPPNLQEKLREELAGLPGpfRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgaTIGGYYIPGGTIVsT 326
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 396 LNIGrMHRL-EFFPKPNEF---------TLENFAKNvpyRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTlqg 465
Cdd:cd11059   327 QAYS-LHRDpEVFPDPEEFdperwldpsGETAREMK---RAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTST--- 399
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1109516678 466 qcvesiqkihdlslHPDETKNMLEMIFTPRNSDRCL 501
Cdd:cd11059   400 --------------TTDDDMEQEDAFLAAPKGRRCL 421
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
245-458 7.30e-20

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 90.82  E-value: 7.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 245 EKSVKDLKDAIEVLIAEKRRRISTeekleecmDFATELILAEKRG-DLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIA 323
Cdd:cd20629   149 EAAAAELYDYVLPLIAERRRAPGD--------DLISRLLRAEVEGeKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLL 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 324 KHPNVEEAiikeiqtVIGERDIkiddIQKLkvmenfIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR 403
Cdd:cd20629   221 QHPEQLER-------VRRDRSL----IPAA------IEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANR 283
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1109516678 404 LE-FFPKPNEFTLenfaknvpYRYFQP---FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20629   284 DEdVYPDPDVFDI--------DRKPKPhlvFGGGAHRCLGEHLARVELREALNALLDRL 334
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
304-462 7.92e-20

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: 91.82  E-value: 7.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 304 LIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQtVIGERDIKID--DIQKLKVMENFIYESMRYQPVVDLVMRKALEDD 381
Cdd:cd20649   270 LIAGYETTTNTLSFATYLLATHPECQKKLLREVD-EFFSKHEMVDyaNVQELPYLDMVIAETLRMYPPAFRFAREAAEDC 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 382 VIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENF-----AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLL 455
Cdd:cd20649   349 VVLGQRIPAGAVLEIPVGFLHHdPEHWPEPEKFIPERFtaeakQRRHPFVYL-PFGAGPRSCIGMRLALLEIKVTLLHIL 427

                  ....*..
gi 1109516678 456 RRFHVKT 462
Cdd:cd20649   428 RRFRFQA 434
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
239-458 4.86e-19

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: 89.20  E-value: 4.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 239 WL-YKKYEKSVKDL---KDAI-EVLIAEKRRRIsteEKLEECMdFATELILAEKRGDL-TRENVNQCILEMLIAAPDTMS 312
Cdd:cd20653   169 WFdFQGLEKRVKKLakrRDAFlQGLIDEHRKNK---ESGKNTM-IDHLLSLQESQPEYyTDEIIKGLILVMLLAGTDTSA 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 313 VSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPVVD-LVMRKALEDDVIDGYPVKK 390
Cdd:cd20653   245 VTLEWAMSNLLNHPEVLKKAREEIDTQVGQdRLIEESDLPKLPYLQNIISETLRLYPAAPlLVPHESSEDCKIGGYDIPR 324
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 391 GTNIILNIGRMHR-LEFFPKPNEFTLENFAKNVPYRY-FQPFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20653   325 GTMLLVNAWAIHRdPKLWEDPTKFKPERFEGEEREGYkLIPFGLGRRACPGAGLAQRVVGLALGSLIQCF 394
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
75-466 5.00e-19

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: 89.35  E-value: 5.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  75 NYYNRvyGEFMRVWISGEETLIISKSSSMFHIMKHNHYSS------RFGSKL-GLQCIGMHEKGIIFNNNpeLWKTTRPF 147
Cdd:cd11040     7 KYFSG--GPIFTIRLGGQKIYVITDPELISAVFRNPKTLSfdpiviVVVGRVfGSPESAKKKEGEPGGKG--LIRLLHDL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 148 FMKALSGP-GLVRMVTVCAESLKTHLDRLE-EVTNESGYVDVLTLLRRVMLD-TSNTLFLRIPLDESAIVVKiqgYFDAW 224
Cdd:cd11040    83 HKKALSGGeGLDRLNEAMLENLSKLLDELSlSGGTSTVEVDLYEWLRDVLTRaTTEALFGPKLPELDPDLVE---DFWTF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 225 QALLIKpdIFFKISWLYKKYEKSVKD-LKDAIEVLIAEKRrristeEKLEECMDFATELILAEKRGDLTRENVNQCILEM 303
Cdd:cd11040   160 DRGLPK--LLLGLPRLLARKAYAARDrLLKALEKYYQAAR------EERDDGSELIRARAKVLREAGLSEEDIARAELAL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 304 LIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD---IKIDDIQKLK---VMENFIYESMRYQpVVDLVMRKA 377
Cdd:cd11040   232 LWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSgtnAILDLTDLLTscpLLDSTYLETLRLH-SSSTSVRLV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 378 LEDDV-IDGYPVKKGTNIILNIGRMHRL-EFFPK-PNEFTLENFAKNVP-------YRYFQPFGFGPRGCAGKYIAMVMM 447
Cdd:cd11040   311 TEDTVlGGGYLLRKGSLVMIPPRLLHMDpEIWGPdPEEFDPERFLKKDGdkkgrglPGAFRPFGGGASLCPGRHFAKNEI 390
                         410
                  ....*....|....*....
gi 1109516678 448 KAILVTLLRRFHVKTLQGQ 466
Cdd:cd11040   391 LAFVALLLSRFDVEPVGGG 409
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
208-460 1.44e-18

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: 87.83  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 208 LDESAIVVKIQGYfdawqallikpdIFFKISWLY------KKYEKS---VKDLKDAIevlIAEKRRRISTEEKLEE---- 274
Cdd:cd20679   153 LELSALVVKRQQQ------------LLLHLDFLYyltadgRRFRRAcrlVHDFTDAV---IQERRRTLPSQGVDDFlkak 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 275 ----CMDFATELILA--EKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD---I 345
Cdd:cd20679   218 akskTLDFIDVLLLSkdEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREpeeI 297
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 346 KIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVI-DGYPVKKGTNIILNI-GRMHRLEFFPKPN-----EFTLENF 418
Cdd:cd20679   298 EWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIyGTHHNPTVWPDPEvydpfRFDPENS 377
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1109516678 419 AKNVPYRyFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHV 460
Cdd:cd20679   378 QGRSPLA-FIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRV 418
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
157-458 2.32e-18

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: 87.12  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 157 LVRMVTVCAESLKTHLDRLEEV--TNESGYVDVLTLLRRVMLDT-SNTLFLRiPLDESAIVVKIQG-----YFDAWQALL 228
Cdd:cd20639    85 LKRLVPHVVKSVADMLDKWEAMaeAGGEGEVDVAEWFQNLTEDViSRTAFGS-SYEDGKAVFRLQAqqmllAAEAFRKVY 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 229 IKPDIFF-----KISW-LYKKYEKSVKDLkdaievliAEKRRRISTEEKLEECM-DFATELILAEKRGDLTRENVNQCIL 301
Cdd:cd20639   164 IPGYRFLptkknRKSWrLDKEIRKSLLKL--------IERRQTAADDEKDDEDSkDLLGLMISAKNARNGEKMTVEEIIE 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 E---MLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDI-KIDDIQKLKVMENFIYESMR-YQPVVDLVmRK 376
Cdd:cd20639   236 EcktFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVpTKDHLPKLKTLGMILNETLRlYPPAVATI-RR 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 377 ALEDDVIDGYPVKKGTNIILNIGRMHRLE--FFPKPNEFTLENFAKNVPYRY-----FQPFGFGPRGCAGKYIAMVMMKA 449
Cdd:cd20639   315 AKKDVKLGGLDIPAGTELLIPIMAIHHDAelWGNDAAEFNPARFADGVARAAkhplaFIPFGLGPRTCVGQNLAILEAKL 394

                  ....*....
gi 1109516678 450 ILVTLLRRF 458
Cdd:cd20639   395 TLAVILQRF 403
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
171-444 2.89e-18

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


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 86.92  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 171 HLDRLEEVT-NESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQgYFDAWQALLIKPdIFFKISWLYKKYeKSVK 249
Cdd:cd11082    88 HLAKWLENSkSGDKPIEMRPLIRDLNLETSQTVFVGPYLDDEARRFRID-YNYFNVGFLALP-VDFPGTALWKAI-QARK 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 250 DLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEK----------RGDLTRENVNQCILEMLIAAPDTMSVSLFFML 319
Cdd:cd11082   165 RIVKTLEKCAAKSKKRMAAGEEPTCLLDFWTHEILEEIkeaeeegeppPPHSSDEEIAGTLLDFLFASQDASTSSLVWAL 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 320 FLIAKHPNVEEAIIKEIQTVIGERDIKI--DDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVI-DGYPVKKGTNIIL 396
Cdd:cd11082   245 QLLADHPDVLAKVREEQARLRPNDEPPLtlDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLtEDYTVPKGTIVIP 324
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1109516678 397 NIGRMHRlEFFPKPNEFTLENF----------AKNvpyryFQPFGFGPRGCAGKYIAM 444
Cdd:cd11082   325 SIYDSCF-QGFPEPDKFDPDRFsperqedrkyKKN-----FLVFGAGPHQCVGQEYAI 376
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
220-461 4.04e-18

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


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 86.64  E-value: 4.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 220 YFDAWQallikpDIFfkiswlykKYEKSVKDLKdaievlIAEKRRRISTEEKLEEcmDFATELILAEKrgdLTRENVNQC 299
Cdd:cd20646   183 YVDAWD------TIF--------SFGKKLIDKK------MEEIEERVDRGEPVEG--EYLTYLLSSGK---LSPKEVYGS 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 300 ILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVI-GERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKAL 378
Cdd:cd20646   238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCpGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIV 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 379 EDDVIDG-YPVKKGTNIIL-NIGRMHRLEFFPKPNEFTLENFAKNVPYRY----FQPFGFGPRGCAGKYIAMVMMKAILV 452
Cdd:cd20646   318 EKEVVVGdYLFPKNTLFHLcHYAVSHDETNFPEPERFKPERWLRDGGLKHhpfgSIPFGYGVRACVGRRIAELEMYLALS 397

                  ....*....
gi 1109516678 453 TLLRRFHVK 461
Cdd:cd20646   398 RLIKRFEVR 406
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
234-469 5.95e-18

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 86.37  E-value: 5.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 234 FFKISWLYKKY---------EKSVKDLKDAIEVLIAEKRRRISTEEKLEECM--DFATELILAEKRGD--LTRENVNQCI 300
Cdd:PLN03195  218 FIDPLWKLKKFlnigseallSKSIKVVDDFTYSVIRRRKAEMDEARKSGKKVkhDILSRFIELGEDPDsnFTDKSLRDIV 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 301 LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKI---------------------DDIQKLKVMENF 359
Cdd:PLN03195  298 LNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKALEKERAKEEdpedsqsfnqrvtqfaglltyDSLGKLQYLHAV 377
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 360 IYESMRYQPVVDLVMRKALEDDVI-DGYPVKKG---TNIILNIGRMHRLeFFPKPNEFTLENFAKNVPYRYFQPFGF--- 432
Cdd:PLN03195  378 ITETLRLYPAVPQDPKGILEDDVLpDGTKVKAGgmvTYVPYSMGRMEYN-WGPDAASFKPERWIKDGVFQNASPFKFtaf 456
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1109516678 433 --GPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVE 469
Cdd:PLN03195  457 qaGPRICLGKDSAYLQMKMALALLCRFFKFQLVPGHPVK 495
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
172-482 7.05e-18

