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Conserved domains on  [gi|145337333|ref|NP_177109|]
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cytochrome P450, family 704, subfamily B, polypeptide 1 [Arabidopsis thaliana]

Protein Classification

cytochrome P450( domain architecture ID 10011029)

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
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
1-524 0e+00

fatty acid omega-hydroxylase; Provisional


:

Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 1024.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   1 MSLCLVIACMVTSWIFLHRWGQRNKSGPKTWPLVGAAIEQLTNFDRMHDWLVEYLYNSRTVVVPMPFTTYTYIADPINVE 80
Cdd:PLN03195   8 MSGVLFIALAVLSWIFIHRWSQRNRKGPKSWPIIGAALEQLKNYDRMHDWLVEYLSKDRTVVVKMPFTTYTYIADPVNVE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  81 YVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILSQASFKEQQ 160
Cdd:PLN03195  88 HVLKTNFANYPKGEVYHSYMEVLLGDGIFNVDGELWRKQRKTASFEFASKNLRDFSTVVFREYSLKLSSILSQASFANQV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 161 VDMQELLMRMTLDSICKVGFGVEIGTLAPELPENHFAKAFDTANIIVTLRFIDPLWKMKKFLNIGSEALLGKSIKVVNDF 240
Cdd:PLN03195 168 VDMQDLFMRMTLDSICKVGFGVEIGTLSPSLPENPFAQAFDTANIIVTLRFIDPLWKLKKFLNIGSEALLSKSIKVVDDF 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 241 TYSVIRRRKAELLEAQISPTnnnnnnnnKVKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMI 320
Cdd:PLN03195 248 TYSVIRRRKAEMDEARKSGK--------KVKHDILSRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 321 MMNENVAEKLYSELQELEKESAEatntslhQYDTEDFNSFNEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDP 400
Cdd:PLN03195 320 MMNPHVAEKLYSELKALEKERAK-------EEDPEDSQSFNQRVTQFAGLLTYDSLGKLQYLHAVITETLRLYPAVPQDP 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 401 KGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQ 480
Cdd:PLN03195 393 KGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWGPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQ 472
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 145337333 481 MKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLKVTVSRRS 524
Cdd:PLN03195 473 MKMALALLCRFFKFQLVPGHPVKYRMMTILSMANGLKVTVSRRS 516
 
Name Accession Description Interval E-value
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
1-524 0e+00

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 1024.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   1 MSLCLVIACMVTSWIFLHRWGQRNKSGPKTWPLVGAAIEQLTNFDRMHDWLVEYLYNSRTVVVPMPFTTYTYIADPINVE 80
Cdd:PLN03195   8 MSGVLFIALAVLSWIFIHRWSQRNRKGPKSWPIIGAALEQLKNYDRMHDWLVEYLSKDRTVVVKMPFTTYTYIADPVNVE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  81 YVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILSQASFKEQQ 160
Cdd:PLN03195  88 HVLKTNFANYPKGEVYHSYMEVLLGDGIFNVDGELWRKQRKTASFEFASKNLRDFSTVVFREYSLKLSSILSQASFANQV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 161 VDMQELLMRMTLDSICKVGFGVEIGTLAPELPENHFAKAFDTANIIVTLRFIDPLWKMKKFLNIGSEALLGKSIKVVNDF 240
Cdd:PLN03195 168 VDMQDLFMRMTLDSICKVGFGVEIGTLSPSLPENPFAQAFDTANIIVTLRFIDPLWKLKKFLNIGSEALLSKSIKVVDDF 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 241 TYSVIRRRKAELLEAQISPTnnnnnnnnKVKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMI 320
Cdd:PLN03195 248 TYSVIRRRKAEMDEARKSGK--------KVKHDILSRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 321 MMNENVAEKLYSELQELEKESAEatntslhQYDTEDFNSFNEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDP 400
Cdd:PLN03195 320 MMNPHVAEKLYSELKALEKERAK-------EEDPEDSQSFNQRVTQFAGLLTYDSLGKLQYLHAVITETLRLYPAVPQDP 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 401 KGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQ 480
Cdd:PLN03195 393 KGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWGPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQ 472
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 145337333 481 MKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLKVTVSRRS 524
Cdd:PLN03195 473 MKMALALLCRFFKFQLVPGHPVKYRMMTILSMANGLKVTVSRRS 516
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
59-516 0e+00

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: 609.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  59 RTVVVPMPF-TTYTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFST 137
Cdd:cd11064    1 FTFRGPWPGgPDGIVTADPANVEHILKTNFDNYPKGPEFRDLFFDLLGDGIFNVDGELWKFQRKTASHEFSSRALREFME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 138 VVFKEYSLK-LFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELPENHFAKAFDTANIIVTLRFI--DP 214
Cdd:cd11064   81 SVVREKVEKlLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPEVPFAKAFDDASEAVAKRFIvpPW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 215 LWKMKKFLNIGSEALLGKSIKVVNDFTYSVIRRRKAELLEAQISptnnnnnnnNKVKHDILSRFIEISDDPDSKETEKSL 294
Cdd:cd11064  161 LWKLKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELNSREEE---------NNVREDLLSRFLASEEEEGEPVSDKFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 295 RDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAeatntslhqydtedfnsfnekvTEFAGLLNYD 374
Cdd:cd11064  232 RDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLT----------------------TDESRVPTYE 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 375 SLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWL-KDGVF 453
Cdd:cd11064  290 ELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWGEDALEFKPERWLdEDGGL 369
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145337333 454 QNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGL 516
Cdd:cd11064  370 RPESPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMKGGL 432
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
26-498 3.64e-53

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: 186.72  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   26 SGPKTWPLVGAAIeQLTNFDRMHDWLVEY------LYNSRtvvvpMPFTTYTYIADPINVEYVLKT---NFSNYPKGETY 96
Cdd:pfam00067   2 PGPPPLPLFGNLL-QLGRKGNLHSVFTKLqkkygpIFRLY-----LGPKPVVVLSGPEAVKEVLIKkgeEFSGRPDEPWF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   97 HSYMEVLLGDGIFNSDGELWRKQRKtasfeFASKNLRDFSTV----VFKEYSLKLFTILSQASFKEQQVDMQELLMRMTL 172
Cdd:pfam00067  76 ATSRGPFLGKGIVFANGPRWRQLRR-----FLTPTFTSFGKLsfepRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  173 DSICKVGFGVEIGTLA-PELPE-------------NHFAKAFDTANIIvtLRFIDPLWKMKKflnigseallgKSIKVVN 238
Cdd:pfam00067 151 NVICSILFGERFGSLEdPKFLElvkavqelssllsSPSPQLLDLFPIL--KYFPGPHGRKLK-----------RARKKIK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  239 DFTYSVIRRRKAELLEAQISPTnnnnnnnnkvkhDILSRFIEISDDPDSKE-TEKSLRDIVLNFVIAGRDTTATTLTWAI 317
Cdd:pfam00067 218 DLLDKLIEERRETLDSAKKSPR------------DFLDALLLAKEEEDGSKlTDEELRATVLELFFAGTDTTSSTLSWAL 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  318 YMIMMNENVAEKLYSELQELEKESAEATntslhqydtedfnsfnekvtefagllnYDSLGKLHYLHAVITETLRLYPAVP 397
Cdd:pfam00067 286 YELAKHPEVQEKLREEIDEVIGDKRSPT---------------------------YDDLQNMPYLDAVIKETLRLHPVVP 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  398 -QDPKGVLEDDMLPnGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDS 476
Cdd:pfam00067 339 lLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVF-PNPEEFDPERFLDENG-KFRKSFAFLPFGAGPRNCLGERL 415
                         490       500
                  ....*....|....*....|..
gi 145337333  477 AYLQMKMAMAILCRFYKFHLVP 498
Cdd:pfam00067 416 ARMEMKLFLATLLQNFEVELPP 437
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
63-523 1.52e-36

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: 139.64  E-value: 1.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  63 VPMPFTTYTYIADPINVEYVLKTNfSNYPKGETYHSYME--VLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVf 140
Cdd:COG2124   37 VRLPGGGAWLVTRYEDVREVLRDP-RTFSSDGGLPEVLRplPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 141 KEYSLKLFtilsqASFKEQ-QVDMQELLMRMTLDSICKVGFGVeigtlapelPENHFAKAFDTANIIVTLRFIDPLWKMK 219
Cdd:COG2124  115 REIADELL-----DRLAARgPVDLVEEFARPLPVIVICELLGV---------PEEDRDRLRRWSDALLDALGPLPPERRR 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 220 KFLnigseallgKSIKVVNDFTYSVIRRRKAELleaqisptnnnnnnnnkvKHDILSRFIEISDDpDSKETEKSLRDIVL 299
Cdd:COG2124  181 RAR---------RARAELDAYLRELIAERRAEP------------------GDDLLSALLAARDD-GERLSDEELRDELL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 300 NFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnekvtefagllnydslgkl 379
Cdd:COG2124  233 LLLLAGHETTANALAWALYALLRHPEQLARLRAEP--------------------------------------------- 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 380 HYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERwlkdgvfqnaSPF 459
Cdd:COG2124  268 ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVF-PDPDRFDPDR----------PPN 335
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145337333 460 KFTAFQAGPRICLGKDSAYLQMKMAMA-ILCRFYKFHLVPNHPVKYRMMTILSMAHGLKVTVSRR 523
Cdd:COG2124  336 AHLPFGGGPHRCLGAALARLEARIALAtLLRRFPDLRLAPPEELRWRPSLTLRGPKSLPVRLRPR 400
 
Name Accession Description Interval E-value
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
1-524 0e+00

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 1024.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   1 MSLCLVIACMVTSWIFLHRWGQRNKSGPKTWPLVGAAIEQLTNFDRMHDWLVEYLYNSRTVVVPMPFTTYTYIADPINVE 80
Cdd:PLN03195   8 MSGVLFIALAVLSWIFIHRWSQRNRKGPKSWPIIGAALEQLKNYDRMHDWLVEYLSKDRTVVVKMPFTTYTYIADPVNVE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  81 YVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILSQASFKEQQ 160
Cdd:PLN03195  88 HVLKTNFANYPKGEVYHSYMEVLLGDGIFNVDGELWRKQRKTASFEFASKNLRDFSTVVFREYSLKLSSILSQASFANQV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 161 VDMQELLMRMTLDSICKVGFGVEIGTLAPELPENHFAKAFDTANIIVTLRFIDPLWKMKKFLNIGSEALLGKSIKVVNDF 240
Cdd:PLN03195 168 VDMQDLFMRMTLDSICKVGFGVEIGTLSPSLPENPFAQAFDTANIIVTLRFIDPLWKLKKFLNIGSEALLSKSIKVVDDF 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 241 TYSVIRRRKAELLEAQISPTnnnnnnnnKVKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMI 320
Cdd:PLN03195 248 TYSVIRRRKAEMDEARKSGK--------KVKHDILSRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMI 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 321 MMNENVAEKLYSELQELEKESAEatntslhQYDTEDFNSFNEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDP 400
Cdd:PLN03195 320 MMNPHVAEKLYSELKALEKERAK-------EEDPEDSQSFNQRVTQFAGLLTYDSLGKLQYLHAVITETLRLYPAVPQDP 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 401 KGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQ 480
Cdd:PLN03195 393 KGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWGPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQ 472
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....
gi 145337333 481 MKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLKVTVSRRS 524
Cdd:PLN03195 473 MKMALALLCRFFKFQLVPGHPVKYRMMTILSMANGLKVTVSRRS 516
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
59-516 0e+00

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: 609.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  59 RTVVVPMPF-TTYTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFST 137
Cdd:cd11064    1 FTFRGPWPGgPDGIVTADPANVEHILKTNFDNYPKGPEFRDLFFDLLGDGIFNVDGELWKFQRKTASHEFSSRALREFME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 138 VVFKEYSLK-LFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELPENHFAKAFDTANIIVTLRFI--DP 214
Cdd:cd11064   81 SVVREKVEKlLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPEVPFAKAFDDASEAVAKRFIvpPW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 215 LWKMKKFLNIGSEALLGKSIKVVNDFTYSVIRRRKAELLEAQISptnnnnnnnNKVKHDILSRFIEISDDPDSKETEKSL 294
Cdd:cd11064  161 LWKLKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELNSREEE---------NNVREDLLSRFLASEEEEGEPVSDKFL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 295 RDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAeatntslhqydtedfnsfnekvTEFAGLLNYD 374
Cdd:cd11064  232 RDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLT----------------------TDESRVPTYE 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 375 SLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWL-KDGVF 453
Cdd:cd11064  290 ELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWGEDALEFKPERWLdEDGGL 369
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145337333 454 QNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGL 516
Cdd:cd11064  370 RPESPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMKGGL 432
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
44-524 7.48e-125

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 374.41  E-value: 7.48e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  44 FDRMHDWLVEYLYNSRTVVVPMPFTTYTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTA 123
Cdd:PLN02426  59 FDNLCDWYAHLLRRSPTGTIHVHVLGNTITANPENVEYMLKTRFDNYPKGKPFSAILGDLLGRGIFNVDGDSWRFQRKMA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 124 SFEFASKNLRDFS-TVVFKEYSLKLFTILSQASFKEQQ--VDMQELLMRMTLDSICKVGFGVEIGTLAPELPENHFAKAF 200
Cdd:PLN02426 139 SLELGSVSIRSYAfEIVASEIESRLLPLLSSAADDGEGavLDLQDVFRRFSFDNICKFSFGLDPGCLELSLPISEFADAF 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 201 DTANIIVTLRFIDP---LWKMKKFLNIGSEALLGKSIKVVNDFTYSVIRRRKAELLEAQisptnnnnnnnnkvkHDILSR 277
Cdd:PLN02426 219 DTASKLSAERAMAAsplLWKIKRLLNIGSERKLKEAIKLVDELAAEVIRQRRKLGFSAS---------------KDLLSR 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 278 FIEISDDpdsketEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATNtslhqydtedf 357
Cdd:PLN02426 284 FMASIND------DKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAAS----------- 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 358 nsfnekvtefagllnYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGS 437
Cdd:PLN02426 347 ---------------FEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWGP 411
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 438 DAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLV--PNHPVKYRMMTILSMAHG 515
Cdd:PLN02426 412 DCLEFKPERWLKNGVFVPENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVgrSNRAPRFAPGLTATVRGG 491

                 ....*....
gi 145337333 516 LKVTVSRRS 524
Cdd:PLN02426 492 LPVRVRERV 500
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
59-518 4.45e-77

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: 248.63  E-value: 4.45e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  59 RTVVVPMPFTTYTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFStv 138
Cdd:cd11063    3 NTFEVNLLGTRVIFTIEPENIKAVLATQFKDFGLGERRRDAFKPLLGDGIFTSDGEEWKHSRALLRPQFSRDQISDLE-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 139 VFKEYSLKLFTILSQasfKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELPENH---FAKAFDTANIIVTLRFIdpL 215
Cdd:cd11063   81 LFERHVQNLIKLLPR---DGSTVDLQDLFFRLTLDSATEFLFGESVDSLKPGGDSPPaarFAEAFDYAQKYLAKRLR--L 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 216 WKMKKFLNIGSealLGKSIKVVNDFTYSVIRRRKAELLEAQisptnnnnNNNNKVKHDILSRFIEISDDPdsketeKSLR 295
Cdd:cd11063  156 GKLLWLLRDKK---FREACKVVHRFVDPYVDKALARKEESK--------DEESSDRYVFLDELAKETRDP------KELR 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 296 DIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATntslhqydtedfnsfnekvtefagllnYDS 375
Cdd:cd11063  219 DQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPT---------------------------YED 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 376 LGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLP-----NGTK---VKAGGMVTYVPYSMGRMEYNWGSDAALFKPERW 447
Cdd:cd11063  272 LKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLPrgggpDGKSpifVPKGTRVLYSVYAMHRRKDIWGPDAEEFRPERW 351
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145337333 448 LKDGvfqnASPFKFTAFQAGPRICLGKDSAYLQMKMAMA-ILCRFYKFHLVPNHPVKYRMMTILSMAHGLKV 518
Cdd:cd11063  352 EDLK----RPGWEYLPFNGGPRICLGQQFALTEASYVLVrLLQTFDRIESRDVRPPEERLTLTLSNANGVKV 419
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
29-523 3.65e-73

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 240.68  E-value: 3.65e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  29 KTWPLVGAAIEQLTNFDRMHDWLVEYLYNSR-TVVVPMPFTTYT---YIADPINVEYVLKTNFSNYPKGETYHSYMEVLl 104
Cdd:PLN02169  37 KNWPFLGMLPGMLHQIPRIYDWTVEVLEASNlTFYFKGPWLSGTdmlFTADPKNIHHILSSNFGNYPKGPEFKKIFDVL- 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 105 GDGIFNSDGELWRKQRKTASFEFASKNLRDFStVVFKEYSLK--LFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGV 182
Cdd:PLN02169 116 GEGILTVDFELWEDLRKSNHALFHNQDFIELS-LSSNKSKLKegLVPFLDNAAHENIIIDLQDVFMRFMFDTSSILMTGY 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 183 EIGTLAPELPENHFAKAFDTANIIVTLRFIDP--LWKMKKFLNIGSEALLGKSIKVVNDFTYSVIR-RRKAELLEAQISP 259
Cdd:PLN02169 195 DPMSLSIEMLEVEFGEAADIGEEAIYYRHFKPviLWRLQNWIGIGLERKMRTALATVNRMFAKIISsRRKEEISRAETEP 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 260 TnnnnnnnnkvKHDILSRFIEIsDDPDSK----ETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELq 335
Cdd:PLN02169 275 Y----------SKDALTYYMNV-DTSKYKllkpKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI- 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 336 elekesaeatNTslhQYDTEDfnsfnekvtefagllnydsLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKV 415
Cdd:PLN02169 343 ----------NT---KFDNED-------------------LEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHKV 390
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 416 KAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKD-GVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKF 494
Cdd:PLN02169 391 DAESKIVICIYALGRMRSVWGEDALDFKPERWISDnGGLRHEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDF 470
                        490       500
                 ....*....|....*....|....*....
gi 145337333 495 HLVPNHPVKYRMMTILSMAHGLKVTVSRR 523
Cdd:PLN02169 471 KVIEGHKIEAIPSILLRMKHGLKVTVTKK 499
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
73-518 4.27e-73

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: 238.19  E-value: 4.27e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKTNfSNYPKGETYHsYMEVLLGDGIFNSDGELWRKQRK--TASFEFasKNLRDFsTVVFKEYSLKLFTI 150
Cdd:cd20628   16 VTNPEDIEVILSSS-KLITKSFLYD-FLKPWLGDGLLTSTGEKWRKRRKllTPAFHF--KILESF-VEVFNENSKILVEK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 151 LsQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGtlAPELPENHFAKAFDTANIIVTLRFIDPLWKMKKFLNIGSEA-L 229
Cdd:cd20628   91 L-KKKAGGGEFDIFPYISLCTLDIICETAMGVKLN--AQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFIFRLTSLGkE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 230 LGKSIKVVNDFTYSVIRRRKAELLEAQISPTNNNNNNNNKvKHDILSRFIEISDDPDSKeTEKSLRDIVLNFVIAGRDTT 309
Cdd:cd20628  168 QRKALKVLHDFTNKVIKERREELKAEKRNSEEDDEFGKKK-RKAFLDLLLEAHEDGGPL-TDEDIREEVDTFMFAGHDTT 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 310 ATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedFNSFNEKVTefagllnYDSLGKLHYLHAVITET 389
Cdd:cd20628  246 ASAISFTLYLLGLHPEVQEKVYEELDEI-------------------FGDDDRRPT-------LEDLNKMKYLERVIKET 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 390 LRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVfQNASPFKFTAFQAGPR 469
Cdd:cd20628  300 LRLYPSVPFIGRRLTEDIKL-DGYTIPKGTTVVISIYALHRNPEYF-PDPEKFDPDRFLPENS-AKRHPYAYIPFSAGPR 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 145337333 470 ICLGKDSAYLQMKMAMAILCRFYKFH-LVPNHPVKYRMMTILSMAHGLKV 518
Cdd:cd20628  377 NCIGQKFAMLEMKTLLAKILRNFRVLpVPPGEDLKLIAEIVLRSKNGIRV 426
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
60-518 9.24e-72

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: 234.40  E-value: 9.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  60 TVVVPMPFTTYTYIADPINVEYVLKTNFSNYPKGETYHsYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVV 139
Cdd:cd20620    3 VVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYE-RLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 140 FkEYSLKLFTILSQASfKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELpenhfAKAFDTANIIVTLRFIDPLWKMK 219
Cdd:cd20620   82 V-EATAALLDRWEAGA-RRGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEI-----GDALDVALEYAARRMLSPFLLPL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 220 KFLNIGSEALLgKSIKVVNDFTYSVIRRRKAElleaqisptnnnnnnnNKVKHDILSRFIeISDDPDSKE--TEKSLRDI 297
Cdd:cd20620  155 WLPTPANRRFR-RARRRLDEVIYRLIAERRAA----------------PADGGDLLSMLL-AARDEETGEpmSDQQLRDE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 298 VLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKesaeatntslhqydtedfnsfnekvtefAGLLNYDSLG 377
Cdd:cd20620  217 VMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG----------------------------GRPPTAEDLP 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 378 KLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPnGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVfQNAS 457
Cdd:cd20620  269 QLPYTEMVLQESLRLYPPAWIIGREAVEDDEIG-GYRIPAGSTVLISPYVTHRDPRFW-PDPEAFDPERFTPERE-AARP 345
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145337333 458 PFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLKV 518
Cdd:cd20620  346 RYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPVEPEPLITLRPKNGVRM 406
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
72-506 2.16e-71

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: 234.09  E-value: 2.16e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  72 YIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVvFKEYSLKLF--- 148
Cdd:cd11069   17 LVTDPKALKHILVTNSYDFEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPI-FWSKAEELVdkl 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 -TILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPelPENHFAKAFDTA-------NIIVTLRFIDPLWkMKK 220
Cdd:cd11069   96 eEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLEN--PDNELAEAYRRLfeptllgSLLFILLLFLPRW-LVR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 221 FLNIGSEALLGKSIKVVNDFTYSVIRRRKAELLEAQISPTNnnnnnnnkvkhDILSRFIEISD-DPDSKETEKSLRDIVL 299
Cdd:cd11069  173 ILPWKANREIRRAKDVLRRLAREIIREKKAALLEGKDDSGK-----------DILSILLRANDfADDERLSDEELIDQIL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 300 NFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESaeatntslhqydtedfnsfnekvteFAGLLNYDSLGKL 379
Cdd:cd11069  242 TFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDP-------------------------PDGDLSYDDLDRL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 380 HYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKDGVFQN---- 455
Cdd:cd11069  297 PYLNAVCRETLRLYPPVPLTSREATKDTVI-KGVPIPKGTVVLIPPAAINRSPEIWGPDAEEFNPERWLEPDGAASpgga 375
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145337333 456 ASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRM 506
Cdd:cd11069  376 GSNYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVERPI 426
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
61-517 1.98e-63

