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Conserved domains on  [gi|15220438|ref|NP_172008|]
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cytochrome P450, family 88, subfamily A, polypeptide 3 [Arabidopsis thaliana]

Protein Classification

cytochrome P450 family protein; cytochrome P450( domain architecture ID 10010760)

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| cytochrome P450 catalyzes 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

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List of domain hits

Name Accession Description Interval E-value
PLN02302 PLN02302
ent-kaurenoic acid oxidase
3-490 0e+00

ent-kaurenoic acid oxidase


:

Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 956.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438    3 ETTSWIPVWFPLMVLGCFGLNWLVRKVNVWLYESSLGENRHYLPPGDLGWPFIGNMLSFLRAFKTSDPDSFTRTLIKRYG 82
Cdd:PLN02302   1 MELGSIWVWLAAIVAGVFVLKWVLRRVNSWLYEPKLGEGQPPLPPGDLGWPVIGNMWSFLRAFKSSNPDSFIASFISRYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   83 PKGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIP 162
Cdd:PLN02302  81 RTGIYKAFMFGQPTVLVTTPEACKRVLTDDDAFEPGWPESTVELIGRKSFVGITGEEHKRLRRLTAAPVNGPEALSTYIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  163 YIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARK 242
Cdd:PLN02302 161 YIEENVKSCLEKWSKMGEIEFLTELRKLTFKIIMYIFLSSESELVMEALEREYTTLNYGVRAMAINLPGFAYHRALKARK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  243 TLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEV 322
Cdd:PLN02302 241 KLVALFQSIVDERRNSRKQNISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  323 LQRAKAEQEMILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHI 402
Cdd:PLN02302 321 LQKAKAEQEEIAKKRPPGQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHM 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  403 DPEVFPDPRKFDPARWDNgFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMYLPHTRPTDN 482
Cdd:PLN02302 401 DPEVYPNPKEFDPSRWDN-YTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLNPGCKVMYLPHPRPKDN 479

                 ....*...
gi 15220438  483 CLARISYQ 490
Cdd:PLN02302 480 CLARITKV 487
 
Name Accession Description Interval E-value
PLN02302 PLN02302
ent-kaurenoic acid oxidase
3-490 0e+00

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 956.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438    3 ETTSWIPVWFPLMVLGCFGLNWLVRKVNVWLYESSLGENRHYLPPGDLGWPFIGNMLSFLRAFKTSDPDSFTRTLIKRYG 82
Cdd:PLN02302   1 MELGSIWVWLAAIVAGVFVLKWVLRRVNSWLYEPKLGEGQPPLPPGDLGWPVIGNMWSFLRAFKSSNPDSFIASFISRYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   83 PKGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIP 162
Cdd:PLN02302  81 RTGIYKAFMFGQPTVLVTTPEACKRVLTDDDAFEPGWPESTVELIGRKSFVGITGEEHKRLRRLTAAPVNGPEALSTYIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  163 YIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARK 242
Cdd:PLN02302 161 YIEENVKSCLEKWSKMGEIEFLTELRKLTFKIIMYIFLSSESELVMEALEREYTTLNYGVRAMAINLPGFAYHRALKARK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  243 TLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEV 322
Cdd:PLN02302 241 KLVALFQSIVDERRNSRKQNISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  323 LQRAKAEQEMILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHI 402
Cdd:PLN02302 321 LQKAKAEQEEIAKKRPPGQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHM 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  403 DPEVFPDPRKFDPARWDNgFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMYLPHTRPTDN 482
Cdd:PLN02302 401 DPEVYPNPKEFDPSRWDN-YTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLNPGCKVMYLPHPRPKDN 479

                 ....*...
gi 15220438  483 CLARISYQ 490
Cdd:PLN02302 480 CLARITKV 487
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
78-488 2.11e-177

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: 503.64  E-value: 2.11e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  78 IKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDA-FKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEA 156
Cdd:cd11043   2 IKRYGP--VFKTSLFGRPTVVSADPEANRFILQNEGKlFVSWYPKSVRKLLGKSSLLTVSGEEHKRLRGLLLSFLGPEAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 157 LSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHR 236
Cdd:cd11043  80 KDRLLGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRKEFQAFLEGLLSFPLNLPGTTFHR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 237 ALKARKTLVAAFQSIVTERRNQRKQNilSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFL 316
Cdd:cd11043 160 ALKARKRIRKELKKIIEERRAELEKA--SPKGDLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 317 QEHPEVLQRAKAEQEMILKSRPEGQkGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTW 396
Cdd:cd11043 238 AENPKVLQELLEEHEEIAKRKEEGE-GLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWS 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 397 FRDVHIDPEVFPDPRKFDPARWDNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRsNPECPVMYLPH 476
Cdd:cd11043 317 ARATHLDPEYFPDPLKFNPWRWEGKGKGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEV-VPDEKISRFPL 395
                       410
                ....*....|..
gi 15220438 477 TRPTDNCLARIS 488
Cdd:cd11043 396 PRPPKGLPIRLS 407
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
69-457 8.04e-73

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: 235.94  E-value: 8.04e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  69 DPDSFTRTLiKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAF--KPGWPTSTMEL-IGRKSFVGISFEEHKRLRR 145
Cdd:COG2124  20 DPYPFYARL-REYGP--VFRVRLPGGGAWLVTRYEDVREVLRDPRTFssDGGLPEVLRPLpLLGDSLLTLDGPEHTRLRR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 146 LTAAPVNgHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALnygvrAM 225
Cdd:COG2124  97 LVQPAFT-PRRVAALRPRIREIADELLDRLAARGPVDLVEEFARPLPVIVICELLGVPEEDRDRLRRWSDALL-----DA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 226 AVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQnilsnkkDMLDNLLNVKDeDGKTLDDEEIIDVLLMYLNAGHESS 305
Cdd:COG2124 171 LGPLPPERRRRARRARAELDAYLRELIAERRAEPGD-------DLLSALLAARD-DGERLSDEELRDELLLLLLAGHETT 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 306 GHTIMWATVFLQEHPEVLQRAKAEQEmilksrpegqkglslketrkmeFLSQVVDETLRVITFSLTAFREAKTDVEMNGY 385
Cdd:COG2124 243 ANALAWALYALLRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVPLLPRTATEDVELGGV 300
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220438 386 LIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:COG2124 301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAHLPFGGGPHRCLGAALARLEARIALATLL 365
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
46-472 4.57e-60

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: 204.05  E-value: 4.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438    46 PPGDLGWPFIGNMLSFLRAFKtsdPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVL-TDDDAFKPGWPTSTM 124
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGN---LHSVFTKLQKKYGP--IFRLYLGPKPVVVLSGPEAVKEVLiKKGEEFSGRPDEPWF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   125 ELIGRKSFV-GISF---EEHKRLRRLTAAPVNGHEALStYIPYIEENVITVLDKWTKM----GEFEFLTHLRKLTFRIIM 196
Cdd:pfam00067  76 ATSRGPFLGkGIVFangPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTagepGVIDITDLLFRAALNVIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   197 YIFLSSESENVMDALEREYTALNYGVRAMAVN--------------IPGFAYHRALKARKTLVAAFQSIVTERRNQRKQN 262
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSpspqlldlfpilkyFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   263 iLSNKKDMLDNLLNVKD-EDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrpEGQ 341
Cdd:pfam00067 235 -KKSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVI----GDK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   342 KGLSLKETRKMEFLSQVVDETLRVITFSLTA-FREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-- 418
Cdd:pfam00067 310 RSPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFld 389
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15220438   419 DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVM 472
Cdd:pfam00067 390 ENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443
 
Name Accession Description Interval E-value
PLN02302 PLN02302
ent-kaurenoic acid oxidase
3-490 0e+00

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 956.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438    3 ETTSWIPVWFPLMVLGCFGLNWLVRKVNVWLYESSLGENRHYLPPGDLGWPFIGNMLSFLRAFKTSDPDSFTRTLIKRYG 82
Cdd:PLN02302   1 MELGSIWVWLAAIVAGVFVLKWVLRRVNSWLYEPKLGEGQPPLPPGDLGWPVIGNMWSFLRAFKSSNPDSFIASFISRYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   83 PKGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIP 162
Cdd:PLN02302  81 RTGIYKAFMFGQPTVLVTTPEACKRVLTDDDAFEPGWPESTVELIGRKSFVGITGEEHKRLRRLTAAPVNGPEALSTYIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  163 YIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARK 242
Cdd:PLN02302 161 YIEENVKSCLEKWSKMGEIEFLTELRKLTFKIIMYIFLSSESELVMEALEREYTTLNYGVRAMAINLPGFAYHRALKARK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  243 TLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEV 322
Cdd:PLN02302 241 KLVALFQSIVDERRNSRKQNISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  323 LQRAKAEQEMILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHI 402
Cdd:PLN02302 321 LQKAKAEQEEIAKKRPPGQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHM 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  403 DPEVFPDPRKFDPARWDNgFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMYLPHTRPTDN 482
Cdd:PLN02302 401 DPEVYPNPKEFDPSRWDN-YTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLNPGCKVMYLPHPRPKDN 479

                 ....*...
gi 15220438  483 CLARISYQ 490
Cdd:PLN02302 480 CLARITKV 487
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
78-488 2.11e-177

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: 503.64  E-value: 2.11e-177
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  78 IKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDA-FKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEA 156
Cdd:cd11043   2 IKRYGP--VFKTSLFGRPTVVSADPEANRFILQNEGKlFVSWYPKSVRKLLGKSSLLTVSGEEHKRLRGLLLSFLGPEAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 157 LSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHR 236
Cdd:cd11043  80 KDRLLGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRKEFQAFLEGLLSFPLNLPGTTFHR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 237 ALKARKTLVAAFQSIVTERRNQRKQNilSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFL 316
Cdd:cd11043 160 ALKARKRIRKELKKIIEERRAELEKA--SPKGDLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 317 QEHPEVLQRAKAEQEMILKSRPEGQkGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTW 396
Cdd:cd11043 238 AENPKVLQELLEEHEEIAKRKEEGE-GLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWS 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 397 FRDVHIDPEVFPDPRKFDPARWDNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRsNPECPVMYLPH 476
Cdd:cd11043 317 ARATHLDPEYFPDPLKFNPWRWEGKGKGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEV-VPDEKISRFPL 395
                       410
                ....*....|..
gi 15220438 477 TRPTDNCLARIS 488
Cdd:cd11043 396 PRPPKGLPIRLS 407
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
12-483 1.53e-95

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 296.85  E-value: 1.53e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   12 FPLMVLGCFGLNWLVRKVNVWLYESSLGENRHYLPPGDLGWPFIGNMLSFLrafkTSDPDSFTRTLIKRYGpkGIYKAHM 91
Cdd:PLN02196   3 FSALFLTLFAGALFLCLLRFLAGFRRSSSTKLPLPPGTMGWPYVGETFQLY----SQDPNVFFASKQKRYG--SVFKTHV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   92 FGNPSIIVTTSDTCRRVL-TDDDAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTA---APvnghEALSTYIPYIEEN 167
Cdd:PLN02196  77 LGCPCVMISSPEAAKFVLvTKSHLFKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLrafMP----DAIRNMVPDIESI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  168 VITVLDKW--TKMGEFEfltHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLV 245
Cdd:PLN02196 153 AQESLNSWegTQINTYQ---EMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKGYNSMPINLPGTLFHKSMKARKELA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  246 AAFQSIVTERRNQRkqnilSNKKDMLDNLLnvkdEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQR 325
Cdd:PLN02196 230 QILAKILSKRRQNG-----SSHNDLLGSFM----GDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  326 AKAEQEMILKSRPEGqKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPE 405
Cdd:PLN02196 301 VTEEQMAIRKDKEEG-ESLTWEDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSAD 379
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15220438  406 VFPDPRKFDPARWDngFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMYLPHTRPTDNC 483
Cdd:PLN02196 380 IFSDPGKFDPSRFE--VAPKPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTSNGIQYGPFALPQNGL 455
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
56-487 2.83e-93

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: 289.57  E-value: 2.83e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  56 GNMLSFLRafktsDPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLT-DDDAFKPGWPTSTMELIGRKSFVG 134
Cdd:cd11044   1 GETLEFLR-----DPEDFIQSRYQKYGP--VFKTHLLGRPTVFVIGAEAVRFILSgEGKLVRYGWPRSVRRLLGENSLSL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 135 ISFEEHKRLRRLTAaPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALERE 214
Cdd:cd11044  74 QDGEEHRRRRKLLA-PAFSREALESYVPTIQAIVQSYLRKWLKAGEVALYPELRRLTFDVAARLLLGLDPEVEAEALSQD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 215 YTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVterrNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVL 294
Cdd:cd11044 153 FETWTDGLFSLPVPLPFTPFGRAIRARNKLLARLEQAI----RERQEEENAEAKDALGLLLEAKDEDGEPLSMDELKDQA 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 295 LMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPegqkgLSLKETRKMEFLSQVVDETLRVITFSLTAFR 374
Cdd:cd11044 229 LLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEP-----LTLESLKKMPYLDQVIKEVLRLVPPVGGGFR 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 375 EAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW---DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISI 451
Cdd:cd11044 304 KVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFspaRSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKI 383
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 15220438 452 FLHHFLLKYQ---VKRSNPECPVMylPHTRPTDNCLARI 487
Cdd:cd11044 384 LASELLRNYDwelLPNQDLEPVVV--PTPRPKDGLRVRF 420
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
42-478 4.83e-86

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 272.62  E-value: 4.83e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   42 RHYLPPGDLGWPFIGNMLSFLRAFKTSDPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDA-FKPGWP 120
Cdd:PLN02987  28 RMRLPPGSLGLPLVGETLQLISAYKTENPEPFIDERVARYGS--LFMTHLFGEPTVFSADPETNRFILQNEGKlFECSYP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  121 TSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKmgEFEFLTHLRKLTFRIIMYIFL 200
Cdd:PLN02987 106 GSISNLLGKHSLLLMKGNLHKKMHSLTMSFANSSIIKDHLLLDIDRLIRFNLDSWSS--RVLLMEEAKKITFELTVKQLM 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  201 SSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNiLSNKKDMLDNLLNVKDe 280
Cdd:PLN02987 184 SFDPGEWTESLRKEYVLVIEGFFSVPLPLFSTTYRRAIQARTKVAEALTLVVMKRRKEEEEG-AEKKKDMLAALLASDD- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  281 dgkTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMIlKSRPEGQKGLSLKETRKMEFLSQVVD 360
Cdd:PLN02987 262 ---GFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKI-RAMKSDSYSLEWSDYKSMPFTQCVVN 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  361 ETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPK--AGAFLPFGAGSHL 438
Cdd:PLN02987 338 ETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTvpSNVFTPFGGGPRL 417
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 15220438  439 CPGNDLAKLEISIFLHHFLLKYQVKRSNPEcPVMYLPHTR 478
Cdd:PLN02987 418 CPGYELARVALSVFLHRLVTRFSWVPAEQD-KLVFFPTTR 456
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
45-460 3.98e-81

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 258.90  E-value: 3.98e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   45 LPPGDLGWPFIGNMLSFLRAFKTSDPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDD-DAFKPGWPTST 123
Cdd:PLN03141   8 LPKGSLGWPVIGETLDFISCAYSSRPESFMDKRRSLYGK--VFKSHIFGTPTIVSTDAEVNKVVLQSDgNAFVPAYPKSL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  124 MELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSE 203
Cdd:PLN03141  86 TELMGKSSILLINGSLQRRVHGLIGAFLKSPHLKAQITRDMERYVSESLDSWRDDPPVLVQDETKKIAFEVLVKALISLE 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  204 SENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRK---QNILSNKKDMLDNLLNvkde 280
Cdd:PLN03141 166 PGEEMEFLKKEFQEFIKGLMSLPIKLPGTRLYRSLQAKKRMVKLVKKIIEEKRRAMKnkeEDETGIPKDVVDVLLR---- 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  281 DGK-TLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAkAEQEMILKSRPEgQKGLSLKETRKME--FLSQ 357
Cdd:PLN03141 242 DGSdELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQL-TEENMKLKRLKA-DTGEPLYWTDYMSlpFTQN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  358 VVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVpKAGAFLPFGAGSH 437
Cdd:PLN03141 320 VITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDM-NNSSFTPFGGGQR 398
                        410       420
                 ....*....|....*....|...
gi 15220438  438 LCPGNDLAKLEISIFLHHFLLKY 460
Cdd:PLN03141 399 LCPGLDLARLEASIFLHHLVTRF 421
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
86-481 2.38e-78

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: 250.12  E-value: 2.38e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  86 IYKAHMFGNPSIIVTTSDTCRRVLTDDDAFK--PGWPTSTMELIGRKSFVGISFEEHKRLRRLtAAPVNGHEALSTYIPY 163
Cdd:cd00302   3 VFRVRLGGGPVVVVSDPELVREVLRDPRDFSsdAGPGLPALGDFLGDGLLTLDGPEHRRLRRL-LAPAFTPRALAALRPV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 164 IEENVITVLDKWTKMGEFEFL--THLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKAR 241
Cdd:cd00302  82 IREIARELLDRLAAGGEVGDDvaDLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRLLRPLPSPRLRRLRRA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 242 ktlVAAFQSIVTERRNQRKQNIlsnkKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPE 321
Cdd:cd00302 162 ---RARLRDYLEELIARRRAEP----ADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 322 VLQRAKAEQEMILKSRpegqkglSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVH 401
Cdd:cd00302 235 VQERLRAEIDAVLGDG-------TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYAAH 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 402 IDPEVFPDPRKFDPARWDNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVM--YLPHTRP 479
Cdd:cd00302 308 RDPEVFPDPDEFDPERFLPEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWrpSLGTLGP 387

                ..
gi 15220438 480 TD 481
Cdd:cd00302 388 AS 389
PLN02774 PLN02774
brassinosteroid-6-oxidase
42-461 1.01e-73

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 240.06  E-value: 1.01e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   42 RHYLPPGDLGWPFIGNMLSFLRafktSDPDsFTRTLIKRYGpkGIYKAHMFGNPSIIVTTSDTCRRVLTDDDA-FKPGWP 120
Cdd:PLN02774  29 KKGLPPGTMGWPLFGETTEFLK----QGPD-FMKNQRLRYG--SFFKSHILGCPTIVSMDPELNRYILMNEGKgLVPGYP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  121 TSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWT---------KMGEFEFLTHLRKLT 191
Cdd:PLN02774 102 QSMLDILGTCNIAAVHGSTHRYMRGSLLSLISPTMIRDHLLPKIDEFMRSHLSGWDglktidiqeKTKEMALLSALKQIA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  192 friimyiflSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNilsnkKDML 271
Cdd:PLN02774 182 ---------GTLSKPISEEFKTEFFKLVLGTLSLPIDLPGTNYRSGVQARKNIVRMLRQLIQERRASGETH-----TDML 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  272 DNLLNVKDEDGKtLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMIL-KSRPEgqKGLSLKETR 350
Cdd:PLN02774 248 GYLMRKEGNRYK-LTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEHLAIReRKRPE--DPIDWNDYK 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  351 KMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPKAGAFL 430
Cdd:PLN02774 325 SMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHNYFF 404
                        410       420       430
                 ....*....|....*....|....*....|.
gi 15220438  431 PFGAGSHLCPGNDLAKLEISIFLHHFLLKYQ 461
Cdd:PLN02774 405 LFGGGTRLCPGKELGIVEISTFLHYFVTRYR 435
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
69-457 8.04e-73

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: 235.94  E-value: 8.04e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  69 DPDSFTRTLiKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAF--KPGWPTSTMEL-IGRKSFVGISFEEHKRLRR 145
Cdd:COG2124  20 DPYPFYARL-REYGP--VFRVRLPGGGAWLVTRYEDVREVLRDPRTFssDGGLPEVLRPLpLLGDSLLTLDGPEHTRLRR 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 146 LTAAPVNgHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALnygvrAM 225
Cdd:COG2124  97 LVQPAFT-PRRVAALRPRIREIADELLDRLAARGPVDLVEEFARPLPVIVICELLGVPEEDRDRLRRWSDALL-----DA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 226 AVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQnilsnkkDMLDNLLNVKDeDGKTLDDEEIIDVLLMYLNAGHESS 305
Cdd:COG2124 171 LGPLPPERRRRARRARAELDAYLRELIAERRAEPGD-------DLLSALLAARD-DGERLSDEELRDELLLLLLAGHETT 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 306 GHTIMWATVFLQEHPEVLQRAKAEQEmilksrpegqkglslketrkmeFLSQVVDETLRVITFSLTAFREAKTDVEMNGY 385
Cdd:COG2124 243 ANALAWALYALLRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVPLLPRTATEDVELGGV 300
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220438 386 LIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:COG2124 301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAHLPFGGGPHRCLGAALARLEARIALATLL 365
PLN02500 PLN02500
cytochrome P450 90B1
42-460 2.70e-68

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 226.67  E-value: 2.70e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   42 RHYLPPGDLGWPFIGNMLSFLRAFKTSDPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDA-FKPGWP 120
Cdd:PLN02500  36 RFNLPPGNMGWPFLGETIGYLKPYSATSIGEFMEQHISRYGK--IYRSNLFGEPTIVSADAGLNRFILQNEGRlFECSYP 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  121 TSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFL 200
Cdd:PLN02500 114 RSIGGILGKWSMLVLVGDMHRDMRSISLNFLSHARLRTHLLKEVERHTLLVLDSWKENSTFSAQDEAKKFTFNLMAKHIM 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  201 SSE-SENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQ-RKQNILSNKKDMLDNLLNVK 278
Cdd:PLN02500 194 SMDpGEEETEQLKKEYVTFMKGVVSAPLNFPGTAYRKALKSRATILKFIERKMEERIEKlKEEDESVEEDDLLGWVLKHS 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  279 DedgktLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPE-GQKGLSLKETRKMEFLSQ 357
Cdd:PLN02500 274 N-----LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQsGESELNWEDYKKMEFTQC 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  358 VVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDN---------GFVPKAGA 428
Cdd:PLN02500 349 VINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQnnnrggssgSSSATTNN 428
                        410       420       430
                 ....*....|....*....|....*....|..
gi 15220438  429 FLPFGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:PLN02500 429 FMPFGGGPRLCAGSELAKLEMAVFIHHLVLNF 460
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
72-468 6.96e-63

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: 210.13  E-value: 6.96e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  72 SFTRTLIKRYGPkgIYKAHMFGNPSIIVTTS-DTCRRVLT-DDDAFKPGWPTSTME-LIGRKSFVGISFEEHKRLRRLTA 148
Cdd:cd11053   2 GFLERLRARYGD--VFTLRVPGLGPVVVLSDpEAIKQIFTaDPDVLHPGEGNSLLEpLLGPNSLLLLDGDRHRRRRKLLM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 149 APVNGhEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIM-YIFLSSESEN-------VMDALEREYTALNY 220
Cdd:cd11053  80 PAFHG-ERLRAYGELIAEITEREIDRWPPGQPFDLRELMQEITLEVILrVVFGVDDGERlqelrrlLPRLLDLLSSPLAS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 221 GVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRnqrkQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNA 300
Cdd:cd11053 159 FPALQRDLGPWSPWGRFLRARRRIDALIYAEIAERR----AEPDAERDDILSLLLSARDEDGQPLSDEELRDELMTLLFA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 301 GHESSGHTIMWATVFLQEHPEVLQRAKAEQEmilksrpEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDV 380
Cdd:cd11053 235 GHETTATALAWAFYWLHRHPEVLARLLAELD-------ALGGDPDPEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPV 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 381 EMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDnGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:cd11053 308 ELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFL-GRKPSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRF 386

                ....*...
gi 15220438 461 QVKRSNPE 468
Cdd:cd11053 387 RLELTDPR 394
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
73-478 7.20e-62

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: 207.56  E-value: 7.20e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  73 FTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDD---AFKPGWPTstmeLIG---RKSFVGISFEEHKRLRRL 146
Cdd:cd11045   2 FARQRYRRYGP--VSWTGMLGLRVVALLGPDANQLVLRNRDkafSSKQGWDP----VIGpffHRGLMLLDFDEHRAHRRI 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 147 TAAPVnGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALnygVRA-M 225
Cdd:cd11045  76 MQQAF-TRSALAGYLDRMTPGIERALARWPTGAGFQFYPAIKELTLDLATRVFLGVDLGPEADKVNKAFIDT---VRAsT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 226 AV---NIPGFAYHRALKARKTLVAAFQSIVTERRNqrkqnilSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGH 302
Cdd:cd11045 152 AIirtPIPGTRWWRGLRGRRYLEEYFRRRIPERRA-------GGGDDLFSALCRAEDEDGDRFSDDDIVNHMIFLMMAAH 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 303 ESSGHTIMWATVFLQEHPEVLQRAKAEQEMIlksrpeGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEM 382
Cdd:cd11045 225 DTTTSTLTSMAYFLARHPEWQERLREESLAL------GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 383 NGYLIPKGWKV--LTWFrdVHIDPEVFPDPRKFDPARwdngFVPK-------AGAFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd11045 299 LGYRIPAGTLVavSPGV--THYMPEYWPNPERFDPER----FSPEraedkvhRYAWAPFGGGAHKCIGLHFAGMEVKAIL 372
                       410       420
                ....*....|....*....|....*
gi 15220438 454 HHFLLKYQVkRSNPEcpvMYLPHTR 478
Cdd:cd11045 373 HQMLRRFRW-WSVPG---YYPPWWQ 393
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
46-472 4.57e-60