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: 85.92  E-value: 7.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 172 LDRLEEVTNESG--YVDVLTLlrrvMLDTSNTLfLRIPLDE-SAIVVKI-QGYFDAWQALLIKPDIFFKIswLYKKYEKS 247
Cdd:cd20643   138 LGLLQDYVNPEAqrFIDAITL----MFHTTSPM-LYIPPDLlRLINTKIwRDHVEAWDVIFNHADKCIQN--IYRDLRQK 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 248 VKDLKDAIEVLiaekrrristeekleecmdfaTELILAEKrgdLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPN 327
Cdd:cd20643   211 GKNEHEYPGIL---------------------ANLLLQDK---LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPN 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 328 VEEAIIKEIQTviGERDIKIDDIQKLK---VMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR- 403
Cdd:cd20643   267 VQEMLRAEVLA--ARQEAQGDMVKMLKsvpLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRd 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 404 LEFFPKPNEFTLENFAKNvPYRYFQP--FGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTlqgQCVESIQKIHDLSLHP 481
Cdd:cd20643   345 PTVFPKPEKYDPERWLSK-DITHFRNlgFGFGPRQCLGRRIAETEMQLFLIHMLENFKIET---QRLVEVKTTFDLILVP 420

                  .
gi 1109516678 482 D 482
Cdd:cd20643   421 E 421
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
241-481 1.23e-17

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: 85.04  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 241 YKKYEK-SVKDLKDAIevliaekrrrISTEEKLEEcmdfatelilAEKRGD-LTRENVNQCILEMLIAAPDTMSVSLFFM 318
Cdd:cd11028   195 LDTYDKgHIRDITDAL----------IKASEEKPE----------EEKPEVgLTDEHIISTVQDLFGAGFDTISTTLQWS 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 319 LFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKKGTNIIL 396
Cdd:cd11028   255 LLYMIRYPEIQEKVQAELDRVIGrERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIpHATTRDTTLNGYFIPKGTVVFV 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 397 NI-GRMHRLEFFPKPNEFTlenfaknvPYRY--------------FQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVK 461
Cdd:cd11028   335 NLwSVNHDEKLWPDPSVFR--------PERFlddnglldktkvdkFLPFGAGRRRCLGEELARMELFLFFATLLQQCEFS 406
                         250       260
                  ....*....|....*....|
gi 1109516678 462 TLQGQCVESiQKIHDLSLHP 481
Cdd:cd11028   407 VKPGEKLDL-TPIYGLTMKP 425
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
294-462 1.25e-17

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: 85.16  E-value: 1.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILeMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQPVVDL 372
Cdd:cd20650   228 EILAQSII-FIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKApPTYDTVMQMEYLDMVVNETLRLFPIAGR 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 373 VMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFAKN-----VPYRYFqPFGFGPRGCAGKYIAMVM 446
Cdd:cd20650   307 LERVCKKDVEINGVFIPKGTVVMIPTYALHRdPQYWPEPEEFRPERFSKKnkdniDPYIYL-PFGSGPRNCIGMRFALMN 385
                         170
                  ....*....|....*.
gi 1109516678 447 MKAILVTLLRRFHVKT 462
Cdd:cd20650   386 MKLALVRVLQNFSFKP 401
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
128-461 1.76e-17

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 84.46  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 128 HEKGIIFNNNpELWKTTRPFFMKALSGPGLVR--MVTVCAESLKTHLDRLEevtnesGYVDVLTLLRRVMLDTSNTLFLR 205
Cdd:cd20671    48 HGNGVFFSSG-ERWRTTRRFTVRSMKSLGMGKrtIEDKILEELQFLNGQID------SFNGKPFPLRLLGWAPTNITFAM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 206 I---PLD-ESAIVVKIQGYFDAWQALLIKP--DIFFKISWL------YKKYEKSVKDLKDAIEVLIAEKRRRISteeklE 273
Cdd:cd20671   121 LfgrRFDyKDPTFVSLLDLIDEVMVLLGSPglQLFNLYPVLgaflklHKPILDKVEEVCMILRTLIEARRPTID-----G 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 274 ECMDFATELILAEKRGDLTRE------NVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDI-K 346
Cdd:cd20671   196 NPLHSYIEALIQKQEEDDPKEtlfhdaNVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLpN 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 347 IDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNII-LNIGRMHRLEFFPKPNEFTLENF----AKN 421
Cdd:cd20671   276 YEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIpLLSSVLLDKTQWETPYQFNPNHFldaeGKF 355
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1109516678 422 VPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVK 461
Cdd:cd20671   356 VKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFL 395
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
78-483 2.74e-17

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 84.36  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  78 NRVYGEFMRVWISGEETLIISKSSSMFHIMKHN--HYSSRFGSKlGLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGP 155
Cdd:PLN03234   58 SKLYGPIFTMKIGGRRLAVISSAELAKELLKTQdlNFTARPLLK-GQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSP 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 156 GLV-RMVTVCAESLKTHLDRLEEVTNESGYVDvltlLRRVMLDTSNTLFLRIPLDE--SAIVVKIQGYFDAW---QALLi 229
Cdd:PLN03234  137 NRVaSFRPVREEECQRMMDKIYKAADQSGTVD----LSELLLSFTNCVVCRQAFGKryNEYGTEMKRFIDILyetQALL- 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 230 kPDIFF-----------KISWLYKKYEKSVKDLKDAIEVLIAE----KRRRISTEEKLEECMDFATELILAEKrgdLTRE 294
Cdd:PLN03234  212 -GTLFFsdlfpyfgfldNLTGLSARLKKAFKELDTYLQELLDEtldpNRPKQETESFIDLLMQIYKDQPFSIK---FTHE 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 295 NVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQPVVDLV 373
Cdd:PLN03234  288 NVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGyVSEEDIPNLPYLKAVIKESLRLEPVIPIL 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 374 M-RKALEDDVIDGYPVKKGTNIILNIGRMHR--LEFFPKPNEFTLENFA---KNVPYR----YFQPFGFGPRGCAGKYIA 443
Cdd:PLN03234  368 LhRETIADAKIGGYDIPAKTIIQVNAWAVSRdtAAWGDNPNEFIPERFMkehKGVDFKgqdfELLPFGSGRRMCPAMHLG 447
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1109516678 444 MVMMKAILVTLLRRFHVKTLQGQCVESIQK--IHDLSLHPDE 483
Cdd:PLN03234  448 IAMVEIPFANLLYKFDWSLPKGIKPEDIKMdvMTGLAMHKKE 489
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
233-481 3.27e-17

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: 83.67  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 233 IFFKISWLY-------KKYEKSVKDLKDAIEVLIAEKRRRISTEEKleecMDFATELIL-------AEKRGDLTRENVNQ 298
Cdd:cd20666   156 LVNICPWLYylpfgpfRELRQIEKDITAFLKKIIADHRETLDPANP----RDFIDMYLLhieeeqkNNAESSFNEDYLFY 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 299 CILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRK 376
Cdd:cd20666   232 IIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGpDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLsIPHM 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 377 ALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFAKN----VPYRYFQPFGFGPRGCAGKYIAMVMMKAIL 451
Cdd:cd20666   312 ASENTVLQGYTIPKGTVIVPNLWSVHRdPAIWEKPDDFMPSRFLDEngqlIKKEAFIPFGIGRRVCMGEQLAKMELFLMF 391
                         250       260       270
                  ....*....|....*....|....*....|
gi 1109516678 452 VTLLRRFHVKTLQGQCVESIQKIHDLSLHP 481
Cdd:cd20666   392 VSLMQSFTFLLPPNAPKPSMEGRFGLTLAP 421
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
292-465 4.54e-17

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 83.32  E-value: 4.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 292 TRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDI-KIDDIQKLKVMENFIYESMRYQPVV 370
Cdd:cd20661   235 SMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMpSFEDKCKMPYTEAVLHEVLRFCNIV 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 371 DL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF----AKNVPYRYFQPFGFGPRGCAGKYIAM 444
Cdd:cd20661   315 PLgIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEkYWSDPEVFHPERFldsnGQFAKKEAFVPFSLGRRHCLGEQLAR 394
                         170       180
                  ....*....|....*....|.
gi 1109516678 445 VMMKAILVTLLRRFHVKTLQG 465
Cdd:cd20661   395 MEMFLFFTALLQRFHLHFPHG 415
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
141-471 6.38e-17

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 82.93  E-value: 6.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 141 WKTTRPFFMKALSGPG-LVRMVTVCAESLKTHLDRLEEVTNESGYV-DVLTLLRR--------VMLDTSNTLFLRIPLDE 210
Cdd:cd20645    66 WQRVRSAFQKKLMKPKeVMKLDGKINEVLADFMGRIDELCDETGRVeDLYSELNKwsfeticlVLYDKRFGLLQQNVEEE 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 211 SAIVVK-IQGYFDAWQALLIKPDIFFKI--SWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKleecMDFATELIlaeK 287
Cdd:cd20645   146 ALNFIKaIKTMMSTFGKMMVTPVELHKRlnTKVWQDHTEAWDNIFKTAKHCIDKRLQRYSQGPA----NDFLCDIY---H 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 288 RGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDI-KIDDIQKLKVMENFIYESMRY 366
Cdd:cd20645   219 DNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTpRAEDLKNMPYLKACLKESMRL 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 367 QPVVDLVMRKALEDDVIDGYPVKKGTNIILNigrMHRL----EFFP-----KPNEFTLENFAKNvPYRYFqPFGFGPRGC 437
Cdd:cd20645   299 TPSVPFTSRTLDKDTVLGDYLLPKGTVLMIN---SQALgsseEYFEdgrqfKPERWLQEKHSIN-PFAHV-PFGIGKRMC 373
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1109516678 438 AGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESI 471
Cdd:cd20645   374 IGRRLAELQLQLALCWIIQKYQIVATDNEPVEML 407
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
240-481 8.22e-17

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 82.47  E-value: 8.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 240 LYKKYeksvkdlkDAIEVLIAEKRRRISTEEKLEEcmDFATELILAEKR----GDLTRENVNQCILEMLIAAPDTMSVSL 315
Cdd:cd20657   179 LHKRF--------DALLTKILEEHKATAQERKGKP--DFLDFVLLENDDngegERLTDTNIKALLLNLFTAGTDTSSSTV 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKKGTN 393
Cdd:cd20657   249 EWALAELIRHPDILKKAQEEMDQVIGrDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLpRIASEACEVDGYYIPKGTR 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 394 IILNIGRMHR-LEFFPKPNEFTLENF-----AK-NVPYRYFQ--PFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQ 464
Cdd:cd20657   329 LLVNIWAIGRdPDVWENPLEFKPERFlpgrnAKvDVRGNDFEliPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPA 408
                         250       260
                  ....*....|....*....|....*..
gi 1109516678 465 GQCVESI----------QKIHDLSLHP 481
Cdd:cd20657   409 GQTPEELnmeeafglalQKAVPLVAHP 435
PLN02966 PLN02966
cytochrome P450 83A1
77-465 9.45e-17

