NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|50727139|gb|AAT81230|]
View 

ent-kaurene oxidase [Oryza sativa Japonica Group]

Protein Classification

cytochrome P450 family protein( domain architecture ID 10010852)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PLN02655 PLN02655
ent-kaurene oxidase
42-505 0e+00

ent-kaurene oxidase


:

Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 933.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   42 PAVPGLPIIGNLHQLKEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDK 121
Cdd:PLN02655   2 PAVPGLPVIGNLLQLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  122 SMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLVKDDPHAPLIFRDVFKDELFRLSMIQSLGE 201
Cdd:PLN02655  82 SMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALVKDDPHSPVNFRDVFENELFGLSLIQALGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  202 DVSSVYVDEFGRDISREEIYNATVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRG 281
Cdd:PLN02655 162 DVESVYVEELGTEISKEEIFDVLVHDMMMCAIEVDWRDFFPYLSWIPNKSFETRVQTTEFRRTAVMKALIKQQKKRIARG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  282 EAKTCYLDFLLAENT-LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLP 360
Cdd:PLN02655 242 EERDCYLDFLLSEAThLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  361 YLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTM 440
Cdd:PLN02655 322 YLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTM 401
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50727139  441 AFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEKVDTVQLTAYKLHPLHVHLTRRGRM 505
Cdd:PLN02655 402 AFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREGDEEKEDTVQLTTQKLHPLHAHLKPRGSM 466
 
Name Accession Description Interval E-value
PLN02655 PLN02655
ent-kaurene oxidase
42-505 0e+00

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 933.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   42 PAVPGLPIIGNLHQLKEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDK 121
Cdd:PLN02655   2 PAVPGLPVIGNLLQLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  122 SMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLVKDDPHAPLIFRDVFKDELFRLSMIQSLGE 201
Cdd:PLN02655  82 SMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALVKDDPHSPVNFRDVFENELFGLSLIQALGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  202 DVSSVYVDEFGRDISREEIYNATVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRG 281
Cdd:PLN02655 162 DVESVYVEELGTEISKEEIFDVLVHDMMMCAIEVDWRDFFPYLSWIPNKSFETRVQTTEFRRTAVMKALIKQQKKRIARG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  282 EAKTCYLDFLLAENT-LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLP 360
Cdd:PLN02655 242 EERDCYLDFLLSEAThLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  361 YLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTM 440
Cdd:PLN02655 322 YLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTM 401
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50727139  441 AFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEKVDTVQLTAYKLHPLHVHLTRRGRM 505
Cdd:PLN02655 402 AFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREGDEEKEDTVQLTTQKLHPLHAHLKPRGSM 466
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
71-496 0e+00

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: 565.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  71 IYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVL-TRDKSMVATSDYCDFHKMVKRYVMSSMLGTSA 149
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLfSSNKHMVNSSPYGPLWRTLRRNLVSEVLSPSR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 150 QKQFRDIRDMMIHNMLSTFHKLVKDDPHaPLIFRDVFKDELFRLSMIQSLGEDvssvyvdefgrdiSREEIYNATVTDMM 229
Cdd:cd11075  81 LKQFRPARRRALDNLVERLREEAKENPG-PVNVRDHFRHALFSLLLYMCFGER-------------LDEETVRELERVQR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 230 MCAI---EVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLLA----------ENT 296
Cdd:cd11075 147 ELLLsftDFDVRDFFPALTWLLNRRRWKKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFLLLdlldlkeeggERK 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETLRRHSP 375
Cdd:cd11075 227 LTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAvVTEEDLPKMPYLKAVVLETLRRHPP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 376 VPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEV-----ADMYKTMAFGAGRRACA 450
Cdd:cd11075 307 GHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAAdidtgSKEIKMMPFGAGRRICP 386
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 50727139 451 GSLQATHIACAAVARFVQEFGWRLREGDEEKVDTVQL-TAYKLHPLH 496
Cdd:cd11075 387 GLGLATLHLELFVARLVQEFEWKLVEGEEVDFSEKQEfTVVMKNPLR 433
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
41-481 8.26e-75

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: 243.34  E-value: 8.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139    41 PPAVPGLPIIGNLHQL-KEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKAL---TV 116
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLgRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFatsRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   117 LTRDKSmVATSDYCDFHKMVKRYVMSsmLGTSAQKQFRDIRDMMIHNMLSTFHKLVkDDPHAPLIFRDVFKdelFRLSMI 196
Cdd:pfam00067  81 PFLGKG-IVFANGPRWRQLRRFLTPT--FTSFGKLSFEPRVEEEARDLVEKLRKTA-GEPGVIDITDLLFR---AALNVI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   197 QS---------LGEDVSSVYVDeFGRDISREEIYNATVTDmmmcaievdwrDFFPYLSWVPNKSFETRVFTTETRRtAVM 267
Cdd:pfam00067 154 CSilfgerfgsLEDPKFLELVK-AVQELSSLLSSPSPQLL-----------DLFPILKYFPGPHGRKLKRARKKIK-DLL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   268 RALIKQQKERIVRGEAKTcyLDFLLA---------ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERL 338
Cdd:pfam00067 221 DKLIEERRETLDSAKKSP--RDFLDAlllakeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   339 YQEIREVCGD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWES 417
Cdd:pfam00067 299 REEIDEVIGDkRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPN 378
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139   418 PEEWVPERFAGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEK 481
Cdd:pfam00067 379 PEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPP 442
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-502 9.67e-29

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: 117.69  E-value: 9.67e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  61 PHQTFAKWAEiYGPIYTIRTGASSVVVLNSTEVAKEAMV--AKFSSisTRKLSKALTVLTRDKSMVATSDYcDFHKMVKR 138
Cdd:COG2124  21 PYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRdpRTFSS--DGGLPEVLRPLPLLGDSLLTLDG-PEHTRLRR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 139 YVMSSMlgtsAQKQFRDIRDMM---IHNMLSTFHklvkddPHAPLIFRDVFKDELFRLsMIQSLgedvssvyvdeFGRDI 215
Cdd:COG2124  97 LVQPAF----TPRRVAALRPRIreiADELLDRLA------ARGPVDLVEEFARPLPVI-VICEL-----------LGVPE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 216 SREEIYNATVTDMMmcaievdwrDFFPYLSWVPNKSFETRVftteTRRTAVMRALIKQqkeriVRGEAKTCYLDFLLAE- 294
Cdd:COG2124 155 EDRDRLRRWSDALL---------DALGPLPPERRRRARRAR----AELDAYLRELIAE-----RRAEPGDDLLSALLAAr 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 295 ---NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEirevcgdetvteehlprLPYLNAVFHETLR 371
Cdd:COG2124 217 ddgERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLR 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 372 RHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERfaggrlevaDMYKTMAFGAGRRACAG 451
Cdd:COG2124 280 LYPPVPLLP-RTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLG 349
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 50727139 452 SLQATHIACAAVARFVQEF-GWRLREGDEEKVDTVqLTAYKLHPLHVHLTRR 502
Cdd:COG2124 350 AALARLEARIALATLLRRFpDLRLAPPEELRWRPS-LTLRGPKSLPVRLRPR 400
 
Name Accession Description Interval E-value
PLN02655 PLN02655
ent-kaurene oxidase
42-505 0e+00

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 933.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   42 PAVPGLPIIGNLHQLKEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDK 121
Cdd:PLN02655   2 PAVPGLPVIGNLLQLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  122 SMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLVKDDPHAPLIFRDVFKDELFRLSMIQSLGE 201
Cdd:PLN02655  82 SMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALVKDDPHSPVNFRDVFENELFGLSLIQALGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  202 DVSSVYVDEFGRDISREEIYNATVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRG 281
Cdd:PLN02655 162 DVESVYVEELGTEISKEEIFDVLVHDMMMCAIEVDWRDFFPYLSWIPNKSFETRVQTTEFRRTAVMKALIKQQKKRIARG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  282 EAKTCYLDFLLAENT-LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLP 360
Cdd:PLN02655 242 EERDCYLDFLLSEAThLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLP 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  361 YLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTM 440
Cdd:PLN02655 322 YLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTM 401
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50727139  441 AFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEKVDTVQLTAYKLHPLHVHLTRRGRM 505
Cdd:PLN02655 402 AFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREGDEEKEDTVQLTTQKLHPLHAHLKPRGSM 466
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
71-496 0e+00

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: 565.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  71 IYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVL-TRDKSMVATSDYCDFHKMVKRYVMSSMLGTSA 149
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLfSSNKHMVNSSPYGPLWRTLRRNLVSEVLSPSR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 150 QKQFRDIRDMMIHNMLSTFHKLVKDDPHaPLIFRDVFKDELFRLSMIQSLGEDvssvyvdefgrdiSREEIYNATVTDMM 229
Cdd:cd11075  81 LKQFRPARRRALDNLVERLREEAKENPG-PVNVRDHFRHALFSLLLYMCFGER-------------LDEETVRELERVQR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 230 MCAI---EVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLLA----------ENT 296
Cdd:cd11075 147 ELLLsftDFDVRDFFPALTWLLNRRRWKKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFLLLdlldlkeeggERK 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETLRRHSP 375
Cdd:cd11075 227 LTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAvVTEEDLPKMPYLKAVVLETLRRHPP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 376 VPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEV-----ADMYKTMAFGAGRRACA 450
Cdd:cd11075 307 GHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAAdidtgSKEIKMMPFGAGRRICP 386
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 50727139 451 GSLQATHIACAAVARFVQEFGWRLREGDEEKVDTVQL-TAYKLHPLH 496
Cdd:cd11075 387 GLGLATLHLELFVARLVQEFEWKLVEGEEVDFSEKQEfTVVMKNPLR 433
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
73-495 2.05e-84

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: 267.11  E-value: 2.05e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTEVAKEAMV---AKFSSistRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSA 149
Cdd:cd20618   1 GPLMYLRLGSVPTVVVSSPEMAKEVLKtqdAVFAS---RPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 150 QKQFRDIRDMMIHNMLSTFHKLVKDDphapliFRDVFKDELFRLS------MIQSLGEDVSSVYVDEFGRDisreeiYNA 223
Cdd:cd20618  78 LESFQGVRKEELSHLVKSLLEESESG------KPVNLREHLSDLTlnnitrMLFGKRYFGESEKESEEARE------FKE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 224 TVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLL------AENTL 297
Cdd:cd20618 146 LIDEAFELAGAFNIGDYIPWLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLllldldGEGKL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 298 TDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDE-TVTEEHLPRLPYLNAVFHETLRRHSPV 376
Cdd:cd20618 226 SDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRErLVEESDLPKLPYLQAVVKETLRLHPPG 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 377 PLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGrlEVADM----YKTMAFGAGRRACAGS 452
Cdd:cd20618 306 PLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLES--DIDDVkgqdFELLPFGSGRRMCPGM 383
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 50727139 453 LQATHIACAAVARFVQEFGWRLREGDEEKVDTVQ---LTAYKLHPL 495
Cdd:cd20618 384 PLGLRMVQLTLANLLHGFDWSLPGPKPEDIDMEEkfgLTVPRAVPL 429
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
41-481 8.26e-75

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: 243.34  E-value: 8.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139    41 PPAVPGLPIIGNLHQL-KEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKAL---TV 116
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLgRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFatsRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   117 LTRDKSmVATSDYCDFHKMVKRYVMSsmLGTSAQKQFRDIRDMMIHNMLSTFHKLVkDDPHAPLIFRDVFKdelFRLSMI 196
Cdd:pfam00067  81 PFLGKG-IVFANGPRWRQLRRFLTPT--FTSFGKLSFEPRVEEEARDLVEKLRKTA-GEPGVIDITDLLFR---AALNVI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   197 QS---------LGEDVSSVYVDeFGRDISREEIYNATVTDmmmcaievdwrDFFPYLSWVPNKSFETRVFTTETRRtAVM 267
Cdd:pfam00067 154 CSilfgerfgsLEDPKFLELVK-AVQELSSLLSSPSPQLL-----------DLFPILKYFPGPHGRKLKRARKKIK-DLL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   268 RALIKQQKERIVRGEAKTcyLDFLLA---------ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERL 338
Cdd:pfam00067 221 DKLIEERRETLDSAKKSP--RDFLDAlllakeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   339 YQEIREVCGD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWES 417
Cdd:pfam00067 299 REEIDEVIGDkRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPN 378
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139   418 PEEWVPERFAGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEK 481
Cdd:pfam00067 379 PEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPP 442
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
69-497 1.09e-63

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: 213.55  E-value: 1.09e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  69 AEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTS 148
Cdd:cd11073   1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 149 AQKQFRDIRDMMIHNMLSTFHKlVKDDPHAPLIFRDVFkdelfrLSMIQSLGEDVSSVYVDEFGRDISREeiYNATVTDM 228
Cdd:cd11073  81 RLDATQPLRRRKVRELVRYVRE-KAGSGEAVDIGRAAF------LTSLNLISNTLFSVDLVDPDSESGSE--FKELVREI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 229 MMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKEriVRGEAKTCYLDFLL---------AENTLTD 299
Cdd:cd11073 152 MELAGKPNVADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLA--EREAGGDKKKDDDLlllldleldSESELTR 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 300 EQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPL 378
Cdd:cd11073 230 NHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGkDKIVEESDISKLPYLQAVVKETLRLHPPAPL 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 379 IPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVA-DMYKTMAFGAGRRACAGSLQATH 457
Cdd:cd11073 310 LLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKgRDFELIPFGSGRRICPGLPLAER 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 50727139 458 IACAAVARFVQEFGWRLREG-DEEKVD---TVQLTAYKLHPLHV 497
Cdd:cd11073 390 MVHLVLASLLHSFDWKLPDGmKPEDLDmeeKFGLTLQKAVPLKA 433
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
73-451 1.14e-61

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: 207.45  E-value: 1.14e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDycDFHKMVKRYVMSSMLGTSAQKQ 152
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNG--DYWKELRRFALSSLTKTKLKKK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 153 FRDIRDMMIHNMLSTFHKLVKDDphAPLIFRDVFKdeLFRLSMIQSL--GEDVSSVYVDEFGRDISREEIYNATVTDMMM 230
Cdd:cd20617  79 MEELIEEEVNKLIESLKKHSKSG--EPFDPRPYFK--KFVLNIINQFlfGKRFPDEDDGEFLKLVKPIEEIFKELGSGNP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 231 CaievdwrDFFPYLSWVPNKSFETRVFTTETRRTAVMRaLIKQQKERIVRGEAK---TCYLDFLLAENT---LTDEQLMM 304
Cdd:cd20617 155 S-------DFIPILLPFYFLYLKKLKKSYDKIKDFIEK-IIEEHLKTIDPNNPRdliDDELLLLLKEGDsglFDDDSIIS 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 305 LVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRF 383
Cdd:cd20617 227 TCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGnDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRV 306
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50727139 384 VHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFaggrLE---VADMYKTMAFGAGRRACAG 451
Cdd:cd20617 307 TTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERF----LEndgNKLSEQFIPFGIGKRNCVG 373
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
73-495 1.61e-59

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: 202.44  E-value: 1.61e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQ 152
Cdd:cd20655   1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 153 FRDIRdmmiHNMLSTFHKLVKDDPHApliFRDV-FKDELFRLS------MI--QSLGEDVSSVyvdefgrdisrEEIyNA 223
Cdd:cd20655  81 FRPIR----AQELERFLRRLLDKAEK---GESVdIGKELMKLTnniicrMImgRSCSEENGEA-----------EEV-RK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 224 TVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKE--RIVRGEAKTCYLDFLL-------AE 294
Cdd:cd20655 142 LVKESAELAGKFNASDFIWPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEkrKKRKEGGSKDLLDILLdayedenAE 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 295 NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRH 373
Cdd:cd20655 222 YKITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGkTRLVQESDLPNLPYLQAVVKETLRLH 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 374 SPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF-AGGRLEVAD-----MYKTMAFGAGRR 447
Cdd:cd20655 302 PPGPLLV-RESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFlASSRSGQELdvrgqHFKLLPFGSGRR 380
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 50727139 448 ACAGSLQATHIACAAVARFVQEFGWRLreGDEEKVD---TVQLTAYKLHPL 495
Cdd:cd20655 381 GCPGASLAYQVVGTAIAAMVQCFDWKV--GDGEKVNmeeASGLTLPRAHPL 429
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
72-495 2.18e-59

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: 201.92  E-value: 2.18e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMV---AKFSSistRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTS 148
Cdd:cd11072   2 YGPLMLLRLGSVPTVVVSSPEAAKEVLKthdLVFAS---RPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 149 AQKQFRDIRDMMIHNMLSTfhklvkddphaplIFRDVFKDELFRLS-MIQSLGEDVSSVYVdeFGRdiSREEIYNATVTD 227
Cdd:cd11072  79 RVQSFRSIREEEVSLLVKK-------------IRESASSSSPVNLSeLLFSLTNDIVCRAA--FGR--KYEGKDQDKFKE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 228 MMMCAIEV----DWRDFFPYLSWVpnksfetRVFTTETRRT--------AVMRALIKQQKERIVRGEAKTCYLDFLLAEN 295
Cdd:cd11072 142 LVKEALELlggfSVGDYFPSLGWI-------DLLTGLDRKLekvfkeldAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRL 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 296 --------TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD-ETVTEEHLPRLPYLNAVF 366
Cdd:cd11072 215 qkegdlefPLTRDNIKAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGkGKVTEEDLEKLKYLKAVI 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 367 HETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLevaDM----YKTMAF 442
Cdd:cd11072 295 KETLRLHPPAPLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSI---DFkgqdFELIPF 371
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 50727139 443 GAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDE-EKVDTVQ---LTAYKLHPL 495
Cdd:cd11072 372 GAGRRICPGITFGLANVELALANLLYHFDWKLPDGMKpEDLDMEEafgLTVHRKNPL 428
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
73-495 4.02e-54

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: 187.81  E-value: 4.02e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQ 152
Cdd:cd20653   1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 153 FRDIRDMMIHNMLSTFHKLVKDDPhAPLIFRDVFKDELFR--LSMI---QSLGEDVSSVYVDEFGRDIsreeiynatVTD 227
Cdd:cd20653  81 FSSIRRDEIRRLLKRLARDSKGGF-AKVELKPLFSELTFNniMRMVagkRYYGEDVSDAEEAKLFREL---------VSE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 228 MMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIkqQKERIVRGEAKTCYLDFLLA-----ENTLTDEQL 302
Cdd:cd20653 151 IFELSGAGNPADFLPILRWFDFQGLEKRVKKLAKRRDAFLQGLI--DEHRKNKESGKNTMIDHLLSlqesqPEYYTDEII 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 303 MMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEH-LPRLPYLNAVFHETLRRHSPVPLIPP 381
Cdd:cd20653 229 KGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESdLPKLPYLQNIISETLRLYPAAPLLVP 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 382 RFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVadmYKTMAFGAGRRACAGSLQATHIACA 461
Cdd:cd20653 309 HESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREG---YKLIPFGLGRRACPGAGLAQRVVGL 385
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 50727139 462 AVARFVQEFGWRlREGdEEKVDTVQ---LTAYKLHPL 495
Cdd:cd20653 386 ALGSLIQCFEWE-RVG-EEEVDMTEgkgLTMPKAIPL 420
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
72-488 1.19e-53

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: 186.63  E-value: 1.19e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRyVMSSMLGTSAQK 151
Cdd:cd11065   1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMPYGPRWRLHRR-LFHQLLNPSAVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRDMMIHNMLstfHKLVKDdphaPLIFRDVFKDELFRLSMIQSLGEDVSSVYvdefgrDISREEIYNATVTDMMMC 231
Cdd:cd11065  80 KYRPLQELESKQLL---RDLLES----PDDFLDHIRRYAASIILRLAYGYRVPSYD------DPLLRDAEEAMEGFSEAG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 232 AIEVDWRDFFPYLSWVPN------KSFETRVFTTETRrtaVMRALIKQQKERIVRGEAKTCYLDFLL----AENTLTDEQ 301
Cdd:cd11065 147 SPGAYLVDFFPFLRYLPSwlgapwKRKARELRELTRR---LYEGPFEAAKERMASGTATPSFVKDLLeeldKEGGLSEEE 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 302 LMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETV-TEEHLPRLPYLNAVFHETLRRHSPVPLIP 380
Cdd:cd11065 224 IKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLpTFEDRPNLPYVNAIVKEVLRWRPVAPLGI 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 381 PRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYK--TMAFGAGRRACAGSlqatHI 458
Cdd:cd11065 304 PHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDppHFAFGFGRRICPGR----HL 379
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 50727139 459 ACA----AVARFVQ--EFGWRLREGDEEKVDTVQLT 488
Cdd:cd11065 380 AENslfiAIARLLWafDIKKPKDEGGKEIPDEPEFT 415
PLN02687 PLN02687
flavonoid 3'-monooxygenase
30-502 3.61e-53