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: 204.05  E-value: 4.57e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438    46 PPGDLGWPFIGNMLSFLRAFKtsdPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVL-TDDDAFKPGWPTSTM 124
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGN---LHSVFTKLQKKYGP--IFRLYLGPKPVVVLSGPEAVKEVLiKKGEEFSGRPDEPWF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   125 ELIGRKSFV-GISF---EEHKRLRRLTAAPVNGHEALStYIPYIEENVITVLDKWTKM----GEFEFLTHLRKLTFRIIM 196
Cdd:pfam00067  76 ATSRGPFLGkGIVFangPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTagepGVIDITDLLFRAALNVIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   197 YIFLSSESENVMDALEREYTALNYGVRAMAVN--------------IPGFAYHRALKARKTLVAAFQSIVTERRNQRKQN 262
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSpspqlldlfpilkyFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   263 iLSNKKDMLDNLLNVKD-EDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrpEGQ 341
Cdd:pfam00067 235 -KKSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVI----GDK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   342 KGLSLKETRKMEFLSQVVDETLRVITFSLTA-FREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-- 418
Cdd:pfam00067 310 RSPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFld 389
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15220438   419 DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVM 472
Cdd:pfam00067 390 ENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
79-490 1.05e-54

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: 188.58  E-value: 1.05e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  79 KRYGPkgIYKAHMFGNPSIIVTTSDTCRRVL--TDDD-AFKPGWP-TSTMelIGRKSFVGISFEEHKRLRR--LTAAPVn 152
Cdd:cd11042   3 KKYGD--VFTFNLLGKKVTVLLGPEANEFFFngKDEDlSAEEVYGfLTPP--FGGGVVYYAPFAEQKEQLKfgLNILRR- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 153 ghEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSEsenVMDALERE----YTALNYGVRAMAVN 228
Cdd:cd11042  78 --GKLRGYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKE---VRELLDDEfaqlYHDLDGGFTPIAFF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGF---AYHRALKARKTLVAAFQSIVTERRnqrkQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESS 305
Cdd:cd11042 153 FPPLplpSFRRRDRARAKLKEIFSEIIQKRR----KSPDKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTS 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 306 GHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEgqkGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMN-- 383
Cdd:cd11042 229 SATSAWTGLELLRNPEHLEALREEQKEVLGDGDD---PLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEgg 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 384 GYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAG--AFLPFGAGSHLCPGNDLAKLEISIFLHHFLLK 459
Cdd:cd11042 306 GYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFlkGRAEDSKGGkfAYLPFGAGRHRCIGENFAYLQIKTILSTLLRN 385
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 15220438 460 YQVKRSNPECP-------VMYLPHTrptdnclARISYQ 490
Cdd:cd11042 386 FDFELVDSPFPepdyttmVVWPKGP-------ARVRYK 416
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
73-453 1.79e-48

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: 172.69  E-value: 1.79e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  73 FTRTLIKRYGpkGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAF-KPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPV 151
Cdd:cd20638  13 FLQMKRQKYG--YIYKTHLFGRPTVRVMGAENVRQILLGEHKLvSVQWPASVRTILGSGCLSNLHDSQHKHRKKVIMRAF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 152 NgHEALSTYIPYIEENVITVLDKWTKMGEFEFL-THLRKLTFRIIMYIFLSSESENVMDALERE----YTALNYGVRAMA 226
Cdd:cd20638  91 S-REALENYVPVIQEEVRSSVNQWLQSGPCVLVyPEVKRLMFRIAMRILLGFEPQQTDREQEQQlveaFEEMIRNLFSLP 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 227 VNIPGFAYHRALKARKTLVAAFQSIVteRRNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSG 306
Cdd:cd20638 170 IDVPFSGLYRGLRARNLIHAKIEENI--RAKIQREDTEQQCKDALQLLIEHSRRNGEPLNLQALKESATELLFGGHETTA 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 307 HTIMWATVFLQEHPEVLQRAKAEQEM--ILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNG 384
Cdd:cd20638 248 SAATSLIMFLGLHPEVLQKVRKELQEkgLLSTKPNENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNG 327
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220438 385 YLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPKAG--AFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd20638 328 YQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSrfSFIPFGGGSRSCVGKEFAKVLLKIFT 398
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
138-448 1.36e-47

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: 169.30  E-value: 1.36e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 138 EEHKRLRRLtAAPVNGHEALSTYIPYIEENVITVLDKWTKM---GEFEFLTHLRKLTFRIIMYIFLSSESENVMDALERe 214
Cdd:cd20620  56 DLWRRQRRL-AQPAFHRRRIAAYADAMVEATAALLDRWEAGarrGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGD- 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 215 ytALNYGVRAMAV----------NIPGFAYHRALKARKTLVAAFQSIVTERRNQRKqnilsNKKDMLDNLLNVKD-EDGK 283
Cdd:cd20620 134 --ALDVALEYAARrmlspfllplWLPTPANRRFRRARRRLDEVIYRLIAERRAAPA-----DGGDLLSMLLAARDeETGE 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 284 TLDDEEIID-VLLMYLnAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPegqkgLSLKETRKMEFLSQVVDET 362
Cdd:cd20620 207 PMSDQQLRDeVMTLFL-AGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRP-----PTAEDLPQLPYTEMVLQES 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 363 LR----VITFSltafREAKTDVEMNGYLIPKGWKVLT--WFrdVHIDPEVFPDPRKFDPARWDNGFV---PKaGAFLPFG 433
Cdd:cd20620 281 LRlyppAWIIG----REAVEDDEIGGYRIPAGSTVLIspYV--THRDPRFWPDPEAFDPERFTPEREaarPR-YAYFPFG 353
                       330
                ....*....|....*
gi 15220438 434 AGSHLCPGNDLAKLE 448
Cdd:cd20620 354 GGPRICIGNHFAMME 368
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
95-453 8.16e-47

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: 167.44  E-value: 8.16e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  95 PSIIVTTSDTCRRVLTDD-DAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLtAAPVNGHEALSTYIPYIEENVITVLD 173
Cdd:cd11049  24 PAYVVTSPELVRQVLVNDrVFDKGGPLFDRARPLLGNGLATCPGEDHRRQRRL-MQPAFHRSRIPAYAEVMREEAEALAG 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 174 KWTKMGEFEFLTHLRKLTFRIIMYIFLSSE-SENVMDALEREYTALNYGVRAMAVnIPGFA----------YHRALKARK 242
Cdd:cd11049 103 SWRPGRVVDVDAEMHRLTLRVVARTLFSTDlGPEAAAELRQALPVVLAGMLRRAV-PPKFLerlptpgnrrFDRALARLR 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 243 TLVAafQSIVTERRNQRKQNilsnkkDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEV 322
Cdd:cd11049 182 ELVD--EIIAEYRASGTDRD------DLLSLLLAARDEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEV 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 323 LQRAKAEQEMILKSRPEGQKGLslketRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHI 402
Cdd:cd11049 254 ERRLHAELDAVLGGRPATFEDL-----PRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHR 328
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15220438 403 DPEVFPDPRKFDPARWDNG---FVPKaGAFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd11049 329 DPEVYPDPERFDPDRWLPGraaAVPR-GAFIPFGAGARKCIGDTFALTELTLAL 381
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
85-467 1.61e-46

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: 167.00  E-value: 1.61e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  85 GIYKAHMfGN-PSIIVTTSDTCRRVLTDD-DAFKPGWPTSTMELI-GRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYI 161
Cdd:cd20617   2 GIFTLWL-GDvPTVVLSDPEIIKEAFVKNgDNFSDRPLLPSFEIIsGGKGILFSNGDYWKELRRFALSSLTKTKLKKKME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 162 PYIEENV---ITVLDKWTKMGE-FEFLTHLRKLTFRII-MYIF-------LSSESENVMDALEREYTALNYGVRAMAVNI 229
Cdd:cd20617  81 ELIEEEVnklIESLKKHSKSGEpFDPRPYFKKFVLNIInQFLFgkrfpdeDDGEFLKLVKPIEEIFKELGSGNPSDFIPI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 230 PGFAYHRALKARKTLVAAFQSIVTERRNQRKQNILSNK-KDMLDNLLN--VKDEDGKTLDDEEIIDVLLMYLNAGHESSG 306
Cdd:cd20617 161 LLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNpRDLIDDELLllLKEGDSGLFDDDSIISTCLDLFLAGTDTTS 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 307 HTIMWATVFLQEHPEVlQRaKAEQEmiLKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFS-LTAFREAKTDVEMNGY 385
Cdd:cd20617 241 TTLEWFLLYLANNPEI-QE-KIYEE--IDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILpLGLPRVTTEDTEIGGY 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 386 LIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKR 464
Cdd:cd20617 317 FIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFKS 396

                ...
gi 15220438 465 SNP 467
Cdd:cd20617 397 SDG 399
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
72-481 1.41e-45

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: 164.62  E-value: 1.41e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  72 SFTRTLIKRYGpkGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAF-KPGWPTSTMELIGRKSFVGISFEEHKRlRRLTAAP 150
Cdd:cd20636  13 SFHSSRREKYG--NVFKTHLLGRPVIRVTGAENIRKILLGEHTLvSTQWPQSTRILLGSNTLLNSVGELHRQ-RRKVLAR 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 151 VNGHEALSTYIPYIEENVITVLDKW-TKMGEFEFLTHLRKLTFRIIMYIFLS-SESENVMDALEREYTALNYGVRAMAVN 228
Cdd:cd20636  90 VFSRAALESYLPRIQDVVRSEVRGWcRGPGPVAVYTAAKSLTFRIAVRILLGlRLEEQQFTYLAKTFEQLVENLFSLPLD 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGFAYHRALKARKTLVAAFQSIVTERRnqrKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHT 308
Cdd:cd20636 170 VPFSGLRKGIKARDILHEYMEKAIEEKL---QRQQAAEYCDALDYMIHSARENGKELTMQELKESAVELIFAAFSTTASA 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 309 IMWATVFLQEHPEVLQRAKAE--QEMILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYL 386
Cdd:cd20636 247 STSLVLLLLQHPSAIEKIRQElvSHGLIDQCQCCPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQ 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 387 IPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVP-KAGAF--LPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:cd20636 327 IPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREEsKSGRFnyIPFGGGVRSCIGKELAQVILKTLAVELVTTARWE 406
                       410
                ....*....|....*....
gi 15220438 464 RSNPECPVMY-LPHTRPTD 481
Cdd:cd20636 407 LATPTFPKMQtVPIVHPVD 425
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
92-483 7.39e-45

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: 162.42  E-value: 7.39e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  92 FGNPSIIVTTSDTCRRVLT--DDDAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAaPVNGHEALSTYIPYIEENVI 169
Cdd:cd11082   8 VGKFIVFVTDAELSRKIFSnnRPDAFHLCLHPNAKKILGEDNLIFMFGEEHKELRKSLL-PLFTRKALGLYLPIQERVIR 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 170 TVLDKW-----TKMGEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTL 244
Cdd:cd11082  87 KHLAKWlenskSGDKPIEMRPLIRDLNLETSQTVFVGPYLDDEARRFRIDYNYFNVGFLALPVDFPGTALWKAIQARKRI 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 245 VAAFQSIVTERRNqRKQNilSNK---------KDMLDNLLNVKDEDGKTL---DDEEIIDVLLMYLNAGHESSGHTIMWA 312
Cdd:cd11082 167 VKTLEKCAAKSKK-RMAA--GEEptclldfwtHEILEEIKEAEEEGEPPPphsSDEEIAGTLLDFLFASQDASTSSLVWA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 313 TVFLQEHPEVLQRAKAEQemiLKSRPEGQKGLSLKETRKMEFLSQVVDETLRvitfsltaFR--------EAKTDVEMN- 383
Cdd:cd11082 244 LQLLADHPDVLAKVREEQ---ARLRPNDEPPLTLDLLEEMKYTRQVVKEVLR--------YRppapmvphIAKKDFPLTe 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 384 GYLIPKGWKVLTWFRDVHIDPevFPDPRKFDPARWDNG-----FVPKagAFLPFGAGSHLCPGNDLAKLEISIFLHHFLL 458
Cdd:cd11082 313 DYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPErqedrKYKK--NFLVFGAGPHQCVGQEYAINHLMLFLALFST 388
                       410       420
                ....*....|....*....|....*..
gi 15220438 459 KYQVKR-SNPEC-PVMYLPHTRPTDNC 483
Cdd:cd11082 389 LVDWKRhRTPGSdEIIYFPTIYPKDGC 415
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
86-481 6.83e-44

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: 160.13  E-value: 6.83e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  86 IYKAHMFGNPSIIVTTSDTCRRVL-TDDDAFKPGWPT-STMELIGRKSFVGISFEEHKRLRRLTAaPVNGHEALSTYIPY 163
Cdd:cd11069   5 IRYRGLFGSERLLVTDPKALKHILvTNSYDFEKPPAFrRLLRRILGDGLLAAEGEEHKRQRKILN-PAFSYRHVKELYPI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 164 IEENVITVLDKWTKM--------GEFEFLTHLRKLTFRII-----MYIF--LSSESENVMDALER----------EYTAL 218
Cdd:cd11069  84 FWSKAEELVDKLEEEieesgdesISIDVLEWLSRATLDIIglagfGYDFdsLENPDNELAEAYRRlfeptllgslLFILL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 219 NYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKT-LDDEEIIDVLLMY 297
Cdd:cd11069 164 LFLPRWLVRILPWKANREIRRAKDVLRRLAREIIREKKAALLEGKDDSGKDILSILLRANDFADDErLSDEELIDQILTF 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 298 LNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEGQkgLSLKETRKMEFLSQVVDETLRVITFSLTAFREAK 377
Cdd:cd11069 244 LAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGD--LSYDDLDRLPYLNAVCRETLRLYPPVPLTSREAT 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 378 TDVEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDN-------GFVPKAGAFLPFGAGSHLCPGNDLAKLEI 449
Cdd:cd11069 322 KDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEpdgaaspGGAGSNYALLTFLHGPRSCIGKKFALAEM 401
                       410       420       430
                ....*....|....*....|....*....|....
gi 15220438 450 SIFLHHFLLKYQVKR-SNPECPV-MYLPHTRPTD 481
Cdd:cd11069 402 KVLLAALVSRFEFELdPDAEVERpIGIITRPPVD 435
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
79-447 1.77e-38

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: 145.38  E-value: 1.77e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  79 KRYGpkGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAF-KPGWPTSTMELIGRKSFVGiSFEEHKRLRRLTAAPVNGHEAL 157
Cdd:cd20637  19 EKYG--NVFKTHLLGRPLIRVTGAENVRKILMGEHSLvSTEWPRSTRMLLGPNSLVN-SIGDIHRHKRKVFSKLFSHEAL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 158 STYIPYIEENVITVLDKWTKMGE-FEFLTHLRKLTFRIIMYIFLS-SESENVMDALEREYTALNYGVRAMAVNIPGFAYH 235
Cdd:cd20637  96 ESYLPKIQQVIQDTLRVWSSNPEpINVYQEAQKLTFRMAIRVLLGfRVSEEELSHLFSVFQQFVENVFSLPLDLPFSGYR 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 236 RALKARKTLVAAFQSIVTER--RNQRKqnilsNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWAT 313
Cdd:cd20637 176 RGIRARDSLQKSLEKAIREKlqGTQGK-----DYADALDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLI 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 314 VFLQEHPEVLQRAKAE--QEMILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGW 391
Cdd:cd20637 251 MQLLKHPGVLEKLREElrSNGILHNGCLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGW 330
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15220438 392 KVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVP-KAGAF--LPFGAGSHLCPGNDLAKL 447
Cdd:cd20637 331 SVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEdKDGRFhyLPFGGGVRTCLGKQLAKL 389
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
84-468 3.72e-38

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: 144.20  E-value: 3.72e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  84 KGIYKAHMFGNPSIIVTTSDTCRRVLT---------DDDAFKP----GWPTSTmeliGRKSfvgisfeeHKRLRRLTaaP 150
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEDIEVILSssklitksfLYDFLKPwlgdGLLTST----GEKW--------RKRRKLLT--P 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 151 VNGHEALSTYIPYIEENVITVLDKWTK---MGEFEFLTHLRKLTFRII----MYI---FLSSESENVMDALEReytaLNY 220
Cdd:cd20628  67 AFHFKILESFVEVFNENSKILVEKLKKkagGGEFDIFPYISLCTLDIIcetaMGVklnAQSNEDSEYVKAVKR----ILE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 221 GVRAMAVNI---PGFAYHRA------LKARKTLVAAFQSIVTERRNQRKQNILSN----------KKDMLDNLLNVKdED 281
Cdd:cd20628 143 IILKRIFSPwlrFDFIFRLTslgkeqRKALKVLHDFTNKVIKERREELKAEKRNSeeddefgkkkRKAFLDLLLEAH-ED 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 282 GKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEGqkgLSLKETRKMEFLSQVVDE 361
Cdd:cd20628 222 GGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRR---PTLEDLNKMKYLERVIKE 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 362 TLRVITfSLTAF-REAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPK--AGAFLPFGAGSHL 438
Cdd:cd20628 299 TLRLYP-SVPFIgRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKrhPYAYIPFSAGPRN 377
                       410       420       430
                ....*....|....*....|....*....|
gi 15220438 439 CPGNDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd20628 378 CIGQKFAMLEMKTLLAKILRNFRVLPVPPG 407
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
138-480 1.45e-36

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: 139.50  E-value: 1.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 138 EEHKRLRR----------LTAAPVNGhealstyipYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESEnv 207
Cdd:cd20614  64 ALHRRARAasnpsftpkgLSAAGVGA---------LIAEVIEARIRAWLSRGDVAVLPETRDLTLEVIFRILGVPTDD-- 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 208 MDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTE-RRNqrkqnilSNKKDMLDNLLNVKDEDGKTLD 286
Cdd:cd20614 133 LPEWRRQYRELFLGVLPPPVDLPGMPARRSRRARAWIDARLSQLVATaRAN-------GARTGLVAALIRARDDNGAGLS 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 287 DEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEqemilkSRPEGQKGLSLKETRKMEFLSQVVDETLRVI 366
Cdd:cd20614 206 EQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDE------AAAAGDVPRTPAELRRFPLAEALFRETLRLH 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 367 TFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-DNGFVPKAGAFLPFGAGSHLCPGNDLA 445
Cdd:cd20614 280 PPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWlGRDRAPNPVELLQFGGGPHFCLGYHVA 359
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 15220438 446 KLEISIFLhhFLLKYQVKRSNP-------ECPVMYLPHTRPT 480
Cdd:cd20614 360 CVELVQFI--VALARELGAAGIrpllvgvLPGRRYFPTLHPS 399
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
248-466 2.60e-36

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: 138.87  E-value: 2.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 248 FQSIVTERRNQRKQNILSNKKDMLDNLLN----VKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVL 323
Cdd:cd11055 181 LEDVVKKIIEQRRKNKSSRRKDLLQLMLDaqdsDEDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQ 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 324 QRAkaeQEMILKSRPEGQKgLSLKETRKMEFLSQVVDETLRV--ITFSLTafREAKTDVEMNGYLIPKGWKVLTWFRDVH 401
Cdd:cd11055 261 EKL---IEEIDEVLPDDGS-PTYDTVSKLKYLDMVINETLRLypPAFFIS--RECKEDCTINGVFIPKGVDVVIPVYAIH 334
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220438 402 IDPEVFPDPRKFDPARwdngFVPKA------GAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSN 466
Cdd:cd11055 335 HDPEFWPDPEKFDPER----FSPENkakrhpYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCK 401
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
71-456 6.28e-36

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: 138.09  E-value: 6.28e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  71 DSFTRtLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLtDDDAF--KPGWPTSTM-ELIGRKSFVGISFEE--HKRLRR 145
Cdd:cd11068   3 QSLLR-LADELGP--IFKLTLPGRRVVVVSSHDLIAELC-DESRFdkKVSGPLEELrDFAGDGLFTAYTHEPnwGKAHRI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 146 LtaAPVNGHEALSTYIPYIEENVITVLDKWTKMG---EFEFLTHLRKLTFRIIM-----YIFLSSESENV---MDALERe 214
Cdd:cd11068  79 L--MPAFGPLAMRGYFPMMLDIAEQLVLKWERLGpdePIDVPDDMTRLTLDTIAlcgfgYRFNSFYRDEPhpfVEAMVR- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 215 ytALNY-GVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKD-EDGKTLDDEEIID 292
Cdd:cd11068 156 --ALTEaGRRANRPPILNKLRRRAKRQFREDIALMRDLVDEIIAERRANPDGSPDDLLNLMLNGKDpETGEKLSDENIRY 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 293 VLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPegqkgLSLKETRKMEFLSQVVDETLRvitFSLTA 372
Cdd:cd11068 234 QMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDP-----PPYEQVAKLRYIRRVLDETLR---LWPTA 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 373 ---FREAKTDVEMNG-YLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNGFVPK--AGAFLPFGAGSHLCPGNDLA 445
Cdd:cd11068 306 pafARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKlpPNAWKPFGNGQRACIGRQFA 385
                       410
                ....*....|....*
gi 15220438 446 ----KLEISIFLHHF 456
Cdd:cd11068 386 lqeaTLVLAMLLQRF 400
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
98-457 6.60e-34

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: 131.13  E-value: 6.60e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  98 IVTTSDTCRRVLTDDDAFK---------PGWPTSTMELIG--RKSFVGISFEEHKRLRRLtAAPVNGHEALSTYIPYIEE 166
Cdd:cd20625  12 VVTRHADVSAVLRDPRFGSddpeaaprrRGGEAALRPLARllSRSMLFLDPPDHTRLRRL-VSKAFTPRAVERLRPRIER 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 167 NVITVLDKWTKMGEFEFLTHL-RKLTFRIIMYIF---------LSSESENVMDALEreytalnygvramaVNIPGFAYHR 236
Cdd:cd20625  91 LVDELLDRLAARGRVDLVADFaYPLPVRVICELLgvpeedrprFRGWSAALARALD--------------PGPLLEELAR 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 237 ALKARKTLVAAFQSIVTERRNQRKQnilsnkkDMLDNLLNVKDEDGKtLDDEEIIDVLLMYLNAGHESSGHTIMWATVFL 316
Cdd:cd20625 157 ANAAAAELAAYFRDLIARRRADPGD-------DLISALVAAEEDGDR-LSEDELVANCILLLVAGHETTVNLIGNGLLAL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 317 QEHPEVLQRakaeqemiLKSRPegqkglslketrkmEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTW 396
Cdd:cd20625 229 LRHPEQLAL--------LRADP--------------ELIPAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLL 286
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220438 397 F----RdvhiDPEVFPDPRKFDPARWDNGfvpkagaFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:cd20625 287 LgaanR----DPAVFPDPDRFDITRAPNR-------HLAFGAGIHFCLGAPLARLEAEIALRALL 340
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
81-475 7.14e-34

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: 132.33  E-value: 7.14e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  81 YGPkgIYKAHMFGNPSIIVTTSDTCRRVLT---DDDAFKPgwPTSTMELI--GRKSFVGISFEEHKRLRRLTAapvngHE 155
Cdd:cd11027   1 YGD--VFSLYLGSRLVVVLNSGAAIKEALVkksADFAGRP--KLFTFDLFsrGGKDIAFGDYSPTWKLHRKLA-----HS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 156 ALSTYI---PYIEENVITVLDKWTKMGE------FEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVR--- 223
Cdd:cd11027  72 ALRLYAsggPRLEEKIAEEAEKLLKRLAsqegqpFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFEllg 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 224 -AMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNILS----NKKDMLDNLLNVK-------DEDGKTLDDEEII 291
Cdd:cd11027 152 aGSLLDIFPFLKYFPNKALRELKELMKERDEILRKKLEEHKETfdpgNIRDLTDALIKAKkeaedegDEDSGLLTDDHLV 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 292 DVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAE-QEMILKSRPegqkgLSLKETRKMEFLSQVVDETLRVITFSL 370
Cdd:cd11027 232 MTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAElDDVIGRDRL-----PTLSDRKRLPYLEATIAEVLRLSSVVP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 371 TAF-REAKTDVEMNGYLIPKGWKVLT--WfrDVHIDPEVFPDPRKFDPARW--DNG-FVPKAGAFLPFGAGSHLCPGNDL 444
Cdd:cd11027 307 LALpHKTTCDTTLRGYTIPKGTTVLVnlW--ALHHDPKEWDDPDEFRPERFldENGkLVPKPESFLPFSAGRRVCLGESL 384
                       410       420       430
                ....*....|....*....|....*....|.
gi 15220438 445 AKLEISIFLHHFLLKYQVkrsnpECPVMYLP 475
Cdd:cd11027 385 AKAELFLFLARLLQKFRF-----SPPEGEPP 410
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
86-468 1.13e-33

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: 131.61  E-value: 1.13e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  86 IYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKpgwptSTMELIGRKSFV--GISF---EEHKRLRRLtaapVNGH---EAL 157
Cdd:cd20621   5 IIVSNLGSKPLISLVDPEYIKEFLQNHHYYK-----KKFGPLGIDRLFgkGLLFsegEEWKKQRKL----LSNSfhfEKL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 158 STYIPYIEENVITVLDKwTKMGEFEFLTHLRKLTFRIIMYIFLSSESENV---------------MDALEREYTALNYGV 222
Cdd:cd20621  76 KSRLPMINEITKEKIKK-LDNQNVNIIQFLQKITGEVVIRSFFGEEAKDLkingkeiqvelveilIESFLYRFSSPYFQL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 223 RAM-----AVNIPGFAYHRALKAR-KTLVAAFQSIVTERRNQRKQNILSNK--KDMLDNLLNVKDEDGKTLDDEEIIDVL 294
Cdd:cd20621 155 KRLifgrkSWKLFPTKKEKKLQKRvKELRQFIEKIIQNRIKQIKKNKDEIKdiIIDLDLYLLQKKKLEQEITKEEIIQQF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 295 LMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEgqkgLSLKETRKMEFLSQVVDETLRVITFSLTAF- 373
Cdd:cd20621 235 ITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDD----ITFEDLQKLNYLNAFIKEVLRLYNPAPFLFp 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 374 REAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-------DNGFVpkagaFLPFGAGSHLCPGNDLAK 446
Cdd:cd20621 311 RVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWlnqnnieDNPFV-----FIPFSAGPRNCIGQHLAL 385
                       410       420
                ....*....|....*....|...
gi 15220438 447 LEISIFLHHFLLKYQVKRS-NPE 468
Cdd:cd20621 386 MEAKIILIYILKNFEIEIIpNPK 408
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
86-471 4.54e-33