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 82.87  E-value: 9.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  77 YNRVYGEFMRVWISGEETLIISKSSSMFHIMKHN--HYSSRFGSKlGLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSG 154
Cdd:PLN02966   58 WAKKYGPILSYRIGSRTMVVISSAELAKELLKTQdvNFADRPPHR-GHEFISYGRRDMALNHYTPYYREIRKMGMNHLFS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 155 PGLVRMVT-VCAESLKTHLDRLEEVTNESGYVDVLTLlrrvMLDTSNTLFLRIPL--------DESAIVVKIQGYFDAWQ 225
Cdd:PLN02966  137 PTRVATFKhVREEEARRMMDKINKAADKSEVVDISEL----MLTFTNSVVCRQAFgkkynedgEEMKRFIKILYGTQSVL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 226 ALLIKPDIFFKISWL--------YKK--YEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEkrgDLTREN 295
Cdd:PLN02966  213 GKIFFSDFFPYCGFLddlsgltaYMKecFERQDTYIQEVVNETLDPKRVKPETESMIDLLMEIYKEQPFAS---EFTVDN 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 296 VNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKI---DDIQKLKVMENFIYESMRYQPVVDL 372
Cdd:PLN02966  290 VKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTFvteDDVKNLPYFRALVKETLRIEPVIPL 369
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 373 VM-RKALEDDVIDGYPVKKGTNIILNIGRMHR--LEFFPKPNEFTLENF-AKNVPYR----YFQPFGFGPRGCAGKYIAM 444
Cdd:PLN02966  370 LIpRACIQDTKIAGYDIPAGTTVNVNAWAVSRdeKEWGPNPDEFRPERFlEKEVDFKgtdyEFIPFGSGRRMCPGMRLGA 449
                         410       420
                  ....*....|....*....|.
gi 1109516678 445 VMMKAILVTLLRRFHVKTLQG 465
Cdd:PLN02966  450 AMLEVPYANLLLNFNFKLPNG 470
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
128-482 2.52e-16

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


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 81.04  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 128 HEKGIIFNNNPElWKTTRPFFMKALSGPGLVR----MVTVCAESLKTHL-DRLEEVTNESGYVDVLTLLRRVMLDTSNTL 202
Cdd:cd20644    54 HKCGVFLLNGPE-WRFDRLRLNPEVLSPAAVQrflpMLDAVARDFSQALkKRVLQNARGSLTLDVQPDLFRFTLEASNLA 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 203 FL--RIPLDESAIVVKIQGYFDAWQALL--IKPDIFFKISWLYKKYEKSVKDLKDAIEVLI--AEKR-RRISTEEKLEEC 275
Cdd:cd20644   133 LYgeRLGLVGHSPSSASLRFISAVEVMLktTVPLLFMPRSLSRWISPKLWKEHFEAWDCIFqyADNCiQKIYQELAFGRP 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 276 MDFATelILAE--KRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTV---IGERDIKIddI 350
Cdd:cd20644   213 QHYTG--IVAEllLQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAaaqISEHPQKA--L 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 351 QKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENF-AKNVPYRYFQ 428
Cdd:cd20644   289 TELPLLKAALKETLRLYPVGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRsAALFPRPERYDPQRWlDIRGSGRNFK 368
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1109516678 429 --PFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQgqcVESIQKIHDLSLHPD 482
Cdd:cd20644   369 hlAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLS---QEDIKTVYSFILRPE 421
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
242-480 4.06e-16

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 80.93  E-value: 4.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 242 KKYEKSVKDLKDAIEVLI----AEKRRRI----STEEKLEECmdfATELIL-AEKRGDLTRENVNQCILEMLIAAPDTMS 312
Cdd:PLN02394  234 RGYLKICQDVKERRLALFkdyfVDERKKLmsakGMDKEGLKC---AIDHILeAQKKGEINEDNVLYIVENINVAAIETTL 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 313 VSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQ-PVVDLVMRKALEDDVIDGYPVKK 390
Cdd:PLN02394  311 WSIEWGIAELVNHPEIQKKLRDELDTVLGPGNqVTEPDTHKLPYLQAVVKETLRLHmAIPLLVPHMNLEDAKLGGYDIPA 390
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 391 GTNIILN---IGrmHRLEFFPKPNEFTLENF--------AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:PLN02394  391 ESKILVNawwLA--NNPELWKNPEEFRPERFleeeakveANGNDFRFL-PFGVGRRSCPGIILALPILGIVLGRLVQNFE 467
                         250       260
                  ....*....|....*....|..
gi 1109516678 460 VKTLQGQC-VESIQKIHDLSLH 480
Cdd:PLN02394  468 LLPPPGQSkIDVSEKGGQFSLH 489
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
240-461 4.15e-16

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 80.23  E-value: 4.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 240 LYKKYEKsvkdLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRG-DLTRENVNQCILEMLIAAPDTMSVSLFFM 318
Cdd:cd20662   173 VFSNWKK----LKLFVSDMIDKHREDWNPDEPRDFIDAYLKEMAKYPDPTtSFNEENLICSTLDLFFAGTETTSTTLRWA 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 319 LFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIIL 396
Cdd:cd20662   249 LLYMALYPEIQEKVQAEIDRVIGQkRQPSLADRESMPYTNAVIHEVQRMGNIIPLnVPREVAVDTKLAGFHLPKGTMILT 328
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109516678 397 NIGRMHRlefFPK----PNEFTLENFAKNVPYR---YFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVK 461
Cdd:cd20662   329 NLTALHR---DPKewatPDTFNPGHFLENGQFKkreAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFK 397
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
301-464 7.22e-16

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: 79.46  E-value: 7.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 301 LEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKAL 378
Cdd:cd20668   232 LNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRnRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVT 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 379 EDDVIDGYPVKKGTNIILNIGR-MHRLEFFPKPNEFTLENF-------AKNVPyryFQPFGFGPRGCAGKYIAMVMMKAI 450
Cdd:cd20668   312 KDTKFRDFFLPKGTEVFPMLGSvLKDPKFFSNPKDFNPQHFlddkgqfKKSDA---FVPFSIGKRYCFGEGLARMELFLF 388
                         170
                  ....*....|....
gi 1109516678 451 LVTLLRRFHVKTLQ 464
Cdd:cd20668   389 FTTIMQNFRFKSPQ 402
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
263-456 7.74e-16

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: 79.47  E-value: 7.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 263 RRRISTEEKLEECMDfATELILAEKRGD---LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQT- 338
Cdd:cd20638   196 RAKIQREDTEQQCKD-ALQLLIEHSRRNgepLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEk 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 339 ------VIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRL-EFFPKPN 411
Cdd:cd20638   275 gllstkPNENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVaDIFPNKD 354
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1109516678 412 EFTLENFAKNVP---YRY-FQPFGFGPRGCAGKYIAMVMMKAILVTLLR 456
Cdd:cd20638   355 EFNPDRFMSPLPedsSRFsFIPFGGGSRSCVGKEFAKVLLKIFTVELAR 403
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
130-485 8.72e-16

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: 79.29  E-value: 8.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 130 KGIIFNNNPELWKTTRPFFMKALS--GPGLVRMVTVCAESLKTHLDRLEEVTNESgyVDVLTLLRRVMLDTSNTLFLRIP 207
Cdd:cd20673    51 KDIAFADYSATWQLHRKLVHSAFAlfGEGSQKLEKIICQEASSLCDTLATHNGES--IDLSPPLFRAVTNVICLLCFNSS 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 208 LDES-AIVVKIQGYFDAWQALLIKP---DIFfkiSWLYKKYEKSVKDLKDAIEVliaekrRRISTEEKLEECM-----DF 278
Cdd:cd20673   129 YKNGdPELETILNYNEGIVDTVAKDslvDIF---PWLQIFPNKDLEKLKQCVKI------RDKLLQKKLEEHKekfssDS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 279 ATELILAEKRGDLTRENVNQCILE---------MLIAAPD--------TMSVSLFFMLFLIaKHPNVEEAIIKEIQTVIG 341
Cdd:cd20673   200 IRDLLDALLQAKMNAENNNAGPDQdsvglsddhILMTVGDifgagvetTTTVLKWIIAFLL-HNPEVQKKIQEEIDQNIG 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 342 -ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF 418
Cdd:cd20673   279 fSRTPTLSDRNHLPLLEATIREVLRIRPVAPLLIpHVALQDSSIGEFTIPKGTRVVINLWALHHDEkEWDQPDQFMPERF 358
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1109516678 419 AKN------VPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETK 485
Cdd:cd20673   359 LDPtgsqliSPSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGGQLPSLEGKFGVVLQIDPFK 431
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
264-487 1.08e-15

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: 79.07  E-value: 1.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 264 RRISTEEKLEECMD-----FATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQT 338
Cdd:cd20656   194 KAIMEEHTLARQKSgggqqHFVALLTLKEQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDR 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 339 VIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKKGTNIILNIGRMHR--------LEFfp 408
Cdd:cd20656   274 VVGsDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLpHKASENVKIGGYDIPKGANVHVNVWAIARdpavwknpLEF-- 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 409 KPNEFTLENF-AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIqkihDLSLHPDETKNM 487
Cdd:cd20656   352 RPERFLEEDVdIKGHDFRLL-PFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPEGTPPEEI----DMTENPGLVTFM 426
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
264-458 1.09e-15

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: 79.03  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 264 RRISTEEKLEECMDFatelilaekrgdltrenvnqcilemLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGER 343
Cdd:cd20641   229 RKMSIDEIIDECKTF-------------------------FFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKD 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 344 DIKIDD-IQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE--FFPKPNEFTLENFAK 420
Cdd:cd20641   284 KIPDADtLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKevWGSDADEFNPLRFAN 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1109516678 421 NVPYRYFQP-----FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20641   364 GVSRAATHPnallsFSLGPRACIGQNFAMIEAKTVLAMILQRF 406
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
292-463 2.23e-15

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: 78.07  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 292 TRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYqpvV 370
Cdd:cd20665   223 TLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGrHRSPCMQDRSHMPYTDAVIHEIQRY---I 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 371 DLV----MRKALEDDVIDGYPVKKGTNIILNIGR-MHRLEFFPKPNEFTLE-------NFAKNvpyRYFQPFGFGPRGCA 438
Cdd:cd20665   300 DLVpnnlPHAVTCDTKFRNYLIPKGTTVITSLTSvLHDDKEFPNPEKFDPGhfldengNFKKS---DYFMPFSAGKRICA 376
                         170       180
                  ....*....|....*....|....*
gi 1109516678 439 GKYIAMVMMKAILVTLLRRFHVKTL 463
Cdd:cd20665   377 GEGLARMELFLFLTTILQNFNLKSL 401
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
304-461 3.98e-15