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: 211.99  E-value: 1.98e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  61 VVVPMPFTTYTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVF 140
Cdd:cd00302    4 FRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 141 KEYSLKLFTILSQAsfkEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPElpenhFAKAFDTANIIVTLRFIDPLWKmkk 220
Cdd:cd00302   84 EIARELLDRLAAGG---EVGDDVADLAQPLALDVIARLLGGPDLGEDLEE-----LAELLEALLKLLGPRLLRPLPS--- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 221 flniGSEALLGKSIKVVNDFTYSVIRRRKAELleaqisptnnnnnnnnkvkHDILSRFIEISDDPDSKETEKSLRDIVLN 300
Cdd:cd00302  153 ----PRLRRLRRARARLRDYLEELIARRRAEP-------------------ADDLDLLLLADADDGGGLSDEEIVAELLT 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 301 FVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESaeatntslhqydtedfnsfnekvtefagllNYDSLGKLH 380
Cdd:cd00302  210 LLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG------------------------------TPEDLSKLP 259
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 381 YLHAVITETLRLYPAVPQDPKGVLEDDMLPnGTKVKAGGMVTYVPYSMGRMEyNWGSDAALFKPERWLKDGVfqnASPFK 460
Cdd:cd00302  260 YLEAVVEETLRLYPPVPLLPRVATEDVELG-GYTIPAGTLVLLSLYAAHRDP-EVFPDPDEFDPERFLPERE---EPRYA 334
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145337333 461 FTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLK 517
Cdd:cd00302  335 HLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRPSLGTLGPASLP 391
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
45-510 3.06e-53

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: 185.80  E-value: 3.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  45 DRMHDWLVEYlynSRTVVVPMPFTTYTYIADPINVEYVLKTnfSNYPK-GETYHS----YMEVLLGDGIF-NSDGELWRK 118
Cdd:cd20613    2 DLLLEWAKEY---GPVFVFWILHRPIVVVSDPEAVKEVLIT--LNLPKpPRVYSRlaflFGERFLGNGLVtEVDHEKWKK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 119 QRKTASFEFASKNLRDFsTVVFKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLapELPENHFAK 198
Cdd:cd20613   77 RRAILNPAFHRKYLKNL-MDEFNESADLLVEKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSI--EDPDSPFPK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 199 AFDTANIIVTLRFIDPLWKMKKFlNIGSEALLGKSIKVVNDFTYSVIRRRKAELLEAQISPtnnnnnnnnkvkHDILSRF 278
Cdd:cd20613  154 AISLVLEGIQESFRNPLLKYNPS-KRKYRREVREAIKFLRETGRECIEERLEALKRGEEVP------------NDILTHI 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 279 IEISDDPDSKETEKSLRDIVlNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfn 358
Cdd:cd20613  221 LKASEEEPDFDMEELLDDFV-TFFIAGQETTANLLSFTLLELGRHPEILKRLQAEV------------------------ 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 359 sfnEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKgVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSD 438
Cdd:cd20613  276 ---DEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSR-ELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYF-ED 350
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145337333 439 AALFKPERWLKDgVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTIL 510
Cdd:cd20613  351 PLKFDPERFSPE-APEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELVPGQSFGILEEVTL 421
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
26-498 3.64e-53

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: 186.72  E-value: 3.64e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   26 SGPKTWPLVGAAIeQLTNFDRMHDWLVEY------LYNSRtvvvpMPFTTYTYIADPINVEYVLKT---NFSNYPKGETY 96
Cdd:pfam00067   2 PGPPPLPLFGNLL-QLGRKGNLHSVFTKLqkkygpIFRLY-----LGPKPVVVLSGPEAVKEVLIKkgeEFSGRPDEPWF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   97 HSYMEVLLGDGIFNSDGELWRKQRKtasfeFASKNLRDFSTV----VFKEYSLKLFTILSQASFKEQQVDMQELLMRMTL 172
Cdd:pfam00067  76 ATSRGPFLGKGIVFANGPRWRQLRR-----FLTPTFTSFGKLsfepRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAAL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  173 DSICKVGFGVEIGTLA-PELPE-------------NHFAKAFDTANIIvtLRFIDPLWKMKKflnigseallgKSIKVVN 238
Cdd:pfam00067 151 NVICSILFGERFGSLEdPKFLElvkavqelssllsSPSPQLLDLFPIL--KYFPGPHGRKLK-----------RARKKIK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  239 DFTYSVIRRRKAELLEAQISPTnnnnnnnnkvkhDILSRFIEISDDPDSKE-TEKSLRDIVLNFVIAGRDTTATTLTWAI 317
Cdd:pfam00067 218 DLLDKLIEERRETLDSAKKSPR------------DFLDALLLAKEEEDGSKlTDEELRATVLELFFAGTDTTSSTLSWAL 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  318 YMIMMNENVAEKLYSELQELEKESAEATntslhqydtedfnsfnekvtefagllnYDSLGKLHYLHAVITETLRLYPAVP 397
Cdd:pfam00067 286 YELAKHPEVQEKLREEIDEVIGDKRSPT---------------------------YDDLQNMPYLDAVIKETLRLHPVVP 338
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  398 -QDPKGVLEDDMLPnGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDS 476
Cdd:pfam00067 339 lLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVF-PNPEEFDPERFLDENG-KFRKSFAFLPFGAGPRNCLGERL 415
                         490       500
                  ....*....|....*....|..
gi 145337333  477 AYLQMKMAMAILCRFYKFHLVP 498
Cdd:pfam00067 416 ARMEMKLFLATLLQNFEVELPP 437
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
73-517 2.84e-50

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: 177.78  E-value: 2.84e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKTNFSNYPkGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVfKEYSLKLFTILS 152
Cdd:cd11055   18 VSDPEMIKEILVKEFSNFT-NRPLFILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKLMVPII-NDCCDELVEKLE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 153 QASFKEQQVDMQELLMRMTLDSICKVGFGVEigTLAPELPENHFAKAF-------DTANIIVTLRFIDPLWKMKKFLNIG 225
Cdd:cd11055   96 KAAETGKPVDMKDLFQGFTLDVILSTAFGID--VDSQNNPDDPFLKAAkkifrnsIIRLFLLLLLFPLRLFLFLLFPFVF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 226 SeallGKSIKVVNDFTYSVIRRRKAELleaqisptnnnnnnnNKVKHDILSRFIEISDDpDSKETEKSL--RDIVLN--- 300
Cdd:cd11055  174 G----FKSFSFLEDVVKKIIEQRRKNK---------------SSRRKDLLQLMLDAQDS-DEDVSKKKLtdDEIVAQsfi 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 301 FVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESaeatntslhqydtedfnsfnekvtefaGLLNYDSLGKLH 380
Cdd:cd11055  234 FLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDD---------------------------GSPTYDTVSKLK 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 381 YLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWGsDAALFKPERWLKDGVfQNASPFK 460
Cdd:cd11055  287 YLDMVINETLRLYPPAFFISRECKEDCTI-NGVFIPKGVDVVIPVYAIHHDPEFWP-DPEKFDPERFSPENK-AKRHPYA 363
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145337333 461 FTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH--PVKYRMMTILSMAHGLK 517
Cdd:cd11055  364 YLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETeiPLKLVGGATLSPKNGIY 422
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
69-517 8.02e-50

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: 177.17  E-value: 8.02e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  69 TYTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVvFKEYSLKLF 148
Cdd:cd11046   22 SFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRV-FGRCSERLM 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 TILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELP-----------ENHFAKAFDTANIIVTLRFIDPLWK 217
Cdd:cd11046  101 EKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTEESPvikavylplveAEHRSVWEPPYWDIPAALFIVPRQR 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 218 mkKFLnigseallgKSIKVVNDFTYSVIRRRKAELLEAQISPTNNNNNnnnKVKHDILSRFIEISDDPDSkeTEKSLRDI 297
Cdd:cd11046  181 --KFL---------RDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYL---NEDDPSLLRFLVDMRDEDV--DSKQLRDD 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 298 VLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATntslhqydtedfnsfnekvtefagllnYDSLG 377
Cdd:cd11046  245 LMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPT---------------------------YEDLK 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 378 KLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGT-KVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVF--- 453
Cdd:cd11046  298 KLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGGvKVPAGTDIFISVYNLHRSPELW-EDPEEFDPERFLDPFINppn 376
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145337333 454 QNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPnhPVKYRMMTILSMAH---GLK 517
Cdd:cd11046  377 EVIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDV--GPRHVGMTTGATIHtknGLK 441
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
73-522 8.60e-49

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: 174.44  E-value: 8.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKtNFSNYPKGETYHSYMEVLlGDGIFNSDGELWRKQRK--TASFEFASkNLRDFSTVVfkEYSLKLFTI 150
Cdd:cd11070   17 VTKPEYLTQIFR-RRDDFPKPGNQYKIPAFY-GPNVISSEGEDWKRYRKivAPAFNERN-NALVWEESI--RQAQRLIRY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 151 L--SQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLapelpeNHFAKAFDTANIIVTLRFIDPLWKMKKFLnigsEA 228
Cdd:cd11070   92 LleEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPAL------DEEESSLHDTLNAIKLAIFPPLFLNFPFL----DR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 229 LLGKSIKVVNDfTYSVIRRRKAELL---EAQISPTNNNNNNNNKVKHDILSRfieisDDPDSKETEKSLRDIVLNFVIAG 305
Cdd:cd11070  162 LPWVLFPSRKR-AFKDVDEFLSELLdevEAELSADSKGKQGTESVVASRLKR-----ARRSGGLTEKELLGNLFIFFIAG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 306 RDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeATNTSLHQYDTEDFNsfnekvtefagllnydslgKLHYLHAV 385
Cdd:cd11070  236 HETTANTLSFALYLLAKHPEVQDWLREEIDSV------LGDEPDDWDYEEDFP-------------------KLPYLLAV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 386 ITETLRLYPAVPQDPKGVLEDDM----LPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKD-GVFQNASPFK 460
Cdd:cd11070  291 IYETLRLYPPVQLLNRKTTEPVVvitgLGQEIVIPKGTYVGYNAYATHRDPTIWGPDADEFDPERWGSTsGEIGAATRFT 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 461 -----FTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVK-YRMMTILSMAHGLKVTVSR 522
Cdd:cd11070  371 pargaFIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRVDPEWEEGeTPAGATRDSPAKLRLRFRE 438
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
82-518 9.19e-49

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: 173.90  E-value: 9.19e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  82 VLKTNFsnyPKGETYHSYMEVLLGDGIFNSDGELWRKQRK--TASFEFasKNLRDFSTVvFKEYSLKLFTILSQASFKEQ 159
Cdd:cd20659   26 VLKTSE---PKDRDSYRFLKPWLGDGLLLSNGKKWKRNRRllTPAFHF--DILKPYVPV-YNECTDILLEKWSKLAETGE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 160 QVDMQELLMRMTLDSICKVGFGVEiGTLAPELPENHFAKAFDTANIIVTLRF------IDPLWKM----KKFLnigseal 229
Cdd:cd20659  100 SVEVFEDISLLTLDIILRCAFSYK-SNCQQTGKNHPYVAAVHELSRLVMERFlnpllhFDWIYYLtpegRRFK------- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 230 lgKSIKVVNDFTYSVIRRRKAELlEAQISPtnnnnnNNNKVKH----DILsrfIEISDDPDSKETEKSLRDIVLNFVIAG 305
Cdd:cd20659  172 --KACDYVHKFAEEIIKKRRKEL-EDNKDE------ALSKRKYldflDIL---LTARDEDGKGLTDEEIRDEVDTFLFAG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 306 RDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntsLHQYDTedfnsfnekvtefaglLNYDSLGKLHYLHAV 385
Cdd:cd20659  240 HDTTASGISWTLYSLAKHPEHQQKCREEVDEV-----------LGDRDD----------------IEWDDLSKLPYLTMC 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 386 ITETLRLYPAVPQDPKGVLEDDMLPnGTKVKAGGMVTYVPYSMGRMEyNWGSDAALFKPERWLKDgVFQNASPFKFTAFQ 465
Cdd:cd20659  293 IKESLRLYPPVPFIARTLTKPITID-GVTLPAGTLIAINIYALHHNP-TVWEDPEEFDPERFLPE-NIKKRDPFAFIPFS 369
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145337333 466 AGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLKV 518
Cdd:cd20659  370 AGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPGLVLRSKNGIKL 422
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
64-494 1.05e-48

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: 173.56  E-value: 1.05e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  64 PMPFTtytYIADPINVEYVLkTNFSNYPKgetYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVvFKEY 143
Cdd:cd11057   10 PRPFV---ITSDPEIVQVVL-NSPHCLNK---SFFYDFFRLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPI-FNEE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 144 SLKLFTILsQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPElpENHFAKAFDTANIIVTLRFIDPlWKMKKFLN 223
Cdd:cd11057   82 AQKLVQRL-DTYVGGGEFDILPDLSRCTLEMICQTTLGSDVNDESDG--NEEYLESYERLFELIAKRVLNP-WLHPEFIY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 224 --IGSEALLGKSIKVVNDFTYSVIRRRKAELLEAQISPTNNNNNNNNKVKhdIlsrFIE-ISDDPDSKE--TEKSLRDIV 298
Cdd:cd11057  158 rlTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLDSEEDEENGRKPQ--I---FIDqLLELARNGEefTDEEIMDEI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 299 LNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESaeatntslhqydtEDFNSfnekvtefagllnYDSLGK 378
Cdd:cd11057  233 DTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDD-------------GQFIT-------------YEDLQQ 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 379 LHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKDGVfQNASP 458
Cdd:cd11057  287 LVYLEMVLKETMRLFPVGPLVGRETTADIQLSNGVVIPKGTTIVIDIFNMHRRKDIWGPDADQFDPDNFLPERS-AQRHP 365
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 145337333 459 FKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKF 494
Cdd:cd11057  366 YAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRL 401
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
107-510 2.17e-44

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: 161.93  E-value: 2.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 107 GIFNSDGELWRKQRKTASFEFAS-KNLRDFSTVvFKEYSLKLFTILSQASFKEQQV--DMQELLMRMTLDSICKVGFGVE 183
Cdd:cd11054   57 GLLNSNGEEWHRLRSAVQKPLLRpKSVASYLPA-INEVADDFVERIRRLRDEDGEEvpDLEDELYKWSLESIGTVLFGKR 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 184 IGTLAPELPENH--FAKAFDTANI-IVTLRFIDPLWKM------KKFlnigsEALLGKSIKVVNDFTYSVIRRRKAELLE 254
Cdd:cd11054  136 LGCLDDNPDSDAqkLIEAVKDIFEsSAKLMFGPPLWKYfptpawKKF-----VKAWDTIFDIASKYVDEALEELKKKDEE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 255 AQISPTnnnnnnnnkvkhdILSRFIeiSDDPDSKETEKSlrdIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSEL 334
Cdd:cd11054  211 DEEEDS-------------LLEYLL--SKPGLSKKEIVT---MALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEI 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 335 QElekesaeatntslhqydtedfnsfnekVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPqdpkG---VLEDDMLPN 411
Cdd:cd11054  273 RS---------------------------VLPDGEPITAEDLKKMPYLKACIKESLRLYPVAP----GngrILPKDIVLS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 412 GTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDG-VFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCR 490
Cdd:cd11054  322 GYHIPKGTLVVLSNYVMGRDEEYF-PDPEEFIPERWLRDDsENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQ 400
                        410       420
                 ....*....|....*....|.
gi 145337333 491 fyKFHLVPNH-PVKYRMMTIL 510
Cdd:cd11054  401 --NFKVEYHHeELKVKTRLIL 419
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
72-509 3.46e-42

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: 155.96  E-value: 3.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  72 YIADPINVEYVLKTNFSnYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTIL 151
Cdd:cd11052   26 YVTEPELIKELLSKKEG-YFGKSPLQPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKGMVPAMVESVSDMLERWK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 152 SQASFKEQQVDMQELLMRMTLDSICKVGFGV--EIGTlapELPENHFAKAFDTANIIVTLRFidPLWK-MKKFLNIGSEA 228
Cdd:cd11052  105 KQMGEEGEEVDVFEEFKALTADIISRTAFGSsyEEGK---EVFKLLRELQKICAQANRDVGI--PGSRfLPTKGNKKIKK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 229 LLgksiKVVNDFTYSVIRRRKAELLEAQISPTnnnnnnnnkvKHDILSRFIEiSDDPDSKETEKSLRDIVLN---FVIAG 305
Cdd:cd11052  180 LD----KEIEDSLLEIIKKREDSLKMGRGDDY----------GDDLLGLLLE-ANQSDDQNKNMTVQEIVDEcktFFFAG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 306 RDTTATTLTWAIYMIMMNENVAEKLYSELQELEKEsaeatntslhqydtedfnsfnekvtefaGLLNYDSLGKLHYLHAV 385
Cdd:cd11052  245 HETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGK----------------------------DKPPSDSLSKLKTVSMV 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 386 ITETLRLYPAVPQDPKGVLEDDMLpnGTKVKAGGMVTYVP-YSMGRMEYNWGSDAALFKPERWlKDGVFQ-NASPFKFTA 463
Cdd:cd11052  297 INESLRLYPPAVFLTRKAKEDIKL--GGLVIPKGTSIWIPvLALHHDEEIWGEDANEFNPERF-ADGVAKaAKHPMAFLP 373
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145337333 464 FQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNhpvkYR-----MMTI 509
Cdd:cd11052  374 FGLGPRNCIGQNFATMEAKIVLAMILQRFSFTLSPT----YRhaptvVLTL 420
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
88-501 7.37e-42

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: 155.07  E-value: 7.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  88 SNYPKGETYHSYmeVLLGDGIFNS-DGELWRKQRKTASFEFASKNLRDFSTVVfKEYSLKLFTILSQASFKEQQ--VDMQ 164
Cdd:cd11061   27 SNCLKGPFYDAL--SPSASLTFTTrDKAEHARRRRVWSHAFSDKALRGYEPRI-LSHVEQLCEQLDDRAGKPVSwpVDMS 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 165 ELLMRMTLDSICKVGFGVEIGTLapELPENHFA-----KAFDTANIIVTLRFIDPLWKMKKFLNIGSEALLGksikvVND 239
Cdd:cd11061  104 DWFNYLSFDVMGDLAFGKSFGML--ESGKDRYIldlleKSMVRLGVLGHAPWLRPLLLDLPLFPGATKARKR-----FLD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 240 FTYSVIRRRKAELLEAqisptnnnnnnnnkvKHDILSRFIEISD-DPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIY 318
Cdd:cd11061  177 FVRAQLKERLKAEEEK---------------RPDIFSYLLEAKDpETGEGLDLEELVGEARLLIVAGSDTTATALSAIFY 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 319 MIMMNENVAEKLYSELQELEKESAEATntslhqydtedfnsfnekvtefagllNYDSLGKLHYLHAVITETLRLYPAVP- 397
Cdd:cd11061  242 YLARNPEAYEKLRAELDSTFPSDDEIR--------------------------LGPKLKSLPYLRACIDEALRLSPPVPs 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 398 ----QDPKGVLEDD--MLPNGTKVKAGgmvtyvPYSMGRMEYNWgSDAALFKPERWL--KDGVFQNASPfkFTAFQAGPR 469
Cdd:cd11061  296 glprETPPGGLTIDgeYIPGGTTVSVP------IYSIHRDERYF-PDPFEFIPERWLsrPEELVRARSA--FIPFSIGPR 366
                        410       420       430
                 ....*....|....*....|....*....|..
gi 145337333 470 ICLGKDSAYLQMKMAMAILCRFYKFHLVPNHP 501
Cdd:cd11061  367 GCIGKNLAYMELRLVLARLLHRYDFRLAPGED 398
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
73-506 3.49e-41

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: 153.25  E-value: 3.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKtnfsNYPKGETYHSYMEVLL----GDGIFNSDGELWRKQRKTASFEFASKNLRDFstvvfkEYSLKLF 148
Cdd:cd11083   16 ISDPELIREVLR----RRPDEFRRISSLESVFremgINGVFSAEGDAWRRQRRLVMPAFSPKHLRYF------FPTLRQI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 TI-----LSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTL---APELPEnHFAKAFDTANIIVTLRFidPLWKmkk 220
Cdd:cd11083   86 TErlrerWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLergGDPLQE-HLERVFPMLNRRVNAPF--PYWR--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 221 FLNIGSEALLGKSIKVVNDFTYSVIRRRKAEL-LEAQISPtnnnnnnnnkvKHDILSRFIEISDDPDSKETEKSLRDIVL 299
Cdd:cd11083  160 YLRLPADRALDRALVEVRALVLDIIAAARARLaANPALAE-----------APETLLAMMLAEDDPDARLTDDEIYANVL 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 300 NFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQElEKESAEatntslhqydtedfnsfnekvtefaGLLNYDSLGKL 379
Cdd:cd11083  229 TLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDA-VLGGAR-------------------------VPPLLEALDRL 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 380 HYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNwGSDAALFKPERWLKDGVfqNASPF 459
Cdd:cd11083  283 PYLEAVARETLRLKPVAPLLFLEPNEDTVV-GDIALPAGTPVFLLTRAAGLDAEH-FPDPEEFDPERWLDGAR--AAEPH 358
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145337333 460 KFT---AFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLV-PNHPVKYRM 506
Cdd:cd11083  359 DPSsllPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPePAPAVGEEF 409
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
92-518 3.64e-41