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: 130.13  E-value: 4.54e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  86 IYKAHMFGNPSIIVTTSDTCRRVLTD-DDAFKPgwpTSTMELIGRK-SFVGIsF----EEHKRLRRLTAAPVN-GHeaLS 158
Cdd:cd11083   3 AYRFRLGRQPVLVISDPELIREVLRRrPDEFRR---ISSLESVFREmGINGV-FsaegDAWRRQRRLVMPAFSpKH--LR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 159 TYIPYIEENVITVLDKWTKMGE----FEFLTHLRKLTFRI-IMYIF------LSSESENVMDALEREYTALNYGVRAMav 227
Cdd:cd11083  77 YFFPTLRQITERLRERWERAAAegeaVDVHKDLMRYTVDVtTSLAFgydlntLERGGDPLQEHLERVFPMLNRRVNAP-- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 228 nIP-----GFAYHRAL-KARKTLVAAFQSIVTERRNQRKQNilSNKKDMLDNLLNV---KDEDGKTLDDEEIIDVLLMYL 298
Cdd:cd11083 155 -FPywrylRLPADRALdRALVEVRALVLDIIAAARARLAAN--PALAEAPETLLAMmlaEDDPDARLTDDEIYANVLTLL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 299 NAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEgqkGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKT 378
Cdd:cd11083 232 LAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARV---PPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNE 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 379 DVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW----DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLH 454
Cdd:cd11083 309 DTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWldgaRAAEPHDPSSLLPFGAGPRLCPGRSLALMEMKLVFA 388
                       410
                ....*....|....*..
gi 15220438 455 HFLLKYQVKRSNPECPV 471
Cdd:cd11083 389 MLCRNFDIELPEPAPAV 405
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
99-453 7.58e-33

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


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 128.41  E-value: 7.58e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  99 VTTSDTCRRVLTDDDAFK-------PGWPTSTMELIGRKSFVGISFEEHKRLRRLTA---APvnghEALSTYIPYIEENV 168
Cdd:cd11033  25 VTRHADVVAVSRDPELFSsarggvlIDLPEEDADPAAGRMLINMDPPRHTRLRRLVSrafTP----RAVARLEDRIRERA 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 169 ITVLDKWTKMGEFEFLTHL-RKLTFRIIMYIFlsseseNVMDALEREYTALnyGVRAMAVNIPGFAY---HRALKARKTL 244
Cdd:cd11033 101 RRLVDRALARGECDFVEDVaAELPLQVIADLL------GVPEEDRPKLLEW--TNELVGADDPDYAGeaeEELAAALAEL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 245 VAAFQSIVTERRNQRKQNILSNkkdmldnLLNVkDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQ 324
Cdd:cd11033 173 FAYFRELAEERRANPGDDLISV-------LANA-EVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWE 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 325 RAKAEQEMIlksrpegqkglslketrkmeflSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDP 404
Cdd:cd11033 245 RLRADPSLL----------------------PTAVEEILRWASPVIHFRRTATRDTELGGQRIRAGDKVVLWYASANRDE 302
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 15220438 405 EVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd11033 303 EVFDDPDRFDITR-------SPNPHLAFGGGPHFCLGAHLARLELRVLF 344
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
79-457 1.33e-32

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: 128.79  E-value: 1.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  79 KRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWPTSTMELIGRKSFVGIS------FEEHKRLRRLTAaPVN 152
Cdd:cd20613   9 KEYGP--VFVFWILHRPIVVVSDPEAVKEVLITLNLPKPPRVYSRLAFLFGERFLGNGlvtevdHEKWKKRRAILN-PAF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 153 GHEALSTYIPYIEENVITVLDKWTKMG----EFEFLTHLRKLTFRIIM--------YIFLSSESE------NVMDALERE 214
Cdd:cd20613  86 HRKYLKNLMDEFNESADLLVEKLSKKAdgktEVNMLDEFNRVTLDVIAkvafgmdlNSIEDPDSPfpkaisLVLEGIQES 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 215 YTALnygvrAMAVNIPGFAYHR-ALKARKTLVAAFQSIVTERRNQRKQNILSnKKDMLDNLLNVKDEDGKtLDDEEIIDV 293
Cdd:cd20613 166 FRNP-----LLKYNPSKRKYRReVREAIKFLRETGRECIEERLEALKRGEEV-PNDILTHILKASEEEPD-FDMEELLDD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 294 LLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEgqkgLSLKETRKMEFLSQVVDETLRV--ITFSLT 371
Cdd:cd20613 239 FVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQY----VEYEDLGKLEYLSQVLKETLRLypPVPGTS 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 372 afREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEI 449
Cdd:cd20613 315 --RELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFspEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEA 392

                ....*...
gi 15220438 450 SIFLHHFL 457
Cdd:cd20613 393 KVILAKLL 400
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
139-453 2.33e-32

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: 127.33  E-value: 2.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 139 EHKRLRRL-----TAAPVNGHEalstyiPYIEENVITVLDKWTKMGEFEFLThlrKLTFRIIMYI---FLSSESEnVMDA 210
Cdd:cd11078  71 RHTRLRRLvsrafTPRRIAALE------PRIRELAAELLDRLAEDGRADFVA---DFAAPLPALViaeLLGVPEE-DMER 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 211 LEReytalnYGVRAMAVNIPGFAYHRALKARKTlVAAFQSIVTERRNQRKQNIlsnKKDMLDNLLNVKDEDGKTLDDEEI 290
Cdd:cd11078 141 FRR------WADAFALVTWGRPSEEEQVEAAAA-VGELWAYFADLVAERRREP---RDDLISDLLAAADGDGERLTDEEL 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 291 IDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMIlksrpegqkglslketrkmeflSQVVDETLRVITFSL 370
Cdd:cd11078 211 VAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSLI----------------------PNAVEETLRYDSPVQ 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 371 TAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngfvPKAGAFLPFGAGSHLCPGNDLAKLEIS 450
Cdd:cd11078 269 GLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR------PNARKHLTFGHGIHFCLGAALARMEAR 342

                ...
gi 15220438 451 IFL 453
Cdd:cd11078 343 IAL 345
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
248-465 9.86e-31

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: 123.42  E-value: 9.86e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 248 FQSIVTERRNQRKQNiLSNKKDMLDNLLNVK-------DEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHP 320
Cdd:cd11056 182 FRKLVRDTIEYREKN-NIVRNDFIDLLLELKkkgkiedDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNP 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 321 EVLQRAKAEqemILKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNG--YLIPKGWKVLTWFR 398
Cdd:cd11056 261 EIQEKLREE---IDEVLEKHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPVIIPVY 337
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220438 399 DVHIDPEVFPDPRKFDPARWDNGFVPK--AGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRS 465
Cdd:cd11056 338 ALHHDPKYYPEPEKFDPERFSPENKKKrhPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPS 406
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
105-475 1.04e-30

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: 122.32  E-value: 1.04e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 105 CRRVLTDDDAF---KPGWPTSTMELIGRKSFVGISFEEHKRLRRLTA---APvnghEALSTYIPYIEENVITVLDKWTKM 178
Cdd:cd11032  23 VKRVLSDPATFssdLGRLLPGEDDALTEGSLLTMDPPRHRKLRKLVSqafTP----RLIADLEPRIAEITDELLDAVDGR 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 179 GEFEFLTHL-------------------RKLtFRIIMYIFLSSESEnvmDALEREYtalnygVRAMAvnipgfayhralK 239
Cdd:cd11032  99 GEFDLVEDLayplpviviaellgvpaedREL-FKKWSDALVSGLGD---DSFEEEE------VEEMA------------E 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 240 ARKTLVAAFQSIVTERRNQRKQNILSNkkdmldnLLNVkDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEH 319
Cdd:cd11032 157 ALRELNAYLLEHLEERRRNPRDDLISR-------LVEA-EVDGERLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDED 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 320 PEVLQRAKAEQEMIlksrpegqkglslketrkmeflSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRD 399
Cdd:cd11032 229 PEVAARLRADPSLI----------------------PGAIEEVLRYRPPVQRTARVTTEDVELGGVTIPAGQLVIAWLAS 286
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220438 400 VHIDPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMYLP 475
Cdd:cd11032 287 ANRDERQFEDPDTFDIDR-------NPNPHLSFGHGIHFCLGAPLARLEARIALEALLDRFPRIRVDPDVPLELID 355
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
95-456 2.46e-30

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: 122.28  E-value: 2.46e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  95 PSIIVTTSDTCRRVLTDDD---AFKPgwPTSTMELI--GRKSFVGISFEEH-KRLRRLTA------------APVNGHEA 156
Cdd:cd20618  12 PTVVVSSPEMAKEVLKTQDavfASRP--RTAAGKIFsyNGQDIVFAPYGPHwRHLRKICTlelfsakrlesfQGVRKEEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 157 LSTyipyieenVITVLDKWTKMGEFEFLTHLRKLTFRIIMYI-----FLSSESENVMDAleREYTALNYGVRAMAVN--- 228
Cdd:cd20618  90 SHL--------VKSLLEESESGKPVNLREHLSDLTLNNITRMlfgkrYFGESEKESEEA--REFKELIDEAFELAGAfni 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 ---IPGFA------YHRALKA-RKTLVAAFQSIVTERRnQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYL 298
Cdd:cd20618 160 gdyIPWLRwldlqgYEKRMKKlHAKLDRFLQKIIEEHR-EKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDML 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 299 NAGHESSGHTIMWATVFLQEHPEVLQRAKAE-QEMILKSRPegqkglsLKET--RKMEFLSQVVDETLR---VITFSLTa 372
Cdd:cd20618 239 AAGTDTSAVTIEWAMAELLRHPEVMRKAQEElDSVVGRERL-------VEESdlPKLPYLQAVVKETLRlhpPGPLLLP- 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 373 fREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPKAG----AFLPFGAGSHLCPGNDLA--- 445
Cdd:cd20618 311 -HESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKgqdfELLPFGSGRRMCPGMPLGlrm 389
                       410
                ....*....|..
gi 15220438 446 -KLEISIFLHHF 456
Cdd:cd20618 390 vQLTLANLLHGF 401
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
79-456 5.23e-30

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: 121.40  E-value: 5.23e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  79 KRYGPKGIYkahMFG-NPSIIVTTSDTCRRVLTDD-DAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLtAAPVNGHEA 156
Cdd:cd20639   9 KIYGKTFLY---WFGpTPRLTVADPELIREILLTRaDHFDRYEAHPLVRQLEGDGLVSLRGEKWAHHRRV-ITPAFHMEN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 157 LSTYIPYIEENVITVLDKWTKM----GEFEFLTH--LRKLTFRIIMYI-FLSS-ESENVMDALEREYTALNYGVRaMAVN 228
Cdd:cd20639  85 LKRLVPHVVKSVADMLDKWEAMaeagGEGEVDVAewFQNLTEDVISRTaFGSSyEDGKAVFRLQAQQMLLAAEAF-RKVY 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGFAYHRALKARKTL-------VAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVK-DEDGKTLDDEEIIDVLLMYLNA 300
Cdd:cd20639 164 IPGYRFLPTKKNRKSWrldkeirKSLLKLIERRQTAADDEKDDEDSKDLLGLMISAKnARNGEKMTVEEIIEECKTFFFA 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 301 GHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrpeGQKGLSLKET-RKMEFLSQVVDETLRVITFSLTAFREAKTD 379
Cdd:cd20639 244 GKETTSNLLTWTTVLLAMHPEWQERARREVLAVC-----GKGDVPTKDHlPKLKTLGMILNETLRLYPPAVATIRRAKKD 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 380 VEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNGfVPKA----GAFLPFGAGSHLCPGNDLAKLE----IS 450
Cdd:cd20639 319 VKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADG-VARAakhpLAFIPFGLGPRTCVGQNLAILEakltLA 397

                ....*.
gi 15220438 451 IFLHHF 456
Cdd:cd20639 398 VILQRF 403
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
108-454 6.38e-30

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: 119.71  E-value: 6.38e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 108 VLTDDDAF-KPGWPTSTMELIGRKSFVGISFEEHKRLRRLtAAPVNGHEALSTYIPYIEENVI-TVLDKWTKMGEFEFLT 185
Cdd:cd20629  23 VLRDPRTFsSETYDATLGGPFLGHSILAMDGEEHRRRRRL-LQPAFAPRAVARWEEPIVRPIAeELVDDLADLGRADLVE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 186 HL-RKLTFRIImYIFLSSESENVmdaleREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNIL 264
Cdd:cd20629 102 DFaLELPARVI-YALLGLPEEDL-----PEFTRLALAMLRGLSDPPDPDVPAAEAAAAELYDYVLPLIAERRRAPGDDLI 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 265 SnkkdmldnLLNVKDEDGKTLDDEEIIDVLLMYLNAGHEssghTIMWA----TVFLQEHPEVLQRAKAEQEMIlksrpeg 340
Cdd:cd20629 176 S--------RLLRAEVEGEKLDDEEIISFLRLLLPAGSD----TTYRAlanlLTLLLQHPEQLERVRRDRSLI------- 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 341 qkglslketrkmeflSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdn 420
Cdd:cd20629 237 ---------------PAAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR--- 298
                       330       340       350
                ....*....|....*....|....*....|....
gi 15220438 421 gfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLH 454
Cdd:cd20629 299 ----KPKPHLVFGGGAHRCLGEHLARVELREALN 328
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
92-453 5.31e-29

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: 118.13  E-value: 5.31e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  92 FGNPSIIVTTSDTCRRVLTDDDAFKPGWPTSTME-LIGRKSFVGISFEEHKRLRRLTAaPVNGHEALSTYIPYIEENV-- 168
Cdd:cd11051   8 FAPPLLVVTDPELAEQITQVTNLPKPPPLRKFLTpLTGGSSLISMEGEEWKRLRKRFN-PGFSPQHLMTLVPTILDEVei 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 169 -ITVLDKWTKMGE-FEFLTHLRKLTFRIIMYIFL-----SSESENVMDALEREYTALNYGVRAMavnIPGFAYHRALKar 241
Cdd:cd11051  87 fAAILRELAESGEvFSLEELTTNLTFDVIGRVTLdidlhAQTGDNSLLTALRLLLALYRSLLNP---FKRLNPLRPLR-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 242 ktlvaafqsivtERRNQRKqnilsnkkdmLDNLLnvKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPE 321
Cdd:cd11051 162 ------------RWRNGRR----------LDRYL--KPEVRKRFELERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPE 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 322 VLQRAKAEQEMILKSRPEgQKGLSLKET----RKMEFLSQVVDETLRVITFSLTAfREAKTDVEM---NGYLIP-KGWKV 393
Cdd:cd11051 218 VLAKVRAEHDEVFGPDPS-AAAELLREGpellNQLPYTTAVIKETLRLFPPAGTA-RRGPPGVGLtdrDGKEYPtDGCIV 295
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220438 394 LTWFRDVHIDPEVFPDPRKFDPARW----DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd11051 296 YVCHHAIHRDPEYWPRPDEFIPERWlvdeGHELYPPKSAWRPFERGPRNCIGQELAMLELKIIL 359
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
130-465 6.58e-29

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: 118.09  E-value: 6.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 130 KSFVGISFE----------EHKRLRRLTAAPVNGHEALSTYIPYIEE---NVITVLDKWTKMGEFEFLTHLRKLTFRIIM 196
Cdd:cd11057  34 KSFFYDFFRlgrglfsapyPIWKLQRKALNPSFNPKILLSFLPIFNEeaqKLVQRLDTYVGGGEFDILPDLSRCTLEMIC 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 197 -------YIFLSSESENVMDALEREYTALNYGVrAMAVNIPGF------AYHRALKARKTLVAAFQSIVTERRNQRKQNI 263
Cdd:cd11057 114 qttlgsdVNDESDGNEEYLESYERLFELIAKRV-LNPWLHPEFiyrltgDYKEEQKARKILRAFSEKIIEKKLQEVELES 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 264 LSNKKDM----------LDNLLNVKdEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEqemI 333
Cdd:cd11057 193 NLDSEEDeengrkpqifIDQLLELA-RNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEE---I 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 334 LKSRPEGQKGLSLKETRKMEFLSQVVDETLRVI-TFSLTAfREAKTDVEM-NGYLIPKGWKVLTWFRDVHIDPEVF-PDP 410
Cdd:cd11057 269 MEVFPDDGQFITYEDLQQLVYLEMVLKETMRLFpVGPLVG-RETTADIQLsNGVVIPKGTTIVIDIFNMHRRKDIWgPDA 347
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220438 411 RKFDPARwdngFVP--KAG----AFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRS 465
Cdd:cd11057 348 DQFDPDN----FLPerSAQrhpyAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTS 404
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
234-484 8.51e-29

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: 117.70  E-value: 8.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 234 YHRALKARKTLVAAFQSIVTErrnQRKQNILSNKKDMLDNLL---NVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIM 310
Cdd:cd20651 170 YNLLVELNQKLIEFLKEEIKE---HKKTYDEDNPRDLIDAYLremKKKEPPSSSFTDDQLVMICLDLFIAGSETTSNTLG 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 311 WATVFLQEHPEVLQRAKAE-QEMILKSRPEgqkglSLKETRKMEFLSQVVDETLRVitFSLTAF---REAKTDVEMNGYL 386
Cdd:cd20651 247 FAFLYLLLNPEVQRKVQEEiDEVVGRDRLP-----TLDDRSKLPYTEAVILEVLRI--FTLVPIgipHRALKDTTLGGYR 319
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 387 IPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKR 464
Cdd:cd20651 320 IPKDTTILASLYSVHMDPEYWGDPEEFRPERFldEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSP 399
                       250       260
                ....*....|....*....|
gi 15220438 465 SNPEcpvmyLPHTRPTDNCL 484
Cdd:cd20651 400 PNGS-----LPDLEGIPGGI 414
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
80-473 3.05e-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: 3.05e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  80 RYGPKGIYkahmFGNPSIIvttsdtcRRVLTDDDAFKPGWPTSTMELIGRKS---FVGISFEEHKRLRRLTAAPVNGhEA 156
Cdd:cd11060   5 RIGPNEVS----ISDPEAI-------KTIYGTRSPYTKSDWYKAFRPKDPRKdnlFSERDEKRHAALRRKVASGYSM-SS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 157 LSTYIPYIEENV---ITVLDKWTKMGEFEFLTH-LRKLTFRIIMYIFLSS------ESENVMDALEREYTALNYgvRAMA 226
Cdd:cd11060  73 LLSLEPFVDECIdllVDLLDEKAVSGKEVDLGKwLQYFAFDVIGEITFGKpfgfleAGTDVDGYIASIDKLLPY--FAVV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 227 VNIPgfAYHRALKAR--------KTLVAAFQSIVTERRNQRKQNI---LSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLL 295
Cdd:cd11060 151 GQIP--WLDRLLLKNplgpkrkdKTGFGPLMRFALEAVAERLAEDaesAKGRKDMLDSFLEAGLKDPEKVTDREVVAEAL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 296 MYLNAGHESSGHTIMwATV-FLQEHPEVLQRAKAE-QEMILKSRPEGQkgLSLKETRKMEFLSQVVDETLRV---ITFSL 370
Cdd:cd11060 229 SNILAGSDTTAIALR-AILyYLLKNPRVYAKLRAEiDAAVAEGKLSSP--ITFAEAQKLPYLQAVIKEALRLhppVGLPL 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 371 taFREA-KTDVEMNGYLIPKGWKVL--TWFrdVHIDPEVF-PDPRKFDPARW--DNGFVPKA--GAFLPFGAGSHLCPGN 442
Cdd:cd11060 306 --ERVVpPGGATICGRFIPGGTIVGvnPWV--IHRDKEVFgEDADVFRPERWleADEEQRRMmdRADLTFGAGSRTCLGK 381
                       410       420       430
                ....*....|....*....|....*....|.
gi 15220438 443 DLAKLEISIFLHHFLLKYQVKRSNPECPVMY 473
Cdd:cd11060 382 NIALLELYKVIPELLRRFDFELVDPEKEWKT 412
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
78-453 3.20e-28

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: 116.29  E-value: 3.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  78 IKRYGPKGIYkahMFG-NPSIIVTTSDTCRRVLTDDDA-FKPGWPTS-TMELIGRksfvGISFEEHK---RLRRLtAAPV 151
Cdd:cd11052   8 IKQYGKNFLY---WYGtDPRLYVTEPELIKELLSKKEGyFGKSPLQPgLKKLLGR----GLVMSNGEkwaKHRRI-ANPA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 152 NGHEALSTYIPYIEENVITVLDKWTKM-----GEFEFLTHLRKLTFRIIMYI-FLSSESE-----NVMDALEREYTALNY 220
Cdd:cd11052  80 FHGEKLKGMVPAMVESVSDMLERWKKQmgeegEEVDVFEEFKALTADIISRTaFGSSYEEgkevfKLLRELQKICAQANR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 221 gvramAVNIPG---FAYHRALKARKtLVAAFQSIVTERRNQRKQNIL-----SNKKDMLDNLL--NVKDEDGKTLDDEEI 290
Cdd:cd11052 160 -----DVGIPGsrfLPTKGNKKIKK-LDKEIEDSLLEIIKKREDSLKmgrgdDYGDDLLGLLLeaNQSDDQNKNMTVQEI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 291 IDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAE-QEMIlksrpeGQKGLSLKETRKMEFLSQVVDETLRVITFS 369
Cdd:cd11052 234 VDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEvLEVC------GKDKPPSDSLSKLKTVSMVINESLRLYPPA 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 370 LTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNGfVPKA----GAFLPFGAGSHLCPGNDL 444
Cdd:cd11052 308 VFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADG-VAKAakhpMAFLPFGLGPRNCIGQNF 386

                ....*....
gi 15220438 445 AKLEISIFL 453
Cdd:cd11052 387 ATMEAKIVL 395
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
75-463 5.47e-28

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: 115.54  E-value: 5.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  75 RTLIKRYGPKG-IYKAHMFGNPSIIVTTSDTCRRVLTDDDA--FKP----------GWPTSTMELIGRKSFVGISFEEHK 141
Cdd:cd11040   2 LRNGKKYFSGGpIFTIRLGGQKIYVITDPELISAVFRNPKTlsFDPivivvvgrvfGSPESAKKKEGEPGGKGLIRLLHD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 142 RLRRLTAAPVNGHEALSTYIPYIEeNVIT--VLDKWTKMGEFEFLTHLRKLTFRIIMYIF----LSSESENVMDALeREY 215
Cdd:cd11040  82 LHKKALSGGEGLDRLNEAMLENLS-KLLDelSLSGGTSTVEVDLYEWLRDVLTRATTEALfgpkLPELDPDLVEDF-WTF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 216 TAlnyGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTERRNQRKQ--NILSNKKDMLDNLlnvkdedgkTLDDEEIIDV 293
Cdd:cd11040 160 DR---GLPKLLLGLPRLLARKAYAARDRLLKALEKYYQAAREERDDgsELIRARAKVLREA---------GLSEEDIARA 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 294 LLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEGQKGLSLKETR-KMEFLSQVVDETLRVITFSLTA 372
Cdd:cd11040 228 ELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDLTDLLtSCPLLDSTYLETLRLHSSSTSV 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 373 fREAKTD-VEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARW-----DNGFVPKAGAFLPFGAGSHLCPGNDLA 445
Cdd:cd11040 308 -RLVTEDtVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkdgDKKGRGLPGAFRPFGGGASLCPGRHFA 386
                       410
                ....*....|....*...
gi 15220438 446 KLEISIFLHHFLLKYQVK 463
Cdd:cd11040 387 KNEILAFVALLLSRFDVE 404
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
141-475 9.88e-28

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


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 114.96  E-value: 9.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 141 KRLRRL-TAApvnGH-EALSTYIPYIEENVITVLDKWTKMGE----FEFLTHLRKLTFRIIMYIFLSSESENVMDALERE 214
Cdd:cd20659  58 KRNRRLlTPA---FHfDILKPYVPVYNECTDILLEKWSKLAEtgesVEVFEDISLLTLDIILRCAFSYKSNCQQTGKNHP 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 215 YTA----LNYGVRAMAVNIP---GFAYHRALKARKTLVAAFQ------SIVTERRNQRKQN---ILSNKK--DMLDNLLN 276
Cdd:cd20659 135 YVAavheLSRLVMERFLNPLlhfDWIYYLTPEGRRFKKACDYvhkfaeEIIKKRRKELEDNkdeALSKRKylDFLDILLT 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 277 VKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrpEGQKGLSLKETRKMEFLS 356
Cdd:cd20659 215 ARDEDGKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVL----GDRDDIEWDDLSKLPYLT 290
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 357 QVVDETLR------VItfsltaFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngFVPK----- 425
Cdd:cd20659 291 MCIKESLRlyppvpFI------ARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPER----FLPEnikkr 360
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 15220438 426 -AGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSnPECPVMYLP 475
Cdd:cd20659 361 dPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVD-PNHPVEPKP 410
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
93-451 1.07e-27