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: 77.29  E-value: 3.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 304 LIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG------ERDIKIDD--IQKLKVMENFIYESMRYQPVVdLVMR 375
Cdd:cd11051   194 LFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGpdpsaaAELLREGPelLNQLPYTTAVIKETLRLFPPA-GTAR 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 376 KA-----LEDDVIDGYPVKkGTNIILNIGRMHRLE-FFPKPNEFTLENF------AKNVPYRYFQPFGFGPRGCAGKYIA 443
Cdd:cd11051   273 RGppgvgLTDRDGKEYPTD-GCIVYVCHHAIHRDPeYWPRPDEFIPERWlvdeghELYPPKSAWRPFERGPRNCIGQELA 351
                         170
                  ....*....|....*...
gi 1109516678 444 MVMMKAILVTLLRRFHVK 461
Cdd:cd11051   352 MLELKIILAMTVRRFDFE 369
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
286-458 8.35e-15

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: 76.30  E-value: 8.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 286 EKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESM 364
Cdd:cd20674   217 KGMGQLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGpGASPSYKDRARLPLLNATIAEVL 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 365 RYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNI-GRMHRLEFFPKPNEFTLENFAK-NVPYRYFQPFGFGPRGCAGKY 441
Cdd:cd20674   297 RLRPVVPLaLPHRTTRDSSIAGYDIPKGTVVIPNLqGAHLDETVWEQPHEFRPERFLEpGAANRALLPFGCGARVCLGEP 376
                         170
                  ....*....|....*..
gi 1109516678 442 IAMVMMKAILVTLLRRF 458
Cdd:cd20674   377 LARLELFVFLARLLQAF 393
PLN02500 PLN02500
cytochrome P450 90B1
241-459 8.52e-15

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 76.44  E-value: 8.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 241 YKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFateLILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLF 320
Cdd:PLN02500  228 YRKALKSRATILKFIERKMEERIEKLKEEDESVEEDDL---LGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIF 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 321 LIAKHPNV-----EEAI-IKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNI 394
Cdd:PLN02500  305 FLQGCPKAvqelrEEHLeIARAKKQSGESELNWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKV 384
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109516678 395 ILNIGRMH-RLEFFPKPNEFTLENFAKNVPYR-----------YFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:PLN02500  385 LPVIAAVHlDSSLYDQPQLFNPWRWQQNNNRGgssgsssattnNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFN 461
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
242-459 1.12e-14

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 76.40  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 242 KKYEKSVKDLKDAIevlIAEKRRRISTEEKLEECMDFATELIlaekrgDLTREN---------VNQCILEMLIAAPDTMS 312
Cdd:PLN03112  243 REVEKRVDEFHDKI---IDEHRRARSGKLPGGKDMDFVDVLL------SLPGENgkehmddveIKALMQDMIAAATDTSA 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 313 VSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVD-LVMRKALEDDVIDGYPVKK 390
Cdd:PLN03112  314 VTNEWAMAEVIKNPRVLRKIQEELDSVVGrNRMVQESDLVHLNYLRCVVRETFRMHPAGPfLIPHESLRATTINGYYIPA 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 391 GTNIILNI---GRMHR-----LEFFPK---PNEFTLENFAKNVPYRYFqPFGFGPRGCAGKYIAMVMmkaILVTLLRRFH 459
Cdd:PLN03112  394 KTRVFINThglGRNTKiwddvEEFRPErhwPAEGSRVEISHGPDFKIL-PFSAGKRKCPGAPLGVTM---VLMALARLFH 469
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
252-468 1.15e-14

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: 75.95  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 252 KDAIEVLIAEKRRRISTEEKLEEcmDFATELILAEKrgdLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEA 331
Cdd:cd20648   196 KGHIDRRMAEVAAKLPRGEAIEG--KYLTYFLAREK---LPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTA 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 332 IIKEIQTVIGERDI-KIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDV-IDGYPVKKGTNIILNIGRMHRLE-FFP 408
Cdd:cd20648   271 LHREITAALKDNSVpSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDIqVGEYIIPKKTLITLCHYATSRDEnQFP 350
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1109516678 409 KPNEFTLENFAKNV----PYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCV 468
Cdd:cd20648   351 DPNSFRPERWLGKGdthhPYASL-PFGFGKRSCIGRRIAELEVYLALARILTHFEVRPEPGGSP 413
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
88-474 1.94e-14

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 75.43  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678  88 WISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGlQCIGMHEKGIIfNNNPELWKTTRPFFMKALSGPGLVRM-VTVCAE 166
Cdd:PLN02169   76 WLSGTDMLFTADPKNIHHILSSNFGNYPKGPEFK-KIFDVLGEGIL-TVDFELWEDLRKSNHALFHNQDFIELsLSSNKS 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 167 SLKTHL-DRLEEVTNESGYVDVLTLLRRVMLDTSNTLF------------LRIPLDESAIVVKIQGYFDAWqalliKPDI 233
Cdd:PLN02169  154 KLKEGLvPFLDNAAHENIIIDLQDVFMRFMFDTSSILMtgydpmslsiemLEVEFGEAADIGEEAIYYRHF-----KPVI 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 234 FFKI-SW----LYKKYEKSVKDLKDAIEVLIAEKRR----RISTEEKLEECMDFATEL------ILAEKRGDLTREnvnq 298
Cdd:PLN02169  229 LWRLqNWigigLERKMRTALATVNRMFAKIISSRRKeeisRAETEPYSKDALTYYMNVdtskykLLKPKKDKFIRD---- 304
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 299 CILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGErdikiDDIQKLKVMENFIYESMRYQPVVDLVMRKAL 378
Cdd:PLN02169  305 VIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN-----EDLEKLVYLHAALSESMRLYPPLPFNHKAPA 379
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 379 EDDVI-DGYPVKKGTNIILNI---GRMHR------LEFfpKPNEFTLENFA-KNVPYRYFQPFGFGPRGCAGKYIAMVMM 447
Cdd:PLN02169  380 KPDVLpSGHKVDAESKIVICIyalGRMRSvwgedaLDF--KPERWISDNGGlRHEPSYKFMAFNSGPRTCLGKHLALLQM 457
                         410       420
                  ....*....|....*....|....*..
gi 1109516678 448 KAILVTLLRRFHVKTLQGQCVESIQKI 474
Cdd:PLN02169  458 KIVALEIIKNYDFKVIEGHKIEAIPSI 484
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
294-458 2.39e-14

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: 74.84  E-value: 2.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLV 373
Cdd:cd20664   224 DNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKNMPYTDAVIHEIQRFANIVPMN 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 374 MRKALEDDV-IDGYPVKKGTNII-LNIGRMHRLEFFPKPNEFTLENF----AKNVPYRYFQPFGFGPRGCAGKYIAMVMM 447
Cdd:cd20664   304 LPHATTRDVtFRGYFIPKGTYVIpLLTSVLQDKTEWEKPEEFNPEHFldsqGKFVKRDAFMPFSAGRRVCIGETLAKMEL 383
                         170
                  ....*....|.
gi 1109516678 448 KAILVTLLRRF 458
Cdd:cd20664   384 FLFFTSLLQRF 394
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
231-459 2.64e-14

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 75.03  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 231 PDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRR---RISTEEKLEECMDF--ATELILAEKRGdltRE-NVNQCIL--E 302
Cdd:cd20622   190 PKLSHWFYRNQPSYRRAAKIKDDFLQREIQAIARsleRKGDEGEVRSAVDHmvRRELAAAEKEG---RKpDYYSQVIhdE 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 303 M---LIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-----RDIKIDDIQKLKV--MENFIYESMRYQPVVDL 372
Cdd:cd20622   267 LfgyLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEavaegRLPTAQEIAQARIpyLDAVIEEILRCANTAPI 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 373 VMRKALEDDVIDGYPVKKGTNIIL--NIG-----------------RMHRLEFFPKPNEFTLENFaknVPYR-------- 425
Cdd:cd20622   347 LSREATVDTQVLGYSIPKGTNVFLlnNGPsylsppieidesrrsssSAAKGKKAGVWDSKDIADF---DPERwlvtdeet 423
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1109516678 426 ----------YFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:cd20622   424 getvfdpsagPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFE 467
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
248-463 3.40e-14

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: 74.58  E-value: 3.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 248 VKDLKDAI--EVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKH 325
Cdd:cd20670   177 IEELKDFIasRVKINEASLDPQNPRDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKY 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 326 PNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHR 403
Cdd:cd20670   257 PEVEAKIHEEINQVIGpHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLgVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLK 336
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109516678 404 -LEFFPKPNEFTLEN-------FAKNvpyRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTL 463
Cdd:cd20670   337 dPKYFRYPEAFYPQHfldeqgrFKKN---EAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRSL 401
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
161-456 3.71e-14

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: 74.23  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 161 VTVCAESLKTHLDRLEEVTNESGYVDV-----LTLLRRVM-----------LDTSNTLFLRIPLDESAIVvkiqgyFDAW 224
Cdd:cd20678    88 VKLMADSVRVMLDKWEKLATQDSSLEIfqhvsLMTLDTIMkcafshqgscqLDGRSNSYIQAVSDLSNLI------FQRL 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 225 QALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEEC-----MDFATELILA--EKRGDLTRENVN 297
Cdd:cd20678   162 RNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIkkkrhLDFLDILLFAkdENGKSLSDEDLR 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 298 QCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERD-IKIDDIQKLKVMENFIYESMRYQPVVDLVMRK 376
Cdd:cd20678   242 AEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDsITWEHLDQMPYTTMCIKEALRLYPPVPGISRE 321
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 377 aLEDDVI--DGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFAK-NVPYRY---FQPFGFGPRGCAGKYIAMVMMK- 448
Cdd:cd20678   322 -LSKPVTfpDGRSLPAGITVSLSIYGLHHnPAVWPNPEVFDPLRFSPeNSSKRHshaFLPFSAGPRNCIGQQFAMNEMKv 400

                  ....*...
gi 1109516678 449 AILVTLLR 456
Cdd:cd20678   401 AVALTLLR 408
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
244-460 5.64e-14

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 73.82  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 244 YEKSVKDLKDAIEVL--IAEKRRRISTEEkleecmdfaTELI--LAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFML 319
Cdd:PLN02196  218 FHKSMKARKELAQILakILSKRRQNGSSH---------NDLLgsFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWIL 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 320 FLIAKHPNVEEAIIKEIQTVIGERD----IKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNII 395
Cdd:PLN02196  289 KYLAENPSVLEAVTEEQMAIRKDKEegesLTWEDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVL 368
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 396 ---LNIgrMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAIL--VTLLRRFHV 460
Cdd:PLN02196  369 plfRNI--HHSADIFSDPGKFDPSRFEVAPKPNTFMPFGNGTHSCPGNELAKLEISVLIhhLTTKYRWSI 436
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
242-480 6.45e-14