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 187.71  E-value: 3.61e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   30 GVIAPRKRPnAPPAVPGLPIIGNLHQLKEKkPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRK 109
Cdd:PLN02687  26 GGSGKHKRP-LPPGPRGWPVLGNLPQLGPK-PHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  110 LSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLstfHKLVKDDPHAPLIFRDVFK-- 187
Cdd:PLN02687 104 PNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLV---RELARQHGTAPVNLGQLVNvc 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  188 --DELFRlsmiQSLGEDVSSVYVDEFGRDisreeiYNATVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTA 265
Cdd:PLN02687 181 ttNALGR----AMVGRRVFAGDGDEKARE------FKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGKMKRLHRRFDA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  266 VMRALIKQQK-ERIVRGEAKTCYLDFLLA----------ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDK 334
Cdd:PLN02687 251 MMNGIIEEHKaAGQTGSEEHKDLLSTLLAlkreqqadgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDI 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  335 QERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRK 413
Cdd:PLN02687 331 LKKAQEELDAVVGrDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPE 410
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  414 EWESPEEWVPERF-AGGRLEVADM----YKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG-DEEKVDTVQ- 486
Cdd:PLN02687 411 QWPDPLEFRPDRFlPGGEHAGVDVkgsdFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGqTPDKLNMEEa 490
                        490
                 ....*....|....*...
gi 50727139  487 --LTAYKLHPLHVHLTRR 502
Cdd:PLN02687 491 ygLTLQRAVPLMVHPRPR 508
PLN00168 PLN00168
Cytochrome P450; Provisional
35-502 4.49e-53

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 187.46  E-value: 4.49e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   35 RKRPNAPPAVPGLPIIGNL----HQLKEKKPhqTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKL 110
Cdd:PLN00168  31 KKGRRLPPGPPAVPLLGSLvwltNSSADVEP--LLRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  111 SKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRdMMIHNMLSTFHKLVKDDPHAPLIFrDVFKDEL 190
Cdd:PLN00168 109 VASSRLLGESDNTITRSSYGPVWRLLRRNLVAETLHPSRVRLFAPAR-AWVRRVLVDKLRREAEDAAAPRVV-ETFQYAM 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  191 FRLSMIQSLGEDVSSVYVdefgRDISreeiyNATVTDMMMCAIEVDWRDFFPYLSwvpnksfeTRVFTtetRRTAVMRAL 270
Cdd:PLN00168 187 FCLLVLMCFGERLDEPAV----RAIA-----AAQRDWLLYVSKKMSVFAFFPAVT--------KHLFR---GRLQKALAL 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  271 IKQQKERIV-----RGEAKT-----------------CYLDFLLAEN-------TLTDEQLMMLVWEALIEAADTTLVTT 321
Cdd:PLN00168 247 RRRQKELFVplidaRREYKNhlgqggeppkkettfehSYVDTLLDIRlpedgdrALTDDEIVNLCSEFLNAGTDTTSTAL 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  322 EWAMYELAKNPDKQERLYQEIREVCGD--ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGT 399
Cdd:PLN00168 327 QWIMAELVKNPSIQSKLHDEIKAKTGDdqEEVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEVGGYLIPKGA 406
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  400 emVINLYGCNMNR--KEWESPEEWVPERF-AGGRLEVADMYKT-----MAFGAGRRACAGSLQATHIACAAVARFVQEFG 471
Cdd:PLN00168 407 --TVNFMVAEMGRdeREWERPMEFVPERFlAGGDGEGVDVTGSreirmMPFGVGRRICAGLGIAMLHLEYFVANMVREFE 484
                        490       500       510
                 ....*....|....*....|....*....|..
gi 50727139  472 WRLREGDE-EKVDTVQLTAYKLHPLHVHLTRR 502
Cdd:PLN00168 485 WKEVPGDEvDFAEKREFTTVMAKPLRARLVPR 516
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
72-451 1.84e-52

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: 183.57  E-value: 1.84e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSM-LGTSAQ 150
Cdd:cd11027   1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKLAHSALrLYASGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 151 KQFRDIrdmmIHNMLSTF-HKLVKDD--PHAPlifrdvfKDELFRLSM--IQSL--GE-------DVSSV--YVDEFGRD 214
Cdd:cd11027  81 PRLEEK----IAEEAEKLlKRLASQEgqPFDP-------KDELFLAVLnvICSItfGKryklddpEFLRLldLNDKFFEL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 215 ISreeiynatvtdmMMCAIevdwrDFFPYLSWVPNKSFETRVFTTETRRTAVMR-------------------ALIKQQK 275
Cdd:cd11027 150 LG------------AGSLL-----DIFPFLKYFPNKALRELKELMKERDEILRKkleehketfdpgnirdltdALIKAKK 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 276 ERIVRGEAKTcyldfllaeNTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTE-E 354
Cdd:cd11027 213 EAEDEGDEDS---------GLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTlS 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 355 HLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVA 434
Cdd:cd11027 284 DRKRLPYLEATIAEVLRLSSVVPLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLV 363
                       410
                ....*....|....*...
gi 50727139 435 DMYKT-MAFGAGRRACAG 451
Cdd:cd11027 364 PKPESfLPFSAGRRVCLG 381
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
35-487 2.45e-52

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 185.03  E-value: 2.45e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   35 RKRPNAPPAVPGLPIIGNLHQLKEKkPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKAL 114
Cdd:PLN03112  28 RKSLRLPPGPPRWPIVGNLLQLGPL-PHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTLAA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  115 TVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIR----DMMIHNMLSTFHKlvkddpHAPLIFRDVFKDel 190
Cdd:PLN03112 107 VHLAYGCGDVALAPLGPHWKRMRRICMEHLLTTKRLESFAKHRaeeaRHLIQDVWEAAQT------GKPVNLREVLGA-- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  191 frLSMiqslgEDVSSVYVDEfgRDISREEIYNATVTDMMMCAIEVDW-------RDFFPYLSWVPNKSFETRVFTTETRR 263
Cdd:PLN03112 179 --FSM-----NNVTRMLLGK--QYFGAESAGPKEAMEFMHITHELFRllgviylGDYLPAWRWLDPYGCEKKMREVEKRV 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  264 TAVMRALIKQQKERIVRGEAKTCYLDF------LLAENT---LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDK 334
Cdd:PLN03112 250 DEFHDKIIDEHRRARSGKLPGGKDMDFvdvllsLPGENGkehMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRV 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  335 QERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRK 413
Cdd:PLN03112 330 LRKIQEELDSVVGrNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTK 409
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  414 EWESPEEWVPERF---AGGRLEVADM--YKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG-DEEKVDTVQL 487
Cdd:PLN03112 410 IWDDVEEFRPERHwpaEGSRVEISHGpdFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGlRPEDIDTQEV 489
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
72-497 8.21e-52

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: 181.91  E-value: 8.21e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQK 151
Cdd:cd20656   1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRDMMIHNML-STFHKLVKDDPHA-PLIFRD----VFKDELFRLSMIQSLGEDVSSVyvDEFGRDisreeiYNATV 225
Cdd:cd20656  81 SLRPIREDEVTAMVeSIFNDCMSPENEGkPVVLRKylsaVAFNNITRLAFGKRFVNAEGVM--DEQGVE------FKAIV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 226 TDMMMCAIEVDWRDFFPYLSWVpnKSFETRVFTTE-TRRTAVMRALIKQQKERIVRGEAKTCYLDFLLA---ENTLTDEQ 301
Cdd:cd20656 153 SNGLKLGASLTMAEHIPWLRWM--FPLSEKAFAKHgARRDRLTKAIMEEHTLARQKSGGGQQHFVALLTlkeQYDLSEDT 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 302 LMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIP 380
Cdd:cd20656 231 VIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGsDRVMTEADFPQLPYLQCVVKEALRLHPPTPLML 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 381 PRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAggrLEVADM----YKTMAFGAGRRACAGSLQAT 456
Cdd:cd20656 311 PHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFL---EEDVDIkghdFRLLPFGAGRRVCPGAQLGI 387
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 50727139 457 HIACAAVARFVQEFGWRLREGDE-EKVDTVQ---LTAYKLHPLHV 497
Cdd:cd20656 388 NLVTLMLGHLLHHFSWTPPEGTPpEEIDMTEnpgLVTFMRTPLQA 432
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
32-502 2.58e-50

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 179.66  E-value: 2.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   32 IAPRKRPNAPPAVPGLPIIGNLHQLKEKkPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLS 111
Cdd:PLN00110  24 LLPKPSRKLPPGPRGWPLLGALPLLGNM-PHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPN 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  112 KALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLV-KDDPhaplifrdVFKDEL 190
Cdd:PLN00110 103 AGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLGGKALEDWSQVRTVELGHMLRAMLELSqRGEP--------VVVPEM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  191 FRLSMIQSLGEDVSSVYVdeFGRDISREEIYNATVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRAL 270
Cdd:PLN00110 175 LTFSMANMIGQVILSRRV--FETKGSESNEFKDMVVELMTTAGYFNIGDFIPSIAWMDIQGIERGMKHLHKKFDKLLTRM 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  271 IKQQKERIVRGEAKTCYLDFLLAEN-TLTDEQLMMLVWEAL-----IEAADTTLVTTEWAMYELAKNPDKQERLYQEIRE 344
Cdd:PLN00110 253 IEEHTASAHERKGNPDFLDVVMANQeNSTGEKLTLTNIKALllnlfTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQ 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  345 VCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVP 423
Cdd:PLN00110 333 VIGrNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRP 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  424 ERFAGGRLEVADM----YKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEKVDTV-QLTAYKLHPLHVH 498
Cdd:PLN00110 413 ERFLSEKNAKIDPrgndFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDEAfGLALQKAVPLSAM 492

                 ....
gi 50727139  499 LTRR 502
Cdd:PLN00110 493 VTPR 496
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
73-479 3.41e-50

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: 176.55  E-value: 3.41e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDycDFHKMVKRyVMSSMLGTSAQKQ 152
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDG--PEHRRLRR-LLAPAFTPRALAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 153 FRDIRDMMIHNMLSTFHKLVKDDphaplifrDVFKDELFRLSMiQSLGEdvsSVYVDEFGRDISReeiynatvtdmmmca 232
Cdd:cd00302  78 LRPVIREIARELLDRLAAGGEVG--------DDVADLAQPLAL-DVIAR---LLGGPDLGEDLEE--------------- 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 233 IEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLLAE---NTLTDEQLMMLVWEA 309
Cdd:cd00302 131 LAELLEALLKLLGPRLLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLLADAddgGGLSDEEIVAELLTL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 310 LIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETvtEEHLPRLPYLNAVFHETLRRHSPVPLIPpRFVHEDTK 389
Cdd:cd00302 211 LLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGT--PEDLSKLPYLEAVVEETLRLYPPVPLLP-RVATEDVE 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 390 LAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYktMAFGAGRRACAGSLQATHIACAAVARFVQE 469
Cdd:cd00302 288 LGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYAH--LPFGAGPHRCLGARLARLELKLALATLLRR 365
                       410
                ....*....|
gi 50727139 470 FGWRLREGDE 479
Cdd:cd00302 366 FDFELVPDEE 375
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
73-502 5.93e-49

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: 174.34  E-value: 5.93e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQ 152
Cdd:cd20654   1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 153 FRDIRDMMIHNMLSTFHKLVKDD----PHAPLIFRDVFKDELFR--LSMI---QSLGEDVSSvyvdefgrDISREEIYNA 223
Cdd:cd20654  81 LKHVRVSEVDTSIKELYSLWSNNkkggGGVLVEMKQWFADLTFNviLRMVvgkRYFGGTAVE--------DDEEAERYKK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 224 TVTDMM-MCAIEVDwRDFFPYLSWVPNKSFETrvfttETRRTA-----VMRALIKQQKERIVRGEAKTCYLDFLLAENTL 297
Cdd:cd20654 153 AIREFMrLAGTFVV-SDAIPFLGWLDFGGHEK-----AMKRTAkeldsILEEWLEEHRQKRSSSGKSKNDEDDDDVMMLS 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 298 TDEQLMML-----------VWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAV 365
Cdd:cd20654 227 ILEDSQISgydadtvikatCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGkDRWVEESDIKNLVYLQAI 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 366 FHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYgcNMNR--KEWESPEEWVPERFAGGRLEVaDM----YKT 439
Cdd:cd20654 307 VKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVW--KIQRdpNVWSDPLEFKPERFLTTHKDI-DVrgqnFEL 383
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50727139 440 MAFGAGRRACAG---SLQATHIacaAVARFVQEFgwRLREGDEEKVD---TVQLTAYKLHPLHVHLTRR 502
Cdd:cd20654 384 IPFGSGRRSCPGvsfGLQVMHL---TLARLLHGF--DIKTPSNEPVDmteGPGLTNPKATPLEVLLTPR 447
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
73-502 7.83e-49

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: 174.15  E-value: 7.83e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQ 152
Cdd:cd20657   1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALED 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 153 FRDIRD----MMIHNMLSTFHKLVKddphaplifrdVFKDELFRLSMIQSLGEDVSS--VYVDEFGRDiSREeiYNATVT 226
Cdd:cd20657  81 WAHVREnevgHMLKSMAEASRKGEP-----------VVLGEMLNVCMANMLGRVMLSkrVFAAKAGAK-ANE--FKEMVV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 227 DMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLLAEN-------TLTD 299
Cdd:cd20657 147 ELMTVAGVFNIGDFIPSLAWMDLQGVEKKMKRLHKRFDALLTKILEEHKATAQERKGKPDFLDFVLLENddngegeRLTD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 300 EQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPL 378
Cdd:cd20657 227 TNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGrDRRLLESDIPNLPYLQAICKETFRLHPSTPL 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 379 IPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADM----YKTMAFGAGRRACAGSLQ 454
Cdd:cd20657 307 NLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKVDVrgndFELIPFGAGRRICAGTRM 386
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 50727139 455 ATHIACAAVARFVQEFGWRLREGDE-EKVD---TVQLTAYKLHPLHVHLTRR 502
Cdd:cd20657 387 GIRMVEYILATLVHSFDWKLPAGQTpEELNmeeAFGLALQKAVPLVAHPTPR 438
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
35-493 3.05e-46

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 168.33  E-value: 3.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   35 RKRPNAPPAVPGLPIIGNLHQLKEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKAL 114
Cdd:PLN03234  24 KKSLRLPPGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  115 TVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLVkdDPHAPLIFRDVFKDELFRLS 194
Cdd:PLN03234 104 QTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAA--DQSGTVDLSELLLSFTNCVV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  195 MIQSLGEDVssvyvDEFGRDISReeiYNATVTDMMMCAIEVDWRDFFPYLSWVPN-KSFETRVFTTETRRTAVMRALIKQ 273
Cdd:PLN03234 182 CRQAFGKRY-----NEYGTEMKR---FIDILYETQALLGTLFFSDLFPYFGFLDNlTGLSARLKKAFKELDTYLQELLDE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  274 QKERIVRGEAKTCYLDFLLA-------ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVC 346
Cdd:PLN03234 254 TLDPNRPKQETESFIDLLMQiykdqpfSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVI 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  347 GDET-VTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPE 424
Cdd:PLN03234 334 GDKGyVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPE 413
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50727139  425 RFAGGRLEV---ADMYKTMAFGAGRRACAgslqATHIACAAV----ARFVQEFGWRLREG-DEEKVDTVQLTAYKLH 493
Cdd:PLN03234 414 RFMKEHKGVdfkGQDFELLPFGSGRRMCP----AMHLGIAMVeipfANLLYKFDWSLPKGiKPEDIKMDVMTGLAMH 486
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
36-484 4.41e-46

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 167.99  E-value: 4.41e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   36 KRPNAPPAVPGLPIIGNLHQLKEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALT 115
Cdd:PLN02394  27 KKLKLPPGPAAVPIFGNWLQVGDDLNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  116 VLT-RDKSMVATSdYCD-FHKMvkRYVMSSMLGTSaqKQFRDIRDMMIHNMLSTFhKLVKDDPHAP---LIFRDVFK--- 187
Cdd:PLN02394 107 IFTgKGQDMVFTV-YGDhWRKM--RRIMTVPFFTN--KVVQQYRYGWEEEADLVV-EDVRANPEAAtegVVIRRRLQlmm 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  188 -DELFRLsMIQSLGEDVSS---VYVDEFGRDISReeiynatvtdmMMCAIEVDWRDFFPYLSwvP------NKSFETRvf 257
Cdd:PLN02394 181 yNIMYRM-MFDRRFESEDDplfLKLKALNGERSR-----------LAQSFEYNYGDFIPILR--PflrgylKICQDVK-- 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  258 tteTRRTAVMRALIKQQKERIV-----RGEAKTCYLDFLL-AENT--LTDEQLMMLVWEALIEAADTTLVTTEWAMYELA 329
Cdd:PLN02394 245 ---ERRLALFKDYFVDERKKLMsakgmDKEGLKCAIDHILeAQKKgeINEDNVLYIVENINVAAIETTLWSIEWGIAELV 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  330 KNPDKQERLYQEIREVCGD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGC 408
Cdd:PLN02394 322 NHPEIQKKLRDELDTVLGPgNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWL 401
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50727139  409 NMNRKEWESPEEWVPERFAGGRLEV---ADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGdEEKVDT 484
Cdd:PLN02394 402 ANNPELWKNPEEFRPERFLEEEAKVeanGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPPG-QSKIDV 479
PLN02183 PLN02183
ferulate 5-hydroxylase
35-477 3.43e-44

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 163.10  E-value: 3.43e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   35 RKRPNAPPAVPGLPIIGNLHQLkEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKAL 114
Cdd:PLN02183  32 RRRLPYPPGPKGLPIIGNMLMM-DQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  115 TVLTRDKSMVATSDYCDF-HKMVKRYVMSSMLGTSAQ--KQFRDIRDMMIHNMLSTFHKLVKddpHAPLIFrDVFKDELF 191
Cdd:PLN02183 111 SYLTYDRADMAFAHYGPFwRQMRKLCVMKLFSRKRAEswASVRDEVDSMVRSVSSNIGKPVN---IGELIF-TLTRNITY 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  192 RLSMIQSLGEDVssvyvDEFGRdISRE--EIYNAtvtdmmmcaieVDWRDFFPYLSWVPNKSFETRVFTTETRRTAVMRA 269
Cdd:PLN02183 187 RAAFGSSSNEGQ-----DEFIK-ILQEfsKLFGA-----------FNVADFIPWLGWIDPQGLNKRLVKARKSLDGFIDD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  270 LI-------KQQKERIVRGEAKTCYLDFLLA--------------ENT--LTDEQLMMLVWEALIEAADTTLVTTEWAMY 326
Cdd:PLN02183 250 IIddhiqkrKNQNADNDSEEAETDMVDDLLAfyseeakvnesddlQNSikLTRDNIKAIIMDVMFGGTETVASAIEWAMA 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  327 ELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpprfVHE---DTKLAGYDVPAGTEMV 402
Cdd:PLN02183 330 ELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLTYLKCTLKETLRLHPPIPLL----LHEtaeDAEVAGYFIPKRSRVM 405
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50727139  403 INLYGCNMNRKEWESPEEWVPERFAGGrlEVADM----YKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG 477
Cdd:PLN02183 406 INAWAIGRDKNSWEDPDTFKPSRFLKP--GVPDFkgshFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELPDG 482
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
72-500 2.47e-43