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: 114.17  E-value: 1.07e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  93 GNPSIIVTTSDTCRRVLTD-------------DDAFKPGWPTSTMELIGRkSFVGISFEEHKRLRRL-----TAAPVngh 154
Cdd:cd11029  22 GVPAWLVTRYDDARAALADprlskdprkawpaFRGRAPGAPPDLPPVLSD-NMLTSDPPDHTRLRRLvakafTPRRV--- 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 155 EALStyiPYIEENVITVLDKWTKMGEFEFLTHL-RKLTFRIImyiflsseSENV-MDALEREYTAlnYGVRAMAVNIPGF 232
Cdd:cd11029  98 EALR---PRIEEITDELLDALAARGVVDLVADFaYPLPITVI--------CELLgVPEEDRDRFR--RWSDALVDTDPPP 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 233 AyhRALKARKTLVAAFQSIVTERRNQRKQnilsnkkDMLDNLLNVKDEDGKtLDDEEIIDVLLMYLNAGHESSGHTIMWA 312
Cdd:cd11029 165 E--EAAAALRELVDYLAELVARKRAEPGD-------DLLSALVAARDEGDR-LSEEELVSTVFLLLVAGHETTVNLIGNG 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 313 TVFLQEHPEvlQRAKaeqemiLKSRPEGqkglslketrkmefLSQVVDETLRVIT-FSLTAFREAKTDVEMNGYLIPKGW 391
Cdd:cd11029 235 VLALLTHPD--QLAL------LRADPEL--------------WPAAVEELLRYDGpVALATLRFATEDVEVGGVTIPAGE 292
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 392 KVLTWFRDVHIDPEVFPDPRKFDPARWDNGfvpkagaFLPFGAGSHLCPGNDLAKLEISI 451
Cdd:cd11029 293 PVLVSLAAANRDPARFPDPDRLDITRDANG-------HLAFGHGIHYCLGAPLARLEAEI 345
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
98-457 2.71e-27

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: 112.43  E-value: 2.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  98 IVTTSDTCRRVLTDDDAFkpgwpTSTMELIGRKSFVGISF-------EEHKRLRRLTAaPVNGHEALSTYIPYIEENVIT 170
Cdd:cd11034  17 VLTRYAEVQAVARDTDTF-----SSKGVTFPRPELGEFRLmpietdpPEHKKYRKLLN-PFFTPEAVEAFRPRVRQLTND 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 171 VLDKWTKMGEFEFLTHLRKLTFRIIMYIFL---SSESENVMDALEREYTALNYgvramavnipgfayHRALKARKTLVAA 247
Cdd:cd11034  91 LIDAFIERGECDLVTELANPLPARLTLRLLglpDEDGERLRDWVHAILHDEDP--------------EEGAAAFAELFGH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 248 FQSIVTERRNQRKQnilsnkkDMLDNLLNvKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAK 327
Cdd:cd11034 157 LRDLIAERRANPRD-------DLISRLIE-GEIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLI 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 328 AEQEMILKSrpegqkglslketrkmeflsqvVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVF 407
Cdd:cd11034 229 ADPSLIPNA----------------------VEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKF 286
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 15220438 408 PDPRKFDPARWDNgfvpkagAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:cd11034 287 EDPDRIDIDRTPN-------RHLAFGSGVHRCLGSHLARVEARVALTEVL 329
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
249-481 4.71e-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: 113.13  E-value: 4.71e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 249 QSIVTERRNQRKQNILSNKKD-------------MLDNLLNVKDEDGKtLDDEEIIDVLLMYLNAGHESSGHTIMWATVF 315
Cdd:cd20660 180 NKVIQERKAELQKSLEEEEEDdedadigkrkrlaFLDLLLEASEEGTK-LSDEDIREEVDTFMFEGHDTTAAAINWALYL 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 316 LQEHPEVLQRAKAEQEMILKSRPEGQKGLSLKEtrkMEFLSQVVDETLRVITfSLTAF-REAKTDVEMNGYLIPKGWKVL 394
Cdd:cd20660 259 IGSHPEVQEKVHEELDRIFGDSDRPATMDDLKE---MKYLECVIKEALRLFP-SVPMFgRTLSEDIEIGGYTIPKGTTVL 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 395 TWFRDVHIDPEVFPDPRKFDPARwdngFVP--KAG----AFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd20660 335 VLTYALHRDPRQFPDPEKFDPDR----FLPenSAGrhpyAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQKR 410
                       250
                ....*....|....*
gi 15220438 469 CPVMYLPH--TRPTD 481
Cdd:cd20660 411 EDLKPAGEliLRPVD 425
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
131-460 5.33e-27

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: 111.75  E-value: 5.33e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 131 SFVGISFEEHKRLRRLTAaPVNGHEALSTYIPYIEENVITVLDKWTKMGEF----EFLTHLrklTFRIImyiflssesEN 206
Cdd:cd20630  57 GLFLLAPEDHARVRKLVA-PAFTPRAIDRLRAEIQAIVDQLLDELGEPEEFdvirEIAEHI---PFRVI---------SA 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 207 VMDALEREYTALNYGVRAMAVNIPGFAYHRALKARKTLVAA----FQSIVTERRNQRKQNILSNkkdmldnLLNVKDEDG 282
Cdd:cd20630 124 MLGVPAEWDEQFRRFGTATIRLLPPGLDPEELETAAPDVTEglalIEEVIAERRQAPVEDDLLT-------TLLRAEEDG 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 283 KTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMilksrpegqkglslketrkmefLSQVVDET 362
Cdd:cd20630 197 ERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPEL----------------------LRNALEEV 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 363 LRVITFSLTAF-REAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPG 441
Cdd:cd20630 255 LRWDNFGKMGTaRYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR-------DPNANIAFGYGPHFCIG 327
                       330
                ....*....|....*....
gi 15220438 442 NDLAKLEISIFLHHFLLKY 460
Cdd:cd20630 328 AALARLELELAVSTLLRRF 346
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
79-456 5.74e-27

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: 112.63  E-value: 5.74e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  79 KRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDD-AFKPGWPTSTMELIG--RKSFVGISFEEH-KRLRRLTAAPVNGH 154
Cdd:cd11073   2 KKYGP--IMSLKLGSKTTVVVSSPEAAREVLKTHDrVLSGRDVPDAVRALGhhKSSIVWPPYGPRwRMLRKICTTELFSP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 155 EAL-STY----------IPYIEENVITVldKWTKMGEFEFLThlrklTFRIIMYIFLS-------SESENVMDALEREYT 216
Cdd:cd11073  80 KRLdATQplrrrkvrelVRYVREKAGSG--EAVDIGRAAFLT-----SLNLISNTLFSvdlvdpdSESGSEFKELVREIM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 217 ALnygvrAMAVNI----PGFAY-------HRALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTL 285
Cdd:cd11073 153 EL-----AGKPNVadffPFLKFldlqglrRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSESEL 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 286 DDEEIIDVLL-MYLnAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEgqkglsLKETR--KMEFLSQVVDET 362
Cdd:cd11073 228 TRNHIKALLLdLFV-AGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKI------VEESDisKLPYLQAVVKET 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 363 LR---VITFSLTafREAKTDVEMNGYLIPKGWKVL--TWfrDVHIDPEVFPDPRKFDPARwdngFVPKAGAF-------L 430
Cdd:cd11073 301 LRlhpPAPLLLP--RKAEEDVEVMGYTIPKGTQVLvnVW--AIGRDPSVWEDPLEFKPER----FLGSEIDFkgrdfelI 372
                       410       420       430
                ....*....|....*....|....*....|
gi 15220438 431 PFGAGSHLCPGNDLAK----LEISIFLHHF 456
Cdd:cd11073 373 PFGSGRRICPGLPLAErmvhLVLASLLHSF 402
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
80-460 7.23e-27

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: 112.42  E-value: 7.23e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  80 RYGPKGIYKAhmfGNPSIIVTTSDTCRRVLTDDDAF-KPGWPTSTMELIGrKSFVGISFEEHKRLRRLTAAPVNGHEALS 158
Cdd:cd11070   1 KLGAVKILFV---SRWNILVTKPEYLTQIFRRRDDFpKPGNQYKIPAFYG-PNVISSEGEDWKRYRKIVAPAFNERNNAL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 159 TYIPYIEE-----NVITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLSSESEnVMDALEREYTALNYGVRAMAVniPGFA 233
Cdd:cd11070  77 VWEESIRQaqrliRYLLEEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLP-ALDEEESSLHDTLNAIKLAIF--PPLF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 234 YH------RALKARKTLVAAFQsIVTERRN------QRKQNILSNKKDMLDNLLN---VKDEDGKTLDDEEIIDVLLMYL 298
Cdd:cd11070 154 LNfpfldrLPWVLFPSRKRAFK-DVDEFLSelldevEAELSADSKGKQGTESVVAsrlKRARRSGGLTEKELLGNLFIFF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 299 NAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEGQKGLSLKEtrKMEFLSQVVDETLRVITFSLTAFREAKT 378
Cdd:cd11070 233 IAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDFP--KLPYLLAVIYETLRLYPPVQLLNRKTTE 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 379 DVEM-----NGYLIPKGWKVLTWFRDVHIDPEV-FPDPRKFDPARWDNG---------FVPKAGAFLPFGAGSHLCPGND 443
Cdd:cd11070 311 PVVVitglgQEIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWGSTsgeigaatrFTPARGAFIPFSAGPRACLGRK 390
                       410
                ....*....|....*..
gi 15220438 444 LAKLEISIFLHHFLLKY 460
Cdd:cd11070 391 FALVEFVAALAELFRQY 407
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
229-475 1.22e-26

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: 111.62  E-value: 1.22e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGFAY--HRALKARKTLVAAFQSIvteRRNQRKQNILSNKK----DMLDNLLNVKDE------DGKTLDDEEIIDVLLM 296
Cdd:cd11028 162 MPWLRYltRRKLQKFKELLNRLNSF---ILKKVKEHLDTYDKghirDITDALIKASEEkpeeekPEVGLTDEHIISTVQD 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 297 YLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMI--LKSRPEgqkglsLKETRKMEFLSQVVDETLRVITFSLTAFR 374
Cdd:cd11028 239 LFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVigRERLPR------LSDRPNLPYTEAFILETMRHSSFVPFTIP 312
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 375 EAKT-DVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFV--PKAGAFLPFGAGSHLCPGNDLAKLEI 449
Cdd:cd11028 313 HATTrDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLdkTKVDKFLPFGAGRRRCLGEELARMEL 392
                       250       260
                ....*....|....*....|....*.
gi 15220438 450 SIFLHHFLLKYQVKrSNPECPVMYLP 475
Cdd:cd11028 393 FLFFATLLQQCEFS-VKPGEKLDLTP 417
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
80-453 1.59e-26

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: 111.57  E-value: 1.59e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  80 RYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAF----KPGWPTSTMeLIGRKSFVGISF--EEHKRLRRLTAAPVNG 153
Cdd:cd11075   1 KYGP--IFTLRMGSRPLIVVASRELAHEALVQKGSSfasrPPANPLRVL-FSSNKHMVNSSPygPLWRTLRRNLVSEVLS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 154 HEALSTYIPYIEENVITVLDKW-----TKMGEFEFLTHLRKLTFRIIMYI-FLSSESENVMDALEREytalnygVRAMAV 227
Cdd:cd11075  78 PSRLKQFRPARRRALDNLVERLreeakENPGPVNVRDHFRHALFSLLLYMcFGERLDEETVRELERV-------QRELLL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 228 NIPGF---AYHRALKA--RKTLVAAFQSIVTERR-------NQRKQNILSNKKDM------LDNLLNVKDEDGK-TLDDE 288
Cdd:cd11075 151 SFTDFdvrDFFPALTWllNRRRWKKVLELRRRQEevllpliRARRKRRASGEADKdytdflLLDLLDLKEEGGErKLTDE 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 289 EIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVlqRAKAEQEMilKSRPEGQKGLSLKETRKMEFLSQVVDETLRV--- 365
Cdd:cd11075 231 ELVSLCSEFLNAGTDTTATALEWAMAELVKNPEI--QEKLYEEI--KEVVGDEAVVTEEDLPKMPYLKAVVLETLRRhpp 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 366 ITFSLTafREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-DNGFVPKAGA------FLPFGAGSHL 438
Cdd:cd11075 307 GHFLLP--HAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFlAGGEAADIDTgskeikMMPFGAGRRI 384
                       410
                ....*....|....*
gi 15220438 439 CPGNDLAKLEISIFL 453
Cdd:cd11075 385 CPGLGLATLHLELFV 399
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
244-475 1.94e-26

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: 111.30  E-value: 1.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 244 LVAAFQSIVTERRNQRKQNILSNKKDM--LDNLLNVKDEDGktlDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPE 321
Cdd:cd11046 196 LIRKRKEMRQEEDIELQQEDYLNEDDPslLRFLVDMRDEDV---DSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPE 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 322 VLQRAKAEQEMILKSRPEGqkglSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEM--NGYLIPKGWKVLTWFRD 399
Cdd:cd11046 273 LMAKVQAEVDAVLGDRLPP----TYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLpgGGVKVPAGTDIFISVYN 348
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 400 VHIDPEVFPDPRKFDPARWDNGFVPKAG------AFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMY 473
Cdd:cd11046 349 LHRSPELWEDPEEFDPERFLDPFINPPNeviddfAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGM 428

                ..
gi 15220438 474 LP 475
Cdd:cd11046 429 TT 430
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
81-453 6.90e-26

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: 109.59  E-value: 6.90e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  81 YGPkgIYKAHMFGNPSIIVTTSDTCRRVLTdddafKPGW-----PTSTM--ELIGRKSFVGISF--EEHKRLRRLTAAPV 151
Cdd:cd11065   1 YGP--IISLKVGGQTIIVLNSPKAAKDLLE-----KRSAiyssrPRMPMagELMGWGMRLLLMPygPRWRLHRRLFHQLL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 152 NGHeALSTYIPYIEENVITVLDKWTKMGEFeFLTHLRKLTFRIIM-----YIFLSSESENVMDALEREYTALNYGV-RAM 225
Cdd:cd11065  74 NPS-AVRKYRPLQELESKQLLRDLLESPDD-FLDHIRRYAASIILrlaygYRVPSYDDPLLRDAEEAMEGFSEAGSpGAY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 226 AVN-IPGFAY----------HRALKARKTLVAAFQSIVTERRNQRKQNilSNKKDMLDNLLNVKDEDGKtLDDEEIIDVL 294
Cdd:cd11065 152 LVDfFPFLRYlpswlgapwkRKARELRELTRRLYEGPFEAAKERMASG--TATPSFVKDLLEELDKEGG-LSEEEIKYLA 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 295 LMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAE-QEMILKSRPegqkgLSLKETRKMEFLSQVVDETLRVITFSLTAF 373
Cdd:cd11065 229 GSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEElDRVVGPDRL-----PTFEDRPNLPYVNAIVKEVLRWRPVAPLGI 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 374 -REAKTDVEMNGYLIPKGWKVL--TWFrdVHIDPEVFPDPRKFDPARW----DNGFVPKAGAFLPFGAGSHLCPGNDLAk 446
Cdd:cd11065 304 pHALTEDDEYEGYFIPKGTTVIpnAWA--IHHDPEVYPDPEEFDPERYlddpKGTPDPPDPPHFAFGFGRRICPGRHLA- 380

                ....*..
gi 15220438 447 lEISIFL 453
Cdd:cd11065 381 -ENSLFI 386
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
79-468 8.84e-25

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: 106.46  E-value: 8.84e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  79 KRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFkPGWPTSTMELIGRKSF---VGISF---EEHKRLRRLTAAPVN 152
Cdd:cd11054   2 KKYGP--IVREKLGGRDIVHLFDPDDIEKVFRNEGKY-PIRPSLEPLEKYRKKRgkpLGLLNsngEEWHRLRSAVQKPLL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 153 GHEALSTYIPYIEEnVIT-VLDKWTKM------GEFEFLTHLRKLTFRIIMYIFL-----------SSESENVMDALEre 214
Cdd:cd11054  79 RPKSVASYLPAINE-VADdFVERIRRLrdedgeEVPDLEDELYKWSLESIGTVLFgkrlgclddnpDSDAQKLIEAVK-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 215 yTALNYGVRAMavNIPGFAYHRALKARKTLVAA---FQSIVTERRNQRKQNILSN------KKDMLDNLLNVKDedgktL 285
Cdd:cd11054 156 -DIFESSAKLM--FGPPLWKYFPTPAWKKFVKAwdtIFDIASKYVDEALEELKKKdeedeeEDSLLEYLLSKPG-----L 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 286 DDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEqemILKSRPEGQKgLSLKETRKMEFLSQVVDETLRV 365
Cdd:cd11054 228 SKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEE---IRSVLPDGEP-ITAEDLKKMPYLKACIKESLRL 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 366 ITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW----DNGFVPKAGAFLPFGAGSHLCPG 441
Cdd:cd11054 304 YPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrddSENKNIHPFASLPFGFGPRMCIG 383
                       410       420
                ....*....|....*....|....*..
gi 15220438 442 NDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd11054 384 RRFAELEMYLLLAKLLQNFKVEYHHEE 410
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
300-465 8.85e-25

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: 106.34  E-value: 8.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 300 AGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEGQKGLslketRKMEFLSQVVDETLRVITFSLTAFREAKTD 379
Cdd:cd20640 241 AGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDADSL-----SRMKTVTMVIQETLRLYPPAAFVSREALRD 315
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 380 VEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNGfVPKAG----AFLPFGAGSHLCPGNDLAKLEISIFLH 454
Cdd:cd20640 316 MKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNG-VAAACkpphSYMPFGAGARTCLGQNFAMAELKVLVS 394
                       170
                ....*....|.
gi 15220438 455 HFLLKYQVKRS 465
Cdd:cd20640 395 LILSKFSFTLS 405
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
236-453 1.02e-24

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: 106.15  E-value: 1.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 236 RALKARKTLVAAFQSIVTERRNQRKqnilSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVF 315
Cdd:cd20653 178 RVKKLAKRRDAFLQGLIDEHRKNKE----SGKNTMIDHLLSLQESQPEYYTDEIIKGLILVMLLAGTDTSAVTLEWAMSN 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 316 LQEHPEVLQRAKAE-QEMIlksrpeGQKGLsLKE--TRKMEFLSQVVDETLRVitFSLTAF---REAKTDVEMNGYLIPK 389
Cdd:cd20653 254 LLNHPEVLKKAREEiDTQV------GQDRL-IEEsdLPKLPYLQNIISETLRL--YPAAPLlvpHESSEDCKIGGYDIPR 324
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220438 390 GWKVLT--WfrDVHIDPEVFPDPRKFDPARWDnGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd20653 325 GTMLLVnaW--AIHRDPKLWEDPTKFKPERFE-GEEREGYKLIPFGLGRRACPGAGLAQRVVGLAL 387
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
267-468 2.21e-24

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: 105.07  E-value: 2.21e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 267 KKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEqemiLKSRPEGQKGL-S 345
Cdd:cd11059 199 ESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREE----LAGLPGPFRGPpD 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 346 LKETRKMEFLSQVVDETLRV---ITFSLTafREAKTDVEM-NGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNG 421
Cdd:cd11059 275 LEDLDKLPYLNAVIRETLRLyppIPGSLP--RVVPEGGATiGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDP 352
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15220438 422 ----FVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd11059 353 sgetAREMKRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTSTTTDD 403
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
236-456 1.23e-23

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: 102.93  E-value: 1.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 236 RALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKT-LDDEEIIDVLL-MYLnAGHESSGHTIMWAT 313
Cdd:cd11072 174 KLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFpLTRDNIKAIILdMFL-AGTDTSATTLEWAM 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 314 VFLQEHPEVLQRAKAEQEMILKsrpeGQKGLSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWK 392
Cdd:cd11072 253 TELIRNPRVMKKAQEEVREVVG----GKGKVTEEDLEKLKYLKAVIKETLRLhPPAPLLLPRECREDCKINGYDIPAKTR 328
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220438 393 VL--TWfrDVHIDPEVFPDPRKFDPARWDNGFVPKAGA---FLPFGAGSHLCPGND--LAKLEISI--FLHHF 456
Cdd:cd11072 329 VIvnAW--AIGRDPKYWEDPEEFRPERFLDSSIDFKGQdfeLIPFGAGRRICPGITfgLANVELALanLLYHF 399
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
236-473 2.37e-23

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: 102.28  E-value: 2.37e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 236 RALKARKTLVAAF-QSIVTERRNQRKQNILSN--KKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWA 312
Cdd:cd11064 174 KKLREAIRVIDDFvYEVISRRREELNSREEENnvREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWF 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 313 TVFLQEHPEVLQRAKAEQEMILKSRP-EGQKGLSLKETRKMEFLSQVVDETLR---VITFSltaFREA-KTDVEMNGYLI 387
Cdd:cd11064 254 FWLLSKNPRVEEKIREELKSKLPKLTtDESRVPTYEELKKLVYLHAALSESLRlypPVPFD---SKEAvNDDVLPDGTFV 330
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 388 PKGWKVL-----------TWFrdvhidpevfPDPRKFDPARW---DNGFVPK-AGAFLPFGAGSHLCPGNDLAKLEISIF 452
Cdd:cd11064 331 KKGTRIVysiyamgrmesIWG----------EDALEFKPERWldeDGGLRPEsPYKFPAFNAGPRICLGKDLAYLQMKIV 400
                       250       260
                ....*....|....*....|.
gi 15220438 453 LHHFLLKYQVKRSNPEcPVMY 473
Cdd:cd11064 401 AAAILRRFDFKVVPGH-KVEP 420
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
99-448 3.30e-23

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: 101.10  E-value: 3.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  99 VTTSDTCRRVLTDD-----DAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRL-----TAAPVnghEALStyiPYIEENV 168
Cdd:cd11031  28 VTRYADVRQVLADPrfsraAAAPPDAPRLTPEPLLPGSLMSMDPPEHTRLRRLvakafTARRV---ERLR---PRIEEIA 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 169 ITVLDKWTKMG-EFEFLTHL-RKLTFRIImyiflsseSEnVMDALEREYTALNYGVRAMaVNIPGFAYHRALKARKTLVA 246
Cdd:cd11031 102 DELLDAMEAQGpPADLVEALaLPLPVAVI--------CE-LLGVPYEDRERFRAWSDAL-LSTSALTPEEAEAARQELRG 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 247 AFQSIVTERRNQRKQNILSNkkdmldnLLNVKDEDGKtLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRA 326
Cdd:cd11031 172 YMAELVAARRAEPGDDLLSA-------LVAARDDDDR-LSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARL 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 327 KAEQEMIlksrpegqkglslketrkmeflSQVVDETLRVITFSLTA--FREAKTDVEMNGYLIPKGWKVLTWFRDVHIDP 404
Cdd:cd11031 244 RADPELV----------------------PAAVEELLRYIPLGAGGgfPRYATEDVELGGVTIRAGEAVLVSLNAANRDP 301
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15220438 405 EVFPDPRKFDPARWDNgfvpkagAFLPFGAGSHLCPGNDLAKLE 448
Cdd:cd11031 302 EVFPDPDRLDLDREPN-------PHLAFGHGPHHCLGAPLARLE 338
PTZ00404 PTZ00404
cytochrome P450; Provisional
47-463 4.19e-23

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 102.11  E-value: 4.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   47 PGDLGWPFIGNMLSFlrafkTSDPDSFTRTLIKRYGpkGIYKAHMFGNPSIIVTTSDTCRRVLTDD-DAFK--PGWPTST 123
Cdd:PTZ00404  32 KGPIPIPILGNLHQL-----GNLPHRDLTKMSKKYG--GIFRIWFADLYTVVLSDPILIREMFVDNfDNFSdrPKIPSIK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  124 MELIGRKSfVGISFEEHKRLRRLTaapvnGHEALSTYIPYIEENV-------ITVLDKWTKMGE-FEFLTHLRKLTFRII 195
Cdd:PTZ00404 105 HGTFYHGI-VTSSGEYWKRNREIV-----GKAMRKTNLKHIYDLLddqvdvlIESMKKIESSGEtFEPRYYLTKFTMSAM 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  196 M-YIFLS--SESENV--------MDALEREYTALNYGVRAMAVNIPGFAYHRALKARKtlvAAFQSIVTERRNQRKQNIL 264
Cdd:PTZ00404 179 FkYIFNEdiSFDEDIhngklaelMGPMEQVFKDLGSGSLFDVIEITQPLYYQYLEHTD---KNFKKIKKFIKEKYHEHLK 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  265 S----NKKDMLDNLLNvkdEDGKTLDDE--EIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRP 338
Cdd:PTZ00404 256 TidpeVPRDLLDLLIK---EYGTNTDDDilSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRN 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  339 EgqkgLSLKETRKMEFLSQVVDETLR---VITFSLTafREAKTDVEM-NGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFD 414
Cdd:PTZ00404 333 K----VLLSDRQSTPYTVAIIKETLRykpVSPFGLP--RSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFD 406
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 15220438  415 PARWDNGFVPKagAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:PTZ00404 407 PSRFLNPDSND--AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLK 453
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
232-463 6.62e-23

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: 100.68  E-value: 6.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 232 FAYHRALKarktlvaafqSIVTERRNQRKQNILSNKKDMLDNLL----NVKDEDGKTLDDEEIIDVLLMYLNAGHESSGH 307
Cdd:cd20667 174 FAYHDAVR----------SFIKKEVIRHELRTNEAPQDFIDCYLaqitKTKDDPVSTFSEENMIQVVIDLFLGGTETTAT 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 308 TIMWATVFLQEHPEVLQRAKAEQEMILksrpEGQKGLSLKETRKMEFLSQVVDETLRVITF-SLTAFREAKTDVEMNGYL 386
Cdd:cd20667 244 TLHWALLYMVHHPEIQEKVQQELDEVL----GASQLICYEDRKRLPYTNAVIHEVQRLSNVvSVGAVRQCVTSTTMHGYY 319
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 387 IPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW---DNGFVPKAgAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:cd20667 320 VEKGTIILPNLASVLYDPECWETPHKFNPGHFldkDGNFVMNE-AFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQ 398
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
140-462 8.56e-23