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: 73.66  E-value: 6.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 242 KKYEKSVKDLKDA-----IEVLIAEKRRRISTEEKLEECMDFATELIL-AEKRGDLTRENVNQCILEMLIAAPDTMSVSL 315
Cdd:cd11074   174 RGYLKICKEVKERrlqlfKDYFVDERKKLGSTKSTKNEGLKCAIDHILdAQKKGEINEDNVLYIVENINVAAIETTLWSI 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQ-PVVDLVMRKALEDDVIDGYPVKKGTN 393
Cdd:cd11074   254 EWGIAELVNHPEIQKKLRDELDTVLGPgVQITEPDLHKLPYLQAVVKETLRLRmAIPLLVPHMNLHDAKLGGYDIPAESK 333
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 394 IILNIGRM-HRLEFFPKPNEFTLENF--------AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQ 464
Cdd:cd11074   334 ILVNAWWLaNNPAHWKKPEEFRPERFleeeskveANGNDFRYL-PFGVGRRSCPGIILALPILGITIGRLVQNFELLPPP 412
                         250
                  ....*....|....*..
gi 1109516678 465 GQC-VESIQKIHDLSLH 480
Cdd:cd11074   413 GQSkIDTSEKGGQFSLH 429
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
292-458 1.34e-13

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: 72.70  E-value: 1.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 292 TRENVNQCILEMLiAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMR-YQPVV 370
Cdd:cd20642   232 TEDVIEECKLFYF-AGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPDFEGLNHLKVVTMILYEVLRlYPPVI 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 371 DLVmrKALEDDVIDG-YPVKKGTNIILNIGRMHR---------LEFfpKPNEFTlENFAKNVPYR--YFqPFGFGPRGCA 438
Cdd:cd20642   311 QLT--RAIHKDTKLGdLTLPAGVQVSLPILLVHRdpelwgddaKEF--NPERFA-EGISKATKGQvsYF-PFGWGPRICI 384
                         170       180
                  ....*....|....*....|
gi 1109516678 439 GKYIAMVMMKAILVTLLRRF 458
Cdd:cd20642   385 GQNFALLEAKMALALILQRF 404
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
145-459 1.40e-13

cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 72.25  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 145 RPFFMKALSGP------GLVRmvTVCAEslktHLDRLEEvtneSGYVDVLT-----LLRRVMLDtsntlFLRIPLDEsai 213
Cdd:cd11078    76 RRLVSRAFTPRriaalePRIR--ELAAE----LLDRLAE----DGRADFVAdfaapLPALVIAE-----LLGVPEED--- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 214 VVKIQGYFDAWQALLIKPDIFFKISWLYKkyekSVKDLKDAIEVLIAEKRRRISTeekleecmDFATELILAEKRGD--L 291
Cdd:cd11078   138 MERFRRWADAFALVTWGRPSEEEQVEAAA----AVGELWAYFADLVAERRREPRD--------DLISDLLAAADGDGerL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 292 TRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIiKEIQTVIGerdikiddiqklkvmeNFIYESMRYQPVVD 371
Cdd:cd11078   206 TDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRL-RADPSLIP----------------NAVEETLRYDSPVQ 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 372 LVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTL--ENFAKNVpyryfqPFGFGPRGCAGKYIAMVMMK 448
Cdd:cd11078   269 GLRRTATRDVEIGGVTIPAGARVLLLFGSANRDErVFPDPDRFDIdrPNARKHL------TFGHGIHFCLGAALARMEAR 342
                         330
                  ....*....|.
gi 1109516678 449 AILVTLLRRFH 459
Cdd:cd11078   343 IALEELLRRLP 353
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
262-481 2.72e-13

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: 71.79  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 262 KRRRISTEEKLEECMDFATELILAEKR---GDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQT 338
Cdd:cd20667   189 IRHELRTNEAPQDFIDCYLAQITKTKDdpvSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 339 VIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGR-MHRLEFFPKPNEFTL 415
Cdd:cd20667   269 VLGaSQLICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCVTSTTMHGYYVEKGTIILPNLASvLYDPECWETPHKFNP 348
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 416 ENFA-KNVPYRY---FQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHP 481
Cdd:cd20667   349 GHFLdKDGNFVMneaFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQLPEGVQELNLEYVFGGTLQP 418
PLN02687 PLN02687
flavonoid 3'-monooxygenase
242-481 2.83e-13

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 71.77  E-value: 2.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 242 KKYEKSVKDLKDAIevlIAEkrRRISTEEKLEECMDFATELI-------LAEKRGDLTRENVNQCILEMLIAAPDTMSVS 314
Cdd:PLN02687  242 KRLHRRFDAMMNGI---IEE--HKAAGQTGSEEHKDLLSTLLalkreqqADGEGGRITDTEIKALLLNLFTAGTDTTSST 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 315 LFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKKGT 392
Cdd:PLN02687  317 VEWAIAELIRHPDILKKAQEELDAVVGrDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLpRMAAEECEINGYHIPKGA 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 393 NIILNIGRMHR-LEFFPKPNEFTLENFAK-------NVPYRYFQ--PFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKT 462
Cdd:PLN02687  397 TLLVNVWAIARdPEQWPDPLEFRPDRFLPggehagvDVKGSDFEliPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWEL 476
                         250       260
                  ....*....|....*....|....*....
gi 1109516678 463 LQGQCVE----------SIQKIHDLSLHP 481
Cdd:PLN02687  477 ADGQTPDklnmeeayglTLQRAVPLMVHP 505
PLN00168 PLN00168
Cytochrome P450; Provisional
294-473 8.05e-13

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 70.36  E-value: 8.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCIlEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKI--DDIQKLKVMENFIYESMRYQPVVD 371
Cdd:PLN00168  306 EIVNLCS-EFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEVseEDVHKMPYLKAVVLEGLRKHPPAH 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 372 LVM-RKALEDDVIDGYPVKKGTNIILNIGRMHRLEF-FPKPNEFTLENF-------------AKNVpyrYFQPFGFGPRG 436
Cdd:PLN00168  385 FVLpHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEReWERPMEFVPERFlaggdgegvdvtgSREI---RMMPFGVGRRI 461
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1109516678 437 CAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQK 473
Cdd:PLN00168  462 CAGLGIAMLHLEYFVANMVREFEWKEVPGDEVDFAEK 498
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
300-464 1.11e-12

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: 69.79  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 300 ILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKAL 378
Cdd:cd20669   231 THNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGrNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAV 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 379 EDDV-IDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFA------KNVPyrYFQPFGFGPRGCAGKYIAMVMMKAI 450
Cdd:cd20669   311 TRDTnFRGFLIPKGTDVIPLLNSVHYdPTQFKDPQEFNPEHFLddngsfKKND--AFMPFSAGKRICLGESLARMELFLY 388
                         170
                  ....*....|....
gi 1109516678 451 LVTLLRRFHVKTLQ 464
Cdd:cd20669   389 LTAILQNFSLQPLG 402
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
294-460 1.14e-12

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: 69.81  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDL 372
Cdd:cd20672   225 QNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGsHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPI 304
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 373 -VMRKALEDDVIDGYPVKKGTNI--ILNiGRMHRLEFFPKPNEFTLENF-------AKNvpyRYFQPFGFGPRGCAGKYI 442
Cdd:cd20672   305 gVPHRVTKDTLFRGYLLPKNTEVypILS-SALHDPQYFEQPDTFNPDHFldangalKKS---EAFMPFSTGKRICLGEGI 380
                         170
                  ....*....|....*...
gi 1109516678 443 AMVMMKAILVTLLRRFHV 460
Cdd:cd20672   381 ARNELFLFFTTILQNFSV 398
PLN02971 PLN02971
tryptophan N-hydroxylase
259-479 1.37e-12

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 70.07  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 259 IAEKRRRISTEEKLEECMDFATELI-LAEKRGD--LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKE 335
Cdd:PLN02971  288 IIDERIKMWREGKRTQIEDFLDIFIsIKDEAGQplLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEE 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 336 IQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKKGTNIILN---IGRMHR-----LE 405
Cdd:PLN02971  368 IDRVVGkERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLpHVALSDTTVAGYHIPKGSQVLLSrygLGRNPKvwsdpLS 447
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109516678 406 FFPKP--NEFTLENFAKNvpYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQC-VESIQKIHDLSL 479
Cdd:PLN02971  448 FKPERhlNECSEVTLTEN--DLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETrVELMESSHDMFL 522
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
251-456 1.66e-12

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 69.09  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 251 LKDAIEVLIAEKRRRisteEKLEECMDFATELILAEKRGD--LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNV 328
Cdd:cd20636   185 LHEYMEKAIEEKLQR----QQAAEYCDALDYMIHSARENGkeLTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSA 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 329 EEAIIKEI-------QTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRM 401
Cdd:cd20636   261 IEKIRQELvshglidQCQCCPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDT 340
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1109516678 402 HRL-EFFPKPNEFTLENF------AKNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTLLR 456
Cdd:cd20636   341 HETaAVYQNPEGFDPDRFgvereeSKSGRFNYI-PFGGGVRSCIGKELAQVILKTLAVELVT 401
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
214-458 5.53e-12

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 67.70  E-value: 5.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 214 VVKIQGYFDAWQALLikpdiffkiSWLYKKYEKSVKDLKDAIEVLIaeKRRRISTEEKLEECMDFATELILAEKrgDLTR 293
Cdd:PLN02987  199 VLVIEGFFSVPLPLF---------STTYRRAIQARTKVAEALTLVV--MKRRKEEEEGAEKKKDMLAALLASDD--GFSD 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPnVEEAIIKE----IQTVIGERD-IKIDDIQKLKVMENFIYESMRYQP 368
Cdd:PLN02987  266 EEIVDFLVALLVAGYETTSTIMTLAVKFLTETP-LALAQLKEehekIRAMKSDSYsLEWSDYKSMPFTQCVVNETLRVAN 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 369 VVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMH-RLEFFPKPNEFT----LENFAKNVPYRYFQPFGFGPRGCAGKYIA 443
Cdd:PLN02987  345 IIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHlDHEYFKDARTFNpwrwQSNSGTTVPSNVFTPFGGGPRLCPGYELA 424
                         250
                  ....*....|....*
gi 1109516678 444 MVMMKAILVTLLRRF 458
Cdd:PLN02987  425 RVALSVFLHRLVTRF 439
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
294-466 5.95e-12

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 67.41  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 294 ENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPVVDL 372
Cdd:cd20663   229 ENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQvRRPEMADQARMPYTNAVIHEVQRFGDIVPL 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 373 -VMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF----AKNVPYRYFQPFGFGPRGCAGKYIAMVM 446
Cdd:cd20663   309 gVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDEtVWEKPLRFHPEHFldaqGHFVKPEAFMPFSAGRRACLGEPLARME 388
                         170       180
                  ....*....|....*....|
gi 1109516678 447 MKAILVTLLRRFHVKTLQGQ 466
Cdd:cd20663   389 LFLFFTCLLQRFSFSVPAGQ 408
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
253-458 7.46e-12