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: 158.73  E-value: 2.47e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMlgtsaQK 151
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQGGQDLSLGDYSLLWKAHRKLTRSAL-----QL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRDMMIHNMLSTFHKLVKDDPHAPLifrDVFKDELFRL-SMIQSLgedvssVYVDEFGRDISREEIYnATVTDMMM 230
Cdd:cd20674  76 GIRNSLEPVVEQLTQELCERMRAQAGTPV---DIQEEFSLLTcSIICCL------TFGDKEDKDTLVQAFH-DCVQELLK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 231 CaievdWR-------DFFPYLSWVPNKSFEtRVFTTETRRTAVMRALIKQQKERIVRGEAKTcYLDFLL----------A 293
Cdd:cd20674 146 T-----WGhwsiqalDSIPFLRFFPNPGLR-RLKQAVENRDHIVESQLRQHKESLVAGQWRD-MTDYMLqglgqprgekG 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 294 ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDE-TVTEEHLPRLPYLNAVFHETLRR 372
Cdd:cd20674 219 MGQLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGaSPSYKDRARLPLLNATIAEVLRL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 373 HSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFA-GGRLEVAdmykTMAFGAGRRACAG 451
Cdd:cd20674 299 RPVVPLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLePGAANRA----LLPFGCGARVCLG 374
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 50727139 452 SLQATHIACAAVARFVQEFgwRLREGDEEKVDTVQLTA---YKLHPLHVHLT 500
Cdd:cd20674 375 EPLARLELFVFLARLLQAF--TLLPPSDGALPSLQPVAginLKVQPFQVRLQ 424
PLN02966 PLN02966
cytochrome P450 83A1
36-477 2.03e-42

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 157.99  E-value: 2.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   36 KRPNAPPAVPGLPIIGNLHQLKEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALT 115
Cdd:PLN02966  26 KRYKLPPGPSPLPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPHRGHE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  116 VLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLVKddphaplifrdvfKDELFRLSM 195
Cdd:PLN02966 106 FISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAAD-------------KSEVVDISE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  196 IQsLGEDVSSVYVDEFGRDISR--EEI--YNATVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTT--ETRRTAVMRA 269
Cdd:PLN02966 173 LM-LTFTNSVVCRQAFGKKYNEdgEEMkrFIKILYGTQSVLGKIFFSDFFPYCGFLDDLSGLTAYMKEcfERQDTYIQEV 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  270 LIKQQKERIVRGEAKTcYLDFLLA-------ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEI 342
Cdd:PLN02966 252 VNETLDPKRVKPETES-MIDLLMEiykeqpfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEV 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  343 REVC---GDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEW-ESP 418
Cdd:PLN02966 331 REYMkekGSTFVTEDDVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNP 410
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  419 EEWVPERFAGGRLEVADM-YKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG 477
Cdd:PLN02966 411 DEFRPERFLEKEVDFKGTdYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNG 470
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
267-480 2.86e-42

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: 155.76  E-value: 2.86e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 267 MRALIKQQKERIVRGEAKTCYLDFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVC 346
Cdd:cd11054 197 VDEALEELKKKDEEDEEEDSLLEYLLSKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVL 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 347 GD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPER 425
Cdd:cd11054 277 PDgEPITAEDLKKMPYLKACIKESLRLYPVAPGN-GRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPER 355
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 426 F--AGGRLEVADMYKTMAFGAGRRACAG---SLQATHIacaAVARFVQEFgwRLREGDEE 480
Cdd:cd11054 356 WlrDDSENKNIHPFASLPFGFGPRMCIGrrfAELEMYL---LLAKLLQNF--KVEYHHEE 410
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
72-496 4.97e-41

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


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 152.47  E-value: 4.97e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTR-------KLSKALTVLTrdksmVATSDYCDFHKMvKRYVMSSM 144
Cdd:cd11066   1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRptfytfhKVVSSTQGFT-----IGTSPWDESCKR-RRKAAASA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 145 LGTSAQKQFRDIRDMMIHNMLSTFHKLVKDDpHAPLIFRDVFKDELFRLSMIQSLGEDVSSVYVDEFGRDISREE----I 220
Cdd:cd11066  75 LNRPAVQSYAPIIDLESKSFIRELLRDSAEG-KGDIDPLIYFQRFSLNLSLTLNYGIRLDCVDDDSLLLEIIEVEsaisK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 221 YNATVTDmmmcaievdWRDFFPYLSWVPNKS-FETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLL--AENTL 297
Cdd:cd11066 154 FRSTSSN---------LQDYIPILRYFPKMSkFRERADEYRNRRDKYLKKLLAKLKEEIEDGTDKPCIVGNILkdKESKL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 298 TDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDK--QERLYQEIREVCGDETVTEEHL---PRLPYLNAVFHETLRR 372
Cdd:cd11066 225 TDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGQeiQEKAYEEILEAYGNDEDAWEDCaaeEKCPYVVALVKETLRY 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 373 HSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEvADMYKtMAFGAGRRACA 450
Cdd:cd11066 305 FTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWldASGDLI-PGPPH-FSFGAGSRMCA 382
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 50727139 451 GSLQATHIACAAVARFVqeFGWRLREGDEEkvdtvqlTAYKLHPLH 496
Cdd:cd11066 383 GSHLANRELYTAICRLI--LLFRIGPKDEE-------EPMELDPFE 419
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
81-472 5.51e-41

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: 152.48  E-value: 5.51e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  81 GASSVVVLNSTEVAKEAMVAkfSSISTRKLSKALTVLTRDKSMvATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMM 160
Cdd:cd11076  11 GETRVVITSHPETAREILNS--PAFADRPVKESAYELMFNRAI-GFAPYGEYWRNLRRIASNHLFSPRRIAASEPQRQAI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 161 IHNMLSTFHKLVKDDPHAPLifRDVFKdelfrlsmIQSLGEDVSSVYVDEFGRDISREEIynATVTDMMMCAIEV----D 236
Cdd:cd11076  88 AAQMVKAIAKEMERSGEVAV--RKHLQ--------RASLNNIMGSVFGRRYDFEAGNEEA--EELGEMVREGYELlgafN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 237 WRDFFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQK-ERIVRGEAKTCYLDFLL---AENTLTDEQLMMLVWEALIE 312
Cdd:cd11076 156 WSDHLPWLRWLDLQGIRRRCSALVPRVNTFVGKIIEEHRaKRSNRARDDEDDVDVLLslqGEEKLSDSDMIAVLWEMIFR 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 313 AADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDE-TVTEEHLPRLPYLNAVFHETLRRHSPVPLIP-PRFVHEDTKL 390
Cdd:cd11076 236 GTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSrRVADSDVAKLPYLQAVVKETLRLHPPGPLLSwARLAIHDVTV 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 391 AGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEVADM---YKTMAFGAGRRACAG---SLQATHIacaA 462
Cdd:cd11076 316 GGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFvaAEGGADVSVLgsdLRLAPFGAGRRVCPGkalGLATVHL---W 392
                       410
                ....*....|
gi 50727139 463 VARFVQEFGW 472
Cdd:cd11076 393 VAQLLHEFEW 402
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
72-455 6.62e-40

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: 149.37  E-value: 6.62e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMvATSDYCDFHKMVKRYVMSSMLGTSAQK 151
Cdd:cd11028   1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSM-AFSDYGPRWKLHRKLAQNALRTFSNAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRDMM-------IHNMLSTFHKLVKDDPHaPLIFrdvfkdelfrlsmiQSLGEDVSSVYvdeFGRDISRE-----E 219
Cdd:cd11028  80 THNPLEEHVteeaeelVTELTENNGKPGPFDPR-NEIY--------------LSVGNVICAIC---FGKRYSRDdpeflE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 220 IYNaTVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVFTTETRRTaVMRALIKQQKERIVRGEAKTCyLDFLL------- 292
Cdd:cd11028 142 LVK-SNDDFGAFVGAGNPVDVMPWLRYLTRRKLQKFKELLNRLNS-FILKKVKEHLDTYDKGHIRDI-TDALIkaseekp 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 ----AENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTE-EHLPRLPYLNAVFH 367
Cdd:cd11028 219 eeekPEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRlSDRPNLPYTEAFIL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 368 ETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEVADMYKTMAFGAG 445
Cdd:cd11028 299 ETMRHSSFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDKTKVDKFLPFGAG 378
                       410
                ....*....|
gi 50727139 446 RRACAGSLQA 455
Cdd:cd11028 379 RRRCLGEELA 388
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
240-482 1.07e-39

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: 148.96  E-value: 1.07e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 240 FFPYLSWVPNKSFETRVFTTETRRTAVmRALIKQQKERIVRGEAKT--CYLDFLLAENT------LTDEQLM--MLVwea 309
Cdd:cd11069 167 PRWLVRILPWKANREIRRAKDVLRRLA-REIIREKKAALLEGKDDSgkDILSILLRANDfadderLSDEELIdqILT--- 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 310 LIEAA-DTTLVTTEWAMYELAKNPDKQERLYQEIREV---CGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVH 385
Cdd:cd11069 243 FLAAGhETTSTALTWALYLLAKHPDVQERLREEIRAAlpdPPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLT-SREAT 321
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 386 EDTKLAGYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERF-----AGGRLEVADMYKTMAFGAGRRACAGSLQA-THI 458
Cdd:cd11069 322 KDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlepdgAASPGGAGSNYALLTFLHGPRSCIGKKFAlAEM 401
                       250       260
                ....*....|....*....|....
gi 50727139 459 ACaAVARFVQEFGWRLREGDEEKV 482
Cdd:cd11069 402 KV-LLAALVSRFEFELDPDAEVER 424
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
257-451 1.36e-37

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: 143.05  E-value: 1.36e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 257 FTTE---TRRTAVMRALIKQQKERIVRGEAKTCYLDFLLA----ENTLTDEQL------MMlvwealIEAADTTLVTTEW 323
Cdd:cd20628 178 FTNKvikERREELKAEKRNSEEDDEFGKKKRKAFLDLLLEahedGGPLTDEDIreevdtFM------FAGHDTTASAISF 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 324 AMYELAKNPDKQERLYQEIREVCGD--ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEM 401
Cdd:cd20628 252 TLYLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVIKETLRLYPSVPFIG-RRLTEDIKLDGYTIPKGTTV 330
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 50727139 402 VINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd20628 331 VISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIG 380
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
211-477 1.56e-37

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: 142.33  E-value: 1.56e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 211 FGRDISRE--EIYNA--TVTDMMMcaieVDWRDFFPYLSWVPNKSfeTRVFTTETRR-TAVMRALIKqqkERIVRGEAKT 285
Cdd:cd20620 120 FGTDVEGEadEIGDAldVALEYAA----RRMLSPFLLPLWLPTPA--NRRFRRARRRlDEVIYRLIA---ERRAAPADGG 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 286 CYLDFLLA---ENT---LTDEQL------MMLVwealieAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTE 353
Cdd:cd20620 191 DLLSMLLAardEETgepMSDQQLrdevmtLFLA------GHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTA 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 354 EHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEV 433
Cdd:cd20620 265 EDLPQLPYTEMVLQESLRLYPPAWII-GREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAA 343
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 50727139 434 ADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG 477
Cdd:cd20620 344 RPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPG 387
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
239-455 2.10e-37

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: 142.36  E-value: 2.10e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 239 DFFPYLSWV-PNKSFETRVFTTETRRTAVMRALIKQQKERIVRGEAKtCYLDFLLAE--------NTLTDEQLMMLVWEA 309
Cdd:cd20651 155 NQFPWLRFIaPEFSGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNPR-DLIDAYLREmkkkeppsSSFTDDQLVMICLDL 233
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 310 LIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETV-TEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDT 388
Cdd:cd20651 234 FIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLpTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDT 313
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 50727139 389 KLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLeVADMYkTMAFGAGRRACAGSLQA 455
Cdd:cd20651 314 TLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFldEDGKL-LKDEW-FLPFGAGKRRCLGESLA 380
PTZ00404 PTZ00404
cytochrome P450; Provisional
46-494 2.17e-35

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 137.93  E-value: 2.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   46 GLPIIGNLHQLKeKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVA 125
Cdd:PTZ00404  36 PIPILGNLHQLG-NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVT 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  126 TSDycDFHKMVKRYVMSSMLGTSAqKQFRDIRDMMIHNMLSTFHKLVKD----DPHapLIFRDVFKDELFRlsmiqslge 201
Cdd:PTZ00404 115 SSG--EYWKRNREIVGKAMRKTNL-KHIYDLLDDQVDVLIESMKKIESSgetfEPR--YYLTKFTMSAMFK--------- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  202 dvssvYVdeFGRDISREE-IYNATVTDMMMCAIEV-------DWRDFF-----PYLSWVpnkSFETRVFTTetrrtaVMR 268
Cdd:PTZ00404 181 -----YI--FNEDISFDEdIHNGKLAELMGPMEQVfkdlgsgSLFDVIeitqpLYYQYL---EHTDKNFKK------IKK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  269 ALIKQQKERI--VRGEAKTCYLDFLLAE-NTLTDEQLMML---VWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEI 342
Cdd:PTZ00404 245 FIKEKYHEHLktIDPEVPRDLLDLLIKEyGTNTDDDILSIlatILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEI 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  343 REVCGDET-VTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLA-GYDVPAGTEMVINLYGCNMNRKEWESPEE 420
Cdd:PTZ00404 325 KSTVNGRNkVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIGgGHFIPKDAQILINYYSLGRNEKYFENPEQ 404
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139  421 WVPERFaggrLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFgwRLREGDEEKVDTVQLTAYKLHP 494
Cdd:PTZ00404 405 FDPSRF----LNPDSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNF--KLKSIDGKKIDETEEYGLTLKP 472
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
72-451 4.37e-35

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: 135.77  E-value: 4.37e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMV---AKFSSistrklskaltvltRDKSMVatsdycdFHKMVKRY--VMSSMLG 146
Cdd:cd11026   1 YGPVFTVYLGSKPVVVLCGYEAVKEALVdqaEEFSG--------------RPPVPL-------FDRVTKGYgvVFSNGER 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 147 TSAQKQF--RDIRDM-M------------IHNMLSTFHKlVKDDPHAP--------------LIFRDVF--KDELFrLSM 195
Cdd:cd11026  60 WKQLRRFslTTLRNFgMgkrsieeriqeeAKFLVEAFRK-TKGKPFDPtfllsnavsnvicsIVFGSRFdyEDKEF-LKL 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 196 IQSLGED---VSSVYVdefgrdisreEIYNAtvtdmmmcaievdwrdFFPYLSWVPnkSFETRVFTTETRRTAVMRALIK 272
Cdd:cd11026 138 LDLINENlrlLSSPWG----------QLYNM----------------FPPLLKHLP--GPHQKLFRNVEEIKSFIRELVE 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 273 QQKERIVRGEAKT---CYLDFLLAEN-----TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIRE 344
Cdd:cd11026 190 EHRETLDPSSPRDfidCFLLKMEKEKdnpnsEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDR 269
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 345 VCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVP 423
Cdd:cd11026 270 VIGrNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNP 349
                       410       420       430
                ....*....|....*....|....*....|
gi 50727139 424 ERF--AGGRLEVADMYktMAFGAGRRACAG 451
Cdd:cd11026 350 GHFldEQGKFKKNEAF--MPFSAGKRVCLG 377
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
72-451 5.40e-35

cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 135.79  E-value: 5.40e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSkALTVLTRDKSMVATSDYcDFHKMvkRYVMSSMLGTSAQK 151
Cdd:cd11055   2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLF-ILLDEPFDSSLLFLKGE-RWKRL--RTTLSPTFSSGKLK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRDMMIHNMLSTFHKLVKDDphAPLIFRDVFKdeLFRLSMIQSLG----EDVSSVYVDEFGRDISReeIYNATVTD 227
Cdd:cd11055  78 LMVPIINDCCDELVEKLEKAAETG--KPVDMKDLFQ--GFTLDVILSTAfgidVDSQNNPDDPFLKAAKK--IFRNSIIR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 228 MMMCAIEVDWRdFFPYLSWVPNKSFETRVFTTEtrrtaVMRALIKQQKErivrgEAKTCYLDFL------------LAEN 295
Cdd:cd11055 152 LFLLLLLFPLR-LFLFLLFPFVFGFKSFSFLED-----VVKKIIEQRRK-----NKSSRRKDLLqlmldaqdsdedVSKK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 296 TLTDEQLM---MLVweaLIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD-ETVTEEHLPRLPYLNAVFHETLR 371
Cdd:cd11055 221 KLTDDEIVaqsFIF---LLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDdGSPTYDTVSKLKYLDMVINETLR 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 372 RHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd11055 298 LYPPAFFIS-RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIG 376
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
282-470 6.15e-35

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: 135.68  E-value: 6.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 282 EAKTCYLDFLL---AENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLP 357
Cdd:cd11074 211 EGLKCAIDHILdaqKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGpGVQITEPDLH 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 358 RLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEV---A 434
Cdd:cd11074 291 KLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVeanG 370
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 50727139 435 DMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd11074 371 NDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNF 406
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
72-451 2.59e-34

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: 133.99  E-value: 2.59e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSS--MLGTSA 149
Cdd:cd20673   1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGKDIAFADYSATWQLHRKLVHSAfaLFGEGS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 150 QKQFRDIRD--MMIHNMLSTFHKLVKDdpHAPLIFRDV------------FKDELFRLSMIQSLGEDVssvyVDEFGRDi 215
Cdd:cd20673  81 QKLEKIICQeaSSLCDTLATHNGESID--LSPPLFRAVtnvicllcfnssYKNGDPELETILNYNEGI----VDTVAKD- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 216 sreeiynatvtdmmmcaievDWRDFFPYLSWVPNKSFETRVFTTETRrTAVMRALIKQQKERIvRGEAKTCYLDFLL--- 292
Cdd:cd20673 154 --------------------SLVDIFPWLQIFPNKDLEKLKQCVKIR-DKLLQKKLEEHKEKF-SSDSIRDLLDALLqak 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 --AENT----------LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRL 359
Cdd:cd20673 212 mnAENNnagpdqdsvgLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGfSRTPTLSDRNHL 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 360 PYLNAVFHETLR-RhsPV-PLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF---AGGRLEVA 434
Cdd:cd20673 292 PLLEATIREVLRiR--PVaPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFldpTGSQLISP 369
                       410
                ....*....|....*...
gi 50727139 435 DM-YktMAFGAGRRACAG 451
Cdd:cd20673 370 SLsY--LPFGAGPRVCLG 385
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
119-470 2.26e-33

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: 131.27  E-value: 2.26e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 119 RDKSMVATSDYcDFH----KMV-KRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKL--VkddphaplifrDVFKdeLF 191
Cdd:cd11059  42 GGPNLFSTLDP-KEHsarrRLLsGVYSKSSLLRAAMEPIIRERVLPLIDRIAKEAGKSgsV-----------DVYP--LF 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 192 RLsmiqsLGEDVSSVYV-------DEFGRDISREEIYNATVTDMMMCAIeVDWRDFFPYLSWVPNKSFetrVFTTETRRT 264
Cdd:cd11059 108 TA-----LAMDVVSHLLfgesfgtLLLGDKDSRERELLRRLLASLAPWL-RWLPRYLPLATSRLIIGI---YFRAFDEIE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 265 AVMRALIKQQKERIVRGEAKTCYLDFLLA------ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERL 338
Cdd:cd11059 179 EWALDLCARAESSLAESSDSESLTVLLLEklkglkKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKL 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 339 YQEIREVCGDETVTEEH--LPRLPYLNAVFHETLRRHSPVPLIPPRFVHED-TKLAGYDVPAGTemVINLYGCNMNRKE- 414
Cdd:cd11059 259 REELAGLPGPFRGPPDLedLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgATIGGYYIPGGT--IVSTQAYSLHRDPe 336
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50727139 415 -WESPEEWVPERFAGGRLEVADMYKT--MAFGAGRRACAGSlqatHIACA----AVARFVQEF 470
Cdd:cd11059 337 vFPDPEEFDPERWLDPSGETAREMKRafWPFGSGSRMCIGM----NLALMemklALAAIYRNY 395
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
260-470 3.43e-33