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: 153.19  E-value: 3.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  92 KGETYhSYMEVLLGDGIFNSDGELWRKQRK--TASFEFasKNLRDFSTVvFKEYSLKLFTILsQASFKEQQVDMQELLMR 169
Cdd:cd20660   34 KSFEY-DFLHPWLGTGLLTSTGEKWHSRRKmlTPTFHF--KILEDFLDV-FNEQSEILVKKL-KKEVGKEEFDIFPYITL 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 170 MTLDSICKVGFGVEIGtlAPELPENHFAKAFDTANIIVTLRFIDP-LWK--MKKFLNIGSEAllGKSIKVVNDFTYSVIR 246
Cdd:cd20660  109 CALDIICETAMGKSVN--AQQNSDSEYVKAVYRMSELVQKRQKNPwLWPdfIYSLTPDGREH--KKCLKILHGFTNKVIQ 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 247 RRKAELLEAQISPTNNNNNNNNKVKHDI--LSRFIEISDDpDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNE 324
Cdd:cd20660  185 ERKAELQKSLEEEEEDDEDADIGKRKRLafLDLLLEASEE-GTKLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHP 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 325 NVAEKLYSELQELekesaeatntslhqydtedFNSFNEKVTEfagllnyDSLGKLHYLHAVITETLRLYPAVPQDPKGVL 404
Cdd:cd20660  264 EVQEKVHEELDRI-------------------FGDSDRPATM-------DDLKEMKYLECVIKEALRLFPSVPMFGRTLS 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 405 EDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMA 484
Cdd:cd20660  318 EDIEI-GGYTIPKGTTVLVLTYALHRDPRQF-PDPEKFDPDRFLPENS-AGRHPYAYIPFSAGPRNCIGQKFALMEEKVV 394
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 145337333 485 MAILCRFYKFH-LVPNHPVKYRMMTILSMAHGLKV 518
Cdd:cd20660  395 LSSILRNFRIEsVQKREDLKPAGELILRPVDGIRV 429
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
72-506 7.49e-41

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: 152.41  E-value: 7.49e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  72 YIADPINVEYVLKTNFSNYPK-GETYHSYmevLLGDGIFNSDGELWRKQRK--TASFEFasKNLRDFSTVVfKEYSLKLF 148
Cdd:cd20621   17 SLVDPEYIKEFLQNHHYYKKKfGPLGIDR---LFGKGLLFSEGEEWKKQRKllSNSFHF--EKLKSRLPMI-NEITKEKI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 tilsqASFKEQQVDMQELLMRMTLDSICKVGFG----------VEIGTLAPELPENHFAKAFdTANIIVTLRFI--DPLW 216
Cdd:cd20621   91 -----KKLDNQNVNIIQFLQKITGEVVIRSFFGeeakdlkingKEIQVELVEILIESFLYRF-SSPYFQLKRLIfgRKSW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 217 KMKKFLNigsEALLGKSIKVVNDFTYSVIRRRKAELLEAQISPtnnnnnnnnKVKHDILSRFIEISDDPDSKETEKSLRD 296
Cdd:cd20621  165 KLFPTKK---EKKLQKRVKELRQFIEKIIQNRIKQIKKNKDEI---------KDIIIDLDLYLLQKKKLEQEITKEEIIQ 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 297 IVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedFNSFNEkvtefaglLNYDSL 376
Cdd:cd20621  233 QFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSV-------------------VGNDDD--------ITFEDL 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 377 GKLHYLHAVITETLRLYPAVPQD-PKGVLEDDMLPNgTKVKAGGMVTYVPYSMGRMEyNWGSDAALFKPERWLKDGVFQN 455
Cdd:cd20621  286 QKLNYLNAFIKEVLRLYNPAPFLfPRVATQDHQIGD-LKIKKGWIVNVGYIYNHFNP-KYFENPDEFNPERWLNQNNIED 363
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145337333 456 aSPFKFTAFQAGPRICLGKDSAYLQMKMamaILCRF---YKFHLVPNHPVKYRM 506
Cdd:cd20621  364 -NPFVFIPFSAGPRNCIGQHLALMEAKI---ILIYIlknFEIEIIPNPKLKLIF 413
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
73-515 9.80e-41

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: 151.92  E-value: 9.80e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRD-FSTVVfkEYSLKLFTIL 151
Cdd:cd11056   18 VRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELRQKLTPAFTSGKLKNmFPLMV--EVGDELVDYL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 152 SQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLapELPENHFAKAfdtANIIVTLRFIDPLWKMKKFLNIGSEALLG 231
Cdd:cd11056   96 KKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSL--NDPENEFREM---GRRLFEPSRLRGLKFMLLFFFPKLARLLR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 232 KSI--KVVNDFTYSVIRRRKAELLEAQIsptnnnnnnnnkVKHDILSRFIEI--SDDPDSKETEKSLRDIVL-----NFV 302
Cdd:cd11056  171 LKFfpKEVEDFFRKLVRDTIEYREKNNI------------VRNDFIDLLLELkkKGKIEDDKSEKELTDEELaaqafVFF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 303 IAGRDTTATTLTWAIYMIMMNENVAEKLYSELQE-LEKESaeatntslhqydtedfnsfnekvtefaGLLNYDSLGKLHY 381
Cdd:cd11056  239 LAGFETSSSTLSFALYELAKNPEIQEKLREEIDEvLEKHG---------------------------GELTYEALQEMKY 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 382 LHAVITETLRLYPAVPQDPKGVLEDDMLPN-GTKVKAGGMVtYVP-YSMGRMEYNWgSDAALFKPERWLKDGVfQNASPF 459
Cdd:cd11056  292 LDQVVNETLRKYPPLPFLDRVCTKDYTLPGtDVVIEKGTPV-IIPvYALHHDPKYY-PEPEKFDPERFSPENK-KKRHPY 368
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 460 KFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPN--HPVKYRMMTILSMAHG 515
Cdd:cd11056  369 TYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKtkIPLKLSPKSFVLSPKG 426
PLN02738 PLN02738
carotene beta-ring hydroxylase
69-524 9.45e-40

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 152.76  E-value: 9.45e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  69 TYTYIADPINVEYVLKTNFSNYPKGeTYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVvFKEYSLKLF 148
Cdd:PLN02738 176 SFLIVSDPSIAKHILRDNSKAYSKG-ILAEILEFVMGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISL-FGQASDRLC 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 TILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPElpeNHFAKAfdtanIIVTLRFID-------PLWKMKKF 221
Cdd:PLN02738 254 QKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDSLSND---TGIVEA-----VYTVLREAEdrsvspiPVWEIPIW 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 222 LNIG-SEALLGKSIKVVNDFTYSVIR--RRKAELLEAQIsptnnnnnnnnkvkHD---------ILSRFIEISDDPDSKE 289
Cdd:PLN02738 326 KDISpRQRKVAEALKLINDTLDDLIAicKRMVEEEELQF--------------HEeymnerdpsILHFLLASGDDVSSKQ 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 290 teksLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKEsaeatntslhqydtedfnsfnekvtefaG 369
Cdd:PLN02738 392 ----LRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGD----------------------------R 439
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 370 LLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLK 449
Cdd:PLN02738 440 FPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDML-GGYPIKRGEDIFISVWNLHRSPKHW-DDAEKFNPERWPL 517
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 450 DGVFQNAS--PFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH-PVKYRMMTILSMAHGLKVTVSRRS 524
Cdd:PLN02738 518 DGPNPNETnqNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPGApPVKMTTGATIHTTEGLKMTVTRRT 595
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
70-520 1.17e-38

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: 146.19  E-value: 1.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  70 YTYIADPINVEYVLKTNFSNYPKGETyHSYMEVLLGD-GIFNSDGELWRKQRKTASFEFASKNLRDFSTVVfkeyslklf 148
Cdd:cd11053   25 VVVLSDPEAIKQIFTADPDVLHPGEG-NSLLEPLLGPnSLLLLDGDRHRRRRKLLMPAFHGERLRAYGELI--------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 TILSQASFKE----QQVDMQELLMRMTLDSICKVGFGVEIGTLAPELpenhfakafdTANIIVTLRFIDPLWKMKKFL-- 222
Cdd:cd11053   95 AEITEREIDRwppgQPFDLRELMQEITLEVILRVVFGVDDGERLQEL----------RRLLPRLLDLLSSPLASFPALqr 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 223 NIGSEALLGK---SIKVVNDFTYSVIRRRKAELLEAqisptnnnnnnnnkvKHDILSRFIEISDDPDSKETEKSLRDIVL 299
Cdd:cd11053  165 DLGPWSPWGRflrARRRIDALIYAEIAERRAEPDAE---------------RDDILSLLLSARDEDGQPLSDEELRDELM 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 300 NFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedfnsfnekvtefAGLLNYDSLGKL 379
Cdd:cd11053  230 TLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDAL------------------------------GGDPDPEDIAKL 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 380 HYLHAVITETLRLYPAVPQDPKgVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKdgvfQNASPF 459
Cdd:cd11053  280 PYLDAVIKETLRLYPVAPLVPR-RVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLY-PDPERFRPERFLG----RKPSPY 353
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145337333 460 KFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRM-MTILSMAHGLKVTV 520
Cdd:cd11053  354 EYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPERPVRrGVTLAPSRGVRMVV 415
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
73-505 1.93e-38

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: 145.80  E-value: 1.93e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKTNfSNYPKGETYH-SYMEVLLGDGIFNS-DGELWRKQRKTASFEFASKNLRDFSTVVfKEYSLKLFTI 150
Cdd:cd11060   13 ISDPEAIKTIYGTR-SPYTKSDWYKaFRPKDPRKDNLFSErDEKRHAALRRKVASGYSMSSLLSLEPFV-DECIDLLVDL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 151 LSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELPENHF----AKAFDTANIIVTLRFIDPLWKMKKFLNIgs 226
Cdd:cd11060   91 LDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLEAGTDVDGYiasiDKLLPYFAVVGQIPWLDRLLLKNPLGPK-- 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 227 eALLGKSIKVVNDFTYSVIRRRKAELLEAqisptnnnnnnnNKVKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGR 306
Cdd:cd11060  169 -RKDKTGFGPLMRFALEAVAERLAEDAES------------AKGRKDMLDSFLEAGLKDPEKVTDREVVAEALSNILAGS 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 307 DTTATTLTWAIYMIMMNENVAEKLYSELQELEKEsaeatntslhqYDTEDFNSFNEKVtefagllnydslgKLHYLHAVI 386
Cdd:cd11060  236 DTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAE-----------GKLSSPITFAEAQ-------------KLPYLQAVI 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 387 TETLRLYPAVP-----QDPKG--VLEDDMLPNGTKVkagGMVTYVpysMGRMEYNWGSDAALFKPERWL-----KDGVFQ 454
Cdd:cd11060  292 KEALRLHPPVGlplerVVPPGgaTICGRFIPGGTIV---GVNPWV---IHRDKEVFGEDADVFRPERWLeadeeQRRMMD 365
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145337333 455 NAspfkFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLV-PNHPVKYR 505
Cdd:cd11060  366 RA----DLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVdPEKEWKTR 413
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
63-523 1.52e-36

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: 139.64  E-value: 1.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  63 VPMPFTTYTYIADPINVEYVLKTNfSNYPKGETYHSYME--VLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVf 140
Cdd:COG2124   37 VRLPGGGAWLVTRYEDVREVLRDP-RTFSSDGGLPEVLRplPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 141 KEYSLKLFtilsqASFKEQ-QVDMQELLMRMTLDSICKVGFGVeigtlapelPENHFAKAFDTANIIVTLRFIDPLWKMK 219
Cdd:COG2124  115 REIADELL-----DRLAARgPVDLVEEFARPLPVIVICELLGV---------PEEDRDRLRRWSDALLDALGPLPPERRR 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 220 KFLnigseallgKSIKVVNDFTYSVIRRRKAELleaqisptnnnnnnnnkvKHDILSRFIEISDDpDSKETEKSLRDIVL 299
Cdd:COG2124  181 RAR---------RARAELDAYLRELIAERRAEP------------------GDDLLSALLAARDD-GERLSDEELRDELL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 300 NFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnekvtefagllnydslgkl 379
Cdd:COG2124  233 LLLLAGHETTANALAWALYALLRHPEQLARLRAEP--------------------------------------------- 267
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 380 HYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERwlkdgvfqnaSPF 459
Cdd:COG2124  268 ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVF-PDPDRFDPDR----------PPN 335
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145337333 460 KFTAFQAGPRICLGKDSAYLQMKMAMA-ILCRFYKFHLVPNHPVKYRMMTILSMAHGLKVTVSRR 523
Cdd:COG2124  336 AHLPFGGGPHRCLGAALARLEARIALAtLLRRFPDLRLAPPEELRWRPSLTLRGPKSLPVRLRPR 400
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
68-501 1.25e-35

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: 137.73  E-value: 1.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  68 TTYT-YIADPINVEYVLKTN---FSNYPKGETYHSYMEvllGDGIFNSDGELWRKQRKTASFEF-ASKNLRDFSTVVFKE 142
Cdd:cd20617   10 DVPTvVLSDPEIIKEAFVKNgdnFSDRPLLPSFEIISG---GKGILFSNGDYWKELRRFALSSLtKTKLKKKMEELIEEE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 143 YSlKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLapELPENH-----FAKAFDTANiivTLRFIDPLWK 217
Cdd:cd20617   87 VN-KLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDE--DDGEFLklvkpIEEIFKELG---SGNPSDFIPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 218 MKKFLNIGSEaLLGKSIKVVNDFTYSVIRRRKAELleaqisptnnnnnNNNKVKHDILSRFIEISDDPDS-KETEKSLRD 296
Cdd:cd20617  161 LLPFYFLYLK-KLKKSYDKIKDFIEKIIEEHLKTI-------------DPNNPRDLIDDELLLLLKEGDSgLFDDDSIIS 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 297 IVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKesaeatntslhqydTEDFNSFNEKVtefagllnydsl 376
Cdd:cd20617  227 TCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVG--------------NDRRVTLSDRS------------ 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 377 gKLHYLHAVITETLRLYPAVPQD-PKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEyNWGSDAALFKPERWLKDGvfQN 455
Cdd:cd20617  281 -KLPYLNAVIKEVLRLRPILPLGlPRVTTEDTEI-GGYFIPKGTQIIINIYSLHRDE-KYFEDPEEFNPERFLEND--GN 355
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 145337333 456 ASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHP 501
Cdd:cd20617  356 KLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFKSSDGLP 401
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
106-496 1.89e-35

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: 137.33  E-value: 1.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 106 DGIFNSDGELWRKQRKTASFEFASKNLRDFStVVFKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIG 185
Cdd:cd11058   48 PSISTADDEDHARLRRLLAHAFSEKALREQE-PIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGESFG 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 186 TLapELPENH-----FAKAFDTANIIVTLRFIDPLWKMKKFLNIgseALLGKSIKVVNDFTYSVIRRRkaelLEAQISpt 260
Cdd:cd11058  127 CL--ENGEYHpwvalIFDSIKALTIIQALRRYPWLLRLLRLLIP---KSLRKKRKEHFQYTREKVDRR----LAKGTD-- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 261 nnnnnnnnkvKHDILSRFIEISDDpDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQeleke 340
Cdd:cd11058  196 ----------RPDFMSYILRNKDE-KKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIR----- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 341 SAeatntslhqydtedFNSFNEkvtefaglLNYDSLGKLHYLHAVITETLRLYPAVP-----QDPKG--VLEDDMLPNGT 413
Cdd:cd11058  260 SA--------------FSSEDD--------ITLDSLAQLPYLNAVIQEALRLYPPVPaglprVVPAGgaTIDGQFVPGGT 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 414 KVkaggmvtYVP-YSMGRMEYNWgSDAALFKPERWLKDGVFQNASPFK--FTAFQAGPRICLGKDSAYLQMKMamaILCR 490
Cdd:cd11058  318 SV-------SVSqWAAYRSPRNF-HDPDEFIPERWLGDPRFEFDNDKKeaFQPFSVGPRNCIGKNLAYAEMRL---ILAK 386

                 ....*..
gi 145337333 491 F-YKFHL 496
Cdd:cd11058  387 LlWNFDL 393
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
117-496 1.14e-34

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: 135.07  E-value: 1.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 117 RKQRKTA--SFeFASKNLRDFSTVVfKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELPEN 194
Cdd:cd11062   55 HRLRRKAlsPF-FSKRSILRLEPLI-QEKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPDFGP 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 195 HFAKAFD-TANIIVTLRFIDplWkMKKFLNIGSEALLGKSIKVVNDFT--YSVIRRRKAELLEAQISPTNnnnnnnnKVK 271
Cdd:cd11062  133 EFLDALRaLAEMIHLLRHFP--W-LLKLLRSLPESLLKRLNPGLAVFLdfQESIAKQVDEVLRQVSAGDP-------PSI 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 272 HDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAeatntslhq 351
Cdd:cd11062  203 VTSLFHALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPD--------- 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 352 ydtedfnsfnekvtefaGLLNYDSLGKLHYLHAVITETLRLYPAVPQD-----PKGVLEDD--MLPNGTKVkagGMVTyv 424
Cdd:cd11062  274 -----------------SPPSLAELEKLPYLTAVIKEGLRLSYGVPTRlprvvPDEGLYYKgwVIPPGTPV---SMSS-- 331
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145337333 425 pYSMGRMEYNWGsDAALFKPERWLKDGVFQNASPFkFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHL 496
Cdd:cd11062  332 -YFVHHDEEIFP-DPHEFRPERWLGAAEKGKLDRY-LVPFSKGSRSCLGINLAYAELYLALAALFRRFDLEL 400
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
72-519 1.85e-34

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: 134.33  E-value: 1.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  72 YIADPINVEYVLktnfSNYPKGETYHSY--MEVLLGDG-IFNSDGELWRKQRKTASfefasknlRDFSTVVFKEYSLKLF 148
Cdd:cd11044   36 FVIGAEAVRFIL----SGEGKLVRYGWPrsVRRLLGENsLSLQDGEEHRRRRKLLA--------PAFSREALESYVPTIQ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 TILSQAS---FKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELPEnhfakAFDTaniivtlrFIDPLWKMKkfLNI- 224
Cdd:cd11044  104 AIVQSYLrkwLKAGEVALYPELRRLTFDVAARLLLGLDPEVEAEALSQ-----DFET--------WTDGLFSLP--VPLp 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 225 GSeaLLGKSI----KVVNDFTYSVIRRRKAELLEAQisptnnnnnnnnkvkhDILSRFIEISDDPDSKETEKSLRDIVLN 300
Cdd:cd11044  169 FT--PFGRAIrarnKLLARLEQAIRERQEEENAEAK----------------DALGLLLEAKDEDGEPLSMDELKDQALL 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 301 FVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedfnSFNEKVTefagllnYDSLGKLH 380
Cdd:cd11044  231 LLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDAL---------------------GLEEPLT-------LESLKKMP 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 381 YLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVFQNASPFK 460
Cdd:cd11044  283 YLDQVIKEVLRLVPPVGGGFRKVLEDFEL-GGYQIPKGWLVYYSIRDTHRDPELY-PDPERFDPERFSPARSEDKKKPFS 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145337333 461 FTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLKVT 519
Cdd:cd11044  361 LIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLPNQDLEPVVVPTPRPKDGLRVR 419
PLN02936 PLN02936
epsilon-ring hydroxylase
32-524 2.02e-34

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 135.69  E-value: 2.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  32 PLVGAAIEQLTN------FDRMHDWLVEYLYNSRTVVVPmpfTTYTYIADPINVEYVLKTNFSNYPKGeTYHSYMEVLLG 105
Cdd:PLN02936  21 PVADAKLEDVTDllggalFLPLFKWMNEYGPVYRLAAGP---RNFVVVSDPAIAKHVLRNYGSKYAKG-LVAEVSEFLFG 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 106 DGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIG 185
Cdd:PLN02936  97 SGFAIAEGELWTARRRAVVPSLHRRYLSVMVDRVFCKCAERLVEKLEPVALSGEAVNMEAKFSQLTLDVIGLSVFNYNFD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 186 TLAPELPenhFAKAFDTANIIVTLRFID--PLWKMKKFLNIGSEALLG-KSIKVVNDFTYSVIRRRKaELLEAQiSPTNN 262
Cdd:PLN02936 177 SLTTDSP---VIQAVYTALKEAETRSTDllPYWKVDFLCKISPRQIKAeKAVTVIRETVEDLVDKCK-EIVEAE-GEVIE 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 263 NNNNNNKVKHDILsRFIEISDDPDSketEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESA 342
Cdd:PLN02936 252 GEEYVNDSDPSVL-RFLLASREEVS---SVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRP 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 343 EAtntslhqydtedfnsfnekvtefagllnYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVT 422
Cdd:PLN02936 328 PT----------------------------YEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIM 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 423 YVPYSMGRMEYNWGSdAALFKPERWLKDGVFQNAS--PFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH 500
Cdd:PLN02936 380 ISVYNIHRSPEVWER-AEEFVPERFDLDGPVPNETntDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPDQ 458
                        490       500
                 ....*....|....*....|....*..
gi 145337333 501 PVKyrmMTILSMAH---GLKVTVSRRS 524
Cdd:PLN02936 459 DIV---MTTGATIHttnGLYMTVSRRR 482
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
139-495 1.46e-33

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


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 132.04  E-value: 1.46e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 139 VFKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLapELPENHFAKAFDTANIIVTLRFidPLWKM 218
Cdd:cd11059   79 IIRERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTL--LLGDKDSRERELLRRLLASLAP--WLRWL 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 219 KKFLNIgseallgKSIKVVNDFTYsvirRRKAELLEAQISPTNNNNNNNNKVKHDILSRFIEISDDPDSKETEKSLRDI- 297
Cdd:cd11059  155 PRYLPL-------ATSRLIIGIYF----RAFDEIEEWALDLCARAESSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIa 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 298 --VLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntSLHQYDTEDFnsfnekvtefagllnyDS 375
Cdd:cd11059  224 seALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGL----------PGPFRGPPDL----------------ED 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 376 LGKLHYLHAVITETLRLYPAVP-QDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDgvfq 454
Cdd:cd11059  278 LDKLPYLNAVIRETLRLYPPIPgSLPRVVPEGGATIGGYYIPGGTIVSTQAYSLHRDPEVF-PDPEEFDPERWLDP---- 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 145337333 455 NASPFK-----FTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFH 495
Cdd:cd11059  353 SGETARemkraFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTS 398
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
64-492 7.33e-33