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 66.68  E-value: 7.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 253 DAIEVLIAEkRRRISTEEkleecmDFATELILAEKRGD-LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEA 331
Cdd:cd20630   167 ALIEEVIAE-RRQAPVED------DLLTTLLRAEEDGErLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 332 IIKEIQTvigerdikiddiqklkvMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPK 409
Cdd:cd20630   240 VKAEPEL-----------------LRNALEEVLRWDNFGKMgTARYATEDVELCGVTIRKGQMVLLLLPSALRdEKVFSD 302
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1109516678 410 PNEFTLEnfaknvpyRYFQP---FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20630   303 PDRFDVR--------RDPNAniaFGYGPHFCIGAALARLELELAVSTLLRRF 346
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
245-458 1.10e-11

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 66.42  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 245 EKSVKDLKDAIEVLIAEKRRRISTeekleecmDFATELILAEKRGD-LTR-ENVNQCILeMLIAAPDTmSVSLFF--MLF 320
Cdd:cd20625   158 NAAAAELAAYFRDLIARRRADPGD--------DLISALVAAEEDGDrLSEdELVANCIL-LLVAGHET-TVNLIGngLLA 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 321 LiAKHPnveeaiikeiqtvigerdikiDDIQKLK----VMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIIL 396
Cdd:cd20625   228 L-LRHP---------------------EQLALLRadpeLIPAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLL 285
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1109516678 397 NIGRMHR-LEFFPKPNEFTLEnfaknvpyRYFQP---FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20625   286 LLGAANRdPAVFPDPDRFDIT--------RAPNRhlaFGAGIHFCLGAPLARLEAEIALRALLRRF 343
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
239-485 1.59e-11

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 66.24  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 239 WLYKKYEKSVKDLKDAIEVL---IAEKRRRISTEEKLEECMDFATELI-LAEKRGD--LTRENVNQCILEMLIAAPDTMS 312
Cdd:cd20658   175 LDLDGHEKIVREAMRIIRKYhdpIIDERIKQWREGKKKEEEDWLDVFItLKDENGNplLTPDEIKAQIKELMIAAIDNPS 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 313 VSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKK 390
Cdd:cd20658   255 NAVEWALAEMLNQPEILRKATEELDRVVGkERLVQESDIPNLNYVKACAREAFRLHPVAPFNVpHVAMSDTTVGGYFIPK 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 391 GTNIILN---IGRmhRLEFFPKPNEFTLE---NFAKNV----PYRYFQPFGFGPRGCAGKYIAMVMMkailVTLLRRFhv 460
Cdd:cd20658   335 GSHVLLSrygLGR--NPKVWDDPLKFKPErhlNEDSEVtltePDLRFISFSTGRRGCPGVKLGTAMT----VMLLARL-- 406
                         250       260
                  ....*....|....*....|....*
gi 1109516678 461 ktLQGqcvesiqkiHDLSLHPDETK 485
Cdd:cd20658   407 --LQG---------FTWTLPPNVSS 420
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
291-465 1.67e-11

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 66.41  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 291 LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPV 369
Cdd:PLN00110  285 LTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRnRRLVESDLPKLPYLQAICKESFRKHPS 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 370 VDLVM-RKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENF-----AKNVPY-RYFQ--PFGFGPRGCAG 439
Cdd:PLN00110  365 TPLNLpRVSTQACEVNGYYIPKNTRLSVNIWAIGRdPDVWENPEEFRPERFlseknAKIDPRgNDFEliPFGAGRRICAG 444
                         170       180
                  ....*....|....*....|....*.
gi 1109516678 440 KYIAMVMMKAILVTLLRRFHVKTLQG 465
Cdd:PLN00110  445 TRMGIVLVEYILGTLVHSFDWKLPDG 470
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
150-457 2.39e-11

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: 65.44  E-value: 2.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 150 KALSGPGLVRMVtVCAESLKTHLDRLEEVTNESGY--VD-VLTLLRRVMLDTSNTLF-LRIPLDESAI-VVKIQGYFDAW 224
Cdd:cd20612    68 KALYSPDLAKDV-VFFYELQTRALLVESSRLGGSGgqVDiVRDVANLVPARFCADLFgLPLKTKENPRgGYTEAELYRAL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 225 QALLIkpDIFFkiswlykkyeksvkdlkdAIEVLIAEKRRRISteekleecMDFATELilaekrGDLTRENVNQCILEML 304
Cdd:cd20612   147 AAIFA--YIFF------------------DLDPAKSFQLRRAA--------QAAAARL------GALLDAAVADEVRDNV 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 305 IaapdtmsvslffmLFLIAKHPNVEEAIIKEIQTVIGERDIK-IDDIQKL--------KVMENFIYESMRYQPVVDLVMR 375
Cdd:cd20612   193 L-------------GTAVGGVPTQSQAFAQILDFYLRRPGAAhLAEIQALarendeadATLRGYVLEALRLNPIAPGLYR 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 376 KALEDDVID-----GYPVKKGTNIILNIGR-MHRLEFFPKPNEFTLENfaknvPYRYFQPFGFGPRGCAGKYIAMVMMKA 449
Cdd:cd20612   260 RATTDTTVAdgggrTVSIKAGDRVFVSLASaMRDPRAFPDPERFRLDR-----PLESYIHFGHGPHQCLGEEIARAALTE 334

                  ....*...
gi 1109516678 450 ILVTLLRR 457
Cdd:cd20612   335 MLRVVLRL 342
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
240-462 4.90e-11

cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is an all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of similar metabolites as CYP26A1. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. In rats, CYP26B1 regulates sex-specific timing of meiotic initiation, independent of RA signaling. CYP26B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 64.49  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 240 LYKKYEKSV---------KDLKDAIEVLIaEKRRRISTEEKLEECMDFATELILAEkrgdltrenvnqcilemlIAAPDT 310
Cdd:cd20637   184 LQKSLEKAIreklqgtqgKDYADALDILI-ESAKEHGKELTMQELKDSTIELIFAA------------------FATTAS 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 311 MSVSLFFMLFliaKHPNVEEAIIKEIQT-------VIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVI 383
Cdd:cd20637   245 ASTSLIMQLL---KHPGVLEKLREELRSngilhngCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFEL 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 384 DGYPVKKGTNIILNIGRMH-RLEFFPKPNEFTLENFA------KNVPYRYFqPFGFGPRGCAGKYIAMVMMKAILVTL-- 454
Cdd:cd20637   322 DGFQIPKGWSVLYSIRDTHdTAPVFKDVDAFDPDRFGqersedKDGRFHYL-PFGGGVRTCLGKQLAKLFLKVLAVELas 400

                  ....*...
gi 1109516678 455 LRRFHVKT 462
Cdd:cd20637   401 TSRFELAT 408
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
166-458 5.48e-11

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: 64.25  E-value: 5.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 166 ESLKTHLDRLeevtNESGYVDVLTLLRRVMLD-TSNTLFLR--IPLDESAIVVKIQGY--FDA---WQALLikPDIFFK- 236
Cdd:cd20635    93 EEFKEQLELL----GSEGTGDLNDLVRHVMYPaVVNNLFGKglLPTSEEEIKEFEEHFvkFDEqfeYGSQL--PEFFLRd 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 237 ----ISWLYKKYEKSVKDLKDaievliaekrrristEEKLEECMDFATELILAEKRGDLTrenVNQCILEMLIAAPDTMS 312
Cdd:cd20635   167 wsssKQWLLSLFEKVVPDAEK---------------TKPLENNSKTLLQHLLDTVDKENA---PNYSLLLLWASLANAIP 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 313 VSlFFMLFLIAKHPNVEEAIIKEIQTVIGERD---IKI--DDIQKLKVMENFIYESMRYQPVvDLVMRKALEDDVIDGYP 387
Cdd:cd20635   229 IT-FWTLAFILSHPSVYKKVMEEISSVLGKAGkdkIKIseDDLKKMPYIKRCVLEAIRLRSP-GAITRKVVKPIKIKNYT 306
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109516678 388 VKKGTNIILNIGRMHR-LEFFPKPNEFTLE-----NFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20635   307 IPAGDMLMLSPYWAHRnPKYFPDPELFKPErwkkaDLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKY 383
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
240-397 8.08e-11

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


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 63.87  E-value: 8.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 240 LYKKYEKSVKDLKDAIEVLIAEKRRRISTEeKLEECMDFATELILAEKRGD----LTRENVNQCILEMLIAAPDTMSVSL 315
Cdd:cd20675   177 VFRNFKQLNREFYNFVLDKVLQHRETLRGG-APRDMMDAFILALEKGKSGDsgvgLDKEYVPSTVTDIFGASQDTLSTAL 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDV-IDGYPVKKGTN 393
Cdd:cd20675   256 QWILLLLVRYPDVQARLQEELDRVVGrDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTIPHATTADTsILGYHIPKDTV 335

                  ....
gi 1109516678 394 IILN 397
Cdd:cd20675   336 VFVN 339
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
232-458 8.64e-11

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 63.54  E-value: 8.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 232 DIFFKISWLYK----KYEKSVKDLKDAIEVLIaEKRRRISTEekleecmDFATELILAEKRGD-LTRENVNQCILEMLIA 306
Cdd:cd11038   154 DLGLAFGLEVKdhlpRIEAAVEELYDYADALI-EARRAEPGD-------DLISTLVAAEQDGDrLSDEELRNLIVALLFA 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 307 APDTMSVSLFFMLFLIAKHPNVEEAIikeiqtviGERDikiDDIqklkvmENFIYESMRYQPVVDLVMRKALEDDVIDGY 386
Cdd:cd11038   226 GVDTTRNQLGLAMLTFAEHPDQWRAL--------REDP---ELA------PAAVEEVLRWCPTTTWATREAVEDVEYNGV 288
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1109516678 387 PVKKGTNIILNIGRMHRleffpKPNEFTLENF---AKNVPyryfqPFGF--GPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11038   289 TIPAGTVVHLCSHAANR-----DPRVFDADRFditAKRAP-----HLGFggGVHHCLGAFLARAELAEALTVLARRL 355
PLN02183 PLN02183
ferulate 5-hydroxylase
240-458 2.14e-10

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 62.95  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 240 LYKKYEKSVKDLKDAIEVLIAE---KRRRISTEEKLEEC--------MDFATELILAEKRGDL------TRENVNQCILE 302
Cdd:PLN02183  232 LNKRLVKARKSLDGFIDDIIDDhiqKRKNQNADNDSEEAetdmvddlLAFYSEEAKVNESDDLqnsiklTRDNIKAIIMD 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 303 MLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDD 381
Cdd:PLN02183  312 VMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDA 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 382 VIDGYPVKKGTNIILN---IGRMHRLefFPKPNEFTLENFAK-NVP-----YRYFQPFGFGPRGCAGKYIAMVMMKAILV 452
Cdd:PLN02183  392 EVAGYFIPKRSRVMINawaIGRDKNS--WEDPDTFKPSRFLKpGVPdfkgsHFEFIPFGSGRRSCPGMQLGLYALDLAVA 469