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: 130.75  E-value: 3.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 260 ETRRtavmRALIKQQKERIVRGEaktcYLDFL----LAE----NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKN 331
Cdd:cd20659 186 KKRR----KELEDNKDEALSKRK----YLDFLdillTARdedgKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKH 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 332 PDKQERLYQEIREVCGD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNM 410
Cdd:cd20659 258 PEHQQKCREEVDEVLGDrDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIA-RTLTKPITIDGVTLPAGTLIAINIYALHH 336
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 411 NRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd20659 337 NPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRF 396
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
75-486 7.29e-33

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: 130.18  E-value: 7.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  75 IYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFR 154
Cdd:cd20658   3 IACIRLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQWLH 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 155 DIRDMMIHNMLSTFHKLVKDDPHAPLI-FRD--------VFKDELFrlsmiqslgedvSSVYVDEfGRDISR---EEIYN 222
Cdd:cd20658  83 GKRTEEADNLVAYVYNMCKKSNGGGLVnVRDaarhycgnVIRKLMF------------GTRYFGK-GMEDGGpglEEVEH 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 223 A-TVTDMMMCAIEVDWRDFFPYLSWVPNKSFETRVftteTRRTAVMRAL---IKQQKERIVRGEAKTCYLDFL-----LA 293
Cdd:cd20658 150 MdAIFTALKCLYAFSISDYLPFLRGLDLDGHEKIV----REAMRIIRKYhdpIIDERIKQWREGKKKEEEDWLdvfitLK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 294 EN----TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHE 368
Cdd:cd20658 226 DEngnpLLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGkERLVQESDIPNLNYVKACARE 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 369 TLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVA----DMyKTMAFGA 444
Cdd:cd20658 306 AFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTltepDL-RFISFST 384
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 50727139 445 GRRACAGSLQATHIACAAVARFVQEFGWRLrEGDEEKVDTVQ 486
Cdd:cd20658 385 GRRGCPGVKLGTAMTVMLLARLLQGFTWTL-PPNVSSVDLSE 425
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
297-500 7.36e-32

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: 126.60  E-value: 7.36e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVFHETLRRHSPV 376
Cdd:cd11049 216 LSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPATFEDLPRLTYTRRVVTEALRLYPPV 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 377 PLIPPRFVhEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAG---SL 453
Cdd:cd11049 296 WLLTRRTT-ADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGdtfAL 374
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 50727139 454 QATHIACAAVARfvqefGWRLREGDEEKVDTVQLTAykLHPLHVHLT 500
Cdd:cd11049 375 TELTLALATIAS-----RWRLRPVPGRPVRPRPLAT--LRPRRLRMR 414
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
72-477 1.37e-31

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


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 125.79  E-value: 1.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVlTRDKSMVATSDYCDFHKMVKryvmsSMLGTSAQK 151
Cdd:cd11042   5 YGDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTP-PFGGGVVYYAPFAEQKEQLK-----FGLNILRRG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRDMMIHNMLSTFHKLVKDDPhaplifRDVFKD--ELFRLSMIQSL-GEDVSSVYVDEFGrdisreEIYNatvtDM 228
Cdd:cd11042  79 KLRGYVPLIVEEVEKYFAKWGESGE------VDLFEEmsELTILTASRCLlGKEVRELLDDEFA------QLYH----DL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 229 MMCAIEVDWrdFFPYLswvPNKSFETRvftTETRR--TAVMRALIKQQKERIVRGEaktcyLDFL--LAENT------LT 298
Cdd:cd11042 143 DGGFTPIAF--FFPPL---PLPSFRRR---DRARAklKEIFSEIIQKRRKSPDKDE-----DDMLqtLMDAKykdgrpLT 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 299 DEQL--MMLvweALIEAA-DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD--ETVTEEHLPRLPYLNAVFHETLRRH 373
Cdd:cd11042 210 DDEIagLLI---ALLFAGqHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDgdDPLTYDVLKEMPLLHACIKETLRLH 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 374 SPVPLIpPRFVHEDTKL--AGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLE--VADMYKTMAFGAGRRAC 449
Cdd:cd11042 287 PPIHSL-MRKARKPFEVegGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEdsKGGKFAYLPFGAGRHRC 365
                       410       420       430
                ....*....|....*....|....*....|..
gi 50727139 450 AGS----LQATHIacaaVARFVQEFGWRLREG 477
Cdd:cd11042 366 IGEnfayLQIKTI----LSTLLRNFDFELVDS 393
PLN03018 PLN03018
homomethionine N-hydroxylase
41-493 1.44e-31

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 127.82  E-value: 1.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   41 PPAVPGLPIIGNLHQLKEKKPHQTFAKWA--EIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTR-KLSKALTVL 117
Cdd:PLN03018  42 PPGPPGWPILGNLPELIMTRPRSKYFHLAmkELKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRpQLSIMETIG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  118 TRDKSMvATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLVKDDPHAPLifRDVFKDELFRLSMIQ 197
Cdd:PLN03018 122 DNYKSM-GTSPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYQRSETVDV--RELSRVYGYAVTMRM 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  198 SLGE---DVSSVYVDEfGRDISREEIYNATVTDMMMCAIEVDWRDFFPylSWVPNKSF---ETRVFTTETRRTAVMRALI 271
Cdd:PLN03018 199 LFGRrhvTKENVFSDD-GRLGKAEKHHLEVIFNTLNCLPGFSPVDYVE--RWLRGWNIdgqEERAKVNVNLVRSYNNPII 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  272 KQQKERIVRGEAKTCYLDFLLAENTLTDEQLMMLVW---------EALIEAADTTLVTTEWAMYELAKNPDKQERLYQEI 342
Cdd:PLN03018 276 DERVELWREKGGKAAVEDWLDTFITLKDQNGKYLVTpdeikaqcvEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKEL 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  343 REVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEW 421
Cdd:PLN03018 356 DEVVGkDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVY 435
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  422 VPERFAGGR---LEVADMYKTM---AFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG----DEEKVDTVQLTAYK 491
Cdd:PLN03018 436 EPERHLQGDgitKEVTLVETEMrfvSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDfgplSLEEDDASLLMAKP 515

                 ..
gi 50727139  492 LH 493
Cdd:PLN03018 516 LL 517
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
72-451 1.60e-31

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: 126.04  E-value: 1.60e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVaTSDYCDFHKMVKRYVMSSM------- 144
Cdd:cd20666   1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIV-FAPYGPVWRQQRKFSHSTLrhfglgk 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 145 --LGTSAQKQFRDIRDMMIHNmlstfhklvKDDPHAPlifrdvfkDELFRLSmiqslgedVSSVYVD-EFGRDISREEIY 221
Cdd:cd20666  80 lsLEPKIIEEFRYVKAEMLKH---------GGDPFNP--------FPIVNNA--------VSNVICSmSFGRRFDYQDVE 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 222 NATVTDMMMCAIEVDWR------DFFPYLSWVPNKSFEtRVFTTETRRTAVMRALIKQQKERIVRGEAKTcYLDFLL--- 292
Cdd:cd20666 135 FKTMLGLMSRGLEISVNsaailvNICPWLYYLPFGPFR-ELRQIEKDITAFLKKIIADHRETLDPANPRD-FIDMYLlhi 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 -------AENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNA 364
Cdd:cd20666 213 eeeqknnAESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGpDRAPSLTDKAQMPFTEA 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 365 VFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGA 444
Cdd:cd20666 293 TIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGI 372

                ....*..
gi 50727139 445 GRRACAG 451
Cdd:cd20666 373 GRRVCMG 379
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
241-501 2.24e-31

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: 125.90  E-value: 2.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 241 FPYLSWVPNKSFETRVFTTE--TRRTAVMRALIKQQKERIVRGEAKTCY-----LDFLLAENTLTDEQLMMLVWEALIEA 313
Cdd:cd11070 156 FPFLDRLPWVLFPSRKRAFKdvDEFLSELLDEVEAELSADSKGKQGTESvvasrLKRARRSGGLTEKELLGNLFIFFIAG 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 314 ADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDE---TVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKL 390
Cdd:cd11070 236 HETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEpddWDYEEDFPKLPYLLAVIYETLRLYPPVQLL-NRKTTEPVVV 314
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 391 -----AGYDVPAGTEMVINLYGCNMNRKEWES-PEEWVPERFAGG--------RLEVADMykTM-AFGAGRRACAGSLQA 455
Cdd:cd11070 315 itglgQEIVIPKGTYVGYNAYATHRDPTIWGPdADEFDPERWGSTsgeigaatRFTPARG--AFiPFSAGPRACLGRKFA 392
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 50727139 456 THIACAAVARFVQEFGWRLREGDEEKVDTVQLTAYKLHPLHVHLTR 501
Cdd:cd11070 393 LVEFVAALAELFRQYEWRVDPEWEEGETPAGATRDSPAKLRLRFRE 438
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
67-483 1.21e-30

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: 123.08  E-value: 1.21e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  67 KWAEIYGPIYTIR-TGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDycDFHKMVKRYVMSSML 145
Cdd:cd11053   6 RLRARYGDVFTLRvPGLGPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLLLLDG--DRHRRRRKLLMPAFH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 146 GtsaqKQFRDIRDMMIHNMLSTFHKLVKDDPhapliFRDVfkDELFRLSM---IQSL-GEDVSSVYvDEFGRDISReeIY 221
Cdd:cd11053  84 G----ERLRAYGELIAEITEREIDRWPPGQP-----FDLR--ELMQEITLeviLRVVfGVDDGERL-QELRRLLPR--LL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 222 NATVTDMMMC-AIEVDWRDFFPYLswvpnksfetRVFTTETRRTAVMRALIKQqkERIVRGEAKTCYLDFLLA-----EN 295
Cdd:cd11053 150 DLLSSPLASFpALQRDLGPWSPWG----------RFLRARRRIDALIYAEIAE--RRAEPDAERDDILSLLLSardedGQ 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 296 TLTDE----QLMMLVwealieAA--DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVteEHLPRLPYLNAVFHET 369
Cdd:cd11053 218 PLSDEelrdELMTLL------FAghETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP--EDIAKLPYLDAVIKET 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 370 LRRHSPVPLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLevaDMYKTMAFGAGRRAC 449
Cdd:cd11053 290 LRLYPVAPLV-PRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKP---SPYEYLPFGGGVRRC 365
                       410       420       430
                ....*....|....*....|....*....|....
gi 50727139 450 AGSLQATHIACAAVARFVQEFGWRLREGDEEKVD 483
Cdd:cd11053 366 IGAAFALLEMKVVLATLLRRFRLELTDPRPERPV 399
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
239-483 2.92e-30

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: 122.52  E-value: 2.92e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 239 DFFPYLSWVPNKSFETRVFTTETRRT-AVMRALIKQQKERIVRGEAK------TCYLDFLLAENT--------LTDEQLM 303
Cdd:cd20652 157 NFLPFLRHLPSYKKAIEFLVQGQAKThAIYQKIIDEHKRRLKPENPRdaedfeLCELEKAKKEGEdrdlfdgfYTDEQLH 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 304 MLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETLRRHSPVPLIPPR 382
Cdd:cd20652 237 HLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDlVTLEDLSSLPYLQACISESQRIRSVVPLGIPH 316
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 383 FVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEVADMYktMAFGAGRRACAGSLQATHIAC 460
Cdd:cd20652 317 GCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEAF--IPFQTGKRMCLGDELARMILF 394
                       250       260
                ....*....|....*....|...
gi 50727139 461 AAVARFVQEFgwRLREGDEEKVD 483
Cdd:cd20652 395 LFTARILRKF--RIALPDGQPVD 415
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
72-451 8.45e-30

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: 121.07  E-value: 8.45e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDycDFHKMVKRYVMSSMLGTSAQK 151
Cdd:cd20664   1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNG--ENWKEMRRFTLTTLRDFGMGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 qfRDIRDmmihnmlstfhKLVKDDPHAPLIFrDVFKDELF--RLSMIQSLGEDVSSVYvdeFGrdiSREEIYNATVTDMM 229
Cdd:cd20664  79 --KTSED-----------KILEEIPYLIEVF-EKHKGKPFetTLSMNVAVSNIIASIV---LG---HRFEYTDPTLLRMV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 230 MCAIE---------VDWRDFFPYLSWVPNK-------SFETRVFTTET------------RRTAVMRALIKQQKERivrg 281
Cdd:cd20664 139 DRINEnmkltgspsVQLYNMFPWLGPFPGDinkllrnTKELNDFLMETfmkhldvlepndQRGFIDAFLVKQQEEE---- 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 282 EAKTCYLDfllaentltDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPY 361
Cdd:cd20664 215 ESSDSFFH---------DDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKNMPY 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 362 LNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEVADMYkt 439
Cdd:cd20664 286 TDAVIHEIQRFANIVPMNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFldSQGKFVKRDAF-- 363
                       410
                ....*....|..
gi 50727139 440 MAFGAGRRACAG 451
Cdd:cd20664 364 MPFSAGRRVCIG 375
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
310-502 3.19e-29

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: 119.60  E-value: 3.19e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 310 LIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTK 389
Cdd:cd11068 239 LIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRLWPTAPAF-ARKPKEDTV 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 390 LAG-YDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERFAGGRLEV--ADMYKtmAFGAGRRACAGSLQATHIACAAVAR 465
Cdd:cd11068 318 LGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKlpPNAWK--PFGNGQRACIGRQFALQEATLVLAM 395
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 50727139 466 FVQEFGWRLREGDEEKVDtVQLTAyKLHPLHVHLTRR 502
Cdd:cd11068 396 LLQRFDFEDDPDYELDIK-ETLTL-KPDGFRLKARPR 430
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
61-470 3.44e-29

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


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 119.37  E-value: 3.44e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  61 PHqtFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALtvltrdKSM----VATSDYCDFHKMv 136
Cdd:cd11052   2 PH--YYHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPGL------KKLlgrgLVMSNGEKWAKH- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 137 kRYVMS---------SMLGtsaqkqfrdirdMMI---HNMLSTFHKLVKDDPHAPLIFRDvfkdelfrlsmIQSLGEDVS 204
Cdd:cd11052  73 -RRIANpafhgeklkGMVP------------AMVesvSDMLERWKKQMGEEGEEVDVFEE-----------FKALTADII 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 205 SVyvDEFGRDISR-EEIYNaTVTDMMMCAIEVDWRDFFPYLSWVPNKSfETRVFTTETRRTAVMRALIKQQKERIVRGEA 283
Cdd:cd11052 129 SR--TAFGSSYEEgKEVFK-LLRELQKICAQANRDVGIPGSRFLPTKG-NKKIKKLDKEIEDSLLEIIKKREDSLKMGRG 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 284 KTCYLDFL---LAENTLTDEQLMMLVWEALIEAA-------DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTE 353
Cdd:cd11052 205 DDYGDDLLgllLEANQSDDQNKNMTVQEIVDECKtfffaghETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPS 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 354 EHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERFAGGrle 432
Cdd:cd11052 285 DSLSKLKTVSMVINESLRLYPPAVFL-TRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADG--- 360
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 50727139 433 VADMYKT----MAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd11052 361 VAKAAKHpmafLPFGLGPRNCIGQNFATMEAKIVLAMILQRF 402
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-502 9.67e-29

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: 117.69  E-value: 9.67e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  61 PHQTFAKWAEiYGPIYTIRTGASSVVVLNSTEVAKEAMV--AKFSSisTRKLSKALTVLTRDKSMVATSDYcDFHKMVKR 138
Cdd:COG2124  21 PYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRdpRTFSS--DGGLPEVLRPLPLLGDSLLTLDG-PEHTRLRR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 139 YVMSSMlgtsAQKQFRDIRDMM---IHNMLSTFHklvkddPHAPLIFRDVFKDELFRLsMIQSLgedvssvyvdeFGRDI 215
Cdd:COG2124  97 LVQPAF----TPRRVAALRPRIreiADELLDRLA------ARGPVDLVEEFARPLPVI-VICEL-----------LGVPE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 216 SREEIYNATVTDMMmcaievdwrDFFPYLSWVPNKSFETRVftteTRRTAVMRALIKQqkeriVRGEAKTCYLDFLLAE- 294
Cdd:COG2124 155 EDRDRLRRWSDALL---------DALGPLPPERRRRARRAR----AELDAYLRELIAE-----RRAEPGDDLLSALLAAr 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 295 ---NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEirevcgdetvteehlprLPYLNAVFHETLR 371
Cdd:COG2124 217 ddgERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLR 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 372 RHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERfaggrlevaDMYKTMAFGAGRRACAG 451
Cdd:COG2124 280 LYPPVPLLP-RTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLG 349
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 50727139 452 SLQATHIACAAVARFVQEF-GWRLREGDEEKVDTVqLTAYKLHPLHVHLTRR 502
Cdd:COG2124 350 AALARLEARIALATLLRRFpDLRLAPPEELRWRPS-LTLRGPKSLPVRLRPR 400
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
62-477 2.28e-28

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: 116.85  E-value: 2.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  62 HQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVakfssisTRKLSKALTVLTRDKSMVAT--------SDyCD-- 131
Cdd:cd20613   1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLI-------TLNLPKPPRVYSRLAFLFGErflgnglvTE-VDhe 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 132 ------------FHKmvkRYVMSSMlgtsaqKQFRDIRDMMIH------------NMLSTFHKLVKDdphapLIFRDVFk 187
Cdd:cd20613  73 kwkkrrailnpaFHR---KYLKNLM------DEFNESADLLVEklskkadgktevNMLDEFNRVTLD-----VIAKVAF- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 188 delfrlSM-IQSLGEDVSsvyvdEFGRDISreeiynatvtdMMMCAIEVDWRDFFpylsWVPNKSfeTRVFTTETRRTA- 265
Cdd:cd20613 138 ------GMdLNSIEDPDS-----PFPKAIS-----------LVLEGIQESFRNPL----LKYNPS--KRKYRREVREAIk 189
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 266 ----VMRALIKQQKERIVRGEAK-----TCYLDFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQE 336
Cdd:cd20613 190 flreTGRECIEERLEALKRGEEVpndilTHILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILK 269
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 337 RLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEW 415
Cdd:cd20613 270 RLQAEVDEVLGSKQyVEYEDLGKLEYLSQVLKETLRLYPPVPGTS-RELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYF 348
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50727139 416 ESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAG----SLQATHIacaaVARFVQEFGWRLREG 477
Cdd:cd20613 349 EDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGqqfaQIEAKVI----LAKLLQNFKFELVPG 410
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
210-470 2.78e-28

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: 116.87  E-value: 2.78e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 210 EFGRDISREEIYNATVTDMMMcaievdwrdFFPYLSwvpnKSFETRVFTTETrrTAVMRALIKQ-----QKERIVRGEak 284
Cdd:cd11056 140 EMGRRLFEPSRLRGLKFMLLF---------FFPKLA----RLLRLKFFPKEV--EDFFRKLVRDtieyrEKNNIVRND-- 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 285 tcYLDFL--LAENTLTDEQLMMLVWEALIEAA----------DTTLVTTEWAMYELAKNPDKQERLYQEIREV--CGDET 350
Cdd:cd11056 203 --FIDLLleLKKKGKIEDDKSEKELTDEELAAqafvfflagfETSSSTLSFALYELAKNPEIQEKLREEIDEVleKHGGE 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 351 VTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYDV--PAGTEMVINLYGCNMNRKEWESPEEWVPERFAG 428
Cdd:cd11056 281 LTYEALQEMKYLDQVVNETLRKYPPLPFL-DRVCTKDYTLPGTDVviEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSP 359
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 50727139 429 GRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd11056 360 ENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNF 401
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
294-480 3.10e-28

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: 116.26  E-value: 3.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 294 ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVcGDETVTEEHLPRLPYLNAVFHETLRRH 373
Cdd:cd11045 204 GDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL-GKGTLDYEDLGQLEVTDWVFKEALRLV 282
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 374 SPVPLIPPRFVHeDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVA-DMYKTMAFGAGRRACAGS 452
Cdd:cd11045 283 PPVPTLPRRAVK-DTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKvHRYAWAPFGGGAHKCIGL 361
                       170       180
                ....*....|....*....|....*...
gi 50727139 453 LQATHIACAAVARFVQEFGWRLREGDEE 480
Cdd:cd11045 362 HFAGMEVKAILHQMLRRFRWWSVPGYYP 389
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
240-451 4.65e-28