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: 100.43  E-value: 8.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 140 HKRLrrLTaaPVNGHEALSTYIPYIEENVITVLDKWTKM----GEFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREY 215
Cdd:cd20678  71 HRRL--LT--PAFHYDILKPYVKLMADSVRVMLDKWEKLatqdSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSY 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 216 TA----LNYGVRAMAVNIP---GFAY------HRALKARKTLVAAFQSIVTERR----NQRKQNILSNKK--DMLDNLLN 276
Cdd:cd20678 147 IQavsdLSNLIFQRLRNFFyhnDFIYklsphgRRFRRACQLAHQHTDKVIQQRKeqlqDEGELEKIKKKRhlDFLDILLF 226
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 277 VKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRpegqKGLSLKETRKMEFLS 356
Cdd:cd20678 227 AKDENGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDG----DSITWEHLDQMPYTT 302
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 357 QVVDETLRVITFSLTAFREAKTDVEM-NGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFG 433
Cdd:cd20678 303 MCIKEALRLYPPVPGISRELSKPVTFpDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFspENSSKRHSHAFLPFS 382
                       330       340
                ....*....|....*....|....*....
gi 15220438 434 AGSHLCPGNDLAKLEISIFLHHFLLKYQV 462
Cdd:cd20678 383 AGPRNCIGQQFAMNEMKVAVALTLLRFEL 411
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
244-468 1.34e-22

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: 99.94  E-value: 1.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 244 LVAAFQSIVTERRNQRKQNI-LSNKKDMLDNLLN----VKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQE 318
Cdd:cd11026 176 NVEEIKSFIRELVEEHRETLdPSSPRDFIDCFLLkmekEKDNPNSEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMK 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 319 HPEVLQRAKAE-QEMILKSRPEgqkglSLKETRKMEFLSQVVDETLRVITFS-LTAFREAKTDVEMNGYLIPKGWKVLTW 396
Cdd:cd11026 256 YPHIQEKVQEEiDRVIGRNRTP-----SLEDRAKMPYTDAVIHEVQRFGDIVpLGVPHAVTRDTKFRGYTIPKGTTVIPN 330
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220438 397 FRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd11026 331 LTSVLRDPKQWETPEEFNPGHFldEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGP 404
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
93-451 1.83e-22

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 98.75  E-value: 1.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  93 GNPSIIVTTSDTCRRVLTDD----DAFKPGWPTSTMELIGRKSFVGISFE----EHKRLRRLtaapVNGH---EALSTYI 161
Cdd:cd11030  22 GRPAWLVTGHDEVRAVLADPrfssDRTRPGFPALSPEGKAAAALPGSFIRmdppEHTRLRRM----LAPEftvRRVRALR 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 162 PYIEENVITVLDKWTKMGE-FEFLTHL-RKLTFRIImyiflsSESENVMDALEREYTALNYGVRAMAVNIPgfayhRALK 239
Cdd:cd11030  98 PRIQEIVDELLDAMEAAGPpADLVEAFaLPVPSLVI------CELLGVPYEDREFFQRRSARLLDLSSTAE-----EAAA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 240 ARKTLVAAFQSIVTERRNQRKQnilsnkkDMLDNLLNVKDEDGKtLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEH 319
Cdd:cd11030 167 AGAELRAYLDELVARKRREPGD-------DLLSRLVAEHGAPGE-LTDEELVGIAVLLLVAGHETTANMIALGTLALLEH 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 320 PEVLQRakaeqemiLKSRPEGqkglslketrkmefLSQVVDETLRVITFSLTAF-REAKTDVEMNGYLIPKGWKVLtwfr 398
Cdd:cd11030 239 PEQLAA--------LRADPSL--------------VPGAVEELLRYLSIVQDGLpRVATEDVEIGGVTIRAGEGVI---- 292
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15220438 399 dVHI-----DPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISI 451
Cdd:cd11030 293 -VSLpaanrDPAVFPDPDRLDITR-------PARRHLAFGHGVHQCLGQNLARLELEI 342
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
231-462 3.07e-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: 99.00  E-value: 3.07e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 231 GFAYHRALKarktLVAAFQS-IVTERR----NQRKQNILSNKK-----DMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNA 300
Cdd:cd20679 180 GRRFRRACR----LVHDFTDaVIQERRrtlpSQGVDDFLKAKAksktlDFIDVLLLSKDEDGKELSDEDIRAEADTFMFE 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 301 GHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRpeGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDV 380
Cdd:cd20679 256 GHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDR--EPEEIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDI 333
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 381 EM-NGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWD--NGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:cd20679 334 VLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDpeNSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTL 413

                ....*
gi 15220438 458 LKYQV 462
Cdd:cd20679 414 LRFRV 418
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
215-467 3.57e-22

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: 98.70  E-value: 3.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 215 YTALNYGVRAMA--VNIPGFAYH------RALKARKTLVAAF-QSIVTERRNQRKQnilSNKKDMLDN-LLNVKDEDGKT 284
Cdd:cd20666 143 SRGLEISVNSAAilVNICPWLYYlpfgpfRELRQIEKDITAFlKKIIADHRETLDP---ANPRDFIDMyLLHIEEEQKNN 219
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 285 LDDEEIIDVLLMYLN----AGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSrpegQKGLSLKETRKMEFLSQVVD 360
Cdd:cd20666 220 AESSFNEDYLFYIIGdlfiAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGP----DRAPSLTDKAQMPFTEATIM 295
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 361 ETLRVITF-SLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSH 437
Cdd:cd20666 296 EVQRMTVVvPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFldENGQLIKKEAFIPFGIGRR 375
                       250       260       270
                ....*....|....*....|....*....|....
gi 15220438 438 LCPGNDLAKLEISIF----LHHFLLKYQVKRSNP 467
Cdd:cd20666 376 VCMGEQLAKMELFLMfvslMQSFTFLLPPNAPKP 409
PLN02687 PLN02687
flavonoid 3'-monooxygenase
250-441 5.38e-22

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 98.73  E-value: 5.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  250 SIVTERRNQRkQNILSNKKDMLDNLLNVKDE-----DGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQ 324
Cdd:PLN02687 254 GIIEEHKAAG-QTGSEEHKDLLSTLLALKREqqadgEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILK 332
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  325 RAKAEQEMIL-KSRPegqkgLSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHI 402
Cdd:PLN02687 333 KAQEELDAVVgRDRL-----VSESDLPQLTYLQAVIKETFRLhPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIAR 407
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 15220438  403 DPEVFPDPRKFDPARwdngFVP---------KAGAF--LPFGAGSHLCPG 441
Cdd:PLN02687 408 DPEQWPDPLEFRPDR----FLPggehagvdvKGSDFelIPFGAGRRICAG 453
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
135-468 1.08e-21

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: 96.91  E-value: 1.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 135 ISFEEHKRLRR-----LTAApvngheALSTYIPYIEENVITVLDKWTKMGEFEFLTHL--RK----LTFRII-------M 196
Cdd:cd11061  49 RDKAEHARRRRvwshaFSDK------ALRGYEPRILSHVEQLCEQLDDRAGKPVSWPVdmSDwfnyLSFDVMgdlafgkS 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 197 YIFLSSESENVM-DALEREYTALNYGVRAMAVnIPGFAYH----RALKARKtlvaAFQSIVTERRNQRKQNILSNKKDML 271
Cdd:cd11061 123 FGMLESGKDRYIlDLLEKSMVRLGVLGHAPWL-RPLLLDLplfpGATKARK----RFLDFVRAQLKERLKAEEEKRPDIF 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 272 DNLLNVKD-EDGKTLDDEEII-DVLLMyLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEGQKGLSLKet 349
Cdd:cd11061 198 SYLLEAKDpETGEGLDLEELVgEARLL-IVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKLK-- 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 350 rKMEFLSQVVDETLRV---ITFSLtaFREA-KTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW---DNGF 422
Cdd:cd11061 275 -SLPYLRACIDEALRLsppVPSGL--PRETpPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWlsrPEEL 351
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 15220438 423 VPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd11061 352 VRARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGE 397
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
239-464 1.11e-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: 97.14  E-value: 1.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 239 KARKTLVAAFQSIVTERRNQRKQNILSN------------KKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSG 306
Cdd:cd20680 181 KNLKILHTFTDNVIAERAEEMKAEEDKTgdsdgespskkkRKAFLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTA 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 307 HTIMWATVFLQEHPEVLQRAKAE-QEMILKS-RPegqkgLSLKETRKMEFLSQVVDETLRVITfSLTAF-REAKTDVEMN 383
Cdd:cd20680 261 AAMNWSLYLLGSHPEVQRKVHKElDEVFGKSdRP-----VTMEDLKKLRYLECVIKESLRLFP-SVPLFaRSLCEDCEIR 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 384 GYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngFVPKAG------AFLPFGAGSHLCPGNDLAKLE----ISIFL 453
Cdd:cd20680 335 GFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPER----FFPENSsgrhpyAYIPFSAGPRNCIGQRFALMEekvvLSCIL 410
                       250
                ....*....|.
gi 15220438 454 HHFLLKYQVKR 464
Cdd:cd20680 411 RHFWVEANQKR 421
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
235-463 1.48e-21

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: 96.98  E-value: 1.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 235 HRALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGhTIMWATV 314
Cdd:cd11041 174 RRLRRLLRRARPLIIPEIERRRKLKKGPKEDKPNDLLQWLIEAAKGEGERTPYDLADRQLALSFAAIHTTSM-TLTHVLL 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 315 FLQEHPEVLQRAKAEQEMILKSRPEGQKGlSLKETRKME-FLSqvvdETLRVITFSLTAF-REAKTDVEM-NGYLIPKGW 391
Cdd:cd11041 253 DLAAHPEYIEPLREEIRSVLAEHGGWTKA-ALNKLKKLDsFMK----ESQRLNPLSLVSLrRKVLKDVTLsDGLTLPKGT 327
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 392 KVLTWFRDVHIDPEVFPDPRKFDPARW-DNGFVPKAGA----------FLPFGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:cd11041 328 RIAVPAHAIHRDPDIYPDPETFDGFRFyRLREQPGQEKkhqfvstspdFLGFGHGRHACPGRFFASNEIKLILAHLLLNY 407

                ...
gi 15220438 461 QVK 463
Cdd:cd11041 408 DFK 410
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
106-450 1.88e-21

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: 95.89  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 106 RRVLTDDDAFKPG--WPTSTMELIG------RKSFVGISFEEHKRLRRLtAAPVNGHEALSTYIPYIEENVITVLDKWTK 177
Cdd:cd11038  37 GQLLRDRRLRQGGhrWLAMNGVTEGpfadwwVDFLLSLEGADHARLRGL-VNPAFTPKAVEALRPRFRATANDLIDGFAE 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 178 MGEFEFLTHLRKLTFRIIMYIFLSSESENvMDALEREYTALNYgvrAMAVNIPGFAyHRALKARKTLVAAFQSIVTERRN 257
Cdd:cd11038 116 GGECEFVEAFAEPYPARVICTLLGLPEED-WPRVHRWSADLGL---AFGLEVKDHL-PRIEAAVEELYDYADALIEARRA 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 258 QRKQNILSNkkdmldnlLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEvlqrakaeQEMILKSR 337
Cdd:cd11038 191 EPGDDLIST--------LVAAEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD--------QWRALRED 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 338 PEgqkglslketrkmeFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRkFDPAR 417
Cdd:cd11038 255 PE--------------LAPAAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRDPRVFDADR-FDITA 319
                       330       340       350
                ....*....|....*....|....*....|...
gi 15220438 418 wdngfvpKAGAFLPFGAGSHLCPGNDLAKLEIS 450
Cdd:cd11038 320 -------KRAPHLGFGGGVHHCLGAFLARAELA 345
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
251-463 2.46e-21

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: 96.02  E-value: 2.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 251 IVTERRNQRKQNILSNK-KDMLDNLLNVKDEDGKTLD---DEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRA 326
Cdd:cd20671 181 ILRTLIEARRPTIDGNPlHSYIEALIQKQEEDDPKETlfhDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRV 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 327 KAEQEMILKSRPEGQkglsLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEV 406
Cdd:cd20671 261 QEEIDRVLGPGCLPN----YEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQ 336
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15220438 407 FPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:cd20671 337 WETPYQFNPNHFldAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFL 395
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
242-459 2.88e-21

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: 95.94  E-value: 2.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 242 KTLVAAFQSIVTERRNQRKQNILSNKKD----MLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQ 317
Cdd:cd20650 177 KDVTNFFYKSVKKIKESRLDSTQKHRVDflqlMIDSQNSKETESHKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELA 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 318 EHPEVLQRAKAEQEMILKSRPEgqkgLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWF 397
Cdd:cd20650 257 THPDVQQKLQEEIDAVLPNKAP----PTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTVVMIPT 332
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 398 RDVHIDPEVFPDPRKFDPARW----DNGFVPKagAFLPFGAGSHLCPGNDLA----KLEISIFLHHFLLK 459
Cdd:cd20650 333 YALHRDPQYWPEPEEFRPERFskknKDNIDPY--IYLPFGSGPRNCIGMRFAlmnmKLALVRVLQNFSFK 400
PLN00168 PLN00168
Cytochrome P450; Provisional
39-463 3.04e-21

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 96.56  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   39 GENRHYLPPGDLGWPFIGNMLSFLRAfkTSDPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPG 118
Cdd:PLN00168  30 GKKGRRLPPGPPAVPLLGSLVWLTNS--SADVEPLLRRLIARYGP--VVSLRVGSRLSVFVADRRLAHAALVERGAALAD 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  119 WPTSTMELIGRKSFVGISFEEH----KRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKlTFRI 194
Cdd:PLN00168 106 RPAVASSRLLGESDNTITRSSYgpvwRLLRRNLVAETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVE-TFQY 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  195 IMYIFLSS-------ESENVMDALEREYTALNYGVRAMAVnipgFAY-------------HRALKARKTLVAAFQSIVTE 254
Cdd:PLN00168 185 AMFCLLVLmcfgerlDEPAVRAIAAAQRDWLLYVSKKMSV----FAFfpavtkhlfrgrlQKALALRRRQKELFVPLIDA 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  255 RRnQRKQNILSNKK----------DMLDNLLNVK--DEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEV 322
Cdd:PLN00168 261 RR-EYKNHLGQGGEppkkettfehSYVDTLLDIRlpEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSI 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  323 LQRAKAEqemILKSRPEGQKGLSLKETRKMEFLSQVVDETLRV---ITFSLTafREAKTDVEMNGYLIPKGWKVLTWFRD 399
Cdd:PLN00168 340 QSKLHDE---IKAKTGDDQEEVSEEDVHKMPYLKAVVLEGLRKhppAHFVLP--HKAAEDMEVGGYLIPKGATVNFMVAE 414
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15220438  400 VHIDPEVFPDPRKFDPARwdngFVP------------KAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:PLN00168 415 MGRDEREWERPMEFVPER----FLAggdgegvdvtgsREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFEWK 486
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
238-460 3.08e-21

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: 95.64  E-value: 3.08e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 238 LKARKTLVAAFQSIVTERRNQRKQNilsNKKDMLDNLLNVKDEDGKTLD----DEEIIDVLLMYLNAGHESSGHTIMWAT 313
Cdd:cd20664 173 LRNTKELNDFLMETFMKHLDVLEPN---DQRGFIDAFLVKQQEEEESSDsffhDDNLTCSVGNLFGAGTDTTGTTLRWGL 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 314 VFLQEHPEVLQRAKAEQEMILKSRPegqkglSLKETRK-MEFLSQVVDETLRVITFS-LTAFREAKTDVEMNGYLIPKGW 391
Cdd:cd20664 250 LLMMKYPEIQKKVQEEIDRVIGSRQ------PQVEHRKnMPYTDAVIHEIQRFANIVpMNLPHATTRDVTFRGYFIPKGT 323
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220438 392 KVLTWFRDVHIDPEVFPDPRKFDPARW---DNGFVpKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:cd20664 324 YVIPLLTSVLQDKTEWEKPEEFNPEHFldsQGKFV-KRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRF 394
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
283-475 3.56e-21

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: 96.06  E-value: 3.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 283 KTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEmILKSRPEGQKGLSLKEtrkMEFLSQVVDET 362
Cdd:cd20649 255 RMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVD-EFFSKHEMVDYANVQE---LPYLDMVIAET 330
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 363 LRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngFVPKAGA------FLPFGAGS 436
Cdd:cd20649 331 LRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPER----FTAEAKQrrhpfvYLPFGAGP 406
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15220438 437 HLCPGNDLAKLEISIFLHHFLLKYQVKrsnpECPVMYLP 475
Cdd:cd20649 407 RSCIGMRLALLEIKVTLLHILRRFRFQ----ACPETEIP 441
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
237-480 3.82e-21

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: 95.56  E-value: 3.82e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 237 ALKARKTLVAAFQSIVTERRNQRKQNILSNK-KDMLDNLLNvkdEDGKTLDDEE------------IIDVLLmylnAGHE 303
Cdd:cd20674 168 GLRRLKQAVENRDHIVESQLRQHKESLVAGQwRDMTDYMLQ---GLGQPRGEKGmgqlleghvhmaVVDLFI----GGTE 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 304 SSGHTIMWATVFLQEHPEVLQRAKaeQEMILKSRPEGQkgLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKT-DVEM 382
Cdd:cd20674 241 TTASTLSWAVAFLLHHPEIQDRLQ--EELDRVLGPGAS--PSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTrDSSI 316
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 383 NGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-DNGfvPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQ 461
Cdd:cd20674 317 AGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFlEPG--AANRALLPFGCGARVCLGEPLARLELFVFLARLLQAFT 394
                       250
                ....*....|....*....
gi 15220438 462 VKRSNPECpvmyLPHTRPT 480
Cdd:cd20674 395 LLPPSDGA----LPSLQPV 409
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
265-470 1.33e-20

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: 93.71  E-value: 1.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 265 SNKKDMLDNLLN---VKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrpeGQ 341
Cdd:cd20662 198 DEPRDFIDAYLKemaKYPDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVI-----GQ 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 342 KGL-SLKETRKMEFLSQVVDETLR---VITFSLTafREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPAR 417
Cdd:cd20662 273 KRQpSLADRESMPYTNAVIHEVQRmgnIIPLNVP--REVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGH 350
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15220438 418 W-DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECP 470
Cdd:cd20662 351 FlENGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPNEKL 404
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
242-468 2.11e-20

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: 93.45  E-value: 2.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 242 KTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTLD--DEEII---DVLLMYLnAGHESSGHTIMWATVFL 316
Cdd:cd20654 190 KELDSILEEWLEEHRQKRSSSGKSKNDEDDDDVMMLSILEDSQISgyDADTVikaTCLELIL-GGSDTTAVTLTWALSLL 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 317 QEHPEVLQRAKAEQEMILKsrpegqKGLSLKET--RKMEFLSQVVDETLRVITFS-LTAFREAKTDVEMNGYLIPKGWKV 393
Cdd:cd20654 269 LNNPHVLKKAQEELDTHVG------KDRWVEESdiKNLVYLQAIVKETLRLYPPGpLLGPREATEDCTVGGYHVPKGTRL 342
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 394 LTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGA---FLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd20654 343 LVNVWKIQRDPNVWSDPLEFKPERFltTHKDIDVRGQnfeLIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIKTPSNE 422
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
242-441 2.26e-20

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: 93.25  E-value: 2.26e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 242 KTLVAAFQSIVTERRNQRKQNILSNK--KDMLDNLL--NVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQ 317
Cdd:cd20657 177 KRLHKRFDALLTKILEEHKATAQERKgkPDFLDFVLleNDDNGEGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELI 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 318 EHPEVLQRAKAEQEMIL-KSRPEGQKGLSlketrKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWKVLT 395
Cdd:cd20657 257 RHPDILKKAQEEMDQVIgRDRRLLESDIP-----NLPYLQAICKETFRLhPSTPLNLPRIASEACEVDGYYIPKGTRLLV 331
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15220438 396 WFRDVHIDPEVFPDPRKFDPARwdngFVPKAGA----------FLPFGAGSHLCPG 441
Cdd:cd20657 332 NIWAIGRDPDVWENPLEFKPER----FLPGRNAkvdvrgndfeLIPFGAGRRICAG 383
PLN02183 PLN02183
ferulate 5-hydroxylase
46-457 4.88e-20

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 92.99  E-value: 4.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   46 PPGDLGWPFIGNMLSFlrafktsdpDSFTR----TLIKRYGpkGIYKAHMFGNPSIIVTTSDTCRRVLTDDD-------- 113
Cdd:PLN02183  38 PPGPKGLPIIGNMLMM---------DQLTHrglaNLAKQYG--GLFHMRMGYLHMVAVSSPEVARQVLQVQDsvfsnrpa 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  114 --------------AFK---PGW----PTSTMELIGRK---SFVGISFEEHKRLRRL---TAAPVNghealstyipyiee 166
Cdd:PLN02183 107 niaisyltydradmAFAhygPFWrqmrKLCVMKLFSRKraeSWASVRDEVDSMVRSVssnIGKPVN-------------- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  167 nvitvldkwtkMGEFEFlTHLRKLTFRIImyiFLSSESENVMDALE--REYTALnYGVRAMAVNIPGFAY-------HRA 237
Cdd:PLN02183 173 -----------IGELIF-TLTRNITYRAA---FGSSSNEGQDEFIKilQEFSKL-FGAFNVADFIPWLGWidpqglnKRL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  238 LKARKTLVAAFQSIVTERRNQRKQNILSN-----KKDMLDNLLNVKDEDGKTLDDEE---------------IIDVLLmy 297
Cdd:PLN02183 237 VKARKSLDGFIDDIIDDHIQKRKNQNADNdseeaETDMVDDLLAFYSEEAKVNESDDlqnsikltrdnikaiIMDVMF-- 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  298 lnAGHESSGHTIMWATVFLQEHPEVLQRAkaEQEMI----LKSRPEGQkglslkETRKMEFLSQVVDETLRVITFSLTAF 373
Cdd:PLN02183 315 --GGTETVASAIEWAMAELMKSPEDLKRV--QQELAdvvgLNRRVEES------DLEKLTYLKCTLKETLRLHPPIPLLL 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  374 REAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPKAGA----FLPFGAGSHLCPGNDLAKLEI 449
Cdd:PLN02183 385 HETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPDFKGshfeFIPFGSGRRSCPGMQLGLYAL 464

                 ....*...
gi 15220438  450 SIFLHHFL 457
Cdd:PLN02183 465 DLAVAHLL 472
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
229-466 5.46e-20

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: 91.94  E-value: 5.46e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGfAYHRALKArktlVAAFQSIVTERRNQRKQNI-LSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLN----AGHE 303
Cdd:cd20665 166 LPG-SHNKLLKN----VAYIKSYILEKVKEHQESLdVNNPRDFIDCFLIKMEQEKHNQQSEFTLENLAVTVTdlfgAGTE 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 304 SSGHTIMWATVFLQEHPEVlqRAKAEQEM---ILKSRPEgqkglSLKETRKMEFLSQVVDETLRVITFSLTAF-REAKTD 379
Cdd:cd20665 241 TTSTTLRYGLLLLLKHPEV--TAKVQEEIdrvIGRHRSP-----CMQDRSHMPYTDAVIHEIQRYIDLVPNNLpHAVTCD 313
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 380 VEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIF----L 453
Cdd:cd20665 314 TKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFldENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFlttiL 393
                       250
                ....*....|...
gi 15220438 454 HHFLLKYQVKRSN 466
Cdd:cd20665 394 QNFNLKSLVDPKD 406
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
91-453 6.16e-20

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: 91.89  E-value: 6.16e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  91 MFGN-PSIIVTTSDTCRRVL-TDDDAF--KPGWPTSTMELIGRKSFVGISFEEH-KRLRRLTAAPVNGHEALSTYIPYIE 165
Cdd:cd20655   7 RIGSvPCVVVSSASVAKEILkTHDLNFssRPVPAAAESLLYGSSGFAFAPYGDYwKFMKKLCMTELLGPRALERFRPIRA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 166 ENV----ITVLDKWTKMGEFEFLTHLRKLTFRIIMYIFLS-------SESENVMDaLEREYTALnygVRAMAVN------ 228
Cdd:cd20655  87 QELerflRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGrscseenGEAEEVRK-LVKESAEL---AGKFNASdfiwpl 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 ----IPGFAyHRALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVKdEDGKT---LDDEEIIDVLLMYLNAG 301
Cdd:cd20655 163 kkldLQGFG-KRIMDVSNRFDELLERIIKEHEEKRKKRKEGGSKDLLDILLDAY-EDENAeykITRNHIKAFILDLFIAG 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 302 HESSGHTIMWATVFLQEHPEVLQRAKAEQEMIL-KSRPEGQKGLSlketrKMEFLSQVVDETLRVITFSLTAFREAKTDV 380
Cdd:cd20655 241 TDTSAATTEWAMAELINNPEVLEKAREEIDSVVgKTRLVQESDLP-----NLPYLQAVVKETLRLHPPGPLLVRESTEGC 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 381 EMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPAR-----WDNGFVPKAGA---FLPFGAGSHLCPGNDLAKLEISIF 452
Cdd:cd20655 316 KINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERflassRSGQELDVRGQhfkLLPFGSGRRGCPGASLAYQVVGTA 395

                .
gi 15220438 453 L 453
Cdd:cd20655 396 I 396
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
246-463 7.91e-20

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


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 91.70  E-value: 7.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 246 AAFQSIVTERRNQRKQNILSNKKDMLDNLLN-------VKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQE 318
Cdd:cd20652 184 AIYQKIIDEHKRRLKPENPRDAEDFELCELEkakkegeDRDLFDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMAL 263
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 319 HPEVLQRAKAEqemiLKSRPEGQKGLSLKETRKMEFLSQVVDETLRVITF-SLTAFREAKTDVEMNGYLIPKGWKV--LT 395
Cdd:cd20652 264 FPKEQRRIQRE----LDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVvPLGIPHGCTEDAVLAGYRIPKGSMIipLL 339
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 396 WFrdVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:cd20652 340 WA--VHMDPNLWEEPEEFRPERFldTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIA 407
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
96-457 8.78e-20