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: 130.27  E-value: 7.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  64 PMPFTTyTYIADpiNVEYVLKTnfSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRK--TASFEFASknLRDFSTVVFK 141
Cdd:cd20680   21 PVPFVI-LYHAE--NVEVILSS--SKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKmlTPTFHFTI--LSDFLEVMNE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 142 EYSL---KLFTILSQASFkeqqvdmqELLMRMTL---DSICKVGFGVEIGtlAPELPENHFAKAFDTANIIVTLRFIDP- 214
Cdd:cd20680   94 QSNIlveKLEKHVDGEAF--------NCFFDITLcalDIICETAMGKKIG--AQSNKDSEYVQAVYRMSDIIQRRQKMPw 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 215 LWKMKKFLNIGSEALLGKSIKVVNDFTYSVIRRRKAELLEAQISPTNNNNNNNNKVKHD-ILSRFIEISDDPDSKETEKS 293
Cdd:cd20680  164 LWLDLWYLMFKEGKEHNKNLKILHTFTDNVIAERAEEMKAEEDKTGDSDGESPSKKKRKaFLDMLLSVTDEEGNKLSHED 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 294 LRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedFNSFNEKVTefagllnY 373
Cdd:cd20680  244 IREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEV-------------------FGKSDRPVT-------M 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 374 DSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRmEYNWGSDAALFKPERWLKDGVf 453
Cdd:cd20680  298 EDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEI-RGFKVPKGVNAVIIPYALHR-DPRYFPEPEEFRPERFFPENS- 374
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 145337333 454 QNASPFKFTAFQAGPRICLGKDSAYLQMKMAMA-ILCRFY 492
Cdd:cd20680  375 SGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLScILRHFW 414
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
161-523 1.12e-32

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: 129.61  E-value: 1.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 161 VDMQELLMRMTLDSICKVGFG-----VEIGTLAPelpenhFAKAFDTA--NIIVTLRFIDPLwkmkKFLNIGSEALLGKS 233
Cdd:cd11068  115 IDVPDDMTRLTLDTIALCGFGyrfnsFYRDEPHP------FVEAMVRAltEAGRRANRPPIL----NKLRRRAKRQFRED 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 234 IKVVNDFTYSVIRRRKAelleaqiSPTNNnnnnnnkvKHDILSRFIEiSDDPDSKE--TEKSLRDIVLNFVIAGRDTTAT 311
Cdd:cd11068  185 IALMRDLVDEIIAERRA-------NPDGS--------PDDLLNLMLN-GKDPETGEklSDENIRYQMITFLIAGHETTSG 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 312 TLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedFNSfnekvtefaGLLNYDSLGKLHYLHAVITETLR 391
Cdd:cd11068  249 LLSFALYYLLKNPEVLAKARAEVDEV-------------------LGD---------DPPPYEQVAKLRYIRRVLDETLR 300
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 392 LYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKDGvFQNASPFKFTAFQAGPRIC 471
Cdd:cd11068  301 LWPTAPAFARKPKEDTVLGGKYPLKKGDPVLVLLPALHRDPSVWGEDAEEFRPERFLPEE-FRKLPPNAWKPFGNGQRAC 379
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 145337333 472 LGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYR-MMTIlsMAHGLKVTVSRR 523
Cdd:cd11068  380 IGRQFALQEATLVLAMLLQRFDFEDDPDYELDIKeTLTL--KPDGFRLKARPR 430
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
66-516 3.04e-31

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: 125.57  E-value: 3.04e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  66 PFTTYTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQRK--TASFEFAsknlrdfstvVFKEY 143
Cdd:cd20679   21 PFYPIIRLFHPDYIRPVLLASAAVAPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRllTPAFHFN----------ILKPY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 144 sLKLFT----ILSQ-----ASFKEQQVDMQELLMRMTLDSICKVGFGVEigTLAPELPENHFAKAFDTANIIVT-----L 209
Cdd:cd20679   91 -VKIFNqstnIMHAkwrrlASEGSARLDMFEHISLMTLDSLQKCVFSFD--SNCQEKPSEYIAAILELSALVVKrqqqlL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 210 RFIDPLWKM----KKFlnigseallGKSIKVVNDFTYSVIRRRKAELLEAQISPtnnnnNNNNKVKHDILSrFIEI---S 282
Cdd:cd20679  168 LHLDFLYYLtadgRRF---------RRACRLVHDFTDAVIQERRRTLPSQGVDD-----FLKAKAKSKTLD-FIDVlllS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 283 DDPDSKE-TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESaeatntslhqyDTEDfnsfn 361
Cdd:cd20679  233 KDEDGKElSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDR-----------EPEE----- 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 362 ekvtefaglLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAAL 441
Cdd:cd20679  297 ---------IEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVW-PDPEV 366
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145337333 442 FKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILcrFYKFHLVPNH-PVKYRMMTILSMAHGL 516
Cdd:cd20679  367 YDPFRFDPENS-QGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALT--LLRFRVLPDDkEPRRKPELILRAEGGL 439
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
82-488 5.18e-30

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: 121.80  E-value: 5.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  82 VLKTN---FSNYPKgetyHSYMEVLLGDG---IFNSDGELWRKQRKTASFE-FASKNLRDFSTVVFKEYSLkLFTILSQA 154
Cdd:cd11072   27 VLKTHdlvFASRPK----LLAARILSYGGkdiAFAPYGEYWRQMRKICVLElLSAKRVQSFRSIREEEVSL-LVKKIRES 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 155 SFKEQQVDMQELLMRMTLDSICKVGFGV--------EIGTLAPELPEnhFAKAFDTANIIVTLRFIDPLWKMKKFLNigs 226
Cdd:cd11072  102 ASSSSPVNLSELLFSLTNDIVCRAAFGRkyegkdqdKFKELVKEALE--LLGGFSVGDYFPSLGWIDLLTGLDRKLE--- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 227 eallgKSIKVVNDFTYSVIRRRKAElleaqisptnNNNNNNNKVKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGR 306
Cdd:cd11072  177 -----KVFKELDAFLEKIIDEHLDK----------KRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNIKAIILDMFLAGT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 307 DTTATTLTWAIYMIMMNENVAEKLYSELQELEKEsaeatntslhqydtedfnsfNEKVTEfagllnyDSLGKLHYLHAVI 386
Cdd:cd11072  242 DTSATTLEWAMTELIRNPRVMKKAQEEVREVVGG--------------------KGKVTE-------EDLEKLKYLKAVI 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 387 TETLRLYPAVPQdpkgvleddMLP---------NGTKVKAGGMVtYV-PYSMGRmEYNWGSDAALFKPERWLKDGVFQNA 456
Cdd:cd11072  295 KETLRLHPPAPL---------LLPrecredckiNGYDIPAKTRV-IVnAWAIGR-DPKYWEDPEEFRPERFLDSSIDFKG 363
                        410       420       430
                 ....*....|....*....|....*....|..
gi 145337333 457 SPFKFTAFQAGPRICLGkdsaylqMKMAMAIL 488
Cdd:cd11072  364 QDFELIPFGAGRRICPG-------ITFGLANV 388
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
160-522 1.71e-29

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: 119.98  E-value: 1.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 160 QVDMQELLMRMTLDSICKVGFGVEIGTLAPELpenhfAKAFdtaniivtLRFIDPLWKMkkFLNI-GSEalLGKSIKV-- 236
Cdd:cd11043  103 SVVVLELAKKMTFELICKLLLGIDPEEVVEEL-----RKEF--------QAFLEGLLSF--PLNLpGTT--FHRALKArk 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 237 -VNDFTYSVIRRRKAELLEAqisptnnnnnnnnKVKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTW 315
Cdd:cd11043  166 rIRKELKKIIEERRAELEKA-------------SPKGDLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTL 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 316 AIYMIMMNENVAEKLYSELQELEKESAEatntslhqydtedfnsfnekvtefAGLLNYDSLGKLHYLHAVITETLRLYPA 395
Cdd:cd11043  233 AVKFLAENPKVLQELLEEHEEIAKRKEE------------------------GEGLTWEDYKSMKYTWQVINETLRLAPI 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 396 VPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMgRMEYNWGSDAALFKPERWLKDGVfqnASPFKFTAFQAGPRICLGKD 475
Cdd:cd11043  289 VPGVFRKALQDVEY-KGYTIPKGWKVLWSARAT-HLDPEYFPDPLKFNPWRWEGKGK---GVPYTFLPFGGGPRLCPGAE 363
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 145337333 476 SAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMahGLKVTVSR 522
Cdd:cd11043  364 LAKLEILVFLHHLVTRFRWEVVPDEKISRFPLPRPPK--GLPIRLSP 408
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
82-489 1.28e-28

Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is considerably larger than in other taxa. In individual plant genomes, CYPs form the third largest family of plant genes; the two largest gene families code for F-box proteins and receptor-like kinases. CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. However, there is a phenomenon called family creep, where a sequence (below 40% identity) is absorbed into a large family; this is seen in the plant CYP71 and CYP89 families. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP71 clan has expanded dramatically and represents 50% of all plant CYPs; it includes several families including CYP71, CYP73, CYP76, CYP81, CYP82, CYP89, and CYP93, among others. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410711 [Multi-domain]  Cd Length: 429  Bit Score: 118.04  E-value: 1.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  82 VLKTN---FSNYPKGeTYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFAS-KNLRDFSTVVfKEYSLKLFTILSQASFK 157
Cdd:cd20618   25 VLKTQdavFASRPRT-AAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSaKRLESFQGVR-KEELSHLVKSLLEESES 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 158 EQQVDMQELLMRMTLDSICKVGFG-VEIGTLAPELPENH-----------FAKAFDTANIIVTLRFIDPLWKMKKFLNIG 225
Cdd:cd20618  103 GKPVNLREHLSDLTLNNITRMLFGkRYFGESEKESEEARefkelideafeLAGAFNIGDYIPWLRWLDLQGYEKRMKKLH 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 226 SEallgksikvVNDFTYSVIRRRKAELLEAQisptnnnNNNNNKVKHDILsrfieISDDPDSKETEKSLRDIVLNFVIAG 305
Cdd:cd20618  183 AK---------LDRFLQKIIEEHREKRGESK-------KGGDDDDDLLLL-----LDLDGEGKLSDDNIKALLLDMLAAG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 306 RDTTATTLTWAIYMIMMNENVAEKLYSELQELEKEsaeatntslhqydtedfnsfNEKVTEfagllnyDSLGKLHYLHAV 385
Cdd:cd20618  242 TDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGR--------------------ERLVEE-------SDLPKLPYLQAV 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 386 ITETLRLYPAVP-QDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEyNWGSDAALFKPERWLKDGV--FQNASpFKFT 462
Cdd:cd20618  295 VKETLRLHPPGPlLLPHESTEDCKV-AGYDIPAGTRVLVNVWAIGRDP-KVWEDPLEFKPERFLESDIddVKGQD-FELL 371
                        410       420
                 ....*....|....*....|....*..
gi 145337333 463 AFQAGPRICLGKDSAYLQMKMAMAILC 489
Cdd:cd20618  372 PFGSGRRMCPGMPLGLRMVQLTLANLL 398
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
239-510 1.99e-28

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: 117.32  E-value: 1.99e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 239 DFTYSVIRRRKAElleaqisptnnnnnnNNKVKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIY 318
Cdd:cd11042  173 EIFSEIIQKRRKS---------------PDKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGL 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 319 MIMMNENVAEKLYSELQELEKESAeatntslhqydtedfnsfnekvtefaGLLNYDSLGKLHYLHAVITETLRLYPAVPQ 398
Cdd:cd11042  238 ELLRNPEHLEALREEQKEVLGDGD--------------------------DPLTYDVLKEMPLLHACIKETLRLHPPIHS 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 399 DPKGVLEDDMLPNGTKV-KAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKD-GVFQNASPFKFTAFQAGPRICLGKDS 476
Cdd:cd11042  292 LMRKARKPFEVEGGGYViPKGHIVLASPAVSHRDPEIF-KNPDEFDPERFLKGrAEDSKGGKFAYLPFGAGRHRCIGENF 370
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 145337333 477 AYLQMKMAMAILCRFYKFHLVPNH--PVKYRMMTIL 510
Cdd:cd11042  371 AYLQIKTILSTLLRNFDFELVDSPfpEPDYTTMVVW 406
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
72-494 1.02e-26

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: 111.96  E-value: 1.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  72 YIADPINVEYVLKTNfsNYPKGETYHSYMEVLLGDG-IFNSDGELWRKQRKTASFEFASKNLRDF------STVVFKEys 144
Cdd:cd11051   14 VVTDPELAEQITQVT--NLPKPPPLRKFLTPLTGGSsLISMEGEEWKRLRKRFNPGFSPQHLMTLvptildEVEIFAA-- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 145 lklftILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEigtLAPELPENHFAKAFdtaniIVTLRFIDPLWKMKKFLNI 224
Cdd:cd11051   90 -----ILRELAESGEVFSLEELTTNLTFDVIGRVTLDID---LHAQTGDNSLLTAL-----RLLLALYRSLLNPFKRLNP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 225 GSEALLGKSIKVVNDFTYSVIRRR-KAELLEAQIsptnnnnnnnnkvkhdilsrfieisddpdsketeKSlrdivlnFVI 303
Cdd:cd11051  157 LRPLRRWRNGRRLDRYLKPEVRKRfELERAIDQI----------------------------------KT-------FLF 195
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 304 AGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATNTSLHQydtedfnsfnekvtefagllNYDSLGKLHYLH 383
Cdd:cd11051  196 AGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPSAAAELLRE--------------------GPELLNQLPYTT 255
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 384 AVITETLRLYP---AVPQDPKGVleDDMLPNGTKVKAGGMVTYV-PYSMGRMEyNWGSDAALFKPERWL-KDGVFQNASP 458
Cdd:cd11051  256 AVIKETLRLFPpagTARRGPPGV--GLTDRDGKEYPTDGCIVYVcHHAIHRDP-EYWPRPDEFIPERWLvDEGHELYPPK 332
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 145337333 459 FKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKF 494
Cdd:cd11051  333 SAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDF 368
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
162-499 1.38e-26

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


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 112.06  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 162 DMQELLMRMTLDSICKVGFGVEIGTLAPELPEN--HFAKAFD---TANIIVTL-----RFIDPLWKmkKFLNigseallg 231
Cdd:cd20646  116 DLANELYKFAFEGISSILFETRIGCLEKEIPEEtqKFIDSIGemfKLSEIVTLlpkwtRPYLPFWK--RYVD-------- 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 232 ksikvVNDFTYSVIRR---RKAELLEAQISPtnnnnnnNNKVKHDILSrFIEISDDPDSKETEKSLRDIVLnfviAGRDT 308
Cdd:cd20646  186 -----AWDTIFSFGKKlidKKMEEIEERVDR-------GEPVEGEYLT-YLLSSGKLSPKEVYGSLTELLL----AGVDT 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 309 TATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATntslhqydTEDFNsfnekvtefagllnydslgKLHYLHAVITE 388
Cdd:cd20646  249 TSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPT--------AEDIA-------------------KMPLLKAVIKE 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 389 TLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGVFQNaSPFKFTAFQAGP 468
Cdd:cd20646  302 TLRLYPVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNF-PEPERFKPERWLRDGGLKH-HPFGSIPFGYGV 379
                        330       340       350
                 ....*....|....*....|....*....|.
gi 145337333 469 RICLGKDSAYLQMKMAMAILCRFYKFHLVPN 499
Cdd:cd20646  380 RACVGRRIAELEMYLALSRLIKRFEVRPDPS 410
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
245-503 2.45e-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: 111.18  E-value: 2.45e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 245 IRRRKAELLEAQISPTNNNNNNNNKVKHDILSRFIEISDDpdsketekslrDIVL---NFVIAGRDTTATTLTWAIYMIM 321
Cdd:cd11075  191 IRARRKRRASGEADKDYTDFLLLDLLDLKEEGGERKLTDE-----------ELVSlcsEFLNAGTDTTATALEWAMAELV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 322 MNENVAEKLYSELQELEKEsaeatntslhqydtedfnsfNEKVTEfagllnyDSLGKLHYLHAVITETLRLYPAVPQ-DP 400
Cdd:cd11075  260 KNPEIQEKLYEEIKEVVGD--------------------EAVVTE-------EDLPKMPYLKAVVLETLRRHPPGHFlLP 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 401 KGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDG----VFQNASPFKFTAFQAGPRICLGkds 476
Cdd:cd11075  313 HAVTEDTVL-GGYDIPAGAEVNFNVAAIGRDPKVW-EDPEEFKPERFLAGGeaadIDTGSKEIKMMPFGAGRRICPG--- 387
                        250       260       270
                 ....*....|....*....|....*....|....
gi 145337333 477 aylqMKMAMAILCRF-------YKFHLVPNHPVK 503
Cdd:cd11075  388 ----LGLATLHLELFvarlvqeFEWKLVEGEEVD 417
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
104-494 1.85e-25

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: 108.66  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 104 LGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVfKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVE 183
Cdd:cd20650   48 MKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMFPII-AQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVN 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 184 IGTLAPelPENHFAKA---------FDTANIIVTL-RFIDPLWKMkkfLNIgseALLGKSikVVNDFTYSVIRRRKAELL 253
Cdd:cd20650  127 IDSLNN--PQDPFVENtkkllkfdfLDPLFLSITVfPFLTPILEK---LNI---SVFPKD--VTNFFYKSVKKIKESRLD 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 254 EAQisptnnnnnnnnKVKHDILSRFIEiSDDPDSKETEKSLRDIVLN-----FVIAGRDTTATTLTWAIYMIMMNENVAE 328
Cdd:cd20650  197 STQ------------KHRVDFLQLMID-SQNSKETESHKALSDLEILaqsiiFIFAGYETTSSTLSFLLYELATHPDVQQ 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 329 KLYSELQELEKESAEATntslhqydtedfnsfnekvtefagllnYDSLGKLHYLHAVITETLRLYPAVPQDPKgVLEDDM 408
Cdd:cd20650  264 KLQEEIDAVLPNKAPPT---------------------------YDTVMQMEYLDMVVNETLRLFPIAGRLER-VCKKDV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 409 LPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAAlFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAIL 488
Cdd:cd20650  316 EINGVFIPKGTVVMIPTYALHRDPQYWPEPEE-FRPERFSKKNK-DNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRV 393

                 ....*.
gi 145337333 489 CRFYKF 494
Cdd:cd20650  394 LQNFSF 399
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
44-492 5.57e-25

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 107.36  E-value: 5.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  44 FDRMHDWLVEYLYnsrtvVVPM---PFTTYTYIADPinvEYVlKTNFSNY-PKGETYHSYMEVLLGDGIFNSDGELWRKQ 119
Cdd:cd20678    1 LQKILKWVEKYPY-----AFPLwfgGFKAFLNIYDP---DYA-KVVLSRSdPKAQGVYKFLIPWIGKGLLVLNGQKWFQH 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 120 RK--TASFEFAsknlrdfstvVFKEYsLKLFT--------ILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEiGTLAP 189
Cdd:cd20678   72 RRllTPAFHYD----------ILKPY-VKLMAdsvrvmldKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQ-GSCQL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 190 ELPENHFAKAFDTANIIVTLRFIDPLWKMKKFLNIGSEA-LLGKSIKVVNDFTYSVIRRRKAELLEAqisptnNNNNNNN 268
Cdd:cd20678  140 DGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPHGrRFRRACQLAHQHTDKVIQQRKEQLQDE------GELEKIK 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 269 KVKH-DILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATnt 347
Cdd:cd20678  214 KKRHlDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSIT-- 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 348 slhqydtedfnsfnekvtefagllnYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYS 427
Cdd:cd20678  292 -------------------------WEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYG 346
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145337333 428 MGRMEYNWgSDAALFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMA-ILCRFY 492
Cdd:cd20678  347 LHHNPAVW-PNPEVFDPLRFSPENS-SKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVAlTLLRFE 410
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
105-501 1.22e-24

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: 106.14  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 105 GDGIFNSD-GELWRKQRKTA--SFEFASKNLRDFSTVVFKEYS--LKLFtilsqASFKEQQVDMQELLMRMTLDSICKVG 179
Cdd:cd11027   50 GKDIAFGDySPTWKLHRKLAhsALRLYASGGPRLEEKIAEEAEklLKRL-----ASQEGQPFDPKDELFLAVLNVICSIT 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 180 FGVEIGTLAPELPE-----NHFAKAFDTANIIVTLRFidplwkMKKFLNIGSEALLgKSIKVVNDFTYSVIRRRKAELLE 254
Cdd:cd11027  125 FGKRYKLDDPEFLRlldlnDKFFELLGAGSLLDIFPF------LKYFPNKALRELK-ELMKERDEILRKKLEEHKETFDP 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 255 AQIsptnnnnnnnnkvkHDILSRFI----EISDDPDSKE---TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVA 327
Cdd:cd11027  198 GNI--------------RDLTDALIkakkEAEDEGDEDSgllTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQ 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 328 EKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQD-PKGVLED 406
Cdd:cd11027  264 AKLHAEL---------------------------DDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLAlPHKTTCD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 407 DMLpNGTKVKAGGMVTYVPYSMGRMEYNWGsDAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMA 486
Cdd:cd11027  317 TTL-RGYTIPKGTTVLVNLWALHHDPKEWD-DPDEFRPERFLDENGKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLA 394
                        410
                 ....*....|....*
gi 145337333 487 ILCRFYKFHLVPNHP 501
Cdd:cd11027  395 RLLQKFRFSPPEGEP 409
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
73-515 5.58e-24

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: 104.45  E-value: 5.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKTNFSNYPKGETyHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILS 152
Cdd:cd20639   27 VADPELIREILLTRADHFDRYEA-HPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVVKSVADMLDKWEA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 153 QA-SFKEQQVDMQELLMRMTLDSICKVGFG--VEIGTLAPELPENH---FAKAFDTAnIIVTLRFIdPLWKMKKFLNIGS 226
Cdd:cd20639  106 MAeAGGEGEVDVAEWFQNLTEDVISRTAFGssYEDGKAVFRLQAQQmllAAEAFRKV-YIPGYRFL-PTKKNRKSWRLDK 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 227 EallgksikvvndftysvIRRRKAELLEAQiSPTNNNNNNNNKVKhDILSRFIEISDDpdSKETEKSLRDIV---LNFVI 303
Cdd:cd20639  184 E-----------------IRKSLLKLIERR-QTAADDEKDDEDSK-DLLGLMISAKNA--RNGEKMTVEEIIeecKTFFF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 304 AGRDTTATTLTWAIYMIMMNENVAEKLYSELQelekesaeatntslhqydtedfnsfneKVTEFAGLLNYDSLGKLHYLH 383
Cdd:cd20639  243 AGKETTSNLLTWTTVLLAMHPEWQERARREVL---------------------------AVCGKGDVPTKDHLPKLKTLG 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 384 AVITETLRLYP-AVPQDPKGV----LEDDMLPNGTKVkaggmvtYVP-YSMGRMEYNWGSDAALFKPERWlKDGVFQNAS 457
Cdd:cd20639  296 MILNETLRLYPpAVATIRRAKkdvkLGGLDIPAGTEL-------LIPiMAIHHDAELWGNDAAEFNPARF-ADGVARAAK 367
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145337333 458 -PFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHG 515
Cdd:cd20639  368 hPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLSPSYAHAPTVLMLLQPQHG 426
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
75-520 6.60e-24