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: 116.14  E-value: 4.65e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 240 FFPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRG-EAKTCYLDFL--------LAENTLTDEQLMMLVWEAL 310
Cdd:cd11060 152 QIPWLDRLLLKNPLGPKRKDKTGFGPLMRFALEAVAERLAEDaESAKGRKDMLdsfleaglKDPEKVTDREVVAEALSNI 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 311 IEAADTTLVTTEWAMYELAKNPDKQERLYQEI----REVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHE 386
Cdd:cd11060 232 LAGSDTTAIALRAILYYLLKNPRVYAKLRAEIdaavAEGKLSSPITFAEAQKLPYLQAVIKEALRLHPPVGLPLERVVPP 311
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50727139 387 --DTkLAGYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERF--AGGRlEVADMYKT-MAFGAGRRACAG 451
Cdd:cd11060 312 ggAT-ICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleADEE-QRRMMDRAdLTFGAGSRTCLG 380
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
257-451 2.31e-27

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: 113.90  E-value: 2.31e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 257 FTTET--RRTAVMRALIKQQKER----IVRGEAKTCYLDFLL----AENTLTDEQLMMLVWEALIEAADTTLVTTEWAMY 326
Cdd:cd20660 178 FTNKViqERKAELQKSLEEEEEDdedaDIGKRKRLAFLDLLLeaseEGTKLSDEDIREEVDTFMFEGHDTTAAAINWALY 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 327 ELAKNPDKQERLYQEIREVCGDET--VTEEHLPRLPYLNAVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVIN 404
Cdd:cd20660 258 LIGSHPEVQEKVHEELDRIFGDSDrpATMDDLKEMKYLECVIKEALRLFPSVPMFG-RTLSEDIEIGGYTIPKGTTVLVL 336
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 50727139 405 LYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd20660 337 TYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIG 383
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
241-494 2.56e-27

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: 113.86  E-value: 2.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 241 FPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQ-KERI-VRGEAKTCYLDFLLA---ENTLTDEQLMMLVWEA--LIEA 313
Cdd:cd11061 148 LGHAPWLRPLLLDLPLFPGATKARKRFLDFVRAQlKERLkAEEEKRPDIFSYLLEakdPETGEGLDLEELVGEArlLIVA 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 314 -ADTTLVTTEWAMYELAKNPDKQERLYQEIREVC--GDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFV-HEDTK 389
Cdd:cd11061 228 gSDTTATALSAIFYYLARNPEAYEKLRAELDSTFpsDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGLPRETpPGGLT 307
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 390 LAGYDVPAGTEMVINLYGcnMNRKE--WESPEEWVPERFAGGRLEVADMYKT-MAFGAGRRACAG------SLQAThiac 460
Cdd:cd11061 308 IDGEYIPGGTTVSVPIYS--IHRDEryFPDPFEFIPERWLSRPEELVRARSAfIPFSIGPRGCIGknlaymELRLV---- 381
                       250       260       270
                ....*....|....*....|....*....|....*
gi 50727139 461 aaVARFVQEFGWRLREGDEEKV-DTVQLTAYKLHP 494
Cdd:cd11061 382 --LARLLHRYDFRLAPGEDGEAgEGGFKDAFGRGP 414
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
72-479 3.04e-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: 113.43  E-value: 3.04e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKlSKALTVLTRDKSMVATSDycDFHKMVKRYVMSSMLGTSAQK 151
Cdd:cd11043   5 YGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWY-PKSVRKLLGKSSLLTVSG--EEHKRLRGLLLSFLGPEALKD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QF-RDIRDMMIHNmLSTFHKLVKddphapLIFRDVFKDELFRLSMIQSLGEDVSSVyVDEFGRDISreeiynaTVTDMMM 230
Cdd:cd11043  82 RLlGDIDELVRQH-LDSWWRGKS------VVVLELAKKMTFELICKLLLGIDPEEV-VEELRKEFQ-------AFLEGLL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 231 cAIEVDWrDFFPYlswvpNKSFETRvftteTRRTAVMRALIKQQKERIVRGEAKTCYLDFLLAE-----NTLTDEQLMML 305
Cdd:cd11043 147 -SFPLNL-PGTTF-----HRALKAR-----KRIRKELKKIIEERRAELEKASPKGDLLDVLLEEkdedgDSLTDEEILDN 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 306 VWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQE----IREVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpP 381
Cdd:cd11043 215 ILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeiAKRKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGV-F 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 382 RFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVAdmYKTMAFGAGRRACAGSLQATHIACA 461
Cdd:cd11043 294 RKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVP--YTFLPFGGGPRLCPGAELAKLEILV 371
                       410
                ....*....|....*...
gi 50727139 462 AVARFVQEFGWRLREGDE 479
Cdd:cd11043 372 FLHHLVTRFRWEVVPDEK 389
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
64-494 6.76e-27

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: 112.84  E-value: 6.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  64 TFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMvakfssistrkLSKALTVltRDKSMVATsdycdfHKMVkryVMSS 143
Cdd:cd11046   2 DLYKWFLEYGPIYKLAFGPKSFLVISDPAIAKHVL-----------RSNAFSY--DKKGLLAE------ILEP---IMGK 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 144 MLGTSAQKQFRDIRDMMIHnmlsTFHKLVKDDphapliFRDVFKDELFRLSM-IQSLGEDVSSVYVDEFGR----DISRE 218
Cdd:cd11046  60 GLIPADGEIWKKRRRALVP----ALHKDYLEM------MVRVFGRCSERLMEkLDAAAETGESVDMEEEFSsltlDIIGL 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 219 EIYN----------ATVTDMMMCAIEVD-------WRDFFPYLSWVPNKSFETRvfTTETRRTAVMRALIKQQKE----- 276
Cdd:cd11046 130 AVFNydfgsvteesPVIKAVYLPLVEAEhrsvwepPYWDIPAALFIVPRQRKFL--RDLKLLNDTLDDLIRKRKEmrqee 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 277 ------RIVRGEAKTCYLDFLLA--ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD 348
Cdd:cd11046 208 dielqqEDYLNEDDPSLLRFLVDmrDEDVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGD 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 349 ET-VTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAG-YDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF 426
Cdd:cd11046 288 RLpPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGgVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERF 367
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50727139 427 ----AGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEKVDTvqlTAYKLHP 494
Cdd:cd11046 368 ldpfINPPNEVIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGMT---TGATIHT 436
PLN02971 PLN02971
tryptophan N-hydroxylase
35-486 8.31e-27

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 113.59  E-value: 8.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   35 RKRPNA-PPAVPGLPIIGNLHQLKEKKPhqtFAKW-----AEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTR 108
Cdd:PLN02971  52 NKKLHPlPPGPTGFPIVGMIPAMLKNRP---VFRWlhslmKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  109 KLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHNMLSTFHKLVKDDphAPLIFRdvFKD 188
Cdd:PLN02971 129 PLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNS--EPVDLR--FVT 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  189 ELFRLSMIQSL--GEDVSSVYVDEFG----RDISR-EEIYNATVTDMMMCAievdwRDFFPYLSWVPNKSFETRVftteT 261
Cdd:PLN02971 205 RHYCGNAIKRLmfGTRTFSEKTEPDGgptlEDIEHmDAMFEGLGFTFAFCI-----SDYLPMLTGLDLNGHEKIM----R 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  262 RRTAVMRAL---IKQQKERIVRGEAKTCYLDFL---------LAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELA 329
Cdd:PLN02971 276 ESSAIMDKYhdpIIDERIKMWREGKRTQIEDFLdifisikdeAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMI 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  330 KNPDKQERLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGC 408
Cdd:PLN02971 356 NKPEILHKAMEEIDRVVGKERfVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGL 435
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  409 NMNRKEWESPEEWVPERFAGGRLEVA---DMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLrEGDEEKVDTV 485
Cdd:PLN02971 436 GRNPKVWSDPLSFKPERHLNECSEVTlteNDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKL-AGSETRVELM 514

                 .
gi 50727139  486 Q 486
Cdd:PLN02971 515 E 515
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
271-470 1.34e-26

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: 111.93  E-value: 1.34e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 271 IKQQKERivRGEAKTCYLDFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET 350
Cdd:cd20647 209 IQKQMDR--GEEVKGGLLTYLLVSKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRV 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 351 V-TEEHLPRLPYLNAVFHETLRRHspvPLIP--PRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF- 426
Cdd:cd20647 287 VpTAEDVPKLPLIRALLKETLRLF---PVLPgnGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWl 363
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 50727139 427 AGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd20647 364 RKDALDRVDNFGSIPFGYGIRSCIGRRIAELEIHLALIQLLQNF 407
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
271-470 1.45e-26

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: 111.68  E-value: 1.45e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 271 IKQQKERIVRGE-AKTCYLDFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVC-GD 348
Cdd:cd20646 202 MEEIEERVDRGEpVEGEYLTYLLSSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCpGD 281
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 349 ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAG 428
Cdd:cd20646 282 RIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLR 361
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 50727139 429 GRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd20646 362 DGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRF 403
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
241-451 1.83e-25

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


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 108.56  E-value: 1.83e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 241 FPYLSWVpnKSFETRVFTTETRRT-AVMRALIKQQKERIVRG----EAKTCYLDFLLA----ENTLTDEQLMMLVWEALI 311
Cdd:cd11083 155 FPYWRYL--RLPADRALDRALVEVrALVLDIIAAARARLAANpalaEAPETLLAMMLAeddpDARLTDDEIYANVLTLLL 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 312 EAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD--ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRfVHEDTK 389
Cdd:cd11083 233 AGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGarVPPLLEALDRLPYLEAVARETLRLKPVAPLLFLE-PNEDTV 311
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139 390 LAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVA--DMYKTMAFGAGRRACAG 451
Cdd:cd11083 312 VGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEphDPSSLLPFGAGPRLCPG 375
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
268-451 2.26e-25

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: 108.52  E-value: 2.26e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 268 RALIKQQKER-IVRGEAKTCYLDFLLA-----ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQE 341
Cdd:cd20678 200 KEQLQDEGELeKIKKKRHLDFLDILLFakdenGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREE 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 342 IREVCGD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEE 420
Cdd:cd20678 280 IREILGDgDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEV 359
                       170       180       190
                ....*....|....*....|....*....|.
gi 50727139 421 WVPERFAGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd20678 360 FDPLRFSPENSSKRHSHAFLPFSAGPRNCIG 390
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
288-475 1.25e-24

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: 106.15  E-value: 1.25e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 288 LDFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD--ETVTEEHLPRLPYLNAV 365
Cdd:cd11057 214 LELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDdgQFITYEDLQQLVYLEMV 293
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 366 FHETLRRHSPVPLIpPRFVHEDTKLA-GYDVPAGTEMVINLYgcNMNRKE--W-ESPEEWVPERFAGGRLEVADMYKTMA 441
Cdd:cd11057 294 LKETMRLFPVGPLV-GRETTADIQLSnGVVIPKGTTIVIDIF--NMHRRKdiWgPDADQFDPDNFLPERSAQRHPYAFIP 370
                       170       180       190
                ....*....|....*....|....*....|....
gi 50727139 442 FGAGRRACAGSLQATHIACAAVARFVQEFgwRLR 475
Cdd:cd11057 371 FSAGPRNCIGWRYAMISMKIMLAKILRNY--RLK 402
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
72-480 2.36e-24

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: 105.31  E-value: 2.36e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCdfHKMVKRYVMSSM--LGTSA 149
Cdd:cd20667   1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTNGLT--WKQQRRFCMTTLreLGLGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 150 QKQFRDIRDMMIHnMLSTFHKLVKD--DPHAPLIfrdvfkdelfrlsmiQSLGEDVSSVYvdeFG-RDISREEIYNATV- 225
Cdd:cd20667  79 QALESQIQHEAAE-LVKVFAQENGRpfDPQDPIV---------------HATANVIGAVV---FGhRFSSEDPIFLELIr 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 226 -TDMMMCAIEVDWR---DFFP----YLSWVPNKSFETRvfttETRRTAVMRALIKQQKERivrGEAKTCYLDFLLAE--- 294
Cdd:cd20667 140 aINLGLAFASTIWGrlyDAFPwlmrYLPGPHQKIFAYH----DAVRSFIKKEVIRHELRT---NEAPQDFIDCYLAQitk 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 295 ------NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFH 367
Cdd:cd20667 213 tkddpvSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGaSQLICYEDRKRLPYTNAVIH 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 368 ETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRR 447
Cdd:cd20667 293 EVQRLSNVVSVGAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHR 372
                       410       420       430
                ....*....|....*....|....*....|...
gi 50727139 448 ACAGSLQATHIACAAVARFVQEFGWRLREGDEE 480
Cdd:cd20667 373 VCLGEQLARMELFIFFTTLLRTFNFQLPEGVQE 405
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
315-451 2.84e-24

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: 105.03  E-value: 2.84e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 315 DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGY 393
Cdd:cd20621 243 DTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDdITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDL 322
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50727139 394 DVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd20621 323 KIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIG 380
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
199-470 5.34e-24

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: 104.18  E-value: 5.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 199 LGEDVSSVyvDEFGRDISREEIYNAtvtdMMMCAIEVDWRDFF-PYLSWVPNKSFE-----TRVFTtetrRTAVMRALIK 272
Cdd:cd11063 119 FGESVDSL--KPGGDSPPAARFAEA----FDYAQKYLAKRLRLgKLLWLLRDKKFReackvVHRFV----DPYVDKALAR 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 273 QQKERIVRGEAKTCYLDFLLAE----NTLTDEQLMMLVwealieAA-DTTLVTTEWAMYELAKNPDKQERLYQEIREVCG 347
Cdd:cd11063 189 KEESKDEESSDRYVFLDELAKEtrdpKELRDQLLNILL------AGrDTTASLLSFLFYELARHPEVWAKLREEVLSLFG 262
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 348 DE-TVTEEHLPRLPYLNAVFHETLRRHSPVPL---IPPRfvheDTKL---AGYD------VPAGTEMVINLYGcnMNRKE 414
Cdd:cd11063 263 PEpTPTYEDLKNMKYLRAVINETLRLYPPVPLnsrVAVR----DTTLprgGGPDgkspifVPKGTRVLYSVYA--MHRRK 336
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50727139 415 --W-ESPEEWVPERFAGGRLEVadmYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd11063 337 diWgPDAEEFRPERWEDLKRPG---WEYLPFNGGPRICLGQQFALTEASYVLVRLLQTF 392
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
72-455 1.67e-23

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: 102.57  E-value: 1.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYcdFHKMVKRYVMSSMLGTSAQK 151
Cdd:cd20662   1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSSGQ--TWKEQRRFALMTLRNFGLGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRdmmihnMLSTFHKLVkddphaplifrDVFKDE---LF--RLSMIQSLGEDVSSV-------YVDEFGRDISRee 219
Cdd:cd20662  79 KSLEER------IQEECRHLV-----------EAIREEkgnPFnpHFKINNAVSNIICSVtfgerfeYHDEWFQELLR-- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 220 IYNATVTDM--MMCAIevdwRDFFPY-LSWVPNkSFETrVFTTETRRTAVMRALIKQQKERIVRGEAKTcYLDFLLAE-- 294
Cdd:cd20662 140 LLDETVYLEgsPMSQL----YNAFPWiMKYLPG-SHQT-VFSNWKKLKLFVSDMIDKHREDWNPDEPRD-FIDAYLKEma 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 295 ------NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD-ETVTEEHLPRLPYLNAVFH 367
Cdd:cd20662 213 kypdptTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQkRQPSLADRESMPYTNAVIH 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 368 ETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFaggrLEVADMYKT---MAFGA 444
Cdd:cd20662 293 EVQRMGNIIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHF----LENGQFKKReafLPFSM 368
                       410
                ....*....|.
gi 50727139 445 GRRACAGSLQA 455
Cdd:cd20662 369 GKRACLGEQLA 379
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
72-451 2.47e-23

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: 102.40  E-value: 2.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRyvmssmLGTSAQK 151
Cdd:cd20676   1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLTFSTDSGPVWRARRK------LAQNALK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDIRDmmihnmlstfhklvKDDPHAPLIFRDVFKDELFRLSMIQSLGEDVSSV----YVDE----------FGRDISR 217
Cdd:cd20676  75 TFSIASS--------------PTSSSSCLLEEHVSKEAEYLVSKLQELMAEKGSFdpyrYIVVsvanvicamcFGKRYSH 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 218 --EEIYNatVTDMMMCAIEV----DWRDFFPYLSWVPN---KSFET-----------------RVFTTETRRTaVMRALI 271
Cdd:cd20676 141 ddQELLS--LVNLSDEFGEVagsgNPADFIPILRYLPNpamKRFKDinkrfnsflqkivkehyQTFDKDNIRD-ITDSLI 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 272 KQQKERIVRGEAKTcyldfllaenTLTDEQLMMLVWEALIEAADTtlVTT--EWAMYELAKNPDKQERLYQEIrevcgDE 349
Cdd:cd20676 218 EHCQDKKLDENANI----------QLSDEKIVNIVNDLFGAGFDT--VTTalSWSLMYLVTYPEIQKKIQEEL-----DE 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 350 TVTEEHLPR------LPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVP 423
Cdd:cd20676 281 VIGRERRPRlsdrpqLPYLEAFILETFRHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRP 360
                       410       420       430
                ....*....|....*....|....*....|.
gi 50727139 424 ERF---AGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd20676 361 ERFltaDGTEINKTESEKVMLFGLGKRRCIG 391
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
211-479 3.11e-23

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: 101.99  E-value: 3.11e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 211 FGRDISREEIY----NATVTDMMMCAIEVD-WRDFF-PYLSWVpnkSFETRVFTTETRRtavMRALIKQQKERIVRGEAK 284
Cdd:cd11041 127 VGPPLCRNEEWldltINYTIDVFAAAAALRlFPPFLrPLVAPF---LPEPRRLRRLLRR---ARPLIIPEIERRRKLKKG 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 285 TCY----------LDFLLAENTLTDEQL---MMLVWealIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETV 351
Cdd:cd11041 201 PKEdkpndllqwlIEAAKGEGERTPYDLadrQLALS---FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGG 277
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 352 -TEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLA-GYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGG 429
Cdd:cd11041 278 wTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSdGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRL 357
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 50727139 430 RLEVADMYKT---------MAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDE 479
Cdd:cd11041 358 REQPGQEKKHqfvstspdfLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGE 416
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
293-497 4.67e-23

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: 101.12  E-value: 4.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 AENTLTDEQLMMLVwEALIEA-ADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETL 370
Cdd:cd11058 209 EKKGLTREELEANA-SLLIIAgSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDdITLDSLAQLPYLNAVIQEAL 287
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 371 RRHSPVPLIPPRFVHEDTKL-AGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAG--GRLEVADMYKTM-AFGAGR 446
Cdd:cd11058 288 RLYPPVPAGLPRVVPAGGATiDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGdpRFEFDNDKKEAFqPFSVGP 367
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 50727139 447 RACAGSLQATHIACAAVARFVQEFGWRLREGDEEKVDtvQLTAYKL---HPLHV 497
Cdd:cd11058 368 RNCIGKNLAYAEMRLILAKLLWNFDLELDPESEDWLD--QQKVYILwekPPLMV 419
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
72-451 4.83e-23