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: 90.99  E-value: 8.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  96 SIIVTTSDTCRRVLTDDDAFkpgwptSTMELIGR-------KSFVGISFEEHKrLRRLTAAPVNGHEALSTYIPYIEENV 168
Cdd:cd11080  11 SYFVSRYEDVRRILKDPDGF------TTKSLAERaepvmrgPVLAQMTGKEHA-AKRAIVVRAFRGDALDHLLPLIKENA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 169 ITVLDKWTKMGEFEFLTHLRKlTFRIimyiflsseseNV---MDALERE----YTALNYGVRAMAVNIPGFAYHRA--LK 239
Cdd:cd11080  84 EELIAPFLERGRVDLVNDFGK-PFAV-----------NVtmdMLGLDKRdhekIHEWHSSVAAFITSLSQDPEARAhgLR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 240 ARKTLVAAFQSIVTERRNQRKQNILSnkkdmldnLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEH 319
Cdd:cd11080 152 CAEQLSQYLLPVIEERRVNPGSDLIS--------ILCTAEYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNN 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 320 PEVLQRAKAEQEmilksrpegqkglslketrkmeFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRD 399
Cdd:cd11080 224 PEQLAAVRADRS----------------------LVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGA 281
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220438 400 VHIDPEVFPDPRKFDPARWDNG----FVPKAgAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:cd11080 282 ANRDPAAFEDPDTFNIHREDLGirsaFSGAA-DHLAFGSGRHFCVGAALAKREIEIVANQVL 342
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
135-453 1.54e-19

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: 90.78  E-value: 1.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 135 ISFEEHKRLRRltaapvngheALSTY---------IPYIEENV---ITVLDKWTKMGEFEFLTHL-RKLTFRIIMYiFLS 201
Cdd:cd11062  50 VDHDLHRLRRK----------ALSPFfskrsilrlEPLIQEKVdklVSRLREAKGTGEPVNLDDAfRALTADVITE-YAF 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 202 SESENVMDALERE---YTALNYGVRAMAVN-----IPGFAYHRALKARKTL------VAAFQSIVTER-----RNQRKQN 262
Cdd:cd11062 119 GRSYGYLDEPDFGpefLDALRALAEMIHLLrhfpwLLKLLRSLPESLLKRLnpglavFLDFQESIAKQvdevlRQVSAGD 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 263 ILSNKKDMLDNLLNVKD-EDGKTLDD--EEIIDVLLmylnAGHESSGHTIMWATVFLQEHPEVLQRAKAEqemiLKSR-P 338
Cdd:cd11062 199 PPSIVTSLFHALLNSDLpPSEKTLERlaDEAQTLIG----AGTETTARTLSVATFHLLSNPEILERLREE----LKTAmP 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 339 EGQKGLSLKETRKMEFLSQVVDETLRvITFSLTAfREA----KTDVEMNGYLIPKGWKV--LTWFrdVHIDPEVFPDPRK 412
Cdd:cd11062 271 DPDSPPSLAELEKLPYLTAVIKEGLR-LSYGVPT-RLPrvvpDEGLYYKGWVIPPGTPVsmSSYF--VHHDEEIFPDPHE 346
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 15220438 413 FDPARW-DNGFVPKAGAFL-PFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd11062 347 FRPERWlGAAEKGKLDRYLvPFSKGSRSCLGINLAYAELYLAL 389
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
234-471 1.60e-19

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: 90.84  E-value: 1.60e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 234 YHRALKARKTLVAAFQSIVTERRNQRKQNIlsNKKDMLDNLLnvKDEDGKTLDDEEIIDVLLMyLNAGHESSGHTIMWAT 313
Cdd:cd11066 178 RERADEYRNRRDKYLKKLLAKLKEEIEDGT--DKPCIVGNIL--KDKESKLTDAELQSICLTM-VSAGLDTVPLNLNHLI 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 314 VFLQEHP--EVLQRAKAEqemILKSRPEGQKGLSLKETR-KMEFLSQVVDETLRVITFSLTAF-REAKTDVEMNGYLIPK 389
Cdd:cd11066 253 GHLSHPPgqEIQEKAYEE---ILEAYGNDEDAWEDCAAEeKCPYVVALVKETLRYFTVLPLGLpRKTTKDIVYNGAVIPA 329
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 390 G-WKVLTWFRDVHiDPEVFPDPRKFDPARW-DNGFVPKAGAF-LPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSN 466
Cdd:cd11066 330 GtILFMNAWAANH-DPEHFGDPDEFIPERWlDASGDLIPGPPhFSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKD 408

                ....*
gi 15220438 467 PECPV 471
Cdd:cd11066 409 EEEPM 413
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
293-468 1.89e-19

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 90.50  E-value: 1.89e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 293 VLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILK-SRPEGQKGLSL-KETRKM----EFLSQVVDETLRVI 366
Cdd:cd20633 228 FMFLLLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVEQVLKeTGQEVKPGGPLiNLTRDMllktPVLDSAVEETLRLT 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 367 TFSLTaFREAKTDVEM---NG--YLIPKGWKVLTW-FRDVHIDPEVFPDPRKFDPARWDNGFVPKAGAF----------- 429
Cdd:cd20633 308 AAPVL-IRAVVQDMTLkmaNGreYALRKGDRLALFpYLAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFykngkklkyyn 386
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15220438 430 LPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd20633 387 MPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLELVNPD 425
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
217-477 2.13e-19

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: 90.31  E-value: 2.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 217 ALNYGVRAMAVN---------IPGFAYHRALKARKTLVAAFQSIVTERRNQRKQNILSNKKDMLDNLLNVkdedgkTLDD 287
Cdd:cd11063 141 AFDYAQKYLAKRlrlgkllwlLRDKKFREACKVVHRFVDPYVDKALARKEESKDEESSDRYVFLDELAKE------TRDP 214
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 288 EEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEqemILKSrpEGQKGLSLKET-RKMEFLSQVVDETLRVI 366
Cdd:cd11063 215 KELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREE---VLSL--FGPEPTPTYEDlKNMKYLRAVINETLRLY 289
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 367 TFSLTAFREAKTDV---------EMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNGfVPKAGAFLPFGAGS 436
Cdd:cd11063 290 PPVPLNSRVAVRDTtlprgggpdGKSPIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDL-KRPGWEYLPFNGGP 368
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15220438 437 HLCPGNDLAKLEISIFLHHFLLKY-QVKRSNPECPVMYLPHT 477
Cdd:cd11063 369 RICLGQQFALTEASYVLVRLLQTFdRIESRDVRPPEERLTLT 410
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
155-457 2.39e-19

unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s, predominantly from bacteria. 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: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 89.34  E-value: 2.39e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 155 EALSTYIPYIEENVITVLDKWTK------MGEFEFLTHLRKLTFriimyiFLSSEsenvmDALEREYTALNYGVRAMAvn 228
Cdd:cd11079  62 ERLARFEPVCRRVAARLVAELPAggggdvVGQFAQPFAVRVQTA------FLGWP-----AALERPLAEWVNKNHAAT-- 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 ipgFAYHRALKARKTLvaAFQSIVTERRNQRKQNILSNKKDMLDNLLNVkDEDGKTLDDEEIIDVLLMYLNAGHESSGHT 308
Cdd:cd11079 129 ---RSGDRAATAEVAE--EFDGIIRDLLADRRAAPRDADDDVTARLLRE-RVDGRPLTDEEIVSILRNWTVGELGTIAAC 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 309 IMWATVFLQEHPEVLQRakaeqemiLKSRPEGqkglslketrkmefLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIP 388
Cdd:cd11079 203 VGVLVHYLARHPELQAR--------LRANPAL--------------LPAAIDEILRLDDPFVANRRITTRDVELGGRTIP 260
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220438 389 KGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:cd11079 261 AGSRVTLNWASANRDERVFGDPDEFDPDR-------HAADNLVYGRGIHVCPGAPLARLELRILLEELL 322
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
251-463 3.00e-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: 89.82  E-value: 3.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 251 IVTERRNQRKQNILSNK-KDMLDNLLNVKDEDGKTLDDEEIIDVLLM----YLNAGHESSGHTIMWATVFLQEHPEVLQR 325
Cdd:cd20669 183 FIAESVREHQESLDPNSpRDFIDCFLTKMAEEKQDPLSHFNMETLVMtthnLLFGGTETVSTTLRYGFLILMKYPKVAAR 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 326 AKAEQEMIL-KSRPEgqkglSLKETRKMEFLSQVVDETLR---VITFSLTafREAKTDVEMNGYLIPKGWKVLTWFRDVH 401
Cdd:cd20669 263 VQEEIDRVVgRNRLP-----TLEDRARMPYTDAVIHEIQRfadIIPMSLP--HAVTRDTNFRGFLIPKGTDVIPLLNSVH 335
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15220438 402 IDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:cd20669 336 YDPTQFKDPQEFNPEHFldDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQ 399
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
239-467 8.67e-19

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: 88.14  E-value: 8.67e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 239 KARKTLVAAFQSIVTERRNQRKQNilSNKKDMLDNLLNvkdedgkTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQE 318
Cdd:cd20635 169 SSKQWLLSLFEKVVPDAEKTKPLE--NNSKTLLQHLLD-------TVDKENAPNYSLLLLWASLANAIPITFWTLAFILS 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 319 HPEVLQRAKAEQEMILKSRPEGQKGLSLKETRKMEFLSQVVDETLR-----VITfsltafREAKTDVEMNGYLIPKG--- 390
Cdd:cd20635 240 HPSVYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRlrspgAIT------RKVVKPIKIKNYTIPAGdml 313
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 391 -----WkvltwfrdVHIDPEVFPDPRKFDPARWD------NGFVPkagAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLK 459
Cdd:cd20635 314 mlspyW--------AHRNPKYFPDPELFKPERWKkadlekNVFLE---GFVAFGGGRYQCPGRWFALMEIQMFVAMFLYK 382

                ....*...
gi 15220438 460 YQVKRSNP 467
Cdd:cd20635 383 YDFTLLDP 390
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
288-453 1.09e-18

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: 88.51  E-value: 1.09e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 288 EEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQR-AKAEQEMILKSRPEGQKGlSLKETRKME--FLSQVVDETLR 364
Cdd:cd20622 261 QVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKlRKALYSAHPEAVAEGRLP-TAQEIAQARipYLDAVIEEILR 339
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 365 VITFSLTAFREAKTDVEMNGYLIPKGWKVL------TWFRDVH-IDPEVF----------------PDPRKFDPARW--- 418
Cdd:cd20622 340 CANTAPILSREATVDTQVLGYSIPKGTNVFllnngpSYLSPPIeIDESRRssssaakgkkagvwdsKDIADFDPERWlvt 419
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15220438 419 --DNG---FVPKAGAFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd20622 420 deETGetvFDPSAGPTLAFGLGPRGCFGRRLAYLEMRLII 459
PLN02936 PLN02936
epsilon-ring hydroxylase
292-456 4.54e-18

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 86.77  E-value: 4.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  292 DVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRPEgqkglSLKETRKMEFLSQVVDETLRVITFSLT 371
Cdd:PLN02936 281 DDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPP-----TYEDIKELKYLTRCINESMRLYPHPPV 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  372 AFREAKT-DVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWD-NGFVPKAG----AFLPFGAGSHLCPGNDLA 445
Cdd:PLN02936 356 LIRRAQVeDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDlDGPVPNETntdfRYIPFSGGPRKCVGDQFA 435
                        170
                 ....*....|....*
gi 15220438  446 KLE----ISIFLHHF 456
Cdd:PLN02936 436 LLEaivaLAVLLQRL 450
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
95-461 7.15e-18

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: 85.58  E-value: 7.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  95 PSIIVTTSDTCRRVLTDDDAF--KPGWPTSTMELIGrKSFVGISFEEHKRLRRLTAaPVNGHEALSTYIPYIEENVITVL 172
Cdd:cd20641  23 PRICISDHELAKQVLSDKFGFfgKSKARPEILKLSG-KGLVFVNGDDWVRHRRVLN-PAFSMDKLKSMTQVMADCTERMF 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 173 DKWTKMG--------EFEFLTHLRKLTFRIIMYIFLSSESENVMDALEREYTALNYGVRAM-AVNIPGFAY------HRA 237
Cdd:cd20641 101 QEWRKQRnnseteriEVEVSREFQDLTADIIATTAFGSSYAEGIEVFLSQLELQKCAAASLtNLYIPGTQYlptprnLRV 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 238 LKARKTLVAAFQSIVTERrnqrkqnILSNKKDMLDNLLNV----------KDEDGKTLDDEEIIDVLLMYLNAGHESSGH 307
Cdd:cd20641 181 WKLEKKVRNSIKRIIDSR-------LTSEGKGYGDDLLGLmleaassnegGRRTERKMSIDEIIDECKTFFFAGHETTSN 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 308 TIMWATVFLQEHPEVLQRAKAEqemILksRPEGQKGLSLKET-RKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYL 386
Cdd:cd20641 254 LLTWTMFLLSLHPDWQEKLREE---VF--RECGKDKIPDADTlSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGGLE 328
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220438 387 IPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNGFVPKA---GAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQ 461
Cdd:cd20641 329 IPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAAthpNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFS 407
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
232-456 9.04e-18

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: 85.23  E-value: 9.04e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 232 FAYHralKARKTLVaaFQSIVTERRNQRKQNilSNKKDMLDNLLNVKDEDGktLDDEEIIDVLLMYLNAGHESSGHTIMW 311
Cdd:cd20656 182 FAKH---GARRDRL--TKAIMEEHTLARQKS--GGGQQHFVALLTLKEQYD--LSEDTVIGLLWDMITAGMDTTAISVEW 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 312 ATVFLQEHPEVLQRAKAEQEMILKSrpegQKGLSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKG 390
Cdd:cd20656 253 AMAEMIRNPRVQEKAQEELDRVVGS----DRVMTEADFPQLPYLQCVVKEALRLhPPTPLMLPHKASENVKIGGYDIPKG 328
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15220438 391 WKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPKAGA---FLPFGAGSHLCPGN----DLAKLEISIFLHHF 456
Cdd:cd20656 329 ANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHdfrLLPFGAGRRVCPGAqlgiNLVTLMLGHLLHHF 401
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
240-457 1.07e-17

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: 84.57  E-value: 1.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 240 ARKTLVAAFQSIVTERRNQRKQnilsnkkDMLDNLLNVkDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEH 319
Cdd:cd11035 149 AAQAVLDYLTPLIAERRANPGD-------DLISAILNA-EIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARH 220
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 320 PEVLQRAKAEQEMILKSrpegqkglslketrkmeflsqvVDETLRVITFsLTAFREAKTDVEMNGYLIPKGWKVLTWFRD 399
Cdd:cd11035 221 PEDRRRLREDPELIPAA----------------------VEELLRRYPL-VNVARIVTRDVEFHGVQLKAGDMVLLPLAL 277
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15220438 400 VHIDPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:cd11035 278 ANRDPREFPDPDTVDFDR-------KPNRHLAFGAGPHRCLGSHLARLELRIALEEWL 328
PLN02290 PLN02290
cytokinin trans-hydroxylase
53-460 1.53e-17

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 85.25  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   53 PFIGNML--SFLRAFKTS-DPDSFTRTLIKRYGPKGIYKAHMFG---------NPSIIVTTSDTCRRVLTDDdAFKPGwp 120
Cdd:PLN02290  51 PLTGNILdvSALVSQSTSkDMDSIHHDIVGRLLPHYVAWSKQYGkrfiywngtEPRLCLTETELIKELLTKY-NTVTG-- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  121 TSTMELIGRKSFVG----ISFEEHKRLRRLTAAPVNGHEALSTYIPYIEE---NVITVLDKWTKMG--EFEFLTHLRKLT 191
Cdd:PLN02290 128 KSWLQQQGTKHFIGrgllMANGADWYHQRHIAAPAFMGDRLKGYAGHMVEctkQMLQSLQKAVESGqtEVEIGEYMTRLT 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  192 FRIIMYIFLSSESEN---VMDALEREYTALNYGVRAMAvnIPGF-----AYHRALKARKTLVAA-FQSIVTERRNQRKQN 262
Cdd:PLN02290 208 ADIISRTEFDSSYEKgkqIFHLLTVLQRLCAQATRHLC--FPGSrffpsKYNREIKSLKGEVERlLMEIIQSRRDCVEIG 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  263 ILSNKKD----MLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRP 338
Cdd:PLN02290 286 RSSSYGDdllgMLLNEMEKKRSNGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGET 365
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  339 EGQKGLSlketrKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPAR 417
Cdd:PLN02290 366 PSVDHLS-----KLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDR 440
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 15220438  418 WDNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:PLN02290 441 FAGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKF 483
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
283-476 2.63e-17

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: 83.82  E-value: 2.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 283 KTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSR--PEGQkglslkETRKMEFLSQVVD 360
Cdd:cd20647 231 KELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRvvPTAE------DVPKLPLIRALLK 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 361 ETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-DNGFVPKAGAF--LPFGAGSH 437
Cdd:cd20647 305 ETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWlRKDALDRVDNFgsIPFGYGIR 384
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15220438 438 LCPGNDLAKLEISIFLHHFLLKYQVKRSNPECPVMYLPH 476
Cdd:cd20647 385 SCIGRRIAELEIHLALIQLLQNFEIKVSPQTTEVHAKTH 423
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
255-463 4.12e-17

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: 83.31  E-value: 4.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 255 RRNQRKQNiLSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMY-LN---AGHESSGHTIMWATVFLQEHPEVLQRAKAEQ 330
Cdd:cd20668 189 EHNQRTLD-PNSPRDFIDSFLIRMQEEKKNPNTEFYMKNLVMTtLNlffAGTETVSTTLRYGFLLLMKHPEVEAKVHEEI 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 331 EMILKSRPEGQkglsLKETRKMEFLSQVVDETLRVITFS-LTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPD 409
Cdd:cd20668 268 DRVIGRNRQPK----FEDRAKMPYTEAVIHEIQRFGDVIpMGLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSN 343
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 410 PRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIF----LHHFLLKYQVK 463
Cdd:cd20668 344 PKDFNPQHFldDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFfttiMQNFRFKSPQS 403
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
45-460 5.45e-17

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 83.59  E-value: 5.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   45 LPPGDLGWPFIGNmlsfLRAFKTSDPDSFTRTLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWP---- 120
Cdd:PLN03234  29 LPPGPKGLPIIGN----LHQMEKFNPQHFLFRLSKLYGP--IFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPllkg 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  121 TSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRII----- 195
Cdd:PLN03234 103 QQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTncvvc 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  196 ------MYIFLSSESENVMDALEREYTALnyGVRAMAVNIPGFAY--------HRALKARKTLVAAFQSIVTER--RNQR 259
Cdd:PLN03234 183 rqafgkRYNEYGTEMKRFIDILYETQALL--GTLFFSDLFPYFGFldnltglsARLKKAFKELDTYLQELLDETldPNRP 260
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  260 KQNILSnkkdMLDNLLNV-KDED-GKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksr 337
Cdd:PLN03234 261 KQETES----FIDLLMQIyKDQPfSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVI--- 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  338 peGQKG-LSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPD-PRKFD 414
Cdd:PLN03234 334 --GDKGyVSEEDIPNLPYLKAVIKESLRLePVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFI 411
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15220438  415 PARWDN-----GFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:PLN03234 412 PERFMKehkgvDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKF 462
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
115-463 6.05e-17

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: 82.63  E-value: 6.05e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 115 FKPGWPTSTMELIGRKSFVGISFEEHKRLRRL-----TAAPVNGHEalstyiPYIEENV---ITVLDKWTKMGE------ 180
Cdd:cd11058  33 PKKDPRFYPPAPNGPPSISTADDEDHARLRRLlahafSEKALREQE------PIIQRYVdllVSRLRERAGSGTpvdmvk 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 181 -FEFLTH--LRKLTF-------------RIIMYIFLSSESENVMDALeREYTALNYGVRAMavnIPGFAYHRALKARKTL 244
Cdd:cd11058 107 wFNFTTFdiIGDLAFgesfgclengeyhPWVALIFDSIKALTIIQAL-RRYPWLLRLLRLL---IPKSLRKKRKEHFQYT 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 245 VAAfqsivTERRNQRKqnilSNKKDMLDNLLnVKDEDGKTLDDEEIID--VLLMYlnAGHESSGHTIMWATVFLQEHPEV 322
Cdd:cd11058 183 REK-----VDRRLAKG----TDRPDFMSYIL-RNKDEKKGLTREELEAnaSLLII--AGSETTATALSGLTYYLLKNPEV 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 323 LQRAKAEqemiLKSRPEGQKGLSLKETRKMEFLSQVVDETLRVitF---SLTAFREAKTDVEM-NGYLIPKGWKVLTWFR 398
Cdd:cd11058 251 LRKLVDE----IRSAFSSEDDITLDSLAQLPYLNAVIQEALRL--YppvPAGLPRVVPAGGATiDGQFVPGGTSVSVSQW 324
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 399 DVHIDPEVFPDPRKFDPARW--DNGFVP---KAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:cd11058 325 AAYRSPRNFHDPDEFIPERWlgDPRFEFdndKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLE 394
PLN02966 PLN02966
cytochrome P450 83A1
42-470 6.68e-17

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 83.26  E-value: 6.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   42 RHYLPPGDLGWPFIGNMLSFLRAfktsDPDSFTRTLIKRYGPKGIYKahmFGNPSIIVTTSDTCRRVL--TDDDAFKPGW 119
Cdd:PLN02966  27 RYKLPPGPSPLPVIGNLLQLQKL----NPQRFFAGWAKKYGPILSYR---IGSRTMVVISSAELAKELlkTQDVNFADRP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  120 PTSTMELI--GRKSFVGISFEEHKR-LRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKL--TFRI 194
Cdd:PLN02966 100 PHRGHEFIsyGRRDMALNHYTPYYReIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELmlTFTN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  195 IMYIFLSSESENVMDALE-REYTALNYGVRAMAVNI---PGFAYHRALKARKTLVAAFQSIVtERRNQRKQNILSNKKD- 269
Cdd:PLN02966 180 SVVCRQAFGKKYNEDGEEmKRFIKILYGTQSVLGKIffsDFFPYCGFLDDLSGLTAYMKECF-ERQDTYIQEVVNETLDp 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  270 ---------MLDNLLNVKDED--GKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSRp 338
Cdd:PLN02966 259 krvkpetesMIDLLMEIYKEQpfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEK- 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  339 eGQKGLSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPA 416
Cdd:PLN02966 338 -GSTFVTEDDVKNLPYFRALVKETLRIePVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPE 416
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15220438  417 RWDNGFVPKAGA---FLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNPECP 470
Cdd:PLN02966 417 RFLEKEVDFKGTdyeFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKP 473
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
289-468 8.77e-17

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: 82.20  E-value: 8.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 289 EIIDVLLMYLNAGHESSGHTIMWATVF-LQEHPEVLQRAKAEqemILKSRPEGQKGLSlKETRKMEFLSQVVDETLRVIT 367
Cdd:cd20644 231 EAIKANITELTAGGVDTTAFPLLFTLFeLARNPDVQQILRQE---SLAAAAQISEHPQ-KALTELPLLKAALKETLRLYP 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 368 FSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW------DNGFvpKAgafLPFGAGSHLCPG 441
Cdd:cd20644 307 VGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWldirgsGRNF--KH---LAFGFGMRQCLG 381
                       170       180
                ....*....|....*....|....*..
gi 15220438 442 NDLAKLEISIFLHHFLLKYQVKRSNPE 468
Cdd:cd20644 382 RRLAEAEMLLLLMHVLKNFLVETLSQE 408
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
86-463 1.16e-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: 81.95  E-value: 1.16e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  86 IYKAHMFGNPSIIVTTSDTCRRVLTDDD--AFKP----GWPTStmELIGRKsfVG-ISFEEHKRLRRLTAAPVnGHEALS 158
Cdd:cd20615   3 IYRIWSGPTPEIVLTTPEHVKEFYRDSNkhHKAPnnnsGWLFG--QLLGQC--VGlLSGTDWKRVRKVFDPAF-SHSAAV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 159 TYIPYIEENVitvlDKWT----------KMGEFEFLTHLRKLTFRIIMYIF---LSSESENVMDALEREYTAL-NYGVRA 224
Cdd:cd20615  78 YYIPQFSREA----RKWVqnlptnsgdgRRFVIDPAQALKFLPFRVIAEILygeLSPEEKEELWDLAPLREELfKYVIKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 225 MAVNIPGF-----AYHRALKARKTLVAAFQSIVTERRNQRKQNILSNKkdmldnlLNVKDEDGkTLDDEEIIDVLLMYLN 299
Cdd:cd20615 154 GLYRFKISrylptAANRRLREFQTRWRAFNLKIYNRARQRGQSTPIVK-------LYEAVEKG-DITFEELLQTLDEMLF 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 300 AGHESSGHTIMWATVFLQEHPEVLQRAKAEqemILKSRPEGQKGLSLKETRKMEFLSQVVDETLR---VITFSLTAFreA 376
Cdd:cd20615 226 ANLDVTTGVLSWNLVFLAANPAVQEKLREE---ISAAREQSGYPMEDYILSTDTLLAYCVLESLRlrpLLAFSVPES--S 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 377 KTDVEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNgfvPKAGA----FLPFGAGSHLCPGNDLAKLEISI 451
Cdd:cd20615 301 PTDKIIGGYRIPANTPVVVDTYALNINNPFWgPDGEAYRPERFLG---ISPTDlrynFWRFGFGPRKCLGQHVADVILKA 377
                       410
                ....*....|..
gi 15220438 452 FLHHFLLKYQVK 463
Cdd:cd20615 378 LLAHLLEQYELK 389
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
232-460 3.36e-16