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: 103.88  E-value: 6.60e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  75 DPINVEYVLKTNFSNYPKGETYhSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLftilsqA 154
Cdd:cd11049   30 SPELVRQVLVNDRVFDKGGPLF-DRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEAEALA------G 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 155 SFKEQQ-VDMQELLMRMTLDSICKVGFGVEIGTLAPELpenhFAKAFDTANIIVTLRFIDPlwkmkKFLnigsEAL---- 229
Cdd:cd11049  103 SWRPGRvVDVDAEMHRLTLRVVARTLFSTDLGPEAAAE----LRQALPVVLAGMLRRAVPP-----KFL----ERLptpg 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 230 ---LGKSIKVVNDFTYSVIRRRKAelleaqiSPTnnnnnnnnkvKHDILSRFIEISDDPDSKE-TEKSLRDIVLNFVIAG 305
Cdd:cd11049  170 nrrFDRALARLRELVDEIIAEYRA-------SGT----------DRDDLLSLLLAARDEEGRPlSDEELRDQVITLLTAG 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 306 RDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnekVTEFAG-LLNYDSLGKLHYLHA 384
Cdd:cd11049  233 TETTASTLAWAFHLLARHPEVERRLHAEL-----------------------------DAVLGGrPATFEDLPRLTYTRR 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 385 VITETLRLYPAVPQDPKGVLEDDMLPnGTKVKAGGMVTYVPYSMGRmeynwgsDAAL------FKPERWLkDGVFQNASP 458
Cdd:cd11049  284 VVTEALRLYPPVWLLTRRTTADVELG-GHRLPAGTEVAFSPYALHR-------DPEVypdperFDPDRWL-PGRAAAVPR 354
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145337333 459 FKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILsMAHGLKVTV 520
Cdd:cd11049  355 GAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGRPVRPRPLATL-RPRRLRMRV 415
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
48-509 2.98e-23

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: 102.36  E-value: 2.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  48 HDWLVEYLYNSRTVVVPMPFTTytyIADPINVEYVLkTNFSNYPKGETyHSYMEvLLGDGIFNSDGELWRKQRKTASFEF 127
Cdd:cd20642    5 HHTVKTYGKNSFTWFGPIPRVI---IMDPELIKEVL-NKVYDFQKPKT-NPLTK-LLATGLASYEGDKWAKHRKIINPAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 128 ASKNLRdfstVVFKEYSLKLFTILSQ----ASFKEQ-QVDMQELLMRMTLDSICKVGFG------VEIGTLAPELPEnHF 196
Cdd:cd20642   79 HLEKLK----NMLPAFYLSCSEMISKweklVSSKGScELDVWPELQNLTSDVISRTAFGssyeegKKIFELQKEQGE-LI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 197 AKAFDTANIivtlrfidPLW---------KMKKflnigsealLGKSIKVVndFTYSVIRRRKAelLEAQISPtnnnnnnn 267
Cdd:cd20642  154 IQALRKVYI--------PGWrflptkrnrRMKE---------IEKEIRSS--LRGIINKREKA--MKAGEAT-------- 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 268 nkvKHDIL-----SRFIEISDDpDSKETEKSLRDIVLN---FVIAGRDTTATTLTWAiyMIMMNEnvaeklYSELQELEK 339
Cdd:cd20642  205 ---NDDLLgilleSNHKEIKEQ-GNKNGGMSTEDVIEEcklFYFAGQETTSVLLVWT--MVLLSQ------HPDWQERAR 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 340 EsaeatntslhqydtEDFNSFNEKVTEFagllnyDSLGKLHYLHAVITETLRLYPAVPQDPKGVLED----DM-LPngtk 414
Cdd:cd20642  273 E--------------EVLQVFGNNKPDF------EGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDtklgDLtLP---- 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 415 vkaGGMVTYVPYSM-GRMEYNWGSDAALFKPERWlKDGVFQNA-SPFKFTAFQAGPRICLGKDSAYLQMKMAMA-ILCRF 491
Cdd:cd20642  329 ---AGVQVSLPILLvHRDPELWGDDAKEFNPERF-AEGISKATkGQVSYFPFGWGPRICIGQNFALLEAKMALAlILQRF 404
                        490       500
                 ....*....|....*....|
gi 145337333 492 YkFHLVPN--HpVKYRMMTI 509
Cdd:cd20642  405 S-FELSPSyvH-APYTVLTL 422
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
284-498 6.47e-23

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: 101.61  E-value: 6.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 284 DPDSKETEksLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQE-LEKESAEATNTSLhqydtEDFNSFne 362
Cdd:cd20622  255 KPDYYSQV--IHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSaHPEAVAEGRLPTA-----QEIAQA-- 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 363 kvtefagllnydslgKLHYLHAVITETLRLYPAVPQDPKGVLED-DML----PNGTKVkagGMVTYVP-YSMGRMEYNW- 435
Cdd:cd20622  326 ---------------RIPYLDAVIEEILRCANTAPILSREATVDtQVLgysiPKGTNV---FLLNNGPsYLSPPIEIDEs 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 436 -----------------GSDAALFKPERWLK------DGVFqNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILcrFY 492
Cdd:cd20622  388 rrssssaakgkkagvwdSKDIADFDPERWLVtdeetgETVF-DPSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLL--VW 464

                 ....*.
gi 145337333 493 KFHLVP 498
Cdd:cd20622  465 NFELLP 470
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
107-503 4.37e-22

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: 98.44  E-value: 4.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 107 GIFNSDGELWRKQRKtasfeFASKNLRDFStvvFKEYSLKLFtILSQA-----SFKEQQ---VDMQELLMRMTLDSICKV 178
Cdd:cd20651   50 GITFTDGPFWKEQRR-----FVLRHLRDFG---FGRRSMEEV-IQEEAeelidLLKKGEkgpIQMPDLFNVSVLNVLWAM 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 179 GFGVEIGTLAPELPE-----NHFAKAFD----TANIIVTLRFIDPLW-KMKKFLNIGSEallgksikvVNDFTYSVIRRR 248
Cdd:cd20651  121 VAGERYSLEDQKLRKllelvHLLFRNFDmsggLLNQFPWLRFIAPEFsGYNLLVELNQK---------LIEFLKEEIKEH 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 249 KAELLEAQISptnnnnnnnnkvkhDILSRFI---EISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNEN 325
Cdd:cd20651  192 KKTYDEDNPR--------------DLIDAYLremKKKEPPSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPE 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 326 VAEKLYSELQELekesaeatntslhqYDTEDFNSFNEKVtefagllnydslgKLHYLHAVITETLRLYPAVPQD-PKGVL 404
Cdd:cd20651  258 VQRKVQEEIDEV--------------VGRDRLPTLDDRS-------------KLPYTEAVILEVLRIFTLVPIGiPHRAL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 405 EDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWGsDAALFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMA 484
Cdd:cd20651  311 KDTTL-GGYRIPKDTTILASLYSVHMDPEYWG-DPEEFRPERFLDEDG-KLLKDEWFLPFGAGKRRCLGESLARNELFLF 387
                        410
                 ....*....|....*....
gi 145337333 485 MAILCRfyKFHLVPNHPVK 503
Cdd:cd20651  388 FTGLLQ--NFTFSPPNGSL 404
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
44-516 5.18e-22

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: 98.25  E-value: 5.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  44 FDRMHDWLVEY----LYNSRTVVVpmpfttyTYIADPINVEYVLKTNFSNYPKGETYHSYMEVLLGDGIFNSDGELWRKQ 119
Cdd:cd20640    1 FPYFDKWRKQYgpifTYSTGNKQF-------LYVSRPEMVKEINLCVSLDLGKPSYLKKTLKPLFGGGILTSNGPHWAHQ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 120 RKTASFEFASKNLR-------DFSTVVFKEYSLKLFTilSQASFKEQQVDmqELLMRMTLDSICKVGFGV------EIGT 186
Cdd:cd20640   74 RKIIAPEFFLDKVKgmvdlmvDSAQPLLSSWEERIDR--AGGMAADIVVD--EDLRAFSADVISRACFGSsyskgkEIFS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 187 LAPELpenhfAKAFDTANIIVTLrfidPLWKmkkFLNIGSEALLGKSIKVVNDFTYSVIRRRKAElleaqisptnnnnnn 266
Cdd:cd20640  150 KLREL-----QKAVSKQSVLFSI----PGLR---HLPTKSNRKIWELEGEIRSLILEIVKEREEE--------------- 202
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 267 nNKVKHDILSRFIEISDDP--DSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKesaea 344
Cdd:cd20640  203 -CDHEKDLLQAILEGARSScdKKAEAEDFIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK----- 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 345 tntslhqydtedfnsfnekvtefAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDML-----PNGTKVkagg 419
Cdd:cd20640  277 -----------------------GGPPDADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLgglvvPKGVNI---- 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 420 mvtYVPYSMGRMEYN-WGSDAALFKPERWlKDGVFQNAS-PFKFTAFQAGPRICLGKDSAYLQMKMAMA-ILCRFyKFHL 496
Cdd:cd20640  330 ---WVPVSTLHLDPEiWGPDANEFNPERF-SNGVAAACKpPHSYMPFGAGARTCLGQNFAMAELKVLVSlILSKF-SFTL 404
                        490       500
                 ....*....|....*....|..
gi 145337333 497 VPN--HPVKYRMmtILSMAHGL 516
Cdd:cd20640  405 SPEyqHSPAFRL--IVEPEFGV 424
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
73-516 5.76e-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: 95.68  E-value: 5.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  73 IADPINVEYVLKTNFSNYPKGETYHSYMEVLLgDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILS 152
Cdd:cd20649   18 IAEPDMIKQVLVKDFNNFTNRMKANLITKPMS-DSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNLKS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 153 QASfKEQQVDMQELLMRMTLDSICKVGFGVEIGTL-APELPENHFAK---AFDTANIIVTLRFIDPLWkMKKFLNIgsea 228
Cdd:cd20649   97 YAE-SGNAFNIQRCYGCFTMDVVASVAFGTQVDSQkNPDDPFVKNCKrffEFSFFRPILILFLAFPFI-MIPLARI---- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 229 LLGKSIKVVNDFTYSVIR-------------RRKAEL---LEAQISPTNNNNNNNNKVKHDILSRFIEISDDPDSKETEK 292
Cdd:cd20649  171 LPNKSRDELNSFFTQCIRnmiafrdqqspeeRRRDFLqlmLDARTSAKFLSVEHFDIVNDADESAYDGHPNSPANEQTKP 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 293 SLRDIVLN----------FVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEAtntslhqydteDFNSFNE 362
Cdd:cd20649  251 SKQKRMLTedeivgqafiFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMV-----------DYANVQE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 363 kvtefagllnydslgkLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYvpySMGRMEYN---WGSDA 439
Cdd:cd20649  320 ----------------LPYLDMVIAETLRMYPPAFRFAREAAEDCVV-LGQRIPAGAVLEI---PVGFLHHDpehWPEPE 379
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145337333 440 AlFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH--PVKYRMMTILSMAHGL 516
Cdd:cd20649  380 K-FIPERFTAEAK-QRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETeiPLQLKSKSTLGPKNGV 456
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
270-503 6.59e-21

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 94.87  E-value: 6.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 270 VKHDILSRFIEISDDP----------DSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEK 339
Cdd:cd20645  193 AKHCIDKRLQRYSQGPandflcdiyhDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLP 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 340 ESAEATNtslhqydtedfnsfnekvtefagllnyDSLGKLHYLHAVITETLRLYPAVP-----QDPKGVLEDDMLPNGTk 414
Cdd:cd20645  273 ANQTPRA---------------------------EDLKNMPYLKACLKESMRLTPSVPftsrtLDKDTVLGDYLLPKGT- 324
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 415 vkaggMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGvfQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKF 494
Cdd:cd20645  325 -----VLMINSQALGSSEEYF-EDGRQFKPERWLQEK--HSINPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQI 396

                 ....*....
gi 145337333 495 HLVPNHPVK 503
Cdd:cd20645  397 VATDNEPVE 405
PLN02687 PLN02687
flavonoid 3'-monooxygenase
7-473 9.76e-21

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 95.26  E-value: 9.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   7 IACMVTSWIFLHRWGQRNKS------GPKTWPLVG-------AAIEQLTNFDRMHDWLVEYLYNSRTVVVPMpfttytyi 73
Cdd:PLN02687  12 VAVSVLVWCLLLRRGGSGKHkrplppGPRGWPVLGnlpqlgpKPHHTMAALAKTYGPLFRLRFGFVDVVVAA-------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  74 ADPINVEYvLKT---NFSNYP--KGETYHSYMevlLGDGIFNSDGELWRKQRKTASFE-FASKNLRDFSTVVFKEYSLKL 147
Cdd:PLN02687  84 SASVAAQF-LRThdaNFSNRPpnSGAEHMAYN---YQDLVFAPYGPRWRALRKICAVHlFSAKALDDFRHVREEEVALLV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 148 FTILSQAsfKEQQVDMQELLMRMTLDSICKVG-----FGVEIGTLAPELPE-----NHFAKAFDTANIIVTLRFIDP--- 214
Cdd:PLN02687 160 RELARQH--GTAPVNLGQLVNVCTTNALGRAMvgrrvFAGDGDEKAREFKEmvvelMQLAGVFNVGDFVPALRWLDLqgv 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 215 LWKMKKFLnigseallgksiKVVNDFTYSVIRRRKAELLEAQISPTnnnnnnnnkvkhDILSRFI-----EISDDPDSKE 289
Cdd:PLN02687 238 VGKMKRLH------------RRFDAMMNGIIEEHKAAGQTGSEEHK------------DLLSTLLalkreQQADGEGGRI 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 290 TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAG 369
Cdd:PLN02687 294 TDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEEL---------------------------DAVVGRDR 346
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 370 LLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWL- 448
Cdd:PLN02687 347 LVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQW-PDPLEFRPDRFLp 425
                        490       500
                 ....*....|....*....|....*...
gi 145337333 449 ---KDGVFQNASPFKFTAFQAGPRICLG 473
Cdd:PLN02687 426 ggeHAGVDVKGSDFELIPFGAGRRICAG 453
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
145-519 1.56e-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: 94.20  E-value: 1.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 145 LKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGV----------EIGTLAPELpeNHFAKAFDTANiivtlrFIDP 214
Cdd:cd20655   90 ERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRscseengeaeEVRKLVKES--AELAGKFNASD------FIWP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 215 LWKMKKFLNigseallGKSIKVVndftysviRRRKAELLEAQISP----TNNNNNNNNKVKHDILsrfIEISDDPDS--K 288
Cdd:cd20655  162 LKKLDLQGF-------GKRIMDV--------SNRFDELLERIIKEheekRKKRKEGGSKDLLDIL---LDAYEDENAeyK 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 289 ETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFA 368
Cdd:cd20655  224 ITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEI---------------------------DSVVGKT 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 369 GLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEdDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWL 448
Cdd:cd20655  277 RLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTE-GCKINGYDIPEKTTLFVNVYAIMRDPNYW-EDPLEFKPERFL 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 449 KDG-----VFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKyrM-----MTiLSMAHGLKV 518
Cdd:cd20655  355 ASSrsgqeLDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGEKVN--MeeasgLT-LPRAHPLKC 431

                 .
gi 145337333 519 T 519
Cdd:cd20655  432 V 432
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
48-500 1.74e-20

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: 94.05  E-value: 1.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  48 HDWLVEY----LYNSRTvvvpmpfTTYTYIADPINVEYVLKTNFSNYPKGETyHSYMEVLLGDGIFNSDGELWRKQRKTA 123
Cdd:cd20641    5 QQWKSQYgetfLYWQGT-------TPRICISDHELAKQVLSDKFGFFGKSKA-RPEILKLSGKGLVFVNGDDWVRHRRVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 124 SFEFASKNLRDFSTVVfKEYSLKLF----TILSQASFKEQQVDMQELLMRMTLDSICKVGFGveigtlapelpeNHFAKA 199
Cdd:cd20641   77 NPAFSMDKLKSMTQVM-ADCTERMFqewrKQRNNSETERIEVEVSREFQDLTADIIATTAFG------------SSYAEG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 200 fdtaniivtlrfIDPLWKMKKFLNIGSEALLGKSIKVVNDF-TYSVIRRRKAE-LLEAQISPTNNNNNNNNKVKH--DIL 275
Cdd:cd20641  144 ------------IEVFLSQLELQKCAAASLTNLYIPGTQYLpTPRNLRVWKLEkKVRNSIKRIIDSRLTSEGKGYgdDLL 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 276 SRFIEI-SDDPDSKETEKSLR-----DIVLNFVIAGRDTTATTLTWAIYMImmnenvaeKLYSELQELEKEsaeatntsl 349
Cdd:cd20641  212 GLMLEAaSSNEGGRRTERKMSideiiDECKTFFFAGHETTSNLLTWTMFLL--------SLHPDWQEKLRE--------- 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 350 hqydtEDFNSFNEKVTEFAgllnyDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDdMLPNGTKVKAGGMVTYVPYSMG 429
Cdd:cd20641  275 -----EVFRECGKDKIPDA-----DTLSKLKLMNMVLMETLRLYGPVINIARRASED-MKLGGLEIPKGTTIIIPIAKLH 343
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145337333 430 RMEYNWGSDAALFKPERWlKDGVFQNAS-PFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH 500
Cdd:cd20641  344 RDKEVWGSDADEFNPLRF-ANGVSRAAThPNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPEY 414
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
109-514 2.94e-20

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: 93.13  E-value: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 109 FNSDGELWRKQRKTASfefasKNLRDFST---------VVFKEYSlKLFTILSQASFKEQQVDMQELLMRMTLDSICKVG 179
Cdd:cd11028   54 FSDYGPRWKLHRKLAQ-----NALRTFSNarthnpleeHVTEEAE-ELVTELTENNGKPGPFDPRNEIYLSVGNVICAIC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 180 FGVEIGTLAPELPE-----NHFAKAFDTAN---IIVTLRFIdPLWKMKKFLNIgseallgksIKVVNDFTYSVIRRRKAE 251
Cdd:cd11028  128 FGKRYSRDDPEFLElvksnDDFGAFVGAGNpvdVMPWLRYL-TRRKLQKFKEL---------LNRLNSFILKKVKEHLDT 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 252 LLEAQIsptnnnnnnnnkvkHDILSRFIEISDD------PDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNEN 325
Cdd:cd11028  198 YDKGHI--------------RDITDALIKASEEkpeeekPEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPE 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 326 VAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQD-PKGVL 404
Cdd:cd11028  264 IQEKVQAEL---------------------------DRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTiPHATT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 405 EDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWGsDAALFKPERWLKDGVFQNASPF-KFTAFQAGPRICLGKDSAYLQMKM 483
Cdd:cd11028  317 RDTTL-NGYFIPKGTVVFVNLWSVNHDEKLWP-DPSVFRPERFLDDNGLLDKTKVdKFLPFGAGRRRCLGEELARMELFL 394
                        410       420       430
                 ....*....|....*....|....*....|.
gi 145337333 484 AMAILCRFYKFHLVPNHPVKYRMMTILSMAH 514
Cdd:cd11028  395 FFATLLQQCEFSVKPGEKLDLTPIYGLTMKP 425
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
82-518 3.15e-20

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: 92.98  E-value: 3.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  82 VLKTN---FSNYP-----KGETYHSYMEVLLgdgifnSDGELWRKQRKTASFE-FASKNLrDFSTVVFKEYSLKLFTILS 152
Cdd:cd11073   29 VLKTHdrvLSGRDvpdavRALGHHKSSIVWP------PYGPRWRMLRKICTTElFSPKRL-DATQPLRRRKVRELVRYVR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 153 QASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTlapelPENHFAKAFDTA--NIIVT------------LRFIDPLWKM 218
Cdd:cd11073  102 EKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVD-----PDSESGSEFKELvrEIMELagkpnvadffpfLKFLDLQGLR 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 219 KKFlnigsEALLGKSIKVVNDFtysvIRRRKAElleaqisptnnNNNNNNKVKHDILSRFIEISDDPDSKETEKSLRDIV 298
Cdd:cd11073  177 RRM-----AEHFGKLFDIFDGF----IDERLAE-----------REAGGDKKKDDDLLLLLDLELDSESELTRNHIKALL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 299 LNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQE-LEKesaeatntslhqydtedfnsfNEKVTEfagllnyDSLG 377
Cdd:cd11073  237 LDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEvIGK---------------------DKIVEE-------SDIS 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 378 KLHYLHAVITETLRLYPAVP--------QDpkGVLEDDMLPNGTKVkaggMVTYvpYSMGRMEYNWgSDAALFKPERWLK 449
Cdd:cd11073  289 KLPYLQAVVKETLRLHPPAPlllprkaeED--VEVMGYTIPKGTQV----LVNV--WAIGRDPSVW-EDPLEFKPERFLG 359
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145337333 450 DGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLvPNHPVKYRM-MT-----ILSMAHGLKV 518
Cdd:cd11073  360 SEIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLASLLHSFDWKL-PDGMKPEDLdMEekfglTLQKAVPLKA 433
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
105-496 1.80e-19

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: 90.93  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 105 GDGIFNSDGELWRKQRKtasfeFASKNLRDFSTVVFKEYSLKL----------FTILSQASfKEQQVDMQELLMRMTLDS 174
Cdd:cd20652   46 GNGIICAEGDLWRDQRR-----FVHDWLRQFGMTKFGNGRAKMekriatgvheLIKHLKAE-SGQPVDPSPVLMHSLGNV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 175 ICKVGFGVeigTLAPELPE------------NHFAKAfDTANIIVTLRFIDPLWKMKKFLNIGSEAllgksikvVNDFTY 242
Cdd:cd20652  120 INDLVFGF---RYKEDDPTwrwlrflqeegtKLIGVA-GPVNFLPFLRHLPSYKKAIEFLVQGQAK--------THAIYQ 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 243 SVI-RRRKAELLEAQISPTNNNNNNNNKVKHdilsrFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIM 321
Cdd:cd20652  188 KIIdEHKRRLKPENPRDAEDFELCELEKAKK-----EGEDRDLFDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMA 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 322 MNENVAEKLYSELQELEKEsaeatntslHQYDTedfnsfnekvtefagllnYDSLGKLHYLHAVITETLRLYPAVPQD-P 400
Cdd:cd20652  263 LFPKEQRRIQRELDEVVGR---------PDLVT------------------LEDLSSLPYLQACISESQRIRSVVPLGiP 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 401 KGVLEDDMLpNGTKVKAGGMVTYVPYSMgRMEYNWGSDAALFKPERWL-KDGVFQnaSPFKFTAFQAGPRICLGKDsayl 479
Cdd:cd20652  316 HGCTEDAVL-AGYRIPKGSMIIPLLWAV-HMDPNLWEEPEEFRPERFLdTDGKYL--KPEAFIPFQTGKRMCLGDE---- 387
                        410       420
                 ....*....|....*....|..
gi 145337333 480 qmkMAMAILCRF-----YKFHL 496
Cdd:cd20652  388 ---LARMILFLFtarilRKFRI 406
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
1-512 3.90e-19