                  ....*.
gi 1109516678 453 TLLRRF 458
Cdd:PLN02183  470 HLLHCF 475
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
247-477 1.15e-09

cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410685 [Multi-domain]  Cd Length: 425  Bit Score: 60.34  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 247 SVKDLKDAIEVLIAEkRRRISTEEKLEECMDFATELILAEK--RGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAK 324
Cdd:cd11062   175 VFLDFQESIAKQVDE-VLRQVSAGDPPSIVTSLFHALLNSDlpPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLS 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 325 HPNVEEAIIKEIQTVIGERDIKID--DIQKLKVMENFIYESMRYQPVVdlVMRKAL----EDDVIDGYPVKKGTNIILNI 398
Cdd:cd11062   254 NPEILERLREELKTAMPDPDSPPSlaELEKLPYLTAVIKEGLRLSYGV--PTRLPRvvpdEGLYYKGWVIPPGTPVSMSS 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 399 GRMHRLE-FFPKPNEFT----LENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKtLQGQCVESIQK 473
Cdd:cd11062   332 YFVHHDEeIFPDPHEFRperwLGAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRFDLE-LYETTEEDVEI 410

                  ....
gi 1109516678 474 IHDL 477
Cdd:cd11062   411 VHDF 414
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
241-482 2.57e-09

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 59.26  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 241 YKKYEK-SVKDLKDAievLIAEkrrriSTEEKLEEcmdfatelilaEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFML 319
Cdd:cd20676   201 YQTFDKdNIRDITDS---LIEH-----CQDKKLDE-----------NANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSL 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 320 FLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLVM-RKALEDDVIDGYPVKKGTNIILN 397
Cdd:cd20676   262 MYLVTYPEIQKKIQEELDEVIGrERRPRLSDRPQLPYLEAFILETFRHSSFVPFTIpHCTTRDTSLNGYYIPKDTCVFIN 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 398 IGRM-HRLEFFPKPNEFTLENFAKN-------VPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVE 469
Cdd:cd20676   342 QWQVnHDEKLWKDPSSFRPERFLTAdgteinkTESEKVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPPGVKVD 421
                         250
                  ....*....|...
gi 1109516678 470 sIQKIHDLSLHPD 482
Cdd:cd20676   422 -MTPEYGLTMKHK 433
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
309-466 2.96e-09

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 58.95  E-value: 2.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 309 DTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRK-ALEDDVIDGY 386
Cdd:cd20677   250 DTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLsRLPRFEDRKSLHYTEAFINEVFRHSSFVPFTIPHcTTADTTLNGY 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 387 PVKKGTNIILNIGRM-HRLEFFPKPNEFTLENFA-------KNVPYRYFQpFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20677   330 FIPKDTCVFINMYQVnHDETLWKDPDLFMPERFLdengqlnKSLVEKVLI-FGMGVRKCLGEDVARNEIFVFLTTILQQL 408

                  ....*...
gi 1109516678 459 HVKTLQGQ 466
Cdd:cd20677   409 KLEKPPGQ 416
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
264-463 3.52e-09

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 58.36  E-value: 3.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 264 RRISTEEKLEECMDFATELILAEK---------------RGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPnv 328
Cdd:cd11037   156 RTRAALPRLKELRDWVAEQCARERlrpggwgaaifeaadRGEITEDEAPLLMRDYLSAGLDTTISAIGNALWLLARHP-- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 329 eeaiikeiqtvigerdikiDDIQKLKV----MENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRL 404
Cdd:cd11037   234 -------------------DQWERLRAdpslAPNAFEEAVRLESPVQTFSRTTTRDTELAGVTIPAGSRVLVFLGSANRD 294
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109516678 405 E-FFPKPNEFTLE-NFAKNVPyryfqpFGFGPRGCAGKYIAMVMMKAILVTLLRRfhVKTL 463
Cdd:cd11037   295 PrKWDDPDRFDITrNPSGHVG------FGHGVHACVGQHLARLEGEALLTALARR--VDRI 347
PLN02302 PLN02302
ent-kaurenoic acid oxidase
244-467 4.42e-09

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 58.57  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 244 YEKSVKDLKDAIEVL--IAEKRRRISTEEKLEECMDFATELILAE-KRGD-LTRENVNQCILEMLIAAPD-TMSVSLFFM 318
Cdd:PLN02302  232 YHRALKARKKLVALFqsIVDERRNSRKQNISPRKKDMLDLLLDAEdENGRkLDDEEIIDLLLMYLNAGHEsSGHLTMWAT 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 319 LFLiAKHPNV-------EEAIIKEIQTviGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKG 391
Cdd:PLN02302  312 IFL-QEHPEVlqkakaeQEEIAKKRPP--GQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKG 388
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109516678 392 TNIILNIGRMH-RLEFFPKPNEFTLENFAKNVPYRY-FQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQC 467
Cdd:PLN02302  389 WKVLAWFRQVHmDPEVYPNPKEFDPSRWDNYTPKAGtFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLNPGC 466
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
262-458 5.43e-09

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


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 57.73  E-value: 5.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 262 KRRRistEEKLEECMDFateLILAEKRGD-LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNveeaiikeiqtvi 340
Cdd:cd11034   162 AERR---ANPRDDLISR---LIEGEIDGKpLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPE------------- 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 341 gERDIKIDDIQKLKVMenfIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFa 419
Cdd:cd11034   223 -DRRRLIADPSLIPNA---VEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRdEEKFEDPDRIDIDRT- 297
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1109516678 420 knvPYRYFQpFGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11034   298 ---PNRHLA-FGSGVHRCLGSHLARVEARVALTEVLKRI 332
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
258-458 5.44e-09

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 57.92  E-value: 5.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 258 LIAEKRRRISTeekleecmDFATELILAEKR-GDLTREN-VNQCILeMLIAAPDTMS--VSLFFMLFLiaKHPNVEEAII 333
Cdd:cd11030   178 LVARKRREPGD--------DLLSRLVAEHGApGELTDEElVGIAVL-LLVAGHETTAnmIALGTLALL--EHPEQLAALR 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 334 KEIQtvigerdikiddiqklkVMENFIYESMRYQPVVDL-VMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPN 411
Cdd:cd11030   247 ADPS-----------------LVPGAVEELLRYLSIVQDgLPRVATEDVEIGGVTIRAGEGVIVSLPAANRdPAVFPDPD 309
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1109516678 412 EFTLEnfaknvpyRYFQP---FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11030   310 RLDIT--------RPARRhlaFGHGVHQCLGQNLARLELEIALPTLFRRF 351
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
300-459 7.70e-09

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 57.45  E-value: 7.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 300 ILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTViGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALE 379
Cdd:cd20614   213 LRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA-GDVPRTPAELRRFPLAEALFRETLRLHPPVPFVFRRVLE 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 380 DDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENF----AKNVPYRYFQpFGFGPRGCAGKYIAMVMMKAILVTL 454
Cdd:cd20614   292 EIELGGRRIPAGTHLGIPLLLFSRdPELYPDPDRFRPERWlgrdRAPNPVELLQ-FGGGPHFCLGYHVACVELVQFIVAL 370

                  ....*
gi 1109516678 455 LRRFH 459
Cdd:cd20614   371 ARELG 375
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
302-459 3.35e-08

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


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 55.80  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 302 EMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGE-RDIKIDDIQKLKVMENFIYESMRYQPVVDLV--MRKAL 378
Cdd:cd11076   231 EMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGsRRVADSDVAKLPYLQAVVKETLRLHPPGPLLswARLAI 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 379 EDDVIDGYPVKKGTNIILNigrM----HRLEFFPKPNEFTLENFAKNVPYRYFQ---------PFGFGPRGCAGKYIAMV 445
Cdd:cd11076   311 HDVTVGGHVVPAGTTAMVN---MwaitHDPHVWEDPLEFKPERFVAAEGGADVSvlgsdlrlaPFGAGRRVCPGKALGLA 387
                         170
                  ....*....|....
gi 1109516678 446 MMKAILVTLLRRFH 459
Cdd:cd11076   388 TVHLWVAQLLHEFE 401
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
316-466 4.80e-08

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 55.46  E-value: 4.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQK-----------LKVMENFIYESMRYQPVvDLVMRKALED---- 380
Cdd:cd20631   248 FWSLFYLLRCPEAMKAATKEVKRTLEKTGQKVSDGGNpivltreqlddMPVLGSIIKEALRLSSA-SLNIRVAKEDftlh 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 381 -DVIDGYPVKKGTNIILNIGRMH-RLEFFPKPNEFTLENF------AKNVPYR-------YFQPFGFGPRGCAGKYIAMV 445
Cdd:cd20631   327 lDSGESYAIRKDDIIALYPQLLHlDPEIYEDPLTFKYDRYldengkEKTTFYKngrklkyYYMPFGSGTSKCPGRFFAIN 406
                         170       180
                  ....*....|....*....|.
gi 1109516678 446 MMKAILVTLLRRFHVKTLQGQ 466
Cdd:cd20631   407 EIKQFLSLMLCYFDMELLDGN 427
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
258-443 5.46e-08

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 54.90  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 258 LIAEkRRRISTEekleecmDFATELILAEKRGD-LTRENVNQCILEMLIAAPDTMSVSL-FFMLFLiAKHPNVEEAIIke 335
Cdd:cd11035   160 LIAE-RRANPGD-------DLISAILNAEIDGRpLTDDELLGLCFLLFLAGLDTVASALgFIFRHL-ARHPEDRRRLR-- 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 336 iqtvigERDIKIDDiqklkvmenFIYESMRYQPVVdLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFT 414
Cdd:cd11035   229 ------EDPELIPA---------AVEELLRRYPLV-NVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPrEFPDPDTVD 292
                         170       180
                  ....*....|....*....|....*....
gi 1109516678 415 LEnfakNVPYRYFQpFGFGPRGCAGKYIA 443
Cdd:cd11035   293 FD----RKPNRHLA-FGAGPHRCLGSHLA 316
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
240-439 9.43e-08

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 54.36  E-value: 9.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 240 LYKKYeKSVKDLKDAIEVLIAEKRRR-ISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFM 318
Cdd:PLN03141  196 LYRSL-QAKKRMVKLVKKIIEEKRRAmKNKEEDETGIPKDVVDVLLRDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLA 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 319 L-FL----IAKHPNVEEAI-IKEIQTVIGErDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGT 392
Cdd:PLN03141  275 VkFLsdcpVALQQLTEENMkLKRLKADTGE-PLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGW 353
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1109516678 393 NIILNIGRMHRLE-FFPKPNEFTlenfaknvPYRY---------FQPFGFGPRGCAG 439
Cdd:PLN03141  354 CVLAYFRSVHLDEeNYDNPYQFN--------PWRWqekdmnnssFTPFGGGQRLCPG 402
PLN03018 PLN03018
homomethionine N-hydroxylase
298-465 1.11e-07

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 54.25  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 298 QCIlEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIG-ERDIKIDDIQKLKVMENFIYESMRYQPVVDLV-MR 375
Cdd:PLN03018  318 QCV-EFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGkDRLVQESDIPNLNYLKACCRETFRIHPSAHYVpPH 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 376 KALEDDVIDGYPVKKGTNIIL---NIGRMHRLEFFP---KPNE-FTLENFAKNVPY----RYFQPFGFGPRGCAGKYIAM 444
Cdd:PLN03018  397 VARQDTTLGGYFIPKGSHIHVcrpGLGRNPKIWKDPlvyEPERhLQGDGITKEVTLveteMRFVSFSTGRRGCVGVKVGT 476
                         170       180
                  ....*....|....*....|.
gi 1109516678 445 VMMKAILVTLLRRFHVKTLQG 465
Cdd:PLN03018  477 IMMVMMLARFLQGFNWKLHQD 497
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
242-470 1.52e-07