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: 80.63  E-value: 3.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 232 FAYHRALKARKTLVAAFQSIVTER--RNQRKQNILSNKKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTI 309
Cdd:cd20661 179 FGKHQQLFRNAAEVYDFLLRLIERfsENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFSVGELIIAGTETTTNVL 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 310 MWATVFLQEHPEVLQRAKAEQEMILksrpeGQKGL-SLKETRKMEFLSQVVDETLRVITFS-LTAFREAKTDVEMNGYLI 387
Cdd:cd20661 259 RWAILFMALYPNIQGQVQKEIDLVV-----GPNGMpSFEDKCKMPYTEAVLHEVLRFCNIVpLGIFHATSKDAVVRGYSI 333
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220438 388 PKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:cd20661 334 PKGTTVITNLYSVHFDEKYWSDPEVFHPERFldSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 408
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
236-470 5.32e-16

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 80.06  E-value: 5.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 236 RALKARKTLVAAFQSIVTERRNQRKQNILSNK-KDMLDNLLNVK----------DEDGKTLDDEEIIDVLLMYLNAGHES 304
Cdd:cd20673 168 KDLEKLKQCVKIRDKLLQKKLEEHKEKFSSDSiRDLLDALLQAKmnaennnagpDQDSVGLSDDHILMTVGDIFGAGVET 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 305 SGHTIMWATVFLQEHPEVLQRAKAE-QEMILKSRPEgqkglSLKETRKMEFLSQVVDETLRVITFS-LTAFREAKTDVEM 382
Cdd:cd20673 248 TTTVLKWIIAFLLHNPEVQKKIQEEiDQNIGFSRTP-----TLSDRNHLPLLEATIREVLRIRPVApLLIPHVALQDSSI 322
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 383 NGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW----DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLl 458
Cdd:cd20673 323 GEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFldptGSQLISPSLSYLPFGAGPRVCLGEALARQELFLFMAWLL- 401
                       250
                ....*....|..
gi 15220438 459 kyqvKRSNPECP 470
Cdd:cd20673 402 ----QRFDLEVP 409
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
298-478 5.58e-16

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: 79.80  E-value: 5.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 298 LNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSR--PegqkglSLKETRKMEFLSQVVDETLR---VITFSltA 372
Cdd:cd20648 243 LLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNsvP------SAADVARMPLLKAVVKEVLRlypVIPGN--A 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 373 FREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW-DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISI 451
Cdd:cd20648 315 RVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWlGKGDTHHPYASLPFGFGKRSCIGRRIAELEVYL 394
                       170       180
                ....*....|....*....|....*..
gi 15220438 452 FLHHFLLKYQVKRSNPECPVMylPHTR 478
Cdd:cd20648 395 ALARILTHFEVRPEPGGSPVK--PMTR 419
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
265-463 6.99e-16

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: 79.58  E-value: 6.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 265 SNKKDMLDN-LLNVKDEDGKTLDDEEIIDVLLMYLN---AGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrpeG 340
Cdd:cd20670 198 QNPRDFIDCfLIKMHQDKNNPHTEFNLKNLVLTTLNlffAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVI-----G 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 341 QKGLSLKETR-KMEFLSQVVDETLRVITF-SLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW 418
Cdd:cd20670 273 PHRLPSVDDRvKMPYTDAVIHEIQRLTDIvPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHF 352
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15220438 419 --DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:cd20670 353 ldEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLR 399
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
43-445 8.91e-16

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 79.51  E-value: 8.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   43 HYLPPGDLGWPFIGnMLSFLRAFktsdPDSFTRTLIKRYGPKGIYKahMFGNPSIIVTTSDTCRRVL-TDDDAF--KPGW 119
Cdd:PLN00110  30 RKLPPGPRGWPLLG-ALPLLGNM----PHVALAKMAKRYGPVMFLK--MGTNSMVVASTPEAARAFLkTLDINFsnRPPN 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  120 PTSTMELIGRKSFVgisFEEH----KRLRRLTAAPVNGHEAL--STYIPYIE-ENVITVLDKWTKMGEFEFLTHLrkLTF 192
Cdd:PLN00110 103 AGATHLAYGAQDMV---FADYgprwKLLRKLSNLHMLGGKALedWSQVRTVElGHMLRAMLELSQRGEPVVVPEM--LTF 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  193 ---RIIMYIFLS--------SESENVMDALEREYTALnyGVRAMAVNIPGFAY---HRALKARKTLVAAFQSIVTE--RR 256
Cdd:PLN00110 178 smaNMIGQVILSrrvfetkgSESNEFKDMVVELMTTA--GYFNIGDFIPSIAWmdiQGIERGMKHLHKKFDKLLTRmiEE 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  257 NQRKQNILSNKKDMLDNLL-NVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMIL- 334
Cdd:PLN00110 256 HTASAHERKGNPDFLDVVMaNQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIg 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  335 KSRPegqkgLSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKF 413
Cdd:PLN00110 336 RNRR-----LVESDLPKLPYLQAICKESFRKhPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEF 410
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15220438  414 DPARWDNG----FVPKAGAF--LPFGAGSHLCPGNDLA 445
Cdd:PLN00110 411 RPERFLSEknakIDPRGNDFelIPFGAGRRICAGTRMG 448
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
229-456 2.28e-15

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: 77.81  E-value: 2.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGFAyHRALKARKTLVAAFQSIVTERRNQRKQNilSNKKDMLDNLL----NVKDEDGKTLDDEEIIDVLLMYLNAGHES 304
Cdd:cd20663 169 IPGLA-GKVFPGQKAFLALLDELLTEHRTTWDPA--QPPRDLTDAFLaemeKAKGNPESSFNDENLRLVVADLFSAGMVT 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 305 SGHTIMWATVFLQEHPEVLQRAKAE-QEMILKSR-PEgqkglsLKETRKMEFLSQVVDETLR---VITFSLTafREAKTD 379
Cdd:cd20663 246 TSTTLSWALLLMILHPDVQRRVQQEiDEVIGQVRrPE------MADQARMPYTNAVIHEVQRfgdIVPLGVP--HMTSRD 317
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 380 VEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW---DNGFVpKAGAFLPFGAGSHLCPGNDLAKLEISIF---- 452
Cdd:cd20663 318 IEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFldaQGHFV-KPEAFMPFSAGRRACLGEPLARMELFLFftcl 396

                ....
gi 15220438 453 LHHF 456
Cdd:cd20663 397 LQRF 400
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
71-456 3.01e-15

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: 77.71  E-value: 3.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  71 DSFTRTLIKRYGPKGIYkahMFG-NPSIIVTTSDTCRRVLTDDDAF--KPGWPTSTMELIGRKSFVGISFEEHKRLrrlt 147
Cdd:cd20642   1 MPFIHHTVKTYGKNSFT---WFGpIPRVIIMDPELIKEVLNKVYDFqkPKTNPLTKLLATGLASYEGDKWAKHRKI---- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 148 AAPVNGHEALSTYIPYIEENVITVLDKWTKM------GEFEFLTHLRKLTFRIIMYI-FLSS--ESENVMDaLEREYTAL 218
Cdd:cd20642  74 INPAFHLEKLKNMLPAFYLSCSEMISKWEKLvsskgsCELDVWPELQNLTSDVISRTaFGSSyeEGKKIFE-LQKEQGEL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 219 nyGVRAM-AVNIPGFAY-----HRALKA-RKTLVAAFQSIVTERRNQRKQNILSNKkDMLDNLL-----NVKDEDGKT-- 284
Cdd:cd20642 153 --IIQALrKVYIPGWRFlptkrNRRMKEiEKEIRSSLRGIINKREKAMKAGEATND-DLLGILLesnhkEIKEQGNKNgg 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 285 LDDEEIID-VLLMYLnAGHESSGHTIMWATVFLQEHPEVLQRAKAE-QEMILKSRPEGQkGLSlketrKMEFLSQVVDET 362
Cdd:cd20642 230 MSTEDVIEeCKLFYF-AGQETTSVLLVWTMVLLSQHPDWQERAREEvLQVFGNNKPDFE-GLN-----HLKVVTMILYEV 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 363 LRVIT--FSLTafREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARWDNGfVPKA----GAFLPFGAG 435
Cdd:cd20642 303 LRLYPpvIQLT--RAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAEG-ISKAtkgqVSYFPFGWG 379
                       410       420
                ....*....|....*....|....*
gi 15220438 436 SHLCPGNDLAKLE----ISIFLHHF 456
Cdd:cd20642 380 PRICIGQNFALLEakmaLALILQRF 404
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
99-454 5.37e-15

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: 76.47  E-value: 5.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  99 VTTSDTCRRVLTDDDAFkpgwpTST----MELIGRKSFVGISFE----EHKRLRRLTAAPVnGHEALSTYIPYIEENVIT 170
Cdd:cd11037  26 LARYDEVRAALRDHETF-----SSArgvgLNDFLNWRLPGSILAsdppEHDRLRAVLSRPL-SPRALRKLRDRIEEAADE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 171 VLDKWTKMGEFEFLTHL-RKLTFRIimyiflssesenVMDAL----EREYTALNYGvrAMAVNIPGFAYHRALKARKTLV 245
Cdd:cd11037 100 LVDELVARGEFDAVTDLaEAFPLRV------------VPDLVglpeEGRENLLPWA--AATFNAFGPLNERTRAALPRLK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 246 AAFQSIVTE-RRNQRK-----QNILSNkkdmldnllnvkdEDGKTLDDEEIidVLLM--YLNAGHESSGHTIMWATVFLQ 317
Cdd:cd11037 166 ELRDWVAEQcARERLRpggwgAAIFEA-------------ADRGEITEDEA--PLLMrdYLSAGLDTTISAIGNALWLLA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 318 EHPEVLQRAKAEQEMIlksrpegqkglslketrkmeflSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWF 397
Cdd:cd11037 231 RHPDQWERLRADPSLA----------------------PNAFEEAVRLESPVQTFSRTTTRDTELAGVTIPAGSRVLVFL 288
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15220438 398 RDVHIDPEVFPDPRKFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLH 454
Cdd:cd11037 289 GSANRDPRKWDDPDRFDITR-------NPSGHVGFGHGVHACVGQHLARLEGEALLT 338
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
177-470 6.23e-15

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 76.65  E-value: 6.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 177 KMGEFEFLTHL-RKLTFRIIMYIFLSSESENVMDALErEYTALNYGVRAMAVNIPGFAYHRALKARKTLVAAFQSIVTER 255
Cdd:cd20631 124 VMFEAGYLTLFgKELTAREDKNARLEAQRALILNALE-NFKEFDKVFPALVAGLPIHMFKTAKSAREALAERLLHENLQK 202
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 256 RNQRKQNIlsnkkdMLDNLLNvkdEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILK 335
Cdd:cd20631 203 RENISELI------SLRMLLN---DTLSTLDEMEKARTHVAMLWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLE 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 336 S-----RPEGQK-GLSLKETRKMEFLSQVVDETLRVITFSLTaFREAKTDVEM---NG--YLIPKGWKVLTWFRDVHIDP 404
Cdd:cd20631 274 KtgqkvSDGGNPiVLTREQLDDMPVLGSIIKEALRLSSASLN-IRVAKEDFTLhldSGesYAIRKDDIIALYPQLLHLDP 352
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220438 405 EVFPDPRKFDPARW--DNG----FVPKAGA-----FLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK--RSNPECP 470
Cdd:cd20631 353 EIYEDPLTFKYDRYldENGkektTFYKNGRklkyyYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYFDMEllDGNAKCP 431
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
236-456 6.80e-15

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: 76.60  E-value: 6.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 236 RALKARktlVAAF-QSIVTERRNQRkQNILSNKKDMLDNLLNVKDEDgkTLDDEEIIDVLLMYLNAGHESSGHTIMWATV 314
Cdd:cd11076 176 SALVPR---VNTFvGKIIEEHRAKR-SNRARDDEDDVDVLLSLQGEE--KLSDSDMIAVLWEMIFRGTDTVAILTEWIMA 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 315 FLQEHPEVLQRAKAEQEMILksrpeGQKGLSLK-ETRKMEFLSQVVDETLRVITFS--LTAFREAKTDVEMNGYLIPKG- 390
Cdd:cd11076 250 RMVLHPDIQSKAQAEIDAAV-----GGSRRVADsDVAKLPYLQAVVKETLRLHPPGplLSWARLAIHDVTVGGHVVPAGt 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 391 ------WKVltwfrdVHiDPEVFPDPRKFDPARwdngFVPKAGA-----------FLPFGAGSHLCPGNDL----AKLEI 449
Cdd:cd11076 325 tamvnmWAI------TH-DPHVWEDPLEFKPER----FVAAEGGadvsvlgsdlrLAPFGAGRRVCPGKALglatVHLWV 393

                ....*..
gi 15220438 450 SIFLHHF 456
Cdd:cd11076 394 AQLLHEF 400
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
15-444 1.87e-14

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 75.63  E-value: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   15 MVLGCFGLNWLVRKVNVWLYESSLgenrhYLPPGDLGWPFIGNMLSFlrafkTSDPDSFTRTLIKRYGPKGIYKahmFGN 94
Cdd:PLN03112   8 LLFSVLIFNVLIWRWLNASMRKSL-----RLPPGPPRWPIVGNLLQL-----GPLPHRDLASLCKKYGPLVYLR---LGS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   95 PSIIVTTS-DTCRRVLTDDDAFKPGWPTSTMELI---GRKSFVGISFEEH-KRLRRLTAapvngHEAL------STYIPY 163
Cdd:PLN03112  75 VDAITTDDpELIREILLRQDDVFASRPRTLAAVHlayGCGDVALAPLGPHwKRMRRICM-----EHLLttkrleSFAKHR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  164 IEENVITVLDKWTK------------MGEFEFLTHLRKLTFRIimyiFLSSESENVMDALE---------REYTALNYGV 222
Cdd:PLN03112 150 AEEARHLIQDVWEAaqtgkpvnlrevLGAFSMNNVTRMLLGKQ----YFGAESAGPKEAMEfmhithelfRLLGVIYLGD 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  223 RAMA---VNIPGFAyHRALKARKTLVAAFQSIVTERRNQRKQNILSNKK-DMLDNLLNVKDEDGKT-LDDEEIIDVLLMY 297
Cdd:PLN03112 226 YLPAwrwLDPYGCE-KKMREVEKRVDEFHDKIIDEHRRARSGKLPGGKDmDFVDVLLSLPGENGKEhMDDVEIKALMQDM 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  298 LNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSrpegQKGLSLKETRKMEFLSQVVDETLRVITFSLTAF-REA 376
Cdd:PLN03112 305 IAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGR----NRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIpHES 380
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15220438  377 KTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPAR-W--DNGFVPKAGA----FLPFGAGSHLCPGNDL 444
Cdd:PLN03112 381 LRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERhWpaEGSRVEISHGpdfkILPFSAGKRKCPGAPL 455
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
229-465 3.86e-14

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: 74.36  E-value: 3.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGFAY--HRALKARKTLVAAFQSIVT----ERRNQRKQNILSNKKDMLDNLLNVKDEDGKT--LDDEEIIDVLLMYLNA 300
Cdd:cd20677 168 IPILRYlpSPSLKALRKFISRLNNFIAksvqDHYATYDKNHIRDITDALIALCQERKAEDKSavLSDEQIISTVNDIFGA 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 301 GHESSGHTIMWATVFLQEHPEVlqRAKAEQEMILKSrpeGQKGLSLKETRK-MEFLSQVVDETLRVITFSLTAFREAKT- 378
Cdd:cd20677 248 GFDTISTALQWSLLYLIKYPEI--QDKIQEEIDEKI---GLSRLPRFEDRKsLHYTEAFINEVFRHSSFVPFTIPHCTTa 322
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 379 DVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGA--FLPFGAGSHLCPGNDLAKLEISIFLH 454
Cdd:cd20677 323 DTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFldENGQLNKSLVekVLIFGMGVRKCLGEDVARNEIFVFLT 402
                       250
                ....*....|.
gi 15220438 455 HFLLKYQVKRS 465
Cdd:cd20677 403 TILQQLKLEKP 413
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
308-462 1.26e-13

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: 72.44  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 308 TIMWATVFLQEHPEVLQRAKAEqemILKSRPEGQkGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLI 387
Cdd:cd20643 253 TLQWTLYELARNPNVQEMLRAE---VLAARQEAQ-GDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHI 328
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15220438 388 PKGWKVLTWFRDVHIDPEVFPDPRKFDPARW----DNGFvpkagAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQV 462
Cdd:cd20643 329 PAGTLVQVGLYAMGRDPTVFPKPEKYDPERWlskdITHF-----RNLGFGFGPRQCLGRRIAETEMQLFLIHMLENFKI 402
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
298-468 1.26e-13

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: 72.77  E-value: 1.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 298 LNAGHESSGHTIMWATVFLQEHPEVLQRAKAEqemILKSRPEGQKGlSLKETRKMEFLSQVVDETLRVITFSLTAFR-EA 376
Cdd:cd20646 242 LLAGVDTTSNTLSWALYHLARDPEIQERLYQE---VISVCPGDRIP-TAEDIAKMPLLKAVIKETLRLYPVVPGNARvIV 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 377 KTDVEMNGYLIPKGwkvlTWFRDVHI----DPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAKLEIS 450
Cdd:cd20646 318 EKEVVVGDYLFPKN----TLFHLCHYavshDETNFPEPERFKPERWlrDGGLKHHPFGSIPFGYGVRACVGRRIAELEMY 393
                       170
                ....*....|....*...
gi 15220438 451 IFLHHFLLKYQVkRSNPE 468
Cdd:cd20646 394 LALSRLIKRFEV-RPDPS 410
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
300-471 1.27e-13

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: 72.53  E-value: 1.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 300 AGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrPEGQKGLSlKETRKMEFLSQVVDETLRVITFSLTAFREAKTD 379
Cdd:cd20645 237 GGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVL---PANQTPRA-EDLKNMPYLKACLKESMRLTPSVPFTSRTLDKD 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 380 VEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW------DNGFvpkagAFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:cd20645 313 TVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWlqekhsINPF-----AHVPFGIGKRMCIGRRLAELQLQLAL 387
                       170
                ....*....|....*...
gi 15220438 454 HHFLLKYQVKRSNPEcPV 471
Cdd:cd20645 388 CWIIQKYQIVATDNE-PV 404
PLN02738 PLN02738
carotene beta-ring hydroxylase
244-448 1.31e-13

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 73.02  E-value: 1.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  244 LVAAFQSIVTERRNQRKQNILsNKKD--MLDNLLNVKDE-DGKTLDDEeiidvLLMYLNAGHESSGHTIMWATVFLQEHP 320
Cdd:PLN02738 349 LIAICKRMVEEEELQFHEEYM-NERDpsILHFLLASGDDvSSKQLRDD-----LMTMLIAGHETSAAVLTWTFYLLSKEP 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  321 EVLQRAKAEQEMILksrpeGQKGLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDV 400
Cdd:PLN02738 423 SVVAKLQEEVDSVL-----GDRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNL 497
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15220438  401 HIDPEVFPDPRKFDPARWD-NGFVPKAG----AFLPFGAGSHLCPGNDLAKLE 448
Cdd:PLN02738 498 HRSPKHWDDAEKFNPERWPlDGPNPNETnqnfSYLPFGGGPRKCVGDMFASFE 550
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
131-461 3.84e-13

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: 71.14  E-value: 3.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 131 SFVGISFEEHKRLRRLTaapvngHEAL----STYIPYIEENVITVLDKW----TKMGEFEFLTHLRKLTFRIIMYIFL-S 201
Cdd:cd11071  70 PYLDTSEPKHAKLKAFL------FELLksrsSRFIPEFRSALSELFDKWeaelAKKGKASFNDDLEKLAFDFLFRLLFgA 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 202 SESENVMDALEREYTALNYGVRamavNIPGfAYHRALKARKTLvaafqsivtERRNQRKQNIL--SNKKDMLD----NLL 275
Cdd:cd11071 144 DPSETKLGSDGPDALDKWLALQ----LAPT-LSLGLPKILEEL---------LLHTFPLPFFLvkPDYQKLYKffanAGL 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 276 NVKDEDGKTLDDEE-----IIDVLLMylNAgheSSGHTIMWATVF--LQEHPEVLQrAKAEQEMILKSRPEGqkGLSLKE 348
Cdd:cd11071 210 EVLDEAEKLGLSREeavhnLLFMLGF--NA---FGGFSALLPSLLarLGLAGEELH-ARLAEEIRSALGSEG--GLTLAA 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 349 TRKMEFLSQVVDETLRV---ITFsltAFREAKTD--VEMNG--YLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdng 421
Cdd:cd11071 282 LEKMPLLKSVVYETLRLhppVPL---QYGRARKDfvIESHDasYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDR---- 354
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 15220438 422 FVPKAGAFLP------------FGAGSHLCPGNDLAKLEISIFLHHFLLKYQ 461
Cdd:cd11071 355 FMGEEGKLLKhliwsngpeteePTPDNKQCPGKDLVVLLARLFVAELFLRYD 406
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
59-445 6.94e-13

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: 70.25  E-value: 6.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  59 LSFLRafktsDPDSFTRTLIKRYGPkGIYKAHMFGNPSIIVTTSDTCRrVLTDDDAFK-----PgwPTSTMELIGRKSFV 133
Cdd:cd11067   4 LALLR-----EGYRFISNRCRRLGS-DAFRTRLMGRPAICLRGPEAAR-LFYDEDRFTrkgamP--PRVQKTLFGKGGVQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 134 GISFEEHKR-----LRRLTAapvnghEALSTYIPYIEENVITVLDKWTKMGEFEFLTHLRKLTFRIIM-YIFLSSESENV 207
Cdd:cd11067  75 GLDGEAHRHrkamfMSLMTP------ERVARLARLFRREWRAALARWEGRDEVVLFDEAQEVLTRAACrWAGVPLPEEDV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 208 mDALEREYTALNYGVRAmavniPGFAYHRALKARKTLVAAFQSIVTERRNQRkqnILSNKKDMLDNLLNVKDEDGKTLDD 287
Cdd:cd11067 149 -ERRARDLAAMIDGAGA-----VGPRHWRARLARRRAERWAAELIEDVRAGR---LAPPEGTPLAAIAHHRDPDGELLPE 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 288 E----EIIDVLLmylnaghessgHT------IMWATVFLQEHPEVLQRakaeqemiLKSRPEgqkglslketrkmEFLSQ 357
Cdd:cd11067 220 RvaavELLNLLR-----------PTvavarfVTFAALALHEHPEWRER--------LRSGDE-------------DYAEA 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 358 VVDETLRVITFS-LTAFReAKTDVEMNGYLIPKGWKVLTwfrDV---HIDPEVFPDPRKFDPAR---WDNGfvpkAGAFL 430
Cdd:cd11067 268 FVQEVRRFYPFFpFVGAR-ARRDFEWQGYRFPKGQRVLL---DLygtNHDPRLWEDPDRFRPERflgWEGD----PFDFI 339
                       410
                ....*....|....*....
gi 15220438 431 PFGAG----SHLCPGNDLA 445
Cdd:cd11067 340 PQGGGdhatGHRCPGEWIT 358
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
268-454 2.15e-12

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: 68.88  E-value: 2.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 268 KDMLDNLLNVKDE-----DGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMIL-KSR-Peg 340
Cdd:cd20675 209 RDMMDAFILALEKgksgdSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVgRDRlP-- 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 341 qkglSLKETRKMEFLSQVVDETLRVITF-SLTAFREAKTDVEMNGYLIPKGWKVLT--WfrDVHIDPEVFPDPRKFDPAR 417
Cdd:cd20675 287 ----CIEDQPNLPYVMAFLYEAMRFSSFvPVTIPHATTADTSILGYHIPKDTVVFVnqW--SVNHDPQKWPNPEVFDPTR 360
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15220438 418 W--DNGFVPK--AGAFLPFGAGSHLCPGNDLAKLEI----SIFLH 454
Cdd:cd20675 361 FldENGFLNKdlASSVMIFSVGKRRCIGEELSKMQLflftSILAH 405
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
290-470 6.14e-12

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 67.50  E-value: 6.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 290 IIDVLLMYLnAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILKSrpegQKGLSLKETRKMEFLSQVVDETLRVITFS 369
Cdd:cd20672 228 MISVLSLFF-AGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGS----HRLPTLDDRAKMPYTDAVIHEIQRFSDLI 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 370 LTAFREAKT-DVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARW--DNGFVPKAGAFLPFGAGSHLCPGNDLAK 446
Cdd:cd20672 303 PIGVPHRVTkDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFldANGALKKSEAFMPFSTGKRICLGEGIAR 382
                       170       180
                ....*....|....*....|....
gi 15220438 447 LEISIFLHHFLLKYQVkrSNPECP 470
Cdd:cd20672 383 NELFLFFTTILQNFSV--ASPVAP 404
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
175-468 7.39e-12

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 67.09  E-value: 7.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 175 WTKMGEFEFLThlrKLTFRIIMYIFLSSESENVMD---ALEREYTALNYG-VRAMAVNIPGFAYHRALKARKTLVAA--- 247
Cdd:cd20634 108 WKKDGLFNFCY---SLLFRAGYLTLFGNENENSTHesqNKDRAHSAEVYHeFRKLDQLLPKLARGTLSKEEKQEAASvke 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 248 -FQSIVTERRNQRKqnilSNKKDMLDNLLNVKDEDGktLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRA 326
Cdd:cd20634 185 rLWKLLSPKRLNRK----ANRSSWLESYLLHLEEEG--VDEEMQARAMLLQLWATQGNAGPAAFWLLLFLLKHPEAMAAV 258
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 327 KAEQEMILKSRPEGQK---GLSLKETRKMEFLSQVVDETLRvitfsLTAF----REAKTDVEM---NG--YLIPKGWKVL 394
Cdd:cd20634 259 RGEIQRIKHQRGQPVSqtlTINQELLDNTPVFDSVLSETLR-----LTAApfitREVLQDMKLrlaDGqeYNLRRGDRLC 333
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 395 TW-FRDVHIDPEVFPDPRKFDPARWDNG-------FVpKAGAFL-----PFGAGSHLCPGNDLAKLEISIFLHHFLLKYQ 461
Cdd:cd20634 334 LFpFLSPQMDPEIHQEPEVFKYDRFLNAdgtekkdFY-KNGKRLkyynmPWGAGDNVCIGRHFAVNSIKQFVFLILTHFD 412