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 90.14  E-value: 3.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   1 MSLCLVIACMVTSWIFLHRWGQRNKS-----GPKTWPLVGAaIEQLTNFDRMHdwlveYLYNSRTVVVPMpFTT------ 69
Cdd:PLN03234   1 MDLFLIIAALVAAAAFFFLRSTTKKSlrlppGPKGLPIIGN-LHQMEKFNPQH-----FLFRLSKLYGPI-FTMkiggrr 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  70 YTYIADPINVEYVLKT---NFSNYP--KGETYHSYMEVLLGDGIFNSdgeLWRKQRKTASFEFASKNLRDFSTVVFKEYS 144
Cdd:PLN03234  74 LAVISSAELAKELLKTqdlNFTARPllKGQQTMSYQGRELGFGQYTA---YYREMRKMCMVNLFSPNRVASFRPVREEEC 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 145 LKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELpENHFAKAFDTANIIVTLRFIDpLWKMKKFLN- 223
Cdd:PLN03234 151 QRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEM-KRFIDILYETQALLGTLFFSD-LFPYFGFLDn 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 224 -IGSEALLGKSIKVVNDFTysvirrrkAELLEAQISPTNNNNNNNNKVkhDILSRFIEisDDPDS-KETEKSLRDIVLNF 301
Cdd:PLN03234 229 lTGLSARLKKAFKELDTYL--------QELLDETLDPNRPKQETESFI--DLLMQIYK--DQPFSiKFTHENVKAMILDI 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 302 VIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESaeatntslhqydtedfnsfnekvtefaGLLNYDSLGKLHY 381
Cdd:PLN03234 297 VVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDK---------------------------GYVSEEDIPNLPY 349
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 382 LHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKD--GVFQNASPF 459
Cdd:PLN03234 350 LKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDNPNEFIPERFMKEhkGVDFKGQDF 429
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 460 KFTAFQAGPRICLGKDSAYLQMKMAMAILcrFYKFHL-----VPNHPVKYRMMTILSM 512
Cdd:PLN03234 430 ELLPFGSGRRMCPAMHLGIAMVEIPFANL--LYKFDWslpkgIKPEDIKMDVMTGLAM 485
PLN02655 PLN02655
ent-kaurene oxidase
290-488 2.69e-18

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 87.49  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 290 TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedfnSFNEKVTEfag 369
Cdd:PLN02655 259 TDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREV---------------------CGDERVTE--- 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 370 llnyDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLk 449
Cdd:PLN02655 315 ----EDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRW-ENPEEWDPERFL- 388
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 145337333 450 DGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAIL 488
Cdd:PLN02655 389 GEKYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARL 427
PLN02966 PLN02966
cytochrome P450 83A1
27-512 3.63e-18

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 87.50  E-value: 3.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  27 GPKTWPLVGAAIE-QLTNFDRMH-DW------LVEYLYNSRTVVVpmpfttytyIADPINVEYVLKT---NFSNYPKGET 95
Cdd:PLN02966  33 GPSPLPVIGNLLQlQKLNPQRFFaGWakkygpILSYRIGSRTMVV---------ISSAELAKELLKTqdvNFADRPPHRG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  96 yHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSI 175
Cdd:PLN02966 104 -HEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 176 CKVGFGVEIGTLAPElpenhfakafdtaniivtlrfidplwkMKKFLNI--GSEALLGKsIKVVNDFTYS---------- 243
Cdd:PLN02966 183 CRQAFGKKYNEDGEE---------------------------MKRFIKIlyGTQSVLGK-IFFSDFFPYCgflddlsglt 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 244 VIRRRKAELLEAQISPTNNNNNNNNKVK---HDILSRFIEI-SDDPDSKE-TEKSLRDIVLNFVIAGRDTTATTLTWAIY 318
Cdd:PLN02966 235 AYMKECFERQDTYIQEVVNETLDPKRVKpetESMIDLLMEIyKEQPFASEfTVDNVKAVILDIVVAGTDTAAAAVVWGMT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 319 MIMMNENVAEKLYSELQELEKESAEATntslhqydtedfnsfnekVTEfagllnyDSLGKLHYLHAVITETLRLYPAVPQ 398
Cdd:PLN02966 315 YLMKYPQVLKKAQAEVREYMKEKGSTF------------------VTE-------DDVKNLPYFRALVKETLRIEPVIPL 369
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 399 -DPKGVLEDDMLPnGTKVKAGGMVTYVPYSMGRMEYNWGSDAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSA 477
Cdd:PLN02966 370 lIPRACIQDTKIA-GYDIPAGTTVNVNAWAVSRDEKEWGPNPDEFRPERFLEKEVDFKGTDYEFIPFGSGRRMCPGMRLG 448
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 145337333 478 YLQMKMAMAILCRFYKFHLvPN----HPVKYRMMTILSM 512
Cdd:PLN02966 449 AAMLEVPYANLLLNFNFKL-PNgmkpDDINMDVMTGLAM 486
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
83-506 1.99e-17

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 84.78  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  83 LKT---NFSNYPK--GETYHSYMEvllGDGIFNSDGELWRKQRKTASFE-FASKNLRDFSTVVFKEYSLKLFTiLSQASF 156
Cdd:cd20657   26 LKThdaNFSNRPPnaGATHMAYNA---QDMVFAPYGPRWRLLRKLCNLHlFGGKALEDWAHVRENEVGHMLKS-MAEASR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 157 KEQQVDMQELLMRMTLDSICKVG-----FGVEIGTLAPELPE-----NHFAKAFDTANIIVTLRFIDPLwkmkkflniGS 226
Cdd:cd20657  102 KGEPVVLGEMLNVCMANMLGRVMlskrvFAAKAGAKANEFKEmvvelMTVAGVFNIGDFIPSLAWMDLQ---------GV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 227 EALLGKSIKVVNDFTYSVIRRRKAELLEaqisptnnnnnnnNKVKHDILSrFIEISDDPDS---KETEKSLRDIVLNFVI 303
Cdd:cd20657  173 EKKMKRLHKRFDALLTKILEEHKATAQE-------------RKGKPDFLD-FVLLENDDNGegeRLTDTNIKALLLNLFT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 304 AGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAGLLNYDSLGKLHYLH 383
Cdd:cd20657  239 AGTDTSSSTVEWALAELIRHPDILKKAQEEM---------------------------DQVIGRDRRLLESDIPNLPYLQ 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 384 AVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRmEYNWGSDAALFKPERWL---KDGVFQNASPFK 460
Cdd:cd20657  292 AICKETFRLHPSTPLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGR-DPDVWENPLEFKPERFLpgrNAKVDVRGNDFE 370
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 145337333 461 FTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLV-PNHPVKYRM 506
Cdd:cd20657  371 LIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPaGQTPEELNM 417
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
169-510 4.61e-17

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


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 83.26  E-value: 4.61e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 169 RMTLDSICKVGFGVEIGTLAPELPEN--HFAKAFDTANIIVTLRFIDPLWKMKKFLniGSEALLGKSIKVVNDFTYSVIR 246
Cdd:cd20648  123 KFGLEGISSVLFESRIGCLEANVPEEteTFIQSINTMFVMTLLTMAMPKWLHRLFP--KPWQRFCRSWDQMFAFAKGHID 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 247 RRKAELLEAQISPtnnnNNNNNKVKHDILSRfieisddpdSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENV 326
Cdd:cd20648  201 RRMAEVAAKLPRG----EAIEGKYLTYFLAR---------EKLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDV 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 327 AEKLYSELQELEKESAEATNTSLHQydtedfnsfnekvtefagllnydslgkLHYLHAVITETLRLYPAVPQDPKGVLED 406
Cdd:cd20648  268 QTALHREITAALKDNSVPSAADVAR---------------------------MPLLKAVVKEVLRLYPVIPGNARVIPDR 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 407 DMLPNGTKVKAGGMVTYVPYSMGRMEyNWGSDAALFKPERWLKDGvfQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMA 486
Cdd:cd20648  321 DIQVGEYIIPKKTLITLCHYATSRDE-NQFPDPNSFRPERWLGKG--DTHHPYASLPFGFGKRSCIGRRIAELEVYLALA 397
                        330       340
                 ....*....|....*....|....*
gi 145337333 487 -ILCRFYKFHLVPNHPVKYRMMTIL 510
Cdd:cd20648  398 rILTHFEVRPEPGGSPVKPMTRTLL 422
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
293-519 6.72e-17

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: 82.75  E-value: 6.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 293 SLRDIV--LNFVI-AGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKesaeatntslhqydtedfnsfnekvtefaG 369
Cdd:cd11045  208 SDDDIVnhMIFLMmAAHDTTTSTLTSMAYFLARHPEWQERLREESLALGK-----------------------------G 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 370 LLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLK 449
Cdd:cd11045  259 TLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV-LGYRIPAGTLVAVSPGVTHYMPEYW-PNPERFDPERFSP 336
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 450 DGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTILSMAHGLKVT 519
Cdd:cd11045  337 ERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGYYPPWWQSPLPAPKDGLPVV 406
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
113-523 9.38e-17

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: 82.66  E-value: 9.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 113 GELWRKQRKTASFEFAS-------KNLRdFSTV--VFKE-YSLKLFTILSQASFKeqqVDMQELLMRMTLDSICKVGFGV 182
Cdd:cd20654   58 GPYWRELRKIATLELLSnrrleklKHVR-VSEVdtSIKElYSLWSNNKKGGGGVL---VEMKQWFADLTFNVILRMVVGK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 183 EIGTLAPELPEN---HFAKAFD----------TANIIVTLRFIDPLW---KMKKflnigsealLGKSIKVVNdftysvir 246
Cdd:cd20654  134 RYFGGTAVEDDEeaeRYKKAIRefmrlagtfvVSDAIPFLGWLDFGGhekAMKR---------TAKELDSIL-------- 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 247 rrkAELLEAQISptnnNNNNNNKVKHDILSRFIEISDDPDSKETEKSLRDIV-----LNFVIAGRDTTATTLTWAIYMIM 321
Cdd:cd20654  197 ---EEWLEEHRQ----KRSSSGKSKNDEDDDDVMMLSILEDSQISGYDADTVikatcLELILGGSDTTAVTLTWALSLLL 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 322 MNENVAEKLYSELqelekesaeatntslhqydteDFNSFNEKVTEFAgllnydSLGKLHYLHAVITETLRLYPAVP-QDP 400
Cdd:cd20654  270 NNPHVLKKAQEEL---------------------DTHVGKDRWVEES------DIKNLVYLQAIVKETLRLYPPGPlLGP 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 401 KGVLEDDMLpNGTKVKAGgmvtyvpysmGRMEYN----------WgSDAALFKPERWL---KDGVF--QNaspFKFTAFQ 465
Cdd:cd20654  323 REATEDCTV-GGYHVPKG----------TRLLVNvwkiqrdpnvW-SDPLEFKPERFLtthKDIDVrgQN---FELIPFG 387
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145337333 466 AGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKyrmMT-----ILSMAHGLKVTVSRR 523
Cdd:cd20654  388 SGRRSCPGVSFGLQVMHLTLARLLHGFDIKTPSNEPVD---MTegpglTNPKATPLEVLLTPR 447
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
291-516 3.11e-16

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: 80.73  E-value: 3.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 291 EKSLRDIVLN---FVIAGRDTTATTLTWAIYMIMMNENVAEKLYSEL-QELEKEsaeatntslHQYDTEDfnsfnekvte 366
Cdd:cd20647  232 ELTLEEIYANmteMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIvRNLGKR---------VVPTAED---------- 292
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 367 fagllnydsLGKLHYLHAVITETLRLYPAVPQDPKgVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPER 446
Cdd:cd20647  293 ---------VPKLPLIRALLKETLRLFPVLPGNGR-VTQDDLIVGGYLIPKGTQLALCHYSTSYDEENF-PRAEEFRPER 361
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 447 WLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPnhpvkyRMMTILSMAHGL 516
Cdd:cd20647  362 WLRKDALDRVDNFGSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKVSP------QTTEVHAKTHGL 425
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
113-488 3.20e-16

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: 80.73  E-value: 3.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 113 GELWRKQRKTASFE-FASKNLRDFSTVVfKEYSLKLFTILSQASFKEQQ-VDMQELLMRMTLDSICK-------VGFGVE 183
Cdd:cd20653   58 GDHWRNLRRITTLEiFSSHRLNSFSSIR-RDEIRRLLKRLARDSKGGFAkVELKPLFSELTFNNIMRmvagkryYGEDVS 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 184 IGTLAPELPE-----NHFAKAFDTANIIVTLRFIDPLWKMKKFLNIGseallgksiKVVNDFTYSVI---RRRKAELLEA 255
Cdd:cd20653  137 DAEEAKLFRElvseiFELSGAGNPADFLPILRWFDFQGLEKRVKKLA---------KRRDAFLQGLIdehRKNKESGKNT 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 256 QIsptnnnnnnnnkvkhDILSRFIEisDDPDSKeTEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELq 335
Cdd:cd20653  208 MI---------------DHLLSLQE--SQPEYY-TDEIIKGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEI- 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 336 elekesaeatntslhqydtedfnsfNEKVtEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKV 415
Cdd:cd20653  269 -------------------------DTQV-GQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDCKIGGYDI 322
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145337333 416 KAGGMVTYVPYSMGRmEYNWGSDAALFKPERwlkdgvFQNAS--PFKFTAFQAGPRICLGKDSAYLQMKMAMAIL 488
Cdd:cd20653  323 PRGTMLLVNAWAIHR-DPKLWEDPTKFKPER------FEGEEreGYKLIPFGLGRRACPGAGLAQRVVGLALGSL 390
PLN02183 PLN02183
ferulate 5-hydroxylase
2-496 6.70e-16

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 80.28  E-value: 6.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333   2 SLCLVIACMVTSWIFLHRWGQRNK--SGPKTWPLVGAA--IEQLTnfdrmHDWLVEY------LYNSRtvvvpMPFTTYT 71
Cdd:PLN02183  13 SFFLILISLFLFLGLISRLRRRLPypPGPKGLPIIGNMlmMDQLT-----HRGLANLakqyggLFHMR-----MGYLHMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  72 YIADPINVEYVLKTN---FSNYPkGETYHSYMEVLLGDGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSlklF 148
Cdd:PLN02183  83 AVSSPEVARQVLQVQdsvFSNRP-ANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKLFSRKRAESWASVRDEVD---S 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 149 TILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAPELPE--NHFAK---AFDTANIIVTLRFIDPLwkmkkfln 223
Cdd:PLN02183 159 MVRSVSSNIGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDEFIKilQEFSKlfgAFNVADFIPWLGWIDPQ-------- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 224 iGSEALLGKSIKVVNDFTYSVIRRRKAEllEAQISPTNNNNNNNNKVKHDILSRFIE---ISDDPDSKETEKSLRD---- 296
Cdd:PLN02183 231 -GLNKRLVKARKSLDGFIDDIIDDHIQK--RKNQNADNDSEEAETDMVDDLLAFYSEeakVNESDDLQNSIKLTRDnika 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 297 IVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEkesaeATNTSLHQYDTEdfnsfnekvtefagllnydsl 376
Cdd:PLN02183 308 IIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVV-----GLNRRVEESDLE--------------------- 361
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 377 gKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGV--FQ 454
Cdd:PLN02183 362 -KLTYLKCTLKETLRLHPPIPLLLHETAEDAEV-AGYFIPKRSRVMINAWAIGRDKNSW-EDPDTFKPSRFLKPGVpdFK 438
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 145337333 455 nASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHL 496
Cdd:PLN02183 439 -GSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWEL 479
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
93-496 1.26e-15

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: 79.11  E-value: 1.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  93 GETYHSYMEVLLGD-GIFNSDGELWRKQRKtasfeFASKNLRDFS------TVVFKEYSLKLFTILSQAsfKEQQVDMQE 165
Cdd:cd20667   36 GRPLTPFFRDLFGEkGIICTNGLTWKQQRR-----FCMTTLRELGlgkqalESQIQHEAAELVKVFAQE--NGRPFDPQD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 166 LLMRMTLDSICKVGFGVEIGTLAPElpenhFAKAFDTANIIVTlrFIDPLW-KMKKFLNIGSEALLGKSIKVV--NDFTY 242
Cdd:cd20667  109 PIVHATANVIGAVVFGHRFSSEDPI-----FLELIRAINLGLA--FASTIWgRLYDAFPWLMRYLPGPHQKIFayHDAVR 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 243 SVIRRR-KAELLEAQISPtnnnnnnnnkvkHDI----LSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAI 317
Cdd:cd20667  182 SFIKKEvIRHELRTNEAP------------QDFidcyLAQITKTKDDPVSTFSEENMIQVVIDLFLGGTETTATTLHWAL 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 318 YMIMMNENVAEKLYSELQElekesaeatntslhqydtedfnsfnekVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVP 397
Cdd:cd20667  250 LYMVHHPEIQEKVQQELDE---------------------------VLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVS 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 398 QdpkGVLEDDMLP---NGTKVKAGGMVTYVPYSMGRMEYNWGSDAAlFKPERWL-KDGVFQNASpfKFTAFQAGPRICLG 473
Cdd:cd20667  303 V---GAVRQCVTSttmHGYYVEKGTIILPNLASVLYDPECWETPHK-FNPGHFLdKDGNFVMNE--AFLPFSAGHRVCLG 376
                        410       420
                 ....*....|....*....|...
gi 145337333 474 KDSAYLQMKMAMAILCRFYKFHL 496
Cdd:cd20667  377 EQLARMELFIFFTTLLRTFNFQL 399
PLN02290 PLN02290
cytokinin trans-hydroxylase
301-500 1.85e-15

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 79.09  E-value: 1.85e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 301 FVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqydtedfnsFNEKVTefagllNYDSLGKLH 380
Cdd:PLN02290 324 FFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEV----------------------CGGETP------SVDHLSKLT 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 381 YLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKagGMVTYVP-YSMGRMEYNWGSDAALFKPERWlkdGVFQNASPF 459
Cdd:PLN02290 376 LLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPK--GLSIWIPvLAIHHSEELWGKDANEFNPDRF---AGRPFAPGR 450
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 145337333 460 KFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH 500
Cdd:PLN02290 451 HFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNY 491
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
107-485 2.19e-15

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: 78.22  E-value: 2.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 107 GIFNSDGELWRKQRKTASFEFASKNL------------RDFSTVVFKEyslklftiLSQASFKEQQVDMQELLMRMTLDS 174
Cdd:cd20643   57 GVLLKNGEAWRKDRLILNKEVLAPKVidnfvpllnevsQDFVSRLHKR--------IKKSGSGKWTADLSNDLFRFALES 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 175 ICKVGFGVEIGTLapelpENHFAKAfdtaniivTLRFIDPLWKMKK----FLNIGSEALLGKSIKVVNDF--TYSVIRRr 248
Cdd:cd20643  129 ICNVLYGERLGLL-----QDYVNPE--------AQRFIDAITLMFHttspMLYIPPDLLRLINTKIWRDHveAWDVIFN- 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 249 KAELLEAQISPTNNNNNNNNKVKHDILSRFIeisddpdsKETEKSLRDI---VLNFVIAGRDTTATTLTWAIYMIMMNEN 325
Cdd:cd20643  195 HADKCIQNIYRDLRQKGKNEHEYPGILANLL--------LQDKLPIEDIkasVTELMAGGVDTTSMTLQWTLYELARNPN 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 326 VAEKLYSELQELEKESaeatntslhQYDTEdfnsfneKVTEFAGLLNydslgklhylhAVITETLRLYP-AVP------Q 398
Cdd:cd20643  267 VQEMLRAEVLAARQEA---------QGDMV-------KMLKSVPLLK-----------AAIKETLRLHPvAVSlqryitE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 399 DPkgVLEDDMLPNGTKVKAGgmvtyvPYSMGRmeynwgsDAALFK------PERWLKdgvfQNASPFKFTAFQAGPRICL 472
Cdd:cd20643  320 DL--VLQNYHIPAGTLVQVG------LYAMGR-------DPTVFPkpekydPERWLS----KDITHFRNLGFGFGPRQCL 380
                        410
                 ....*....|...
gi 145337333 473 GKDSAYLQMKMAM 485
Cdd:cd20643  381 GRRIAETEMQLFL 393
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
114-498 1.16e-13

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: 72.83  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 114 ELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILSQAsfkEQQVDMQELLMRMTLDSICKVGFGVEIgTLAPELPE 193
Cdd:cd20674   60 LLWKAHRKLTRSALQLGIRNSLEPVVEQLTQELCERMRAQA---GTPVDIQEEFSLLTCSIICCLTFGDKE-DKDTLVQA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 194 NH-----FAKAFDTANIivtlRFIDPLWKMKKFLNIGSEALLgKSIKVVNDFTYSVIRRRKAELLEAQIsptnnnnnnnn 268
Cdd:cd20674  136 FHdcvqeLLKTWGHWSI----QALDSIPFLRFFPNPGLRRLK-QAVENRDHIVESQLRQHKESLVAGQW----------- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 269 kvkHDILSRFIEISDDPDSKE-----TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSEL-QELEKEsa 342
Cdd:cd20674  200 ---RDMTDYMLQGLGQPRGEKgmgqlLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELdRVLGPG-- 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 343 eatntslhqydtedfnsfnekvtefaGLLNYDSLGKLHYLHAVITETLRLYPAVPQD-PKGVLEDDMLpNGTKVKAGGMV 421
Cdd:cd20674  275 --------------------------ASPSYKDRARLPLLNATIAEVLRLRPVVPLAlPHRTTRDSSI-AGYDIPKGTVV 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145337333 422 TYVPYSMGRMEYNWgSDAALFKPERWLKDGvfqNASPfKFTAFQAGPRICLGKDSAYLQMKMAMAILCRfyKFHLVP 498
Cdd:cd20674  328 IPNLQGAHLDETVW-EQPHEFRPERFLEPG---AANR-ALLPFGCGARVCLGEPLARLELFVFLARLLQ--AFTLLP 397
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
85-481 1.34e-13