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: 101.33  E-value: 4.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRyVMSSMLGTSAQK 151
Cdd:cd20677   1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSEKYGESWKLHKK-IAKNALRTFSKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 QFRDirdmmihnmlSTFHKLVKDdpHAPLIFRDVFKdELFRLSMIQSLGEDVSSVYVDE--------FGR--DISREEIY 221
Cdd:cd20677  80 EAKS----------STCSCLLEE--HVCAEASELVK-TLVELSKEKGSFDPVSLITCAVanvvcalcFGKryDHSDKEFL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 222 NATVT--DMMMCAIEVDWRDFFPYLSWVP--------------NKSFETRV---FTTETRRTA--VMRALIKQQKERivR 280
Cdd:cd20677 147 TIVEInnDLLKASGAGNLADFIPILRYLPspslkalrkfisrlNNFIAKSVqdhYATYDKNHIrdITDALIALCQER--K 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 281 GEAKTcyldfllaeNTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIrevcgDETVTEEHLPR-- 358
Cdd:cd20677 225 AEDKS---------AVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEI-----DEKIGLSRLPRfe 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 359 ----LPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLE 432
Cdd:cd20677 291 drksLHYTEAFINEVFRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFldENGQLN 370
                       410
                ....*....|....*....
gi 50727139 433 VADMYKTMAFGAGRRACAG 451
Cdd:cd20677 371 KSLVEKVLIFGMGVRKCLG 389
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
72-456 4.95e-23

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: 101.41  E-value: 4.95e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDycDFHKMVKRYVMSSMLGTSAQK 151
Cdd:cd20671   1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSG--ERWRTTRRFTVRSMKSLGMGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 qfRDIRDMMIHNMLSTFHKLvkddphaplifrDVFKDELFRLSMIQSLGEDVSSVYVdeFGRDISREEIYNATVTDM--- 228
Cdd:cd20671  79 --RTIEDKILEELQFLNGQI------------DSFNGKPFPLRLLGWAPTNITFAML--FGRRFDYKDPTFVSLLDLide 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 229 ---MMCAIEVDWRDFFPYLSWV--PNKSFETRVftTETRrtAVMRALIKQQKERIVRGEAKTcYLDFLLA--------EN 295
Cdd:cd20671 143 vmvLLGSPGLQLFNLYPVLGAFlkLHKPILDKV--EEVC--MILRTLIEARRPTIDGNPLHS-YIEALIQkqeeddpkET 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 296 TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRRHS 374
Cdd:cd20671 218 LFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGpGCLPNYEDRKALPYTSAVIHEVQRFIT 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 375 PVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEVADMYktMAFGAGRRACAGS 452
Cdd:cd20671 298 LLPHVP-RCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFldAEGKFVKKEAF--LPFSAGRRVCVGE 374

                ....
gi 50727139 453 LQAT 456
Cdd:cd20671 375 SLAR 378
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
294-451 1.17e-22

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: 100.15  E-value: 1.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 294 ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTE-EHLPRLPYLNAVFHETLRR 372
Cdd:cd20663 223 ESSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEmADQARMPYTNAVIHEVQRF 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 373 HSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEVADMYktMAFGAGRRACA 450
Cdd:cd20663 303 GDIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFldAQGHFVKPEAF--MPFSAGRRACL 380

                .
gi 50727139 451 G 451
Cdd:cd20663 381 G 381
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
294-477 3.04e-22

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: 99.12  E-value: 3.04e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 294 ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNAVFHETLRR 372
Cdd:cd20661 231 ESTFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGpNGMPSFEDKCKMPYTEAVLHEVLRF 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 373 HSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAGS 452
Cdd:cd20661 311 CNIVPLGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGE 390
                       170       180
                ....*....|....*....|....*
gi 50727139 453 LQATHIACAAVARFVQEFGWRLREG 477
Cdd:cd20661 391 QLARMEMFLFFTALLQRFHLHFPHG 415
PLN02290 PLN02290
cytokinin trans-hydroxylase
246-470 4.39e-22

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 99.12  E-value: 4.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  246 WVPNKSF-------ETRVFTTETRRtaVMRALIKQQKERIVRGEAKTC---YLDFLLAE-------NTLTDEQLMMLVWE 308
Cdd:PLN02290 245 CFPGSRFfpskynrEIKSLKGEVER--LLMEIIQSRRDCVEIGRSSSYgddLLGMLLNEmekkrsnGFNLNLQLIMDECK 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  309 ALIEAA-DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHED 387
Cdd:PLN02290 323 TFFFAGhETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLL-PRMAFED 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  388 TKLAGYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERFAGGRLEVADMYktMAFGAGRRACAGSLQATHIACAAVARF 466
Cdd:PLN02290 402 IKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHF--IPFAAGPRNCIGQAFAMMEAKIILAML 479

                 ....
gi 50727139  467 VQEF 470
Cdd:PLN02290 480 ISKF 483
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
268-451 6.51e-22

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: 98.23  E-value: 6.51e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 268 RALIKQQKERIVRGEAKTCYLDF----LLAE----NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLY 339
Cdd:cd20679 203 RTLPSQGVDDFLKAKAKSKTLDFidvlLLSKdedgKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCR 282
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 340 QEIREVCGDETVTE---EHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLA-GYDVPAGTEMVINLYGCNMNRKEW 415
Cdd:cd20679 283 QEVQELLKDREPEEiewDDLAQLPFLTMCIKESLRLHPPVTAI-SRCCTQDIVLPdGRVIPKGIICLISIYGTHHNPTVW 361
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 50727139 416 ESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd20679 362 PDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIG 397
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
240-485 8.17e-22

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: 97.71  E-value: 8.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 240 FFPYLSWVPNK--SFETRVFTTETRRTAVMRALIKQQKERIVRG-------EAKTCYLDFLLAENT----LTDEQLMMLV 306
Cdd:cd11062 150 HFPWLLKLLRSlpESLLKRLNPGLAVFLDFQESIAKQVDEVLRQvsagdppSIVTSLFHALLNSDLppseKTLERLADEA 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 307 WEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET--VTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFV 384
Cdd:cd11062 230 QTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDspPSLAELEKLPYLTAVIKEGLRLSYGVPTRLPRVV 309
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 385 H-EDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRlEVADMYKTM-AFGAGRRACAGSlqatHIACA- 461
Cdd:cd11062 310 PdEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAA-EKGKLDRYLvPFSKGSRSCLGI----NLAYAe 384
                       250       260
                ....*....|....*....|....*..
gi 50727139 462 ---AVARFVQEFGWRLREGDEEKVDTV 485
Cdd:cd11062 385 lylALAALFRRFDLELYETTEEDVEIV 411
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
250-485 1.49e-21

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: 96.80  E-value: 1.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 250 KSFETRVFTTETR------RTAvmRALIKQQKERIVRGEAKtcylDFL---LAENTLTDEQLMMLVWEALIEAADTTLVT 320
Cdd:cd20645 172 KRLNTKVWQDHTEawdnifKTA--KHCIDKRLQRYSQGPAN----DFLcdiYHDNELSKKELYAAITELQIGGVETTANS 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 321 TEWAMYELAKNPDKQERLYQEIREVCGD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYDVPAGT 399
Cdd:cd20645 246 LLWILYNLSRNPQAQQKLLQEIQSVLPAnQTPRAEDLKNMPYLKACLKESMRLTPSVPFT-SRTLDKDTVLGDYLLPKGT 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 400 EMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVaDMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFgwRLREGDE 479
Cdd:cd20645 325 VLMINSQALGSSEEYFEDGRQFKPERWLQEKHSI-NPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKY--QIVATDN 401

                ....*.
gi 50727139 480 EKVDTV 485
Cdd:cd20645 402 EPVEML 407
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
259-451 1.65e-21

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: 96.58  E-value: 1.65e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 259 TETRRTAVMRALIKQQKERIVR----GEAKTC--YLDFLLA-----ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYE 327
Cdd:cd11044 170 TPFGRAIRARNKLLARLEQAIRerqeEENAEAkdALGLLLEakdedGEPLSMDELKDQALLLLFAGHETTASALTSLCFE 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 328 LAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVFHETLRrhspvpLIPP-----RFVHEDTKLAGYDVPAGTEMV 402
Cdd:cd11044 250 LAQHPDVLEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLR------LVPPvgggfRKVLEDFELGGYQIPKGWLVY 323
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 50727139 403 INLYGCNMNRKEWESPEEWVPERFAGGRLEVADM-YKTMAFGAGRRACAG 451
Cdd:cd11044 324 YSIRDTHRDPELYPDPERFDPERFSPARSEDKKKpFSLIPFGGGPRECLG 373
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
291-451 2.42e-21

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: 96.32  E-value: 2.42e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 291 LLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEI----REVCGDETVTeehLPRLPYLNAVF 366
Cdd:cd20643 224 LLLQDKLPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVlaarQEAQGDMVKM---LKSVPLLKAAI 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 367 HETLRRHsPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEvadMYKTMAFGAGR 446
Cdd:cd20643 301 KETLRLH-PVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDIT---HFRNLGFGFGP 376

                ....*
gi 50727139 447 RACAG 451
Cdd:cd20643 377 RQCLG 381
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
72-451 2.64e-21

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: 96.23  E-value: 2.64e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMvATSDYCDFHKMVKRYVMS-----SMLG 146
Cdd:cd20675   1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSL-AFGGYSERWKAHRRVAHStvrafSTRN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 147 TSAQKQFR-----DIRDMmihnmLSTFHKLVKD----DPHAPLIFrdvfkdelfrlsmiqSLGEDVSSV-------YVD- 209
Cdd:cd20675  80 PRTRKAFErhvlgEAREL-----VALFLRKSAGgayfDPAPPLVV---------------AVANVMSAVcfgkrysHDDa 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 210 EFGRDISREEIYNATV-----TDMMmcaievdwrdffPYLSWVPN------KSFET--RVFTT----------ETRRTAV 266
Cdd:cd20675 140 EFRSLLGRNDQFGRTVgagslVDVM------------PWLQYFPNpvrtvfRNFKQlnREFYNfvldkvlqhrETLRGGA 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 267 MR----ALIKQQKERIVRGEAKTcyLDFLLAENTLTDeqlmmlvweaLIEAADTTLVTT-EWAMYELAKNPDKQERLYQE 341
Cdd:cd20675 208 PRdmmdAFILALEKGKSGDSGVG--LDKEYVPSTVTD----------IFGASQDTLSTAlQWILLLLVRYPDVQARLQEE 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 342 IREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEE 420
Cdd:cd20675 276 LDRVVGrDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEV 355
                       410       420       430
                ....*....|....*....|....*....|...
gi 50727139 421 WVPERF--AGGRLEVADMYKTMAFGAGRRACAG 451
Cdd:cd20675 356 FDPTRFldENGFLNKDLASSVMIFSVGKRRCIG 388
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
239-459 3.12e-21

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: 95.89  E-value: 3.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 239 DFFPYLSWVPNKsfetrvfttetRRTAV------MRALIKQQKERIVRGEAKTCYLDF----LLAEN--TLTDEQLMMLV 306
Cdd:cd20616 161 DIFFKISWLYKK-----------YEKAVkdlkdaIEILIEQKRRRISTAEKLEDHMDFatelIFAQKrgELTAENVNQCV 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 307 WEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVFHETLRRHsPVPLIPPRFVHE 386
Cdd:cd20616 230 LEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQ-PVVDFVMRKALE 308
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139 387 DTKLAGYDVPAGTEMVINLygCNMNRKE-WESPEEWVPERFAGgrlEVADMYkTMAFGAGRRACAGSlqatHIA 459
Cdd:cd20616 309 DDVIDGYPVKKGTNIILNI--GRMHRLEfFPKPNEFTLENFEK---NVPSRY-FQPFGFGPRSCVGK----YIA 372
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
315-466 5.04e-21

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: 95.35  E-value: 5.04e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 315 DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLP------RLPYLNAVFHETLRRHSPVPLIpPRFVHEDT 388
Cdd:cd11064 244 DTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESRVPtyeelkKLVYLHAALSESLRLYPPVPFD-SKEAVNDD 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 389 KLA-GYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERF--AGGRLEVADMYKTMAFGAGRRACAGS----LQATHIAC 460
Cdd:cd11064 323 VLPdGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWldEDGGLRPESPYKFPAFNAGPRICLGKdlayLQMKIVAA 402

                ....*.
gi 50727139 461 AAVARF 466
Cdd:cd11064 403 AILRRF 408
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
287-451 9.50e-21

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: 94.44  E-value: 9.50e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 287 YLDFLL-----AENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG--DETVTEEHLPRL 359
Cdd:cd20680 224 FLDMLLsvtdeEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGksDRPVTMEDLKKL 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 360 PYLNAVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKT 439
Cdd:cd20680 304 RYLECVIKESLRLFPSVPLFA-RSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAY 382
                       170
                ....*....|..
gi 50727139 440 MAFGAGRRACAG 451
Cdd:cd20680 383 IPFSAGPRNCIG 394
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
262-475 1.34e-20

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: 93.66  E-value: 1.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 262 RRTAVMRALIKQQKERIV----RGEAKTCYLDFLL----AENTLTDEQLMMLVWEALIEAA-DTTLVTTEWAMYELAKNP 332
Cdd:cd20614 160 RRSRRARAWIDARLSQLVatarANGARTGLVAALIrardDNGAGLSEQELVDNLRLLVLAGhETTASIMAWMVIMLAEHP 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 333 DKQERLYQEIREVcGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNR 412
Cdd:cd20614 240 AVWDALCDEAAAA-GDVPRTPAELRRFPLAEALFRETLRLHPPVPFV-FRRVLEEIELGGRRIPAGTHLGIPLLLFSRDP 317
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 413 KEWESPEEWVPERFAgGRLEVADMYKTMAFGAGRRACAGslqaTHIAC-------AAVARFVQEFGWRLR 475
Cdd:cd20614 318 ELYPDPDRFRPERWL-GRDRAPNPVELLQFGGGPHFCLG----YHVACvelvqfiVALARELGAAGIRPL 382
PLN02936 PLN02936
epsilon-ring hydroxylase
288-502 1.71e-20

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 94.09  E-value: 1.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  288 LDFLLAEN------TLTDEQLMMLVwealiEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPY 361
Cdd:PLN02936 264 LRFLLASReevssvQLRDDLLSMLV-----AGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKY 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  362 LNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRL-EVADMYK 438
Cdd:PLN02936 339 LTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdlDGPVPnETNTDFR 418
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139  439 TMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREgDEEKVDTVQLTAYKLHPLHVHLTRR 502
Cdd:PLN02936 419 YIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVP-DQDIVMTTGATIHTTNGLYMTVSRR 481
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
228-474 1.78e-19

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: 90.59  E-value: 1.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 228 MMMCAIEVDWRDFFPYLSWVPNKSFETR-VFTTETRRTavMRALIKQQKERIVRGEAKTCYLDFL-LAENTLTDEQLMML 305
Cdd:cd20639 151 QMLLAAEAFRKVYIPGYRFLPTKKNRKSwRLDKEIRKS--LLKLIERRQTAADDEKDDEDSKDLLgLMISAKNARNGEKM 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 306 VWEALIE--------AADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETV-TEEHLPRLPYLNAVFHETLRRHSP- 375
Cdd:cd20639 229 TVEEIIEecktfffaGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVpTKDHLPKLKTLGMILNETLRLYPPa 308
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 376 VPLIppRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERFAGGRLEVAdmYKTMA---FGAGRRACAG 451
Cdd:cd20639 309 VATI--RRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAA--KHPLAfipFGLGPRTCVG 384
                       250       260
                ....*....|....*....|...
gi 50727139 452 SLQATHIACAAVARFVQEFGWRL 474
Cdd:cd20639 385 QNLAILEAKLTLAVILQRFEFRL 407
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
73-485 3.85e-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: 89.73  E-value: 3.85e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  73 GPIYTIRTGASSVVVLNSTE----VAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDYCDFHKMVKRYVMSSMLGTS 148
Cdd:cd11040  12 GPIFTIRLGGQKIYVITDPElisaVFRNPKTLSFDPIVIVVVGRVFGSPESAKKKEGEPGGKGLIRLLHDLHKKALSGGE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 149 AQKQFRDIrdmMIHNMLSTFHKLVKDDPHAPLIFrDVFkdELFRLSMIQSLGEDVssvyvdeFGRDIsreeIYNATvtdm 228
Cdd:cd11040  92 GLDRLNEA---MLENLSKLLDELSLSGGTSTVEV-DLY--EWLRDVLTRATTEAL-------FGPKL----PELDP---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 229 mmcAIEVDWRDF---FPYLSWVPNKSFETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLLAENTLTDE----Q 301
Cdd:cd11040 151 ---DLVEDFWTFdrgLPKLLLGLPRLLARKAYAARDRLLKALEKYYQAAREERDDGSELIRARAKVLREAGLSEEdiarA 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 302 LMMLVWEALieaaDTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLP------RLPYLNAVFHETLRRHSP 375
Cdd:cd11040 228 ELALLWAIN----ANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDltdlltSCPLLDSTYLETLRLHSS 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 376 VPLIppRFVHEDTKLAG-YDVPAGTEMVINLYGCNMNRKEWES-PEEWVPERF---AGGRLEVADMYKTMAFGAGRRACA 450
Cdd:cd11040 304 STSV--RLVTEDTVLGGgYLLRKGSLVMIPPRLLHMDPEIWGPdPEEFDPERFlkkDGDKKGRGLPGAFRPFGGGASLCP 381
                       410       420       430
                ....*....|....*....|....*....|....*
gi 50727139 451 GSLQATHIACAAVARFVQEFGWRLREGDEEKVDTV 485
Cdd:cd11040 382 GRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGM 416
PLN02738 PLN02738
carotene beta-ring hydroxylase
288-504 4.63e-19

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 90.36  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  288 LDFLLAE-NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVF 366
Cdd:PLN02738 377 LHFLLASgDDVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVI 456
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  367 HETLRRHSPVPLIPPRFVHEDTkLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF---AGGRLEVADMYKTMAFG 443
Cdd:PLN02738 457 NESLRLYPQPPVLIRRSLENDM-LGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldGPNPNETNQNFSYLPFG 535
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50727139  444 AGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEKVDTVQLTAYKLHPLHVHLTRRGR 504
Cdd:PLN02738 536 GGPRKCVGDMFASFENVVATAMLVRRFDFQLAPGAPPVKMTTGATIHTTEGLKMTVTRRTK 596
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
72-451 9.23e-19

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: 88.28  E-value: 9.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKLSKALTVLTRDKSMVATSDycDFHKMVKRYVMSSMLGTSAQK 151
Cdd:cd20669   1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNG--ERWKILRRFALQTLRNFGMGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 152 qfRDIRDMMI---HNMLSTFHKlVKDDPHAP--------------LIFRDVFKDELFRLSMIQSLGEDVSSVYVDEFGrd 214
Cdd:cd20669  79 --RSIEERILeeaQFLLEELRK-TKGAPFDPtfllsravsniicsVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWG-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 215 isreEIYNatvtdmmmcaievdwrdFFP-YLSWVPNKsfETRVFTTETRRTAVMRALIKQQKERIVRGEAKT---CYLDF 290
Cdd:cd20669 154 ----ELYN-----------------IFPsVMDWLPGP--HQRIFQNFEKLRDFIAESVREHQESLDPNSPRDfidCFLTK 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 291 LLAE-----NTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-DETVTEEHLPRLPYLNA 364
Cdd:cd20669 211 MAEEkqdplSHFNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGrNRLPTLEDRARMPYTDA 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 365 VFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGA 444
Cdd:cd20669 291 VIHEIQRFADIIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSA 370

                ....*..
gi 50727139 445 GRRACAG 451
Cdd:cd20669 371 GKRICLG 377
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
240-474 1.14e-18

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: 88.11  E-value: 1.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 240 FFPYLSWVPNKsFETRVFTTETRRTAVMRALIKQQKERIVRGEAKTCYLDFLLAENTLTDEQL-----MMLVWEALIE-- 312
Cdd:cd20642 161 YIPGWRFLPTK-RNRRMKEIEKEIRSSLRGIINKREKAMKAGEATNDDLLGILLESNHKEIKEqgnknGGMSTEDVIEec 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 313 ------AADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHE 386
Cdd:cd20642 240 klfyfaGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPDFEGLNHLKVVTMILYEVLRLYPPVIQL-TRAIHK 318
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 387 DTKLAGYDVPAGTEMVINLYGCNMNRKEW-ESPEEWVPERFAGGrleVADMYKT----MAFGAGRRACAGSLQATHIACA 461
Cdd:cd20642 319 DTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAEG---ISKATKGqvsyFPFGWGPRICIGQNFALLEAKM 395
                       250
                ....*....|...
gi 50727139 462 AVARFVQEFGWRL 474
Cdd:cd20642 396 ALALILQRFSFEL 408
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
270-451 1.40e-18