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 53.67  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 242 KKYEKSVKDLKDAIEVLIAEKRRRISTEEKLeecMDFATELILAEKRgdltrenvnqcILEmliaapDTMSVSL------ 315
Cdd:cd20627   159 KQYEDALMEMESVLKKVIKERKGKNFSQHVF---IDSLLQGNLSEQQ-----------VLE------DSMIFSLagcvit 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 ----FFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKG 391
Cdd:cd20627   219 anlcTWAIYFLTTSEEVQKKLYKEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKE 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 392 TNIILNIGRM-HRLEFFPKPNEFTLENFAKNVPYRYFQPFGF-GPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVE 469
Cdd:cd20627   299 TLVLYALGVVlQDNTTWPLPYRFDPDRFDDESVMKSFSLLGFsGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVME 378

                  .
gi 1109516678 470 S 470
Cdd:cd20627   379 T 379
PLN02774 PLN02774
brassinosteroid-6-oxidase
286-458 1.60e-07

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 53.63  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 286 EKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEiQTVIGERD-----IKIDDIQKLKVMENFI 360
Cdd:PLN02774  255 GNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKE-HLAIRERKrpedpIDWNDYKSMRFTRAVI 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 361 YESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEF-FPKPNEFT----LENFAKNVPyrYFQPFGFGPR 435
Cdd:PLN02774  334 FETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFlYPDPMTFNpwrwLDKSLESHN--YFFLFGGGTR 411
                         170       180
                  ....*....|....*....|...
gi 1109516678 436 GCAGKYIAMVMMKAILVTLLRRF 458
Cdd:PLN02774  412 LCPGKELGIVEISTFLHYFVTRY 434
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
258-469 1.66e-07

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 53.24  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 258 LIAEKRRRISTeekleecmDFATELILAEKRGD-LTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIkei 336
Cdd:cd11080   163 VIEERRVNPGS--------DLISILCTAEYEGEaLSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVR--- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 337 qtvigerdikiddiQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEF-FPKPNEFTL 415
Cdd:cd11080   232 --------------ADRSLVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAaFEDPDTFNI 297
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1109516678 416 eNFAKNVPYRYFQP------FGFGPRGCAGKYIAMVMMKAILVTLLRRF-HVKTLQGQCVE 469
Cdd:cd11080   298 -HREDLGIRSAFSGaadhlaFGSGRHFCVGAALAKREIEIVANQVLDALpNIRLEPGFEYA 357
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
255-458 5.79e-07

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 51.80  E-value: 5.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 255 IEVLIAEKRRRiSTEekleecmDFATELILA-EKRGDLT-RENVNQCILeMLIAAPDTMSVSLFFMLFLIAKHPnveeai 332
Cdd:cd11031   173 MAELVAARRAE-PGD-------DLLSALVAArDDDDRLSeEELVTLAVG-LLVAGHETTASQIGNGVLLLLRHP------ 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 333 ikeiqtviGERDIKIDDiqkLKVMENFIYESMRYQPV--VDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPK 409
Cdd:cd11031   238 --------EQLARLRAD---PELVPAAVEELLRYIPLgaGGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRdPEVFPD 306
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1109516678 410 PNEFTLENFAKnvpyryfqP---FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11031   307 PDRLDLDREPN--------PhlaFGHGPHHCLGAPLARLELQVALGALLRRL 350
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
259-458 1.71e-06

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 50.29  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 259 IAEKRRRISTEekleecmDFATELILAEKRGD-LT-RENVNQCILeMLIAAPDTMSVSLFFMLFLIAKHPNVEEAiikei 336
Cdd:cd11032   168 HLEERRRNPRD-------DLISRLVEAEVDGErLTdEEIVGFAIL-LLIAGHETTTNLLGNAVLCLDEDPEVAAR----- 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 337 qtVIGERDIkiddiqklkvMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFtl 415
Cdd:cd11032   235 --LRADPSL----------IPGAIEEVLRYRPPVQRTARVTTEDVELGGVTIPAGQLVIAWLASANRDErQFEDPDTF-- 300
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1109516678 416 enfaknVPYRyfQP-----FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11032   301 ------DIDR--NPnphlsFGHGIHFCLGAPLARLEARIALEALLDRF 340
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
305-459 3.08e-06

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 49.38  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 305 IAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDikiddiqkLKVMENFIYESMRYQPVVDLVMRKALEDDVID 384
Cdd:cd20624   201 LFAFDAAGMALLRALALLAAHPEQAARAREEAAVPPGPLA--------RPYLRACVLDAVRLWPTTPAVLRESTEDTVWG 272
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1109516678 385 GYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFAKN--VPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFH 459
Cdd:cd20624   273 GRTVPAGTGFLIFAPFFHRdDEALPFADRFVPEIWLDGraQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAE 350
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
360-457 1.04e-05

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 47.81  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 360 IYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFtleNFAKNVPYRYFQPFGFGPRGCA 438
Cdd:cd20619   238 INEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRdPEVFDDPDVF---DHTRPPAASRNLSFGLGPHSCA 314
                          90
                  ....*....|....*....
gi 1109516678 439 GKYIAMVMMKAILVTLLRR 457
Cdd:cd20619   315 GQIISRAEATTVFAVLAER 333
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
357-458 1.42e-05

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 47.14  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 357 ENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNI-GRMHRLEFFPKPNEFtlenfaknVPYRyFQ-----PF 430
Cdd:cd11067   266 EAFVQEVRRFYPFFPFVGARARRDFEWQGYRFPKGQRVLLDLyGTNHDPRLWEDPDRF--------RPER-FLgwegdPF 336
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1109516678 431 GFGPRG---------CAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11067   337 DFIPQGggdhatghrCPGEWITIALMKEALRLLARRD 373
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
293-458 2.29e-05

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 46.73  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 293 RENVNQCILEMLIAAPDTMSVSlffmlfliAKHPNVEEAI---IKEIQTVIGERDIKI--DDIQKLKVMENFIY------ 361
Cdd:cd11039   180 RSNPNPSLLSVMLNAGMPMSLE--------QIRANIKVAIgggLNEPRDAIAGTCWGLlsNPEQLAEVMAGDVHwlrafe 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 362 ESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLenFAKNVPYryfQPFGFGPRGCAGK 440
Cdd:cd11039   252 EGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEaRFENPDRFDV--FRPKSPH---VSFGAGPHFCAGA 326
                         170
                  ....*....|....*....
gi 1109516678 441 YIAMVMMKAILV-TLLRRF 458
Cdd:cd11039   327 WASRQMVGEIALpELFRRL 345
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
309-458 4.49e-05

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: 45.82  E-value: 4.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 309 DTMSVSLFFMLFLIaKHPNVEEAIIKEIQTVIGER-----------DIKIDDIQKLKVMENFIYESMRYQpVVDLVMRKA 377
Cdd:cd20633   239 NTGPASFWLLLYLL-KHPEAMKAVREEVEQVLKETgqevkpggpliNLTRDMLLKTPVLDSAVEETLRLT-AAPVLIRAV 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 378 LEDDVI---DG--YPVKKGTNIIL--NIGRMHRLEFFPKPNEFTLENF--------------AKNVPYrYFQPFGFGPRG 436
Cdd:cd20633   317 VQDMTLkmaNGreYALRKGDRLALfpYLAVQMDPEIHPEPHTFKYDRFlnpdggkkkdfyknGKKLKY-YNMPWGAGVSI 395
                         170       180
                  ....*....|....*....|..
gi 1109516678 437 CAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd20633   396 CPGRFFAVNEMKQFVFLMLTYF 417
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
356-458 4.91e-05

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 45.56  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 356 MENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENfaknvPYRYFQPFGFGP 434
Cdd:cd11036   221 AAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRdPEAFPDPDRFDLGR-----PTARSAHFGLGR 295
                          90       100
                  ....*....|....*....|....
gi 1109516678 435 RGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11036   296 HACLGAALARAAAAAALRALAARF 319
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
316-466 7.62e-05

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: 44.98  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEIQTVIGERDIKI----------DDIQKLKVMENFIYESMRYQPVvDLVMRKALEDDVID- 384
Cdd:cd20632   236 FWAMYYLLRHPEALAAVRDEIDHVLQSTGQELgpdfdihltrEQLDSLVYLESAINESLRLSSA-SMNIRVVQEDFTLKl 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 385 ----GYPVKKGTNIILNIGRMHR-LEFFPKPNEFTLENFAKN-------------VPYrYFQPFGFGPRGCAGKYIAMVM 446
Cdd:cd20632   315 esdgSVNLRKGDIVALYPQSLHMdPEIYEDPEVFKFDRFVEDgkkkttfykrgqkLKY-YLMPFGSGSSKCPGRFFAVNE 393
                         170       180
                  ....*....|....*....|
gi 1109516678 447 MKAILVTLLRRFHVKTLQGQ 466
Cdd:cd20632   394 IKQFLSLLLLYFDLELLEEQ 413
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
259-458 9.91e-04

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 41.36  E-value: 9.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 259 IAEKRRRISTEekleecmDFATELILAEKRGD-LTREN-VNQCILeMLIAAPDTMSVSLFFMLFLIAKHPnveeaiikei 336
Cdd:cd11033   179 LAEERRANPGD-------DLISVLANAEVDGEpLTDEEfASFFIL-LAVAGNETTRNSISGGVLALAEHP---------- 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 337 qtviGERDIKIDDiqkLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTL 415
Cdd:cd11033   241 ----DQWERLRAD---PSLLPTAVEEILRWASPVIHFRRTATRDTELGGQRIRAGDKVVLWYASANRDEeVFDDPDRFDI 313
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1109516678 416 EnfaknvpyRYFQP---FGFGPRGCAGKYIAMVMMKAILVTLLRRF 458
Cdd:cd11033   314 T--------RSPNPhlaFGGGPHFCLGAHLARLELRVLFEELLDRV 351
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
316-461 5.44e-03

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: 39.36  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 316 FFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLK--------VMENFIYESMRYQPVVdLVMRKALEDDVI---D 384
Cdd:cd20634   242 FWLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVSQTLTINqelldntpVFDSVLSETLRLTAAP-FITREVLQDMKLrlaD 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1109516678 385 G--YPVKKGTNIIL--NIGRMHRLEFFPKPNEFTLE-----------NFAKN---VPYrYFQPFGFGPRGCAGKYIAMVM 446
Cdd:cd20634   321 GqeYNLRRGDRLCLfpFLSPQMDPEIHQEPEVFKYDrflnadgtekkDFYKNgkrLKY-YNMPWGAGDNVCIGRHFAVNS 399
                         170
                  ....*....|....*
gi 1109516678 447 MKAILVTLLRRFHVK 461
Cdd:cd20634   400 IKQFVFLILTHFDVE 414
 
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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