                ....*..
gi 15220438 462 VKRSNPE 468
Cdd:cd20634 413 VELKDPE 419
PLN02655 PLN02655
ent-kaurene oxidase
51-456 3.15e-11

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 65.15  E-value: 3.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   51 GWPFIGNMLSFlrafKTSDP-DSFTRtLIKRYGPkgIYKAHMFGNPSIIVTTSDTCRRVLTDDDAF--KPGWPTSTMELI 127
Cdd:PLN02655   6 GLPVIGNLLQL----KEKKPhRTFTK-WSEIYGP--IYTIRTGASSVVVLNSTEVAKEAMVTKFSSisTRKLSKALTVLT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  128 GRKSFVGIS--FEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKwtkmgefeFLTHLRK-----LTFRIIMYIFL 200
Cdd:PLN02655  79 RDKSMVATSdyGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSG--------LHALVKDdphspVNFRDVFENEL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  201 --------------SSESENVMDALERE--YTALNYGVRAMAVNIPG---FAYHRALKARKtlvaaFQSIV--TERR--- 256
Cdd:PLN02655 151 fglsliqalgedveSVYVEELGTEISKEeiFDVLVHDMMMCAIEVDWrdfFPYLSWIPNKS-----FETRVqtTEFRrta 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  257 -------NQRKQNILSNKKD-MLDNLLnvkdEDGKTLDDEEIidvLLMYLNAGHESSGHTIM---WATVFLQEHPEVlqr 325
Cdd:PLN02655 226 vmkalikQQKKRIARGEERDcYLDFLL----SEATHLTDEQL---MMLVWEPIIEAADTTLVtteWAMYELAKNPDK--- 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  326 akaeQEMILKSRPE--GQKGLSLKETRKMEFLSQVVDETLRVIT-FSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHI 402
Cdd:PLN02655 296 ----QERLYREIREvcGDERVTEEDLPNLPYLNAVFHETLRKYSpVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNM 371
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  403 DPEVFPDPRKFDPARWDNGFVPKAGAF--LPFGAGSHLCPGN----DLAKLEISIFLHHF 456
Cdd:PLN02655 372 DKKRWENPEEWDPERFLGEKYESADMYktMAFGAGKRVCAGSlqamLIACMAIARLVQEF 431
PLN03018 PLN03018
homomethionine N-hydroxylase
45-463 7.32e-11

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 64.26  E-value: 7.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   45 LPPGDLGWPFIGNMLSFLrafkTSDPDSFTRTLIKRYGPKGIYKAHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWPT-ST 123
Cdd:PLN03018  41 LPPGPPGWPILGNLPELI----MTRPRSKYFHLAMKELKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQlSI 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  124 MELIGRK------SFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENVITVLDKWTKMGEFEFLTHL-RKLTFRIIM 196
Cdd:PLN03018 117 METIGDNyksmgtSPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYQRSETVDVRELsRVYGYAVTM 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  197 YIFLSSE---SENVMDALEREYTALNYGVRAM--AVN-IPGFA----------------YHRALKARKTLVAAFQSIVTE 254
Cdd:PLN03018 197 RMLFGRRhvtKENVFSDDGRLGKAEKHHLEVIfnTLNcLPGFSpvdyverwlrgwnidgQEERAKVNVNLVRSYNNPIID 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  255 RRNQ--RKQNILSNKKDMLDNLLNVKDEDGKTL-DDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAE-Q 330
Cdd:PLN03018 277 ERVElwREKGGKAAVEDWLDTFITLKDQNGKYLvTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKElD 356
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  331 EMILKSRPegqkgLSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPD 409
Cdd:PLN03018 357 EVVGKDRL-----VQESDIPNLNYLKACCRETFRIhPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKD 431
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15220438  410 PRKFDPARWDNG--------FVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVK 463
Cdd:PLN03018 432 PLVYEPERHLQGdgitkevtLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWK 493
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
251-457 1.03e-10

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: 63.54  E-value: 1.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 251 IVTERRNQRKQNILSNKKDMLDNLLNVKDEDGK-TLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAE 329
Cdd:cd20658 198 IIDERIKQWREGKKKEEEDWLDVFITLKDENGNpLLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEE 277
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 330 QEMILksrpeGQKGLsLKET--RKMEFLSQVVDETLR---VITFSLTAFreAKTDVEMNGYLIPKGWKVLTWFRDVHIDP 404
Cdd:cd20658 278 LDRVV-----GKERL-VQESdiPNLNYVKACAREAFRlhpVAPFNVPHV--AMSDTTVGGYFIPKGSHVLLSRYGLGRNP 349
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15220438 405 EVFPDPRKFDPARWDNG-----FVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFL 457
Cdd:cd20658 350 KVWDDPLKFKPERHLNEdsevtLTEPDLRFISFSTGRRGCPGVKLGTAMTVMLLARLL 407
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
300-445 1.14e-10

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 63.60  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  300 AGHESSGHTIMWATVFLQEHPEVLQRAKAEQEMILksrpegQKGLSLKE--TRKMEFLSQVVDETLRV-----ITFSLTA 372
Cdd:PLN02394 304 AAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVL------GPGNQVTEpdTHKLPYLQAVVKETLRLhmaipLLVPHMN 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  373 FREAKtdveMNGYLIPKGWKVL--TWFrdVHIDPEVFPDPRKFDPARwdngFVPKAGA---------FLPFGAGSHLCPG 441
Cdd:PLN02394 378 LEDAK----LGGYDIPAESKILvnAWW--LANNPELWKNPEEFRPER----FLEEEAKveangndfrFLPFGVGRRSCPG 447

                 ....
gi 15220438  442 NDLA 445
Cdd:PLN02394 448 IILA 451
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
337-464 1.96e-10

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 62.36  E-value: 1.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 337 RPEGQKgLSLKETRKMEFLSQVVDETLRVITFSLTAFREAKTDVEM-----NGYLIPKGWKVLTWFRDVHIDPEVFPDPR 411
Cdd:cd20612 223 LAEIQA-LARENDEADATLRGYVLEALRLNPIAPGLYRRATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPE 301
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15220438 412 KFDPARwdngfvpKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKR 464
Cdd:cd20612 302 RFRLDR-------PLESYIHFGHGPHQCLGEEIARAALTEMLRVVLRLPNLRR 347
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
229-453 2.25e-10

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: 62.34  E-value: 2.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 229 IPGFAY--HRALKARKTLVAAF----QSIVTER-RNQRKQNIlsnkKDMLDNLLNvKDEDGKT-------LDDEEIIDVL 294
Cdd:cd20676 168 IPILRYlpNPAMKRFKDINKRFnsflQKIVKEHyQTFDKDNI----RDITDSLIE-HCQDKKLdenaniqLSDEKIVNIV 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 295 LMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAE-QEMILKSR-PEgqkglsLKETRKMEFLSQVVDETLRVITF-SLT 371
Cdd:cd20676 243 NDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEElDEVIGRERrPR------LSDRPQLPYLEAFILETFRHSSFvPFT 316
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 372 AFREAKTDVEMNGYLIPKGWKVLT--WfrDVHIDPEVFPDPRKFDPARW---DNGFVPKAGA--FLPFGAGSHLCPGNDL 444
Cdd:cd20676 317 IPHCTTRDTSLNGYYIPKDTCVFInqW--QVNHDEKLWKDPSSFRPERFltaDGTEINKTESekVMLFGLGKRRCIGESI 394

                ....*....
gi 15220438 445 AKLEISIFL 453
Cdd:cd20676 395 ARWEVFLFL 403
PLN02971 PLN02971
tryptophan N-hydroxylase
33-471 3.07e-10

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 62.36  E-value: 3.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438   33 LYESSLGENRHYLPPGDLGWPFIGNMLSFLrafKTSDPDSFTRTLIKRYGPKgiYKAHMFGNPSII-VTTSDTCRRVLTD 111
Cdd:PLN02971  46 LKSSSRNKKLHPLPPGPTGFPIVGMIPAML---KNRPVFRWLHSLMKELNTE--IACVRLGNTHVIpVTCPKIAREIFKQ 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  112 DDAFKPGWPTSTMELI---GRKSFVGISF-EEHKRLRRLTAAPVNG-------HEALSTYIPYIEENVITVLdKWTKMGE 180
Cdd:PLN02971 121 QDALFASRPLTYAQKIlsnGYKTCVITPFgEQFKKMRKVIMTEIVCparhrwlHDNRAEETDHLTAWLYNMV-KNSEPVD 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  181 FEFLTH------LRKLTFRIIMYiflsseSENV----------MDALEREYTALNYGVR-------AMAVNIPGFAYHRA 237
Cdd:PLN02971 200 LRFVTRhycgnaIKRLMFGTRTF------SEKTepdggptledIEHMDAMFEGLGFTFAfcisdylPMLTGLDLNGHEKI 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  238 LKARKTLVAAFQS-IVTERRNQRKQNILSNKKDMLDNLLNVKDEDGKTL-DDEEIIDVLLMYLNAGHESSGHTIMWATVF 315
Cdd:PLN02971 274 MRESSAIMDKYHDpIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAMAE 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  316 LQEHPEVLQRAKAEQEMILKSrpegQKGLSLKETRKMEFLSQVVDETLR---VITFSLTAFreAKTDVEMNGYLIPKGWK 392
Cdd:PLN02971 354 MINKPEILHKAMEEIDRVVGK----ERFVQESDIPKLNYVKAIIREAFRlhpVAAFNLPHV--ALSDTTVAGYHIPKGSQ 427
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  393 VLTWFRDVHIDPEVFPDPRKFDPARWDN-----GFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKRSNP 467
Cdd:PLN02971 428 VLLSRYGLGRNPKVWSDPLSFKPERHLNecsevTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGS 507

                 ....
gi 15220438  468 ECPV 471
Cdd:PLN02971 508 ETRV 511
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
225-462 4.84e-10

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: 61.55  E-value: 4.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 225 MAVNIPGFAYHRALKARKTLVAAFQSivtERRNQRKQ--NILSNKKDMLdnllnvkdEDGKTLDDEEIidvllmylnAGH 302
Cdd:cd20632 160 LVANIPIELLGATKSIREKLIKYFLP---QKMAKWSNpsEVIQARQELL--------EQYDVLQDYDK---------AAH 219
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 303 E------SSGHTI---MWATVFLQEHPEVLQRAKAEQEMILKS-----RPEGQKGLSLKETRKMEFLSQVVDETLRVITF 368
Cdd:cd20632 220 HfaflwaSVGNTIpatFWAMYYLLRHPEALAAVRDEIDHVLQStgqelGPDFDIHLTREQLDSLVYLESAINESLRLSSA 299
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 369 SLTaFREAKTDVEMN-----GYLIPKGWKVLTWFRDVHIDPEVFPDPR--KFDpaRW-DNG-----FVpKAGAFL----- 430
Cdd:cd20632 300 SMN-IRVVQEDFTLKlesdgSVNLRKGDIVALYPQSLHMDPEIYEDPEvfKFD--RFvEDGkkkttFY-KRGQKLkyylm 375
                       250       260       270
                ....*....|....*....|....*....|..
gi 15220438 431 PFGAGSHLCPGNDLAKLEISIFLHHFLLKYQV 462
Cdd:cd20632 376 PFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDL 407
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
115-440 8.65e-10

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: 60.60  E-value: 8.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 115 FKPGW---PTSTM--ELIGRKSFVGISFEEHKRLRRLTAAPVNghEALSTYIPYIEENVITVLDKWTKMGEFEFL---TH 186
Cdd:cd20627  27 INPNKtsdPFETMlkSLLGYQSGSGGDASESHVRKKLYENGVT--KALQSNFPLLLKLSEELLDKWLSYPESQHVplcQH 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 187 LRKLTFRIIMYIFLSSESENvmdalEREYTALNYGVRAMAVNI-PGF-------------AYHRALKARKTLVaafQSIV 252
Cdd:cd20627 105 MLGFAMKSVTQMVMGSTFED-----DQEVIRFRKNHDAIWSEIgKGFldgsleksttrkkQYEDALMEMESVL---KKVI 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 253 TERRNQRkqnilSNKKDMLDNLLNvkdedgKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAEQEM 332
Cdd:cd20627 177 KERKGKN-----FSQHVFIDSLLQ------GNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQ 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 333 ILKSRPegqkgLSLKETRKMEFLSQVVDETLRviTFSLTAFREAKTDVE--MNGYLIPKGWKVLTWFRDVHIDPEVFPDP 410
Cdd:cd20627 246 VLGKGP-----ITLEKIEQLRYCQQVLCETVR--TAKLTPVSARLQELEgkVDQHIIPKETLVLYALGVVLQDNTTWPLP 318
                       330       340       350
                ....*....|....*....|....*....|
gi 15220438 411 RKFDPARWDNGFVPKAGAFLPFgAGSHLCP 440
Cdd:cd20627 319 YRFDPDRFDDESVMKSFSLLGF-SGSQECP 347
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
89-441 1.09e-09

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: 60.21  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  89 AHMFGNPSIIVTTSDTCRRVLTDDDAFKPGWPTSTMELIGRKSFVGISFEEHKRLRRLTAAPVNGHEALSTYIPYIEENV 168
Cdd:cd11039  16 AYVPSLRETLVTRRDDIRAVEKDIEVFSSSQPAGLMNVLMGHNMMRKDGEAHACERRAIFPTFSPKTVKSYWAALFRAVV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 169 ITVLDKWTKMGE-FEFLTHLRKLTFRIIMYIF-LSSESENVMDALEReytalnygvrAMAVNIPGFAYHRALKARKT--- 243
Cdd:cd11039  96 QRFLDDIEPGGAaDLFTELAEPVSARCLKDILgLTETSNAELDRWSQ----------AMIDGAGNYSGDPEVEARCDeat 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 244 --LVAAFQSIVTERRNQRKQNILSNkkdmldnLLNVkdedGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPE 321
Cdd:cd11039 166 agIDAAIDALIPVHRSNPNPSLLSV-------MLNA----GMPMSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 322 VLQRAKAEQEMILksrpegqkglslketrkmeflsQVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVH 401
Cdd:cd11039 235 QLAEVMAGDVHWL----------------------RAFEEGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSAN 292
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 15220438 402 IDPEVFPDPRKFDPARwdngfvPKAgAFLPFGAGSHLCPG 441
Cdd:cd11039 293 RDEARFENPDRFDVFR------PKS-PHVSFGAGPHFCAG 325
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
300-477 2.02e-09

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: 59.40  E-value: 2.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 300 AGHESSGHTIMWATVFLQEHPEvlQRAKAEQEMILKSRPEgqkglslketrKMEFLSQVVDETLRVITFSLTAFREAKTD 379
Cdd:cd20624 202 FAFDAAGMALLRALALLAAHPE--QAARAREEAAVPPGPL-----------ARPYLRACVLDAVRLWPTTPAVLRESTED 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 380 VEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARWDNGFVPKAGAFLPFGAGSHLCPGNDLAKLEISIFLHHFL-- 457
Cdd:cd20624 269 TVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLrr 348
                       170       180
                ....*....|....*....|
gi 15220438 458 LKYQVKRSNPECPVMYLPHT 477
Cdd:cd20624 349 AEIDPLESPRSGPGEPLPGT 368
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
252-445 3.69e-09

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: 58.64  E-value: 3.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 252 VTERRNQRKQNILSNK--KDMLDNLLNVKDEdGKTLDDeeiiDVLLMYLN---AGHESSGHTIMWATVFLQEHPEVLQRA 326
Cdd:cd11074 196 VDERKKLGSTKSTKNEglKCAIDHILDAQKK-GEINED----NVLYIVENinvAAIETTLWSIEWGIAELVNHPEIQKKL 270
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 327 KAEQEMILKSRPEgqkgLSLKETRKMEFLSQVVDETLRV-ITFSLTAFREAKTDVEMNGYLIPKGWKVL--TWFrdVHID 403
Cdd:cd11074 271 RDELDTVLGPGVQ----ITEPDLHKLPYLQAVVKETLRLrMAIPLLVPHMNLHDAKLGGYDIPAESKILvnAWW--LANN 344
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15220438 404 PEVFPDPRKFDPARW--DNGFVPKAGA---FLPFGAGSHLCPGNDLA 445
Cdd:cd11074 345 PAHWKKPEEFRPERFleEESKVEANGNdfrYLPFGVGRRSCPGIILA 391
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
316-478 4.30e-08

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: 55.44  E-value: 4.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 316 LQEHPEVLQRAKAEQEMILksrpeGQKGLSLKETRKMEFLSQVVDETLR---VITFSLtafREAKTDVEMNGYLIPKGWK 392
Cdd:cd20616 251 IAQHPEVEEAILKEIQTVL-----GERDIQNDDLQKLKVLENFINESMRyqpVVDFVM---RKALEDDVIDGYPVKKGTN 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 393 VLTWFRDVHIDpEVFPDPRKFDPARWDNGfVPKAgAFLPFGAGSHLCPGNDLAKLEISIFLHHFLLKYQVKrSNPECPVM 472
Cdd:cd20616 323 IILNIGRMHRL-EFFPKPNEFTLENFEKN-VPSR-YFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVC-TLQGRCVE 398

                ....*.
gi 15220438 473 YLPHTR 478
Cdd:cd20616 399 NIQKTN 404
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
257-449 3.61e-07

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 52.39  E-value: 3.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  257 NQRKQNILSNKKDMLDNLLnvkdedGKTLDDEEIIDVLLMYLNAGHE--SSGHTimwaTVF--LQEHPEVLQRAKAEQEM 332
Cdd:PLN02426 267 RQRRKLGFSASKDLLSRFM------ASINDDKYLRDIVVSFLLAGRDtvASALT----SFFwlLSKHPEVASAIREEADR 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  333 ILKsrpEGQKGLSLKETRKMEFLSQVVDETLRV---ITFSlTAFrEAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVF-P 408
Cdd:PLN02426 337 VMG---PNQEAASFEEMKEMHYLHAALYESMRLfppVQFD-SKF-AAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgP 411
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15220438  409 DPRKFDPARW-DNG-FVPKAGAFLP-FGAGSHLCPGNDLAKLEI 449
Cdd:PLN02426 412 DCLEFKPERWlKNGvFVPENPFKYPvFQAGLRVCLGKEMALMEM 455
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
274-452 1.18e-06

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: 50.51  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 274 LLNVKDEdGKtLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQrakaeqemILKSRPEGQKGlslketrkme 353
Cdd:cd20619 177 LLDAARA-GE-ITESEAIATILVFYAVGHMAIGYLIASGIELFARRPEVFT--------AFRNDESARAA---------- 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 354 flsqVVDETLRVITFSLTAFREAKTDVEMNGYLIPKGWKVLTWFRDVHIDPEVFPDPRKFDPARwdngfVPKAGAFLPFG 433
Cdd:cd20619 237 ----IINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTR-----PPAASRNLSFG 307
                       170       180
                ....*....|....*....|
gi 15220438 434 AGSHLCPGNDLAKLEI-SIF 452
Cdd:cd20619 308 LGPHSCAGQIISRAEAtTVF 327
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
236-447 1.20e-06

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


Pssm-ID: 410716 [Multi-domain]  Cd Length: 367  Bit Score: 50.73  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 236 RALKARKTLVAAFQSIVTERRNQRKQNILSNkkdMLDnllnvkdeDGKTLDDEEIIDVLLMYLNAGHESSGHTImwatvf 315
Cdd:cd20623 154 DALAANARLVGALRELVALRRARPGDDLTSR---LLA--------HPAGLTDEEVVHDLVLLLGAGHEPTTNLI------ 216
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 316 lqehpevlqrAKAEQEMILKSRpegqKGLSLKETRKMefLSQVVDETLRVIT-FSLTAFREAKTDVEMNGYLIPKGWKVL 394
Cdd:cd20623 217 ----------GNTLRLMLTDPR----FAASLSGGRLS--VREALNEVLWRDPpLANLAGRFAARDTELGGQWIRAGDLVV 280
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15220438 395 TWFRDVHIDPEVFPDPrkFDPArWDNGfvpkagAFLPFGAGSHLCPGNDLAKL 447
Cdd:cd20623 281 LGLAAANADPRVRPDP--GASM-SGNR------AHLAFGAGPHRCPAQELAET 324
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
228-463 1.44e-06

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 50.78  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  228 NIPGFAYHRALK-ARKTLVAAFQSIVTERRNQR--KQNILSNKKDMLDNLLNVKDEDGKTL---DDEEIIDVLLMYLNAG 301
Cdd:PLN02169 234 NWIGIGLERKMRtALATVNRMFAKIISSRRKEEisRAETEPYSKDALTYYMNVDTSKYKLLkpkKDKFIRDVIFSLVLAG 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  302 HESSGHTIMWATVFLQEHPEVLqrAKAEQEMILKSRPEgqkglslkETRKMEFLSQVVDETLRV---ITFSLTAfrEAKT 378
Cdd:PLN02169 314 RDTTSSALTWFFWLLSKHPQVM--AKIRHEINTKFDNE--------DLEKLVYLHAALSESMRLyppLPFNHKA--PAKP 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  379 DVEMNGYLIPKGWKVLTWFRDVHIDPEVF-PDPRKFDPARW--DNGFVPKAGA--FLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:PLN02169 382 DVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWisDNGGLRHEPSykFMAFNSGPRTCLGKHLALLQMKIVA 461
                        250
                 ....*....|
gi 15220438  454 HHFLLKYQVK 463
Cdd:PLN02169 462 LEIIKNYDFK 471
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
211-447 2.61e-06

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: 49.41  E-value: 2.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 211 LEREYTALnygVRAMAVNIPGFAYHRALKARKTLVAAfqsivterrnqrkqnilsnkkdMLDNLLNVKDEDGKTLDDEEI 290
Cdd:cd11036 124 FARLFAAL---APALDSLLCARALLAARALLRAALAE----------------------LLALTRSAAADALALSAPGDL 178
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 291 IDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRakaeqemiLKSRPEgqkglslketrkmeFLSQVVDETLRVI-TFS 369
Cdd:cd11036 179 VANAILLAVQGAEAAAGLVGNAVLALLRRPAQWAR--------LRPDPE--------------LAAAAVAETLRYDpPVR 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 370 LTAfREAKTDVEMNGYLIPKGWKVLtwfrdVHI-----DPEVFPDPRKFDPARwdngfvPKAGAFlPFGAGSHLCPGNDL 444
Cdd:cd11036 237 LER-RFAAEDLELAGVTLPAGDHVV-----VLLaaanrDPEAFPDPDRFDLGR------PTARSA-HFGLGRHACLGAAL 303

                ...
gi 15220438 445 AKL 447
Cdd:cd11036 304 ARA 306
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
267-453 8.15e-06

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 48.24  E-value: 8.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  267 KKDMLDNLLNVKDEDGKTLDDEEIIDVLLMYLNAGHESSGHTIMWATVFLQEHPEVLQRAKAE-----QEMILKSRPEGQ 341
Cdd:PLN03195 270 KHDILSRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSElkaleKERAKEEDPEDS 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  342 KGLSLKETR-----------KMEFLSQVVDETLRVI-TFSLTAFREAKTDVEMNGYLIPKGWKV-LTWFRDVHIDPEVFP 408
Cdd:PLN03195 350 QSFNQRVTQfaglltydslgKLQYLHAVITETLRLYpAVPQDPKGILEDDVLPDGTKVKAGGMVtYVPYSMGRMEYNWGP 429
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 15220438  409 DPRKFDPARW-DNGFVPKAG--AFLPFGAGSHLCPGNDLAKLEISIFL 453
Cdd:PLN03195 430 DAASFKPERWiKDGVFQNASpfKFTAFQAGPRICLGKDSAYLQMKMAL 477
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
313-441 1.84e-05

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. 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: 410719  Cd Length: 381  Bit Score: 47.02  E-value: 1.84e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438 313 TVFLQEHPEVLQrakaeqEMILKSRPEGQKGLSLKEtrkmeflsqVVDETLR-----------VITFSLTAFREAKTDVE 381
Cdd:cd20626 231 TLRDPTHPEWRE------ANADFAKSATKDGISAKN---------LVKEALRlypptrriyraFQRPGSSKPEIIAADIE 295
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15220438 382 MngylipkgwkvltwfrdVHIDPEVF-PDPRKFDPARWDNGFVPKAGAFLPFGAGSHLCPG 441
Cdd:cd20626 296 A-----------------CHRSESIWgPDALEFNPSRWSKLTPTQKEAFLPFGSGPFRCPA 339
PLN02648 PLN02648
allene oxide synthase
285-460 3.26e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 43.00  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  285 LDDEEIIDVLLMYL--NA-GhessGHTIMWATVF--LQEHPEVLQRAKAEQemILKSRPEGQKGLSLKETRKMEFLSQVV 359
Cdd:PLN02648 267 ISREEALHNLLFVLgfNAfG----GFKIFFPALLkwVGRAGEELQARLAEE--VRSAVKAGGGGVTFAALEKMPLVKSVV 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15220438  360 DETLRVITFSLTAFREAKTDVEM----NGYLIPKGwKVLTWFRD-VHIDPEVFPDPRKFDPAR--------------WDN 420
Cdd:PLN02648 341 YEALRIEPPVPFQYGRAREDFVIeshdAAFEIKKG-EMLFGYQPlVTRDPKVFDRPEEFVPDRfmgeegekllkyvfWSN 419
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 15220438  421 GfvPKAGAflPfGAGSHLCPGNDLAKLEISIFLHHFLLKY 460
Cdd:PLN02648 420 G--RETES--P-TVGNKQCAGKDFVVLVARLFVAELFLRY 454
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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