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: 87.70  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 270 LIKQQKERivrgeaktcylDFLLAENTLtdEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCG-D 348
Cdd:cd20665 208 LIKMEQEK-----------HNQQSEFTL--ENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGrH 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 349 ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF-- 426
Cdd:cd20665 275 RSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFld 354
                       170       180
                ....*....|....*....|....*
gi 50727139 427 AGGRLEVADMYktMAFGAGRRACAG 451
Cdd:cd20665 355 ENGNFKKSDYF--MPFSAGKRICAG 377
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
297-473 1.18e-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: 1.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET-VTEEHLPRLPYLNAVFHETLRRHSP 375
Cdd:cd20650 224 LSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKApPTYDTVMQMEYLDMVVNETLRLFPI 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 376 VPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAGSLQA 455
Cdd:cd20650 304 AGRLE-RVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFA 382
                       170
                ....*....|....*...
gi 50727139 456 THIACAAVARFVQEFGWR 473
Cdd:cd20650 383 LMNMKLALVRVLQNFSFK 400
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
271-470 2.92e-17

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: 84.03  E-value: 2.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 271 IKQQKERIVRGEAKT-CYLDFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDE 349
Cdd:cd20648 203 MAEVAAKLPRGEAIEgKYLTYFLAREKLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDN 282
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 350 TV-TEEHLPRLPYLNAVFHETLRRHSPVP----LIPPRfvheDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPE 424
Cdd:cd20648 283 SVpSAADVARMPLLKAVVKEVLRLYPVIPgnarVIPDR----DIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPE 358
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 50727139 425 RFaGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd20648 359 RW-LGKGDTHHPYASLPFGFGKRSCIGRRIAELEVYLALARILTHF 403
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
315-451 3.34e-17

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: 83.62  E-value: 3.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 315 DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYD 394
Cdd:cd20640 244 ETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDADSLSRMKTVTMVIQETLRLYPPAAFV-SREALRDMKLGGLV 322
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50727139 395 VPAGTEMVINLYGCNMNRKEW-ESPEEWVPERFAGGRLEV---ADMYktMAFGAGRRACAG 451
Cdd:cd20640 323 VPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAAckpPHSY--MPFGAGARTCLG 381
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
297-451 2.83e-16

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


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 81.04  E-value: 2.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTE-EHLPRLPYLNAVFHETLRrhsp 375
Cdd:cd20649 257 LTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDyANVQELPYLDMVIAETLR---- 332
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 376 vpLIPPRF-----VHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACA 450
Cdd:cd20649 333 --MYPPAFrfareAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCI 410

                .
gi 50727139 451 G 451
Cdd:cd20649 411 G 411
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
61-474 3.97e-16

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: 80.57  E-value: 3.97e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  61 PHqtFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAKFS-SISTRKLSKALTVLTRDKSMVATSDYCDFHKMV--- 136
Cdd:cd20641   2 PH--YQQWKSQYGETFLYWQGTTPRICISDHELAKQVLSDKFGfFGKSKARPEILKLSGKGLVFVNGDDWVRHRRVLnpa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 137 ----KRYVMSSMLGTSAQKQFRDIRDMMIHN--------MLSTFHKLVKDdphapLIFRDVFKD------ELFRLSMiqs 198
Cdd:cd20641  80 fsmdKLKSMTQVMADCTERMFQEWRKQRNNSeterieveVSREFQDLTAD-----IIATTAFGSsyaegiEVFLSQL--- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 199 lgedvssvyvdefgrdiSREEIYNATVTDMmmcaievdwrdFFPYLSWVPNKSfETRVFTTETRrtavMRALIKQQKERI 278
Cdd:cd20641 152 -----------------ELQKCAAASLTNL-----------YIPGTQYLPTPR-NLRVWKLEKK----VRNSIKRIIDSR 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 279 VRGEAKTcYLDFLLA---------ENTLTDEQLMMLvwEALIE--------AADTTLVTTEWAMYELAKNPDKQERLYQE 341
Cdd:cd20641 199 LTSEGKG-YGDDLLGlmleaassnEGGRRTERKMSI--DEIIDecktfffaGHETTSNLLTWTMFLLSLHPDWQEKLREE 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 342 I-REVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEW-ESPE 419
Cdd:cd20641 276 VfRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINI-ARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDAD 354
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 50727139 420 EWVPERFAGGRLEVA-DMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRL 474
Cdd:cd20641 355 EFNPLRFANGVSRAAtHPNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSL 410
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
296-486 9.60e-16

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: 79.25  E-value: 9.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 296 TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETVTEEH--LPRLPYLNAVFHETLRRH 373
Cdd:cd20615 210 DITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDyiLSTDTLLAYCVLESLRLR 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 374 spvPLIP---PRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWES-PEEWVPERFAGgrLEVADM-YKTMAFGAGRRA 448
Cdd:cd20615 290 ---PLLAfsvPESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWGPdGEAYRPERFLG--ISPTDLrYNFWRFGFGPRK 364
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 50727139 449 CAGSLQATHIACAAVARFVQefGWRLREGDEEKVDTVQ 486
Cdd:cd20615 365 CLGQHVADVILKALLAHLLE--QYELKLPDQGENEEDT 400
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
315-451 1.16e-15

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: 79.11  E-value: 1.16e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 315 DTTLVTTEWAMYELAKNPDKQERLYQEIREVcgdETVTEEHLPR----LPYLNAVFHETLRRHsPVPLIPPRFVHEDTKL 390
Cdd:cd20644 246 DTTAFPLLFTLFELARNPDVQQILRQESLAA---AAQISEHPQKalteLPLLKAALKETLRLY-PVGITVQRVPSSDLVL 321
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50727139 391 AGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRlEVADMYKTMAFGAGRRACAG 451
Cdd:cd20644 322 QNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIR-GSGRNFKHLAFGFGMRQCLG 381
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
295-451 1.46e-15

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: 78.88  E-value: 1.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 295 NTLTDEqLMMLvweaLIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCgDETVTEEHLP--------RLPYLNAVF 366
Cdd:cd20622 261 QVIHDE-LFGY----LIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAH-PEAVAEGRLPtaqeiaqaRIPYLDAVI 334
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 367 HETLrRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYG-----------------CNMNRKE----WES-------P 418
Cdd:cd20622 335 EEIL-RCANTAPILSREATVDTQVLGYSIPKGTNVFLLNNGpsylsppieidesrrssSSAAKGKkagvWDSkdiadfdP 413
                       170       180       190
                ....*....|....*....|....*....|....
gi 50727139 419 EEWVPERFAGGRLEV-ADMYKTMAFGAGRRACAG 451
Cdd:cd20622 414 ERWLVTDEETGETVFdPSAGPTLAFGLGPRGCFG 447
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
72-455 4.91e-15

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: 76.89  E-value: 4.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  72 YGPIYTIRTGASSVVVLNSTEVAKEAMVAKFSSISTRKlskalTVLTRDKSM----VATSDyCDFHKMVKRYVMSSMLGT 147
Cdd:cd20670   1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRG-----ELATIERNFqghgVALAN-GERWRILRRFSLTILRNF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 148 SAQKqfRDIRDMMIHN---MLSTFHKlVKDDPHAPLIF--RDV--------------FKDELFR--LSMIQSLGEDVSSV 206
Cdd:cd20670  75 GMGK--RSIEERIQEEagyLLEEFRK-TKGAPIDPTFFlsRTVsnvissvvfgsrfdYEDKQFLslLRMINESFIEMSTP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 207 YvdefgrdisreeiynATVTDMMMCAIEV-------------DWRDFFPYLSWVPNKSFETrvfttETRRTAVMRALIKQ 273
Cdd:cd20670 152 W---------------AQLYDMYSGIMQYlpgrhnriyylieELKDFIASRVKINEASLDP-----QNPRDFIDCFLIKM 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 274 QKERivrGEAKTcylDFLLAENTLTDEQLMMlvweALIEAADTTLvttEWAMYELAKNPDKQERLYQEIREVCGDETV-- 351
Cdd:cd20670 212 HQDK---NNPHT---EFNLKNLVLTTLNLFF----AGTETVSSTL---RYGFLLLMKYPEVEAKIHEEINQVIGPHRLps 278
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 352 TEEHLpRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGG 429
Cdd:cd20670 279 VDDRV-KMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFldEQG 357
                       410       420
                ....*....|....*....|....*.
gi 50727139 430 RLEVADMYktMAFGAGRRACAGSLQA 455
Cdd:cd20670 358 RFKKNEAF--VPFSSGKRVCLGEAMA 381
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
263-451 5.41e-15

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: 76.90  E-value: 5.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 263 RTAVMRAL---IKQQKERIVRGEAKTCYLDF----LLAENT------------LTDEQLMMLVWEALIEAADTTLVTTEW 323
Cdd:cd11082 163 RKRIVKTLekcAAKSKKRMAAGEEPTCLLDFwtheILEEIKeaeeegepppphSSDEEIAGTLLDFLFASQDASTSSLVW 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 324 AMYELAKNPDKQERLYQEIREVCGDE--TVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRfVHEDTKLA-GYDVPAGTe 400
Cdd:cd11082 243 ALQLLADHPDVLAKVREEQARLRPNDepPLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHI-AKKDFPLTeDYTVPKGT- 320
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 50727139 401 MVI-NLYGCNMnrKEWESPEEWVPERFAGGRLEVADMYK-TMAFGAGRRACAG 451
Cdd:cd11082 321 IVIpSIYDSCF--QGFPEPDKFDPDRFSPERQEDRKYKKnFLVFGAGPHQCVG 371
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
294-502 2.08e-14

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 75.59  E-value: 2.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  294 ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIRE----------VCGDETVTEE--------- 354
Cdd:PLN03195 285 DSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKAlekerakeedPEDSQSFNQRvtqfagllt 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  355 --HLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYgcNMNRKE--W-ESPEEWVPER-FAG 428
Cdd:PLN03195 365 ydSLGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGGMVTYVPY--SMGRMEynWgPDAASFKPERwIKD 442
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50727139  429 GRLEVADMYKTMAFGAGRRACAGSLQA---THIACAAVARFvqeFGWRLREGDEEKVDTVQLTAYKlHPLHVHLTRR 502
Cdd:PLN03195 443 GVFQNASPFKFTAFQAGPRICLGKDSAylqMKMALALLCRF---FKFQLVPGHPVKYRMMTILSMA-NGLKVTVSRR 515
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
33-452 2.20e-14

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 75.36  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139   33 APRKRPnAPPAVPGLPIIGNLHQLKEKKPHQTFAKWAEIYGPIYTIRTGASSVVVLNSTEVAKEAMVAK-------FSSI 105
Cdd:PLN02196  30 SSTKLP-LPPGTMGWPYVGETFQLYSQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKshlfkptFPAS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  106 STRKLSKALTVLTRDksmvatsdycDFHKMVKRYVMSSMLGTSAQKQFRDIRDMMIHN-------MLSTFHKLvkddpha 178
Cdd:PLN02196 109 KERMLGKQAIFFHQG----------DYHAKLRKLVLRAFMPDAIRNMVPDIESIAQESlnswegtQINTYQEM------- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  179 plifrdvfKDELFRLSMIQSLGEDvsSVYVDEfgrDISR-----EEIYNATVTDMmmcaievdwrdffpylswvPNKSFE 253
Cdd:PLN02196 172 --------KTYTFNVALLSIFGKD--EVLYRE---DLKRcyyilEKGYNSMPINL-------------------PGTLFH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  254 TRVftteTRRTAVMRALIKQQKERIVRGEAKTCYL-DFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNP 332
Cdd:PLN02196 220 KSM----KARKELAQILAKILSKRRQNGSSHNDLLgSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENP 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  333 DKQERLYQEIREVCGD----ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVhEDTKLAGYDVPAGTEmVINLYgc 408
Cdd:PLN02196 296 SVLEAVTEEQMAIRKDkeegESLTWEDTKKMPLTSRVIQETLRVASILSFTFREAV-EDVEYEGYLIPKGWK-VLPLF-- 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 50727139  409 nmnRKEWESPEEWV-PERFAGGRLEVADMYKT-MAFGAGRRACAGS 452
Cdd:PLN02196 372 ---RNIHHSADIFSdPGKFDPSRFEVAPKPNTfMPFGNGTHSCPGN 414
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
182-502 8.98e-14

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 73.50  E-value: 8.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  182 FRDVFKDELFRLSMIQSLGEDVSSVYVD----EFGR--DISREEIYnatvtdmmmcaievdWRDFFPYLSWVPNK----S 251
Cdd:PLN02169 175 LQDVFMRFMFDTSSILMTGYDPMSLSIEmlevEFGEaaDIGEEAIY---------------YRHFKPVILWRLQNwigiG 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  252 FETRVFTT-ETRRTAVMRALIKQQKERIVRGE-------AKTCYLDFLLAENTL----TDEQLMMLVWEALIEAADTTLV 319
Cdd:PLN02169 240 LERKMRTAlATVNRMFAKIISSRRKEEISRAEtepyskdALTYYMNVDTSKYKLlkpkKDKFIRDVIFSLVLAGRDTTSS 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  320 TTEWAMYELAKNPDKQERLYQEIrevcgDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGT 399
Cdd:PLN02169 320 ALTWFFWLLSKHPQVMAKIRHEI-----NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHKVDAES 394
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  400 EMVINLYGCNMNRKEW-ESPEEWVPERFAG--GRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLRE 476
Cdd:PLN02169 395 KIVICIYALGRMRSVWgEDALDFKPERWISdnGGLRHEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKVIE 474
                        330       340
                 ....*....|....*....|....*..
gi 50727139  477 GdeEKVDTVQLTAYKL-HPLHVHLTRR 502
Cdd:PLN02169 475 G--HKIEAIPSILLRMkHGLKVTVTKK 499
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
315-426 1.31e-13

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: 72.29  E-value: 1.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 315 DTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDET--------VTEEHLPRLPYLNAVFHETLRRHSPVPLIppRFVHE 386
Cdd:cd11051 199 DTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPsaaaellrEGPELLNQLPYTTAVIKETLRLFPPAGTA--RRGPP 276
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 50727139 387 DTKLAgydVPAGTEMV---INLYGCN----MNRKEWESPEEWVPERF 426
Cdd:cd11051 277 GVGLT---DRDGKEYPtdgCIVYVCHhaihRDPEYWPRPDEFIPERW 320
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
302-451 1.26e-12

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: 69.65  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 302 LMMLvWEALIEAADTTLvtteWAMYELAKNPDKQERLYQEIREVCGD-----ETVTEEHLPRLPYLNAVFHETLRRHSPV 376
Cdd:cd20635 216 LLLL-WASLANAIPITF----WTLAFILSHPSVYKKVMEEISSVLGKagkdkIKISEDDLKKMPYIKRCVLEAIRLRSPG 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 377 plIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFaggrlEVADMYKT------MAFGAGRRACA 450
Cdd:cd20635 291 --AITRKVVKPIKIKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERW-----KKADLEKNvflegfVAFGGGRYQCP 363

                .
gi 50727139 451 G 451
Cdd:cd20635 364 G 364
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
265-427 1.05e-11

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: 66.38  E-value: 1.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 265 AVMRALIKQQKERivrGEAKTCYLDFLLAENtLTDEQLMMlvwEALIEAADTTLVTTE---WAMYELAKNPDKQERLYQE 341
Cdd:cd20627 170 SVLKKVIKERKGK---NFSQHVFIDSLLQGN-LSEQQVLE---DSMIFSLAGCVITANlctWAIYFLTTSEEVQKKLYKE 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 342 IREVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPlIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEW 421
Cdd:cd20627 243 VDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTP-VSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYRF 321

                ....*.
gi 50727139 422 VPERFA 427
Cdd:cd20627 322 DPDRFD 327
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
300-451 1.06e-11

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: 66.73  E-value: 1.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 300 EQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGDETV-TEEHLPRLPYLNAVFHETLRRHSPVPL 378
Cdd:cd20672 225 QNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLpTLDDRAKMPYTDAVIHEIQRFSDLIPI 304
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50727139 379 IPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERF--AGGRLEVADMYktMAFGAGRRACAG 451
Cdd:cd20672 305 GVPHRVTKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFldANGALKKSEAF--MPFSTGKRICLG 377
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
297-479 1.56e-11

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: 65.96  E-value: 1.56e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLyQEIREVCgdetvteehlprlpylNAVFHETLRRHSPV 376
Cdd:cd11080 189 LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAV-RADRSLV----------------PRAIAETLRYHPPV 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 377 PLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGG-RLEVADMYKTMAFGAGRRACAGSLQA 455
Cdd:cd11080 252 QLI-PRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREDLGiRSAFSGAADHLAFGSGRHFCVGAALA 330
                       170       180
                ....*....|....*....|....*
gi 50727139 456 THIACAAVARFVQEFG-WRLREGDE 479
Cdd:cd11080 331 KREIEIVANQVLDALPnIRLEPGFE 355
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
302-451 5.60e-11

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: 64.43  E-value: 5.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 302 LMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVCGD--ETVTEEHLpRLPYLNAVFHETLRRHSPVPLI 379
Cdd:cd20668 227 LVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRnrQPKFEDRA-KMPYTEAVIHEIQRFGDVIPMG 305
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139 380 PPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAG--GRLEVADMYktMAFGAGRRACAG 451
Cdd:cd20668 306 LARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDdkGQFKKSDAF--VPFSIGKRYCFG 377
PLN02500 PLN02500
cytochrome P450 90B1
263-479 1.59e-10

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 63.34  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  263 RTAVMRALIKQQKERI--VRGEAKTCYLDFLLA----ENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQE 336
Cdd:PLN02500 235 RATILKFIERKMEERIekLKEEDESVEEDDLLGwvlkHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQ 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  337 RLYQEIREVC------GDETVTEEHLPRLPYLNAVFHETLRRHSPVplippRFVH----EDTKLAGYDVPAGTEMVINLY 406
Cdd:PLN02500 315 ELREEHLEIArakkqsGESELNWEDYKKMEFTQCVINETLRLGNVV-----RFLHrkalKDVRYKGYDIPSGWKVLPVIA 389
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  407 GCNMNRKEWESPEEWVPERF----AGGRLEVADMYKT---MAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDE 479
Cdd:PLN02500 390 AVHLDSSLYDQPQLFNPWRWqqnnNRGGSSGSSSATTnnfMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEADQ 469
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
323-478 9.12e-10

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: 60.62  E-value: 9.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 323 WAMYELAKNPDKQERLyqeiREvcGDETvteehlprlpYLNAVFHEtLRRHSP-VPLIPPRfVHEDTKLAGYDVPAGTEM 401
Cdd:cd11067 242 FAALALHEHPEWRERL----RS--GDED----------YAEAFVQE-VRRFYPfFPFVGAR-ARRDFEWQGYRFPKGQRV 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 402 VINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMyktMAFGAGRRA----CAGSLQATHIACAAVARFVQEFGWRLREG 477
Cdd:cd11067 304 LLDLYGTNHDPRLWEDPDRFRPERFLGWEGDPFDF---IPQGGGDHAtghrCPGEWITIALMKEALRLLARRDYYDVPPQ 380

                .
gi 50727139 478 D 478
Cdd:cd11067 381 D 381
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
364-478 1.32e-09

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: 59.81  E-value: 1.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 364 AVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNrkewesPEEWV-PERFAGGRLEVAdmykTMAF 442
Cdd:cd11036 223 AAVAETLRYDPPVRLER-RFAAEDLELAGVTLPAGDHVVVLLAAANRD------PEAFPdPDRFDLGRPTAR----SAHF 291
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 50727139 443 GAGRRACAGSLQATHIACAAVARFVQEFGWRLREGD 478
Cdd:cd11036 292 GLGRHACLGAALARAAAAAALRALAARFPGLRAAGP 327
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
293-451 8.32e-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: 57.21  E-value: 8.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 AENTLTDEQLMMLVwEALIEAA-DTTLVTTEWAMYELAKNPDKQERLYQEirevcgdetvteehlPRLpyLNAVFHETLR 371
Cdd:cd11037 194 DRGEITEDEAPLLM-RDYLSAGlDTTISAIGNALWLLARHPDQWERLRAD---------------PSL--APNAFEEAVR 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 372 RHSPVPLIPpRFVHEDTKLAGYDVPAGtEMVINLYGCnMNRKE--WESPEEWVPERFAGGRLevadmyktmAFGAGRRAC 449
Cdd:cd11037 256 LESPVQTFS-RTTTRDTELAGVTIPAG-SRVLVFLGS-ANRDPrkWDDPDRFDITRNPSGHV---------GFGHGVHAC 323