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: 72.61  E-value: 1.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  85 TNFSNYPkgetyHSYM-EVLLGDG---IFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSLKLFTILSQASfkeqq 160
Cdd:cd11065   32 AIYSSRP-----RMPMaGELMGWGmrlLLMPYGPRWRLHRRLFHQLLNPSAVRKYRPLQELESKQLLRDLLESPD----- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 161 vDMQELLMRMTLDSICKVGFGVEIGTLAPELPE--NHFAKAFDTANIIVT--------LRFIdPLWKMKKFLNIGSEall 230
Cdd:cd11065  102 -DFLDHIRRYAASIILRLAYGYRVPSYDDPLLRdaEEAMEGFSEAGSPGAylvdffpfLRYL-PSWLGAPWKRKARE--- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 231 gksikvVNDFTYSVIRRRKAELLEAQISPTnnnnnnnnkVKHDILSRFIEiSDDPDSKETEKSLRDIVLNFVIAGRDTTA 310
Cdd:cd11065  177 ------LRELTRRLYEGPFEAAKERMASGT---------ATPSFVKDLLE-ELDKEGGLSEEEIKYLAGSLYEAGSDTTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 311 TTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAGLLNYDSLGKLHYLHAVITETL 390
Cdd:cd11065  241 STLQTFILAMALHPEVQKKAQEEL---------------------------DRVVGPDRLPTFEDRPNLPYVNAIVKEVL 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 391 RLYPAVPQD-PKGVLEDDM-----LPNGTKVkaggmvtyVP--YSMGRMEyNWGSDAALFKPERWLKDGvFQNASPFK-- 460
Cdd:cd11065  294 RWRPVAPLGiPHALTEDDEyegyfIPKGTTV--------IPnaWAIHHDP-EVYPDPEEFDPERYLDDP-KGTPDPPDpp 363
                        410       420
                 ....*....|....*....|....*
gi 145337333 461 FTAFQAGPRIC----LGKDSAYLQM 481
Cdd:cd11065  364 HFAFGFGRRICpgrhLAENSLFIAI 388
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
105-473 2.38e-13

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: 71.82  E-value: 2.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 105 GDGIFNSDGELWRKQRKtasfeFASKNLRDFStvVFKEySLKlFTILSQASF--------KEQQVDMQELLMRMTLDSIC 176
Cdd:cd11026   49 GYGVVFSNGERWKQLRR-----FSLTTLRNFG--MGKR-SIE-ERIQEEAKFlveafrktKGKPFDPTFLLSNAVSNVIC 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 177 KVGFGVEIGTLAPElpenhFAKAFDTANiiVTLRFIDPLWKMkkFLNIGSEAL---------LGKSIKVVNDFTYSVIRR 247
Cdd:cd11026  120 SIVFGSRFDYEDKE-----FLKLLDLIN--ENLRLLSSPWGQ--LYNMFPPLLkhlpgphqkLFRNVEEIKSFIRELVEE 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 248 RKaELLEAQiSPtnnnnnnnnkvKHDI---LSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNE 324
Cdd:cd11026  191 HR-ETLDPS-SP-----------RDFIdcfLLKMEKEKDNPNSEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYP 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 325 NVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQD-PKGV 403
Cdd:cd11026  258 HIQEKVQEEI---------------------------DRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGvPHAV 310
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 404 LEDD-----MLPNGTKVkaggmvtyVP--YSMGRMEYNWgSDAALFKPERWL-KDGVFQnaSPFKFTAFQAGPRICLG 473
Cdd:cd11026  311 TRDTkfrgyTIPKGTTV--------IPnlTSVLRDPKQW-ETPEEFNPGHFLdEQGKFK--KNEAFMPFSAGKRVCLG 377
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
290-503 4.14e-13

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: 71.36  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 290 TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAG 369
Cdd:cd20656  227 SEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEEL---------------------------DRVVGSDR 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 370 LLNYDSLGKLHYLHAVITETLRLYPAVPQdpkgvleddMLPN--GTKVKAGGM------VTYVP-YSMGRMEYNWgSDAA 440
Cdd:cd20656  280 VMTEADFPQLPYLQCVVKEALRLHPPTPL---------MLPHkaSENVKIGGYdipkgaNVHVNvWAIARDPAVW-KNPL 349
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145337333 441 LFKPERWLKDGVFQNASPFKFTAFQAGPRICLGkdsAYLQMKMAMAILCR-FYKFHLVPNHPVK 503
Cdd:cd20656  350 EFRPERFLEEDVDIKGHDFRLLPFGAGRRVCPG---AQLGINLVTLMLGHlLHHFSWTPPEGTP 410
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
307-499 6.78e-13

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: 70.39  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 307 DTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATNTSLHQYDTedfnsfnekvtefagllnydslgklhYLHAVI 386
Cdd:cd20615  229 DVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILSTDT--------------------------LLAYCV 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 387 TETLRLYPA----VPQDPkgvlEDDMLPNGTKVKAGGMV---TYvpysmgRMEYN---WGSDAALFKPERWLkdGVFQNA 456
Cdd:cd20615  283 LESLRLRPLlafsVPESS----PTDKIIGGYRIPANTPVvvdTY------ALNINnpfWGPDGEAYRPERFL--GISPTD 350
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 145337333 457 SPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPN 499
Cdd:cd20615  351 LRYNFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPDQ 393
PLN00168 PLN00168
Cytochrome P450; Provisional
246-524 1.95e-12

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 69.59  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 246 RRRKAELLEAQISPTNNNNNNNNKVkhDILSRfIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNEN 325
Cdd:PLN00168 262 REYKNHLGQGGEPPKKETTFEHSYV--DTLLD-IRLPEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPS 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 326 VAEKLYSELQelekesAEATNTSlhqydtedfnsfnEKVTEfagllnyDSLGKLHYLHAVITETLRLYP----AVPQDPK 401
Cdd:PLN00168 339 IQSKLHDEIK------AKTGDDQ-------------EEVSE-------EDVHKMPYLKAVVLEGLRKHPpahfVLPHKAA 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 402 gvleDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSDAAlFKPERWLK----DGVFQNAS-PFKFTAFQAGPRICLGKDS 476
Cdd:PLN00168 393 ----EDMEVGGYLIPKGATVNFMVAEMGRDEREWERPME-FVPERFLAggdgEGVDVTGSrEIRMMPFGVGRRICAGLGI 467
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145337333 477 AYLQMKMAMAILCRFYKFHLVPNHPVKY---RMMTILsMAHGLKVTVSRRS 524
Cdd:PLN00168 468 AMLHLEYFVANMVREFEWKEVPGDEVDFaekREFTTV-MAKPLRARLVPRR 517
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
44-503 2.43e-12

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: 68.93  E-value: 2.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  44 FDRMHdwlVEYLYNSRTVVVPMPFTTYTYIADPINVEYVLK--TNFSNYPkgetyhsYMEVLLGD--GIFNSDGELWRKQ 119
Cdd:cd11040    1 LLRNG---KKYFSGGPIFTIRLGGQKIYVITDPELISAVFRnpKTLSFDP-------IVIVVVGRvfGSPESAKKKEGEP 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 120 RKTASFEFA----------SKNLRDFSTVVFKEYSLKLFTILSQASFKEQQVDMQELLMRMTLDSICKVGFGVEIGTLAP 189
Cdd:cd11040   71 GGKGLIRLLhdlhkkalsgGEGLDRLNEAMLENLSKLLDELSLSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPELDP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 190 ELPEnHFaKAFDTANIIVTLRFIDPL----WKMKKFLNigseALLGKSIKVVNDFTYSV---IRRRKAELLEAQISptnn 262
Cdd:cd11040  151 DLVE-DF-WTFDRGLPKLLLGLPRLLarkaYAARDRLL----KALEKYYQAAREERDDGselIRARAKVLREAGLS---- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 263 nnnnnnkvkhdilsrfieisddpdsketEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESA 342
Cdd:cd11040  221 ----------------------------EEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDS 272
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 343 EATNTSLHQYDtedfnsfnekvtefagllnydsLGKLHYLHAVITETLRLYpAVPQDPKGVLEDDMLPNGTKVKAGGMVT 422
Cdd:cd11040  273 GTNAILDLTDL----------------------LTSCPLLDSTYLETLRLH-SSSTSVRLVTEDTVLGGGYLLRKGSLVM 329
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 423 YVPYSMGRMEYNWGSDAALFKPERWLKDG--VFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH 500
Cdd:cd11040  330 IPPRLLHMDPEIWGPDPEEFDPERFLKKDgdKKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGG 409

                 ...
gi 145337333 501 PVK 503
Cdd:cd11040  410 DWK 412
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
284-504 3.99e-12

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: 68.11  E-value: 3.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 284 DPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAI-------YMIMMnenvaEKLYSELQELEKESAEATNTSLhqydted 356
Cdd:cd11066  219 DKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIghlshppGQEIQ-----EKAYEEILEAYGNDEDAWEDCA------- 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 357 fnsFNEKVtefagllnydslgklHYLHAVITETLRLYPAVPQD-PKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNW 435
Cdd:cd11066  287 ---AEEKC---------------PYVVALVKETLRYFTVLPLGlPRKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHF 347
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 436 GsDAALFKPERWLKDGVFQNASPFKFtAFQAGPRICLGkdsAYLQMKMAMAILCRF---YKFHLVPN------HPVKY 504
Cdd:cd11066  348 G-DPDEFIPERWLDASGDLIPGPPHF-SFGAGSRMCAG---SHLANRELYTAICRLillFRIGPKDEeepmelDPFEY 420
PTZ00404 PTZ00404
cytochrome P450; Provisional
26-502 1.19e-11

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 66.67  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  26 SGPKTWPLVGAaIEQLTN-----FDRMHD--------WLVEYLynsrTVVVpmpfttytyiADPINVEYVLKTNFSNY-- 90
Cdd:PTZ00404  32 KGPIPIPILGN-LHQLGNlphrdLTKMSKkyggifriWFADLY----TVVL----------SDPILIREMFVDNFDNFsd 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  91 -PK------GETYHsymevllgdGIFNSDGELWRKQRKTASFEFASKNLRDFSTVVFKEYSlKLFTILSQASFKEQQVDM 163
Cdd:PTZ00404  97 rPKipsikhGTFYH---------GIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVD-VLIESMKKIESSGETFEP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 164 QELLMRMTLDSICKVGFGVEIgtlapelPENHFAKAFDTANIIvtlrfiDPLWKMKKFLNIGSealLGKSIKVVNDFTY- 242
Cdd:PTZ00404 167 RYYLTKFTMSAMFKYIFNEDI-------SFDEDIHNGKLAELM------GPMEQVFKDLGSGS---LFDVIEITQPLYYq 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 243 -------------SVIRRRKAELLEAqISPtnnnnnnnnKVKHDILSRFI-EISDDPDSKETekSLRDIVLNFVIAGRDT 308
Cdd:PTZ00404 231 ylehtdknfkkikKFIKEKYHEHLKT-IDP---------EVPRDLLDLLIkEYGTNTDDDIL--SILATILDFFLAGVDT 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 309 TATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATntslhqydtedfnsFNEKvtefagllnydslGKLHYLHAVITE 388
Cdd:PTZ00404 299 SATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVL--------------LSDR-------------QSTPYTVAIIKE 351
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 389 TLRLYPAVPQD-PKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEyNWGSDAALFKPERWLkdgvfQNASPFKFTAFQAG 467
Cdd:PTZ00404 352 TLRYKPVSPFGlPRSTSNDIIIGGGHFIPKDAQILINYYSLGRNE-KYFENPEQFDPSRFL-----NPDSNDAFMPFSIG 425
                        490       500       510
                 ....*....|....*....|....*....|....*
gi 145337333 468 PRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPV 502
Cdd:PTZ00404 426 PRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKI 460
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
283-490 1.20e-11

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: 66.70  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 283 DDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEkeSAEATNTSLHQYdtedfnsfne 362
Cdd:cd20614  198 DDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAG--DVPRTPAELRRF---------- 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 363 kvtEFAgllnydslgklhylHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRmeynwgsDAAL- 441
Cdd:cd20614  266 ---PLA--------------EALFRETLRLHPPVPFVFRRVLEEIEL-GGRRIPAGTHLGIPLLLFSR-------DPELy 320
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 145337333 442 -----FKPERWLKDgvfQNA-SPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCR 490
Cdd:cd20614  321 pdpdrFRPERWLGR---DRApNPVELLQFGGGPHFCLGYHVACVELVQFIVALAR 372
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
107-510 4.20e-11

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: 64.86  E-value: 4.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 107 GIFNSDGELWRKQRKTASFEFASKN------------LRDFSTVVFKEyslklftiLSQASFKEQQVDMQELLMRMTLDS 174
Cdd:cd20644   57 GVFLLNGPEWRFDRLRLNPEVLSPAavqrflpmldavARDFSQALKKR--------VLQNARGSLTLDVQPDLFRFTLEA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 175 ICKVGFGVEIGTL--APELPENHFAKAFDTA-NIIVTLRFIDP---------LWKM-------------KKFLNIGSEAL 229
Cdd:cd20644  129 SNLALYGERLGLVghSPSSASLRFISAVEVMlKTTVPLLFMPRslsrwispkLWKEhfeawdcifqyadNCIQKIYQELA 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 230 LGKsikvvnDFTYSVIrrrKAELLE-AQISPtnnnnnnnnkvkhdilsrfieisddpdsketeKSLRDIVLNFVIAGRDT 308
Cdd:cd20644  209 FGR------PQHYTGI---VAELLLqAELSL--------------------------------EAIKANITELTAGGVDT 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 309 TATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATNTSLHQydtedfnsfnekvtefagllnydslgkLHYLHAVITE 388
Cdd:cd20644  248 TAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTE---------------------------LPLLKAALKE 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 389 TLRLYPAVPQDPKGVLEDDMLPNgTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDGvfQNASPFKFTAFQAGP 468
Cdd:cd20644  301 TLRLYPVGITVQRVPSSDLVLQN-YHIPAGTLVQVFLYSLGRSAALF-PRPERYDPQRWLDIR--GSGRNFKHLAFGFGM 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 145337333 469 RICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTIL 510
Cdd:cd20644  377 RQCLGRRLAEAEMLLLLMHVLKNFLVETLSQEDIKTVYSFIL 418
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
298-495 6.28e-11

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: 64.19  E-value: 6.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 298 VLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSElQELEKESAEATntslhqydtedfnsfnekvtefaglLNYDSLG 377
Cdd:cd11082  225 LLDFLFASQDASTSSLVWALQLLADHPDVLAKVREE-QARLRPNDEPP-------------------------LTLDLLE 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 378 KLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVtyVP--YSMGRMEYnwgSDAALFKPERWLKDGVFQN 455
Cdd:cd11082  279 EMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTEDYTVPKGTIV--IPsiYDSCFQGF---PEPDKFDPDRFSPERQEDR 353
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 145337333 456 ASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFH 495
Cdd:cd11082  354 KYKKNFLVFGAGPHQCVGQEYAINHLMLFLALFSTLVDWK 393
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
273-490 7.04e-11

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: 64.06  E-value: 7.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 273 DILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKesaeatntsLHQY 352
Cdd:cd20638  210 DALQLLIEHSRRNGEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGL---------LSTK 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 353 DTEDFNsfnekvtefaglLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTyvpYSMGRM- 431
Cdd:cd20638  281 PNENKE------------LSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFEL-NGYQIPKGWNVI---YSICDTh 344
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 432 -EYNWGSDAALFKPERWLKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCR 490
Cdd:cd20638  345 dVADIFPNKDEFNPDRFMSPLP-EDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELAR 403
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
87-498 8.54e-11

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: 64.06  E-value: 8.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  87 FSNYPKGETYHSYMEvllGDGIFNSDGELWRKQRKtasfeFASKNLRDFSTvvfkeyslklftilsqasfkeQQVDMQEL 166
Cdd:cd20664   34 FGGRPIIPIFEDFNK---GYGILFSNGENWKEMRR-----FTLTTLRDFGM---------------------GKKTSEDK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 167 LMRmtldsickvgfgvEIGTLAPELpENHFAKAFDT--------ANIIVTL----RFIDPLWKMKKFLNIGSE--ALLGK 232
Cdd:cd20664   85 ILE-------------EIPYLIEVF-EKHKGKPFETtlsmnvavSNIIASIvlghRFEYTDPTLLRMVDRINEnmKLTGS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 233 -SIKVVNDFTY---------SVIRRRKAELLEAQISPTNNNNNNNNKVKHDILSRFI----EISDDPDSKETEKSLRDIV 298
Cdd:cd20664  151 pSVQLYNMFPWlgpfpgdinKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFLvkqqEEEESSDSFFHDDNLTCSV 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 299 LNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESaeatntslhQYDTEDFNsfnekvtefagllnydslgK 378
Cdd:cd20664  231 GNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSR---------QPQVEHRK-------------------N 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 379 LHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWGSdAALFKPERWL-KDGVFQNAS 457
Cdd:cd20664  283 MPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEK-PEEFNPEHFLdSQGKFVKRD 361
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 145337333 458 pfKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVP 498
Cdd:cd20664  362 --AFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPP 400
PLN02302 PLN02302
ent-kaurenoic acid oxidase
235-480 1.20e-10

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 63.58  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 235 KVVNDFTYSVIRRRKAElleAQISPTNnnnnnnnkvKHDILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLT 314
Cdd:PLN02302 241 KLVALFQSIVDERRNSR---KQNISPR---------KKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTM 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 315 WAIYMIMMNENVAEKLYSELQELEKESAEATNTslhqydtedfnsfnekvtefaglLNYDSLGKLHYLHAVITETLRLY- 393
Cdd:PLN02302 309 WATIFLQEHPEVLQKAKAEQEEIAKKRPPGQKG-----------------------LTLKDVRKMEYLSQVIDETLRLIn 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 394 --PAVPQDPKGVLEDD--MLPNGTKVKAGgmvtyvpYSMGRMEYNWGSDAALFKPERWLKDGvfqnASPFKFTAFQAGPR 469
Cdd:PLN02302 366 isLTVFREAKTDVEVNgyTIPKGWKVLAW-------FRQVHMDPEVYPNPKEFDPSRWDNYT----PKAGTFLPFGLGSR 434
                        250
                 ....*....|.
gi 145337333 470 ICLGKDSAYLQ 480
Cdd:PLN02302 435 LCPGNDLAKLE 445
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
244-524 1.30e-10

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: 63.47  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 244 VIRRRKAELLEAQISPTNnnnnnnnKVKHDILSRFIEISDdPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMN 323
Cdd:cd11041  186 LIIPEIERRRKLKKGPKE-------DKPNDLLQWLIEAAK-GEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAH 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 324 ENVAEKLYSELQELEKESaeatntslhqydtedfnsfnekvtefaGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPK-G 402
Cdd:cd11041  258 PEYIEPLREEIRSVLAEH---------------------------GGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRrK 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 403 VLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLK---DGVFQNASPF-----KFTAFQAGPRICLGK 474
Cdd:cd11041  311 VLKDVTLSDGLTLPKGTRIAVPAHAIHRDPDIY-PDPETFDGFRFYRlreQPGQEKKHQFvstspDFLGFGHGRHACPGR 389
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145337333 475 DSAYLQMKMAMAILCRFYKFHLVPNH--PVKYRMMTILSMAHGLKVTVSRRS 524
Cdd:cd11041  390 FFASNEIKLILAHLLLNYDFKLPEGGerPKNIWFGEFIMPDPNAKVLVRRRE 441
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
273-518 1.53e-10

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: 63.33  E-value: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 273 DILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQelekesaeaTNTSLHqy 352
Cdd:cd20637  206 DALDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELR---------SNGILH-- 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 353 dtedfnsfNEKVTEfaGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYvpySMgRME 432
Cdd:cd20637  275 --------NGCLCE--GTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFEL-DGFQIPKGWSVLY---SI-RDT 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 433 YNWGS---DAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKYRMMTI 509
Cdd:cd20637  340 HDTAPvfkDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFELATRTFPRMTTVPV 419

                 ....*....
gi 145337333 510 LSMAHGLKV 518
Cdd:cd20637  420 VHPVDGLRV 428
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
105-498 3.33e-10

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: 62.25  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 105 GDGIFNSDGELWRKQRKtasfeFASKNLRDFStvvFKEYSLKLfTILSQASF--------KEQQVDMQELLMRMTLDSIC 176
Cdd:cd20670   49 GHGVALANGERWRILRR-----FSLTILRNFG---MGKRSIEE-RIQEEAGYlleefrktKGAPIDPTFFLSRTVSNVIS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 177 KVGFGVEIgtlapelpeNHFAKAFDTANIIVTLRFI----------DPLWKMKKFLNiGSEALLGKSIKVVNDFTYSvir 246
Cdd:cd20670  120 SVVFGSRF---------DYEDKQFLSLLRMINESFIemstpwaqlyDMYSGIMQYLP-GRHNRIYYLIEELKDFIAS--- 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 247 rrKAELLEAQISPTNnnnnnnnkvKHDILSRF-IEISDDPDSKETEKSLRDIVL---NFVIAGRDTTATTLTWAIYMIMM 322
Cdd:cd20670  187 --RVKINEASLDPQN---------PRDFIDCFlIKMHQDKNNPHTEFNLKNLVLttlNLFFAGTETVSSTLRYGFLLLMK 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 323 NENVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQD-PK 401
Cdd:cd20670  256 YPEVEAKIHEEI---------------------------NQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGvPH 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 402 GVLEDD-----MLPNGTKVkaggmvtYVPYSMGRMEYNWGSDAALFKPERWL-KDGVFQNASpfKFTAFQAGPRICLGKD 475
Cdd:cd20670  309 NVIRDTqfrgyLLPKGTDV-------FPLLGSVLKDPKYFRYPEAFYPQHFLdEQGRFKKNE--AFVPFSSGKRVCLGEA 379
                        410       420
                 ....*....|....*....|....
gi 145337333 476 SAYLQMKMAM-AILCRFYKFHLVP 498
Cdd:cd20670  380 MARMELFLYFtSILQNFSLRSLVP 403
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
105-491 3.44e-10

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: 61.95  E-value: 3.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 105 GDGI-FNSDGELWRKQRKTASFEFAsknlrdfstvVFKEYSLKLFTILSQ---------ASFKEQQVDMQELLMRMTLDS 174
Cdd:cd20673   50 GKDIaFADYSATWQLHRKLVHSAFA----------LFGEGSQKLEKIICQeasslcdtlATHNGESIDLSPPLFRAVTNV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 175 ICKVGFGVEIGTLAPELPE-NHFAKAF-DT------ANIIVTLRfIDP---LWKMKKFLNIGSEALLGKSIKVVNDFTYS 243
Cdd:cd20673  120 ICLLCFNSSYKNGDPELETiLNYNEGIvDTvakdslVDIFPWLQ-IFPnkdLEKLKQCVKIRDKLLQKKLEEHKEKFSSD 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 244 VIRRRKAELLEAQISPTNNNNNnnnkvkhdilsrfieiSDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMN 323
Cdd:cd20673  199 SIRDLLDALLQAKMNAENNNAG----------------PDQDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHN 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 324 ENVAEKLYSELQElekesaeatNTSLHQYDTedfnsFNEKvtefagllnydslGKLHYLHAVITETLRLYPAVPQ-DPKG 402
Cdd:cd20673  263 PEVQKKIQEEIDQ---------NIGFSRTPT-----LSDR-------------NHLPLLEATIREVLRIRPVAPLlIPHV 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 403 VLEDDML-----PNGTKVkaggMVTYvpYSMGRMEYNWgSDAALFKPERWL-KDGVFQNASPFKFTAFQAGPRICLGKDS 476
Cdd:cd20673  316 ALQDSSIgeftiPKGTRV----VINL--WALHHDEKEW-DQPDQFMPERFLdPTGSQLISPSLSYLPFGAGPRVCLGEAL 388
                        410
                 ....*....|....*.
gi 145337333 477 AYLQMKMAMA-ILCRF 491
Cdd:cd20673  389 ARQELFLFMAwLLQRF 404
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
290-500 4.40e-10

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: 61.61  E-value: 4.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 290 TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAeatntslhqydtedfnsfnekvtefag 369
Cdd:cd20616  221 TAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGERD--------------------------- 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 370 lLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGgmvTYVPYSMGRMEynwgSDAALFKPERWLK 449
Cdd:cd20616  274 -IQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVI-DGYPVKKG---TNIILNIGRMH----RLEFFPKPNEFTL 344
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 145337333 450 DGvFQNASPFK-FTAFQAGPRICLGKDSAYLQMKMAMAILCRfyKFHLVPNH 500
Cdd:cd20616  345 EN-FEKNVPSRyFQPFGFGPRSCVGKYIAMVMMKAILVTLLR--RFQVCTLQ 393
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
86-511 1.08e-09

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: 60.58  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  86 NFSNYPKGETYHsymEVLLGDGIFNSDGELWRKQRKtasfeFASKNLRDFStvvFKEYSLKLfTILSQASF--------K 157
Cdd:cd20662   33 NFMNRPETPLRE---RIFNKNGLIFSSGQTWKEQRR-----FALMTLRNFG---LGKKSLEE-RIQEECRHlveaireeK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 158 EQQVDMQELLMRMTLDSICKVGFGVEIgtlapELPENHFAKAFDTANIIVTL------RFIDPLWKMKKFLNiGSEALLG 231
Cdd:cd20662  101 GNPFNPHFKINNAVSNIICSVTFGERF-----EYHDEWFQELLRLLDETVYLegspmsQLYNAFPWIMKYLP-GSHQTVF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 232 KSIKVVNDFTYSVIRRRKAELLEAQisptnnnnnnnnkvKHDILSRFI-EISDDPD--SKETEKSLRDIVLNFVIAGRDT 308
Cdd:cd20662  175 SNWKKLKLFVSDMIDKHREDWNPDE--------------PRDFIDAYLkEMAKYPDptTSFNEENLICSTLDLFFAGTET 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 309 TATTLTWA-IYMImmnenvaekLYSELQELEKESAEATNTSLHQYDTEDFNSfnekvtefagllnydslgkLHYLHAVIT 387
Cdd:cd20662  241 TSTTLRWAlLYMA---------LYPEIQEKVQAEIDRVIGQKRQPSLADRES-------------------MPYTNAVIH 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 388 ETLRLYPAVPQD-PKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWGSDAAlFKPERWLKDGVFQNASpfKFTAFQA 466
Cdd:cd20662  293 EVQRMGNIIPLNvPREVAVDTKL-AGFHLPKGTMILTNLTALHRDPKEWATPDT-FNPGHFLENGQFKKRE--AFLPFSM 368
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 145337333 467 GPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNH--PVKYRMMTILS 511
Cdd:cd20662  369 GKRACLGEQLARSELFIFFTSLLQKFTFKPPPNEklSLKFRMGITLS 415
PLN03018 PLN03018
homomethionine N-hydroxylase
193-496 2.96e-08

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 56.17  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 193 ENHFAKAFDTANIIVTLRFIDPLWKMKKFLNI-GSEALLGKSIKVVNDFTYSVIRRRkAELLEAQISPTNNnnnnnnkvk 271
Cdd:PLN03018 222 KHHLEVIFNTLNCLPGFSPVDYVERWLRGWNIdGQEERAKVNVNLVRSYNNPIIDER-VELWREKGGKAAV--------- 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 272 HDILSRFIEISD-DPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAeatntslh 350
Cdd:PLN03018 292 EDWLDTFITLKDqNGKYLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDR-------- 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 351 qydtedfnsfnekvtefagLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGR 430
Cdd:PLN03018 364 -------------------LVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGR 424
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145337333 431 MEYNWgSDAALFKPERWLK-DGVFQNA----SPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHL 496
Cdd:PLN03018 425 NPKIW-KDPLVYEPERHLQgDGITKEVtlveTEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKL 494
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
270-496 3.23e-08

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 55.51  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 270 VKHDILSRFIEISDDPDSKEtEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEkesaeatntsl 349
Cdd:cd20630  181 VEDDLLTTLLRAEEDGERLS-EDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPELLR----------- 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 350 hqydtedfNSFNEkvtefagLLNYDSLGKLhylhavitETLRLYPavpqdpkgvleDDMLPNGTKVKAGGMVTYVPYSMG 429
Cdd:cd20630  249 --------NALEE-------VLRWDNFGKM--------GTARYAT-----------EDVELCGVTIRKGQMVLLLLPSAL 294
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 430 RMEYNWgSDAALFKPERWLKDGVfqnaspfkftAFQAGPRICLGKDSAYLQMKMAM-AILCRFYKFHL 496
Cdd:cd20630  295 RDEKVF-SDPDRFDVRRDPNANI----------AFGYGPHFCIGAALARLELELAVsTLLRRFPEMEL 351
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
86-499 4.03e-08

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: 55.45  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333  86 NFSNYPKgetyhSYMEVLLGDG----IFNSDGELWRKQRKTASFEFASKN----LRDFST-----VVFKEYSLklftilS 152
Cdd:cd20658   32 VFASRPL-----TYATEIISGGykttVISPYGEQWKKMRKVLTTELMSPKrhqwLHGKRTeeadnLVAYVYNM------C 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 153 QASFKEQQVDMQEL--------LMRMtLDSICKVGFGVEIGTLAPELPEnHFAKAFDTANIIVTLRFIDPLwKMKKFLNI 224
Cdd:cd20658  101 KKSNGGGLVNVRDAarhycgnvIRKL-MFGTRYFGKGMEDGGPGLEEVE-HMDAIFTALKCLYAFSISDYL-PFLRGLDL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 225 -GSEALLGKSIKVVNDFTYSVIRRRKAELLEAQisptnnnnnnnNKVKHDILSRFIEISDDpDSKE--TEKSLRDIVLNF 301
Cdd:cd20658  178 dGHEKIVREAMRIIRKYHDPIIDERIKQWREGK-----------KKEEEDWLDVFITLKDE-NGNPllTPDEIKAQIKEL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 302 VIAGRDTTATTLTWAIYMIMMNENVAEKLYSEL------QELEKESaeatntslhqydtedfnsfnekvtefagllnydS 375
Cdd:cd20658  246 MIAAIDNPSNAVEWALAEMLNQPEILRKATEELdrvvgkERLVQES---------------------------------D 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 376 LGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKDG--VF 453
Cdd:cd20658  293 IPNLNYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVW-DDPLKFKPERHLNEDseVT 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 145337333 454 QNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPN 499
Cdd:cd20658  372 LTEPDLRFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPN 417
PLN02971 PLN02971
tryptophan N-hydroxylase
273-499 8.58e-08

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 54.66  E-value: 8.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 273 DILSRFIEISDDPDSKE-TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMmneNVAEKLYSELQELEKesaeatntslhq 351
Cdd:PLN02971 306 DFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAMAEMI---NKPEILHKAMEEIDR------------ 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 352 ydtedfnsfnekVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLPNGTKVKAGGMVTYVPYSMGRM 431
Cdd:PLN02971 371 ------------VVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRN 438
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 432 EYNWgSDAALFKPERWLKD--GVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPN 499
Cdd:PLN02971 439 PKVW-SDPLSFKPERHLNEcsEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGS 507
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
270-494 2.08e-07

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: 53.26  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 270 VKHDILSRFIEI----SDDPDSKET---EKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesa 342
Cdd:cd20671  193 IDGNPLHSYIEAliqkQEEDDPKETlfhDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEI-------- 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 343 eatntslhqydtedfnsfnEKVTEFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDD-----MLPNGTKVKA 417
Cdd:cd20671  265 -------------------DRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTqfkgyLIPKGTPVIP 325
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145337333 418 ggMVTYVPYSmgrmEYNWGSDAAlFKPERWL-KDGVFQNASpfKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKF 494
Cdd:cd20671  326 --LLSSVLLD----KTQWETPYQ-FNPNHFLdAEGKFVKKE--AFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTF 394
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
297-488 3.46e-07

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: 52.47  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 297 IVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATNTSLHqydtedfnsfnekvtefagllnydsl 376
Cdd:cd11074  237 IVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLH-------------------------- 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 377 gKLHYLHAVITETLRLYPAVPQ-DPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWL--KDGVF 453
Cdd:cd11074  291 -KLPYLQAVVKETLRLRMAIPLlVPHMNLHDAKL-GGYDIPAESKILVNAWWLANNPAHW-KKPEEFRPERFLeeESKVE 367
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 145337333 454 QNASPFKFTAFQAGPRICLGkdsaylqMKMAMAIL 488
Cdd:cd11074  368 ANGNDFRYLPFGVGRRSCPG-------IILALPIL 395
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
315-496 9.58e-07

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: 51.16  E-value: 9.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 315 WAIYMIMMNENVAEK----LYSELQELEKEsaeatntslhqydtedfnsfNEKVTEfagllnyDSLGKLHYLHAVITETL 390
Cdd:cd20635  232 WTLAFILSHPSVYKKvmeeISSVLGKAGKD--------------------KIKISE-------DDLKKMPYIKRCVLEAI 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 391 RLYpAVPQDPKGVLEDDMLPNGTkVKAGGMVTYVPYSMGRmeyN--WGSDAALFKPERWLKDGVFQNASPFKFTAFQAGP 468
Cdd:cd20635  285 RLR-SPGAITRKVVKPIKIKNYT-IPAGDMLMLSPYWAHR---NpkYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGR 359
                        170       180
                 ....*....|....*....|....*...
gi 145337333 469 RICLGKDSAYLQMKMAMAILCRFYKFHL 496
Cdd:cd20635  360 YQCPGRWFALMEIQMFVAMFLYKYDFTL 387
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
297-473 1.23e-06

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 50.89  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 297 IVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQELEKESAEATNTSLHqydtedfnsfnekvtefagllnydsl 376
Cdd:PLN02394 297 IVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTH-------------------------- 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 377 gKLHYLHAVITETLRLYPAVP-QDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKPERWLKD--GVF 453
Cdd:PLN02394 351 -KLPYLQAVVKETLRLHMAIPlLVPHMNLEDAKL-GGYDIPAESKILVNAWWLANNPELW-KNPEEFRPERFLEEeaKVE 427
                        170       180
                 ....*....|....*....|
gi 145337333 454 QNASPFKFTAFQAGPRICLG 473
Cdd:PLN02394 428 ANGNDFRFLPFGVGRRSCPG 447
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
246-483 1.60e-06

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 50.75  E-value: 1.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 246 RRRKAELLEAQISPTNNNNNNNNKVKHDILSRFIEiSDDPDSKEtekSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNEN 325
Cdd:PLN02987 224 RTKVAEALTLVVMKRRKEEEEGAEKKKDMLAALLA-SDDGFSDE---EIVDFLVALLVAGYETTSTIMTLAVKFLTETPL 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 326 VAEKLYSELQELEKESAEatntslhqydtedfnsfnekvtefAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLE 405
Cdd:PLN02987 300 ALAQLKEEHEKIRAMKSD------------------------SYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMT 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 406 D-----DMLPNGTKVkaggmvtYVPYSMGRMEYNWGSDAALFKPERWLKDGVFQNASPFkFTAFQAGPRICLGKDSAYLQ 480
Cdd:PLN02987 356 DievkgYTIPKGWKV-------FASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNV-FTPFGGGPRLCPGYELARVA 427

                 ...
gi 145337333 481 MKM 483
Cdd:PLN02987 428 LSV 430
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
273-518 2.03e-06

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: 50.22  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 273 DILSRFIEISDDPDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSEL--QELEKEsaeatntslH 350
Cdd:cd20636  207 DALDYMIHSARENGKELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELvsHGLIDQ---------C 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 351 QYdtedfnsfnekvteFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGR 430
Cdd:cd20636  278 QC--------------CPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFEL-DGYQIPKGWSVMYSIRDTHE 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 431 MEYNWgSDAALFKPERWLKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLV-PNHPvkyRMMT- 508
Cdd:cd20636  343 TAAVY-QNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWELAtPTFP---KMQTv 418
                        250
                 ....*....|.
gi 145337333 509 -ILSMAHGLKV 518
Cdd:cd20636  419 pIVHPVDGLQL 429
PLN02500 PLN02500
cytochrome P450 90B1
290-499 4.71e-06

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 49.09  E-value: 4.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 290 TEKSLrDIVLNFVIAGRDTTATTLTWAIYMImmnenvaEKLYSELQELEKESAEATNTSLHQYDTEdfnsfnekvtefag 369
Cdd:PLN02500 277 TEQIL-DLILSLLFAGHETSSVAIALAIFFL-------QGCPKAVQELREEHLEIARAKKQSGESE-------------- 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 370 lLNYDSLGKLHYLHAVITETLRLYPAVPQDPKGVLEDdMLPNGTKVKAGGMVTYVpYSMGRMEYNWGSDAALFKPERWLK 449
Cdd:PLN02500 335 -LNWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKD-VRYKGYDIPSGWKVLPV-IAAVHLDSSLYDQPQLFNPWRWQQ 411
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145337333 450 DGVFQNASPFK------FTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPN 499
Cdd:PLN02500 412 NNNRGGSSGSSsattnnFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEA 467
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
239-490 6.25e-06

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: 48.52  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 239 DFTYSVIRRRKAELLEaqisptnnnnnnnnkvkhDILSRFIEISDDPDsKETEKSLRDIVLNFVIAGRDTTATTLTWAIY 318
Cdd:cd11038  179 DYADALIEARRAEPGD------------------DLISTLVAAEQDGD-RLSDEELRNLIVALLFAGVDTTRNQLGLAML 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 319 MIMMNENVAEKLySELQELEKESAEatntslhqydtedfnsfnekvtefagllnydslgklhylhavitETLRLYPAVPQ 398
Cdd:cd11038  240 TFAEHPDQWRAL-REDPELAPAAVE--------------------------------------------EVLRWCPTTTW 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 399 DPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRmeynwgsDAALFKPERWlkDGVFQNASPFkftAFQAGPRICLGKDSAY 478
Cdd:cd11038  275 ATREAVEDVEY-NGVTIPAGTVVHLCSHAANR-------DPRVFDADRF--DITAKRAPHL---GFGGGVHHCLGAFLAR 341
                        250
                 ....*....|..
gi 145337333 479 LQMKMAMAILCR 490
Cdd:cd11038  342 AELAEALTVLAR 353
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
249-504 7.56e-06

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 48.39  E-value: 7.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 249 KAELLEAQISPTNNNNNNNNKVKH-DILSRFIEisddpdSKE--TEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNEN 325
Cdd:PLN02196 223 KARKELAQILAKILSKRRQNGSSHnDLLGSFMG------DKEglTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPS 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 326 VAEKLYSELQELEKESAEatNTSLHQYDTEdfnsfnekvtefagllnydslgKLHYLHAVITETLRLYPAVPQDPKGVLE 405
Cdd:PLN02196 297 VLEAVTEEQMAIRKDKEE--GESLTWEDTK----------------------KMPLTSRVIQETLRVASILSFTFREAVE 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 406 D-----DMLPNGTKVKAggMVTYVPYSMGRMeynwgSDAALFKPERwlkdgvFQNA-SPFKFTAFQAGPRICLGKDSAYL 479
Cdd:PLN02196 353 DveyegYLIPKGWKVLP--LFRNIHHSADIF-----SDPGKFDPSR------FEVApKPNTFMPFGNGTHSCPGNELAKL 419
                        250       260
                 ....*....|....*....|....*.
gi 145337333 480 QMKMAMAILCRFYKFHLV-PNHPVKY 504
Cdd:PLN02196 420 EISVLIHHLTTKYRWSIVgTSNGIQY 445
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
286-501 7.70e-06

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: 48.23  E-value: 7.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 286 DSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELqelekesaeatntslhqydtedfnsfnEKVT 365
Cdd:cd20666  221 ESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEI---------------------------DTVI 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 366 EFAGLLNYDSLGKLHYLHAVITETLRLYPAVPQD-PKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWgSDAALFKP 444
Cdd:cd20666  274 GPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSiPHMASENTVL-QGYTIPKGTVIVPNLWSVHRDPAIW-EKPDDFMP 351
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145337333 445 ERWLKD--GVFQNASpfkFTAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHP 501
Cdd:cd20666  352 SRFLDEngQLIKKEA---FIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAP 407
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
362-501 1.44e-05

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 47.46  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 362 EKVTEFAGLLNYDSLgkLHYLHAVITETLRLYPAVPQdpkgVLED---DMLPNGTKVKAG-GMVTYVPYsMGRmeynwgS 437
Cdd:cd20624  226 ARAREEAAVPPGPLA--RPYLRACVLDAVRLWPTTPA----VLREsteDTVWGGRTVPAGtGFLIFAPF-FHR------D 292
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145337333 438 DAAL-----FKPERWLkDGVFQNASPfkFTAFQAGPRICLGKDSAYLQMKMAMAILCRfyKFHLVPNHP 501
Cdd:cd20624  293 DEALpfadrFVPEIWL-DGRAQPDEG--LVPFSAGPARCPGENLVLLVASTALAALLR--RAEIDPLES 356
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
285-499 3.36e-05

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: 46.23  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 285 PDSKETEKSLRDIVLNFVIAGRDTTATTLTWAIYMIMMNENVAEKLYSELQEL-----EKESAEATNtslhqydtedfns 359
Cdd:cd20663  222 PESSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVigqvrRPEMADQAR------------- 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 360 fnekvtefagllnydslgkLHYLHAVITETLRLYPAVP--------QDPKgvLEDDMLPNGTkvkaggmvTYVP--YSMG 429
Cdd:cd20663  289 -------------------MPYTNAVIHEVQRFGDIVPlgvphmtsRDIE--VQGFLIPKGT--------TLITnlSSVL 339
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145337333 430 RMEYNWgSDAALFKPERWL-KDGVFqnASPFKFTAFQAGPRICLGKDSAylQMKMAMAILCRFYKFHL-VPN 499
Cdd:cd20663  340 KDETVW-EKPLRFHPEHFLdAQGHF--VKPEAFMPFSAGRRACLGEPLA--RMELFLFFTCLLQRFSFsVPA 406
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
103-514 5.64e-04

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: 42.31  E-value: 5.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 103 LLGDG---IFNSD-GELWRKQRKtasfeFASKNLRDFSTV---------VFKEYSLK----LFTILSQASFKEQQVDMQE 165
Cdd:cd20676   45 FISDGqslTFSTDsGPVWRARRK-----LAQNALKTFSIAssptsssscLLEEHVSKeaeyLVSKLQELMAEKGSFDPYR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 166 LLMRMTLDSICKVGFG----------VEIGTLAPELPENhfAKAFDTANIIVTLRFIdPLWKMKKFLNIGSE--ALLGKS 233
Cdd:cd20676  120 YIVVSVANVICAMCFGkryshddqelLSLVNLSDEFGEV--AGSGNPADFIPILRYL-PNPAMKRFKDINKRfnSFLQKI 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 234 IKV---------VNDFTYSVIRRRKaelleaqisptnnnnnnnnKVKHDILSRfIEISDDpdsketekSLRDIVLNFVIA 304
Cdd:cd20676  197 VKEhyqtfdkdnIRDITDSLIEHCQ-------------------DKKLDENAN-IQLSDE--------KIVNIVNDLFGA 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 305 GRDTTATTLTWAIYMIMMNENVAEKLYSELQELekesaeatntslhqYDTEDFNSFNEKvtefagllnydslGKLHYLHA 384
Cdd:cd20676  249 GFDTVTTALSWSLMYLVTYPEIQKKIQEELDEV--------------IGRERRPRLSDR-------------PQLPYLEA 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 385 VITETLRLYPAVP-QDPKGVLEDDMLpNGTKVKAGGMVTYVPYSMGRMEYNWGsDAALFKPERWL-KDGVFQN-ASPFKF 461
Cdd:cd20676  302 FILETFRHSSFVPfTIPHCTTRDTSL-NGYYIPKDTCVFINQWQVNHDEKLWK-DPSSFRPERFLtADGTEINkTESEKV 379
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 145337333 462 TAFQAGPRICLGKDSAYLQMKMAMAILCRFYKFHLVPNHPVKyrmMTI---LSMAH 514
Cdd:cd20676  380 MLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPPGVKVD---MTPeygLTMKH 432
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
369-493 1.28e-03

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: 41.09  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145337333 369 GLLNYDSLGKLHYLHAVITETLRLYPAVP---QDPKgvlEDDMLPNGT---KVKAGGM-VTYVPYSMgrmeynwgSDAAL 441
Cdd:cd11071  275 GGLTLAALEKMPLLKSVVYETLRLHPPVPlqyGRAR---KDFVIESHDasyKIKKGELlVGYQPLAT--------RDPKV 343
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145337333 442 ------FKPERW------LKDGVFQNASPFKFTAfQAGPRICLGKDSAYLQMKMAMAILCRFYK 493
Cdd:cd11071  344 fdnpdeFVPDRFmgeegkLLKHLIWSNGPETEEP-TPDNKQCPGKDLVVLLARLFVAELFLRYD 406
 
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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