                ..
gi 50727139 450 AG 451
Cdd:cd11037 324 VG 325
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
263-495 2.00e-08

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: 56.38  E-value: 2.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 263 RTAVMRALIKQQKERIVRGEAKTC--YLDFLLA---EN--TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQ 335
Cdd:cd20636 182 RDILHEYMEKAIEEKLQRQQAAEYcdALDYMIHsarENgkELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAI 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 336 ERLYQEIRE-------VCGDETVTEEHLPRLPYLNAVFHETLRrhspvpLIPP-----RFVHEDTKLAGYDVPAGTEMVI 403
Cdd:cd20636 262 EKIRQELVShglidqcQCCPGALSLEKLSRLRYLDCVVKEVLR------LLPPvsggyRTALQTFELDGYQIPKGWSVMY 335
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 404 NLYGCNMNRKEWESPEEWVPERFAGGRLE-VADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDEEKV 482
Cdd:cd20636 336 SIRDTHETAAVYQNPEGFDPDRFGVEREEsKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWELATPTFPKM 415
                       250
                ....*....|...
gi 50727139 483 DTVQLtaykLHPL 495
Cdd:cd20636 416 QTVPI----VHPV 424
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
265-470 2.21e-08

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: 55.89  E-value: 2.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 265 AVMRALIKQQKERIVRGEAKTCYLDFLLAENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEire 344
Cdd:cd20630 167 ALIEEVIAERRQAPVEDDLLTTLLRAEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE--- 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 345 vcgdetvteehlPRLpyLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPE 424
Cdd:cd20630 244 ------------PEL--LRNALEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVR 309
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 50727139 425 RfaggrlevaDMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd20630 310 R---------DPNANIAFGYGPHFCIGAALARLELELAVSTLLRRF 346
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
266-477 2.40e-08

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: 56.36  E-value: 2.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 266 VMRALIKQQ-KERIVRGEAKTCYLDFL--LAENTL-TDEQLMMlvwEALIEAA--------DTTLVT-TEWAMYeLAKNP 332
Cdd:cd20638 186 LIHAKIEENiRAKIQREDTEQQCKDALqlLIEHSRrNGEPLNL---QALKESAtellfgghETTASAaTSLIMF-LGLHP 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 333 DKQERLYQEIRE---VCGDET----VTEEHLPRLPYLNAVFHETLRRHSPVPLiPPRFVHEDTKLAGYDVPAGTEMVINL 405
Cdd:cd20638 262 EVLQKVRKELQEkglLSTKPNenkeLSMEVLEQLKYTGCVIKETLRLSPPVPG-GFRVALKTFELNGYQIPKGWNVIYSI 340
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50727139 406 YGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG 477
Cdd:cd20638 341 CDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNG 412
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
328-466 2.80e-08

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 56.24  E-value: 2.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  328 LAKNPDKQERLYQEIREVCG--DETVTEEHLPRLPYLNAVFHETLRrhspvpLIPPrfVHEDTKLAGYD--------VPA 397
Cdd:PLN02426 320 LSKHPEVASAIREEADRVMGpnQEAASFEEMKEMHYLHAALYESMR------LFPP--VQFDSKFAAEDdvlpdgtfVAK 391
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50727139  398 GTEMVINLYGcnMNRKE--W-ESPEEWVPERF-AGGRLEVADMYKTMAFGAGRRACAGS----LQATHIACAAVARF 466
Cdd:PLN02426 392 GTRVTYHPYA--MGRMEriWgPDCLEFKPERWlKNGVFVPENPFKYPVFQAGLRVCLGKemalMEMKSVAVAVVRRF 466
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
297-499 3.12e-08

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: 55.69  E-value: 3.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLyqeirevCGDETvteehlpRLPylNAVfHETLRRHSPV 376
Cdd:cd11078 205 LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRL-------RADPS-------LIP--NAV-EETLRYDSPV 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 377 PLIpPRFVHEDTKLAGYDVPAGTEMVInLYGcNMNRKEWESPEewvPERFaggRLEVADMYKTMAFGAGRRACAGSLQAT 456
Cdd:cd11078 268 QGL-RRTATRDVEIGGVTIPAGARVLL-LFG-SANRDERVFPD---PDRF---DIDRPNARKHLTFGHGIHFCLGAALAR 338
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 50727139 457 HIACAAVARFVQEF-GWRLregDEEKVDTVQ-LTAYKLHPLHVHL 499
Cdd:cd11078 339 MEARIALEELLRRLpGMRV---PGQEVVYSPsLSFRGPESLPVEW 380
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
241-479 3.89e-08

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 55.76  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  241 FPYLSWVPNKSFETRVFTTETRRTAVMraliKQQKERIVRGEAKTCYLDFLLA-ENTLTDEQLMMLVWEALIEAADTTLV 319
Cdd:PLN02987 210 LPLFSTTYRRAIQARTKVAEALTLVVM----KRRKEEEEGAEKKKDMLAALLAsDDGFSDEEIVDFLVALLVAGYETTST 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  320 TTEWAMYELAKNPDKQERL---YQEIREVCGDETVTE-EHLPRLPYLNAVFHETLRRHSPVPLIPPRfVHEDTKLAGYDV 395
Cdd:PLN02987 286 IMTLAVKFLTETPLALAQLkeeHEKIRAMKSDSYSLEwSDYKSMPFTQCVVNETLRVANIIGGIFRR-AMTDIEVKGYTI 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  396 PAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADMYKTMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLR 475
Cdd:PLN02987 365 PKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPA 444

                 ....
gi 50727139  476 EGDE 479
Cdd:PLN02987 445 EQDK 448
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
293-451 1.17e-07

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: 53.84  E-value: 1.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 AENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERlyqeireVCGDETvteehlprlpYLNAVFHETLRR 372
Cdd:cd20629 184 EGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLER-------VRRDRS----------LIPAAIEEGLRW 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 373 HSPVPLIPpRFVHEDTKLAGYDVPAGTemVINLYGCNMNRKE--WESPEEWvperfaggrlevaDMYKT----MAFGAGR 446
Cdd:cd20629 247 EPPVASVP-RMALRDVELDGVTIPAGS--LLDLSVGSANRDEdvYPDPDVF-------------DIDRKpkphLVFGGGA 310

                ....*
gi 50727139 447 RACAG 451
Cdd:cd20629 311 HRCLG 315
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
317-451 2.13e-07

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: 53.07  E-value: 2.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 317 TLVTTEWAMYELAKNPDKQERLYQEIREVCG----------DETVTEEHLPRLPYLNAVFHETLRRHSPVplIPPRFVHE 386
Cdd:cd20632 231 TIPATFWAMYYLLRHPEALAAVRDEIDHVLQstgqelgpdfDIHLTREQLDSLVYLESAINESLRLSSAS--MNIRVVQE 308
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50727139 387 DTKL---AGYDVPAGTEMVINLY--GCNMNRKEWESPEEWVPERFAGGRLEVADMYKT--------MAFGAGRRACAG 451
Cdd:cd20632 309 DFTLkleSDGSVNLRKGDIVALYpqSLHMDPEIYEDPEVFKFDRFVEDGKKKTTFYKRgqklkyylMPFGSGSSKCPG 386
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
325-470 2.27e-07

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 53.03  E-value: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 325 MYELAK-NPDKQERLYQEIREVCGD-ETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPR----FV---HEdtklAGYDV 395
Cdd:cd11071 249 LARLGLaGEELHARLAEEIRSALGSeGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRarkdFViesHD----ASYKI 324
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 396 PAGTEMVINLYGCNMNRKEWESPEEWVPERFAGGRLEVADM------YKTMAFGAGRRACAG---SLQATHIACAAVARF 466
Cdd:cd11071 325 KKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGEEGKLLKHliwsngPETEEPTPDNKQCPGkdlVVLLARLFVAELFLR 404

                ....
gi 50727139 467 VQEF 470
Cdd:cd11071 405 YDTF 408
PLN02302 PLN02302
ent-kaurenoic acid oxidase
272-452 2.60e-07

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 53.18  E-value: 2.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  272 KQQKERIVRGEaKTCYLDFLLA---EN--TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEIREVC 346
Cdd:PLN02302 254 RNSRKQNISPR-KKDMLDLLLDaedENgrKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIA 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  347 GDETVTEEHLP-----RLPYLNAVFHETLR--RHSPVPLippRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPE 419
Cdd:PLN02302 333 KKRPPGQKGLTlkdvrKMEYLSQVIDETLRliNISLTVF---REAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPK 409
                        170       180       190
                 ....*....|....*....|....*....|...
gi 50727139  420 EWVPERFAGgrlEVADMYKTMAFGAGRRACAGS 452
Cdd:PLN02302 410 EFDPSRWDN---YTPKAGTFLPFGLGSRLCPGN 439
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
297-470 5.56e-07

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: 51.44  E-value: 5.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEirevcgdetvteehlPRLpyLNAVFHETLRRHSPV 376
Cdd:cd11035 186 LTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRED---------------PEL--IPAAVEELLRRYPLV 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 377 plIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAggrlevadmYKTMAFGAGRRACAGSlqat 456
Cdd:cd11035 249 --NVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDRKP---------NRHLAFGAGPHRCLGS---- 313
                       170
                ....*....|....
gi 50727139 457 HIACAAVARFVQEF 470
Cdd:cd11035 314 HLARLELRIALEEW 327
PLN02648 PLN02648
allene oxide synthase
325-428 2.54e-06

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 49.93  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  325 MYELAK-NPDKQERLYQEIREVCGDE--TVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPR----FVHEdTKLAGYDVPA 397
Cdd:PLN02648 296 LKWVGRaGEELQARLAEEVRSAVKAGggGVTFAALEKMPLVKSVVYEALRIEPPVPFQYGRaredFVIE-SHDAAFEIKK 374
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 50727139  398 GtEMvinLYG---CNM-NRKEWESPEEWVPERFAG 428
Cdd:PLN02648 375 G-EM---LFGyqpLVTrDPKVFDRPEEFVPDRFMG 405
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
270-452 3.42e-06

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: 49.26  E-value: 3.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 270 LIKQQKERivRGEAKTCYLDFLLAEN----TLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLYQEirev 345
Cdd:cd11034 157 LRDLIAER--RANPRDDLISRLIEGEidgkPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLIAD---- 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 346 cgdetvtEEHLPRlpylnAVfHETLRRHSPVPLIpPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPER 425
Cdd:cd11034 231 -------PSLIPN-----AV-EEFLRFYSPVAGL-ARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDR 296
                       170       180
                ....*....|....*....|....*..
gi 50727139 426 FAGgrlevadmyKTMAFGAGRRACAGS 452
Cdd:cd11034 297 TPN---------RHLAFGSGVHRCLGS 314
PLN02774 PLN02774
brassinosteroid-6-oxidase
263-479 4.77e-06

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 49.00  E-value: 4.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  263 RTAVMRALIKQQKERIVRGEAKTCYLDFLLA-ENT---LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERL 338
Cdd:PLN02774 222 RKNIVRMLRQLIQERRASGETHTDMLGYLMRkEGNrykLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQEL 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139  339 YQE---IREVCG-DETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKE 414
Cdd:PLN02774 302 RKEhlaIRERKRpEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVL-RKTTQDMELNGYVIPKGWRIYVYTREINYDPFL 380
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50727139  415 WESPEEWVPERFAGGRLEVADMYktMAFGAGRRACAGSLQATHIACAAVARFVQEFGWRLREGDE 479
Cdd:PLN02774 381 YPDPMTFNPWRWLDKSLESHNYF--FLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWEEVGGDK 443
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
296-452 1.56e-05

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: 47.21  E-value: 1.56e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 296 TLTDEQL----MMLvweaLIEAADTTLVTTEWAMYELAKNPDkqerLYQEIREvcgdetvteeHLPRLPylnAVFHETLR 371
Cdd:cd11032 193 RLTDEEIvgfaILL----LIAGHETTTNLLGNAVLCLDEDPE----VAARLRA----------DPSLIP---GAIEEVLR 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 372 RHSPVPLIPpRFVHEDTKLAGYDVPAGtEMVINLYG-CNMNRKEWESPEEWVPERfaggrlevaDMYKTMAFGAGRRACA 450
Cdd:cd11032 252 YRPPVQRTA-RVTTEDVELGGVTIPAG-QLVIAWLAsANRDERQFEDPDTFDIDR---------NPNPHLSFGHGIHFCL 320

                ..
gi 50727139 451 GS 452
Cdd:cd11032 321 GA 322
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
263-466 1.64e-05

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: 47.15  E-value: 1.64e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 263 RTAVMRALIKQQKERIVRGEAKTcYLDFL--LAENT------LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDK 334
Cdd:cd20637 181 RDSLQKSLEKAIREKLQGTQGKD-YADALdiLIESAkehgkeLTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGV 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 335 QERLYQEIRE--------VCgDETVTEEHLPRLPYLNAVFHETLRRHSPVPLiPPRFVHEDTKLAGYDVPAGTEMVINLY 406
Cdd:cd20637 260 LEKLREELRSngilhngcLC-EGTLRLDTISSLKYLDCVIKEVLRLFTPVSG-GYRTALQTFELDGFQIPKGWSVLYSIR 337
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50727139 407 GCNMNRKEWESPEEWVPERFAGGRLEVAD-MYKTMAFGAGRRACAGS------LQATHIACAAVARF 466
Cdd:cd20637 338 DTHDTAPVFKDVDAFDPDRFGQERSEDKDgRFHYLPFGGGVRTCLGKqlaklfLKVLAVELASTSRF 404
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
297-403 2.20e-05

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 46.76  E-value: 2.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTT--LVTTewAMYELAKNPDKQERLYQEirevcgdetvteehlPRLpyLNAVFHETLRRHS 374
Cdd:cd11029 207 LSEEELVSTVFLLLVAGHETTvnLIGN--GVLALLTHPDQLALLRAD---------------PEL--WPAAVEELLRYDG 267
                        90       100
                ....*....|....*....|....*....
gi 50727139 375 PVPLIPPRFVHEDTKLAGYDVPAGtEMVI 403
Cdd:cd11029 268 PVALATLRFATEDVEVGGVTIPAG-EPVL 295
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
267-470 2.22e-05

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: 410716 [Multi-domain]  Cd Length: 367  Bit Score: 46.49  E-value: 2.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 267 MRALIKqqKERIVRGEAKTCYLdfLLAENTLTDEQL---MMLVWEALIEAadttlvTTEWamyelaknpdkqerLYQEIR 343
Cdd:cd20623 166 LRELVA--LRRARPGDDLTSRL--LAHPAGLTDEEVvhdLVLLLGAGHEP------TTNL--------------IGNTLR 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 344 EVCGDETVTEEHLPRLPYLNAVFHETLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNmnrkeweSPEEWVP 423
Cdd:cd20623 222 LMLTDPRFAASLSGGRLSVREALNEVLWRDPPLANLAGRFAARDTELGGQWIRAGDLVVLGLAAAN-------ADPRVRP 294
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 50727139 424 ERFAGGRLEVADmyktMAFGAGRRACAGSLQATHIACAAVARFVQEF 470
Cdd:cd20623 295 DPGASMSGNRAH----LAFGAGPHRCPAQELAETIARTAVEVLLDRL 337
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
297-455 5.13e-05

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: 45.43  E-value: 5.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 297 LTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDkQERLYQEiREVCGDETVTEehlprlpylnavfhetLRRHSPV 376
Cdd:cd11038 210 LSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALRE-DPELAPAAVEE----------------VLRWCPT 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 377 PLIPPRFVHEDTKLAGYDVPAGTemVINLYGCNMNRKewespeewvPERFAGGRLEV-ADMYKTMAFGAGRRACAGSLQA 455
Cdd:cd11038 272 TTWATREAVEDVEYNGVTIPAGT--VVHLCSHAANRD---------PRVFDADRFDItAKRAPHLGFGGGVHHCLGAFLA 340
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
328-477 1.07e-04

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: 44.37  E-value: 1.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 328 LAKNPDKQERLYQEIREVCGDetvteehlPRLPYLNAVFHETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGTEMVINLYG 407
Cdd:cd20624 218 LAAHPEQAARAREEAAVPPGP--------LARPYLRACVLDAVRLWPTTPAVL-RESTEDTVWGGRTVPAGTGFLIFAPF 288
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50727139 408 CNMNRKEWESPEEWVPERFAGGRlevADMYKTMA-FGAGRRACAGSLQATHIACAAVARFVQEFGWRLREG 477
Cdd:cd20624 289 FHRDDEALPFADRFVPEIWLDGR---AQPDEGLVpFSAGPARCPGENLVLLVASTALAALLRRAEIDPLES 356
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
293-465 1.31e-04

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: 44.09  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 AENTLTDEQLMMLVWEALIEAADTTLVTTEWAMYELAKNPDKQERLyqeirevcgdetvtEEHLPRLPylNAVfHETLRR 372
Cdd:cd11031 198 DDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARL--------------RADPELVP--AAV-EELLRY 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 373 HSPVPLI-PPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERFAGgrlevadmyKTMAFGAGRRACAG 451
Cdd:cd11031 261 IPLGAGGgFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDREPN---------PHLAFGHGPHHCLG 331
                       170
                ....*....|....
gi 50727139 452 slqathiacAAVAR 465
Cdd:cd11031 332 ---------APLAR 336
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
324-467 1.39e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 44.03  E-value: 1.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 324 AMYELAKNPDKQERLYQEirevcgdetvtEEHLPRlpylnaVFHETLRRHSPVPLiPPRFVHEDTKLAGYDVPAGTEMVI 403
Cdd:cd11039 225 TCWGLLSNPEQLAEVMAG-----------DVHWLR------AFEEGLRWISPIGM-SPRRVAEDFEIRGVTLPAGDRVFL 286
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50727139 404 NLYGCNMNRKEWESpeewvPERFAGGRlevaDMYKTMAFGAGRRACAGSlqatHIACAAVARFV 467
Cdd:cd11039 287 MFGSANRDEARFEN-----PDRFDVFR----PKSPHVSFGAGPHFCAGA----WASRQMVGEIA 337
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
293-470 1.37e-03

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: 41.00  E-value: 1.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 293 AENTLTDEQL----MMLvweaLIEAADTT--LVTTewAMYELAKNPDKQERLyqeiREvcgdetvteeHLPRLPylNAVf 366
Cdd:cd20625 193 DGDRLSEDELvancILL----LVAGHETTvnLIGN--GLLALLRHPEQLALL----RA----------DPELIP--AAV- 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 367 HETLRRHSPVPLIPpRFVHEDTKLAGYDVPAGtEMVINLYGC-NMNRKEWESPEEWVPERFAGGRLevadmyktmAFGAG 445
Cdd:cd20625 250 EELLRYDSPVQLTA-RVALEDVEIGGQTIPAG-DRVLLLLGAaNRDPAVFPDPDRFDITRAPNRHL---------AFGAG 318
                       170       180
                ....*....|....*....|....*....
gi 50727139 446 RRACAGS----LQAThiacAAVARFVQEF 470
Cdd:cd20625 319 IHFCLGAplarLEAE----IALRALLRRF 343
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
363-453 3.19e-03

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: 39.72  E-value: 3.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50727139 363 NAVFHEtLRRHSPVPLIPPRFVHEDTKLAGYDVPAGTEMVINLYGCNMNRKEWESPEEWVPERfaggrleVADMYKTMAF 442
Cdd:cd20619 235 AAIINE-MVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTR-------PPAASRNLSF 306
                        90
                ....*....|.
gi 50727139 443 GAGRRACAGSL 453
Cdd:cd20619 307 GLGPHSCAGQI 317
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH