NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|807744981|ref|XP_012177285|]
View 

uncharacterized protein FIBRA_09612 [Fibroporia radiculosa]

Protein Classification

cytochrome P450( domain architecture ID 15296315)

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

CATH:  1.10.630.10
Gene Ontology:  GO:0004497|GO:0005506|GO:0016705|GO:0020037
PubMed:  27267697|8405421|7678494|28124606
SCOP:  4001206

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 2-172 4.32e-69

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: 222.94  E-value: 4.32e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG-WTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSDGTFIPAGTYL 80
Cdd:cd11041  250 VLLDLAAHPEYIEPLREEIRSVLAEHGgWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSDGLTLPKGTRI 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD----------------FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd11041  330 AVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGqekkhqfvstspdflgFGHGRHACPGRFFASNEIKLILAHLLLNYDF 409

                        170       180
                 ....*....|....*....|....*...
gi 807744981 145 KMEQEGVIPTPIMIGHICAPSRKAEILV 172
Cdd:cd11041  410 KLPEGGERPKNIWFGEFIMPDPNAKVLV 437
 
Name Accession Description Interval E-value
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 2-172 4.32e-69

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: 222.94  E-value: 4.32e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG-WTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSDGTFIPAGTYL 80
Cdd:cd11041  250 VLLDLAAHPEYIEPLREEIRSVLAEHGgWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSDGLTLPKGTRI 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD----------------FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd11041  330 AVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGqekkhqfvstspdflgFGHGRHACPGRFFASNEIKLILAHLLLNYDF 409

                        170       180
                 ....*....|....*....|....*...
gi 807744981 145 KMEQEGVIPTPIMIGHICAPSRKAEILV 172
Cdd:cd11041  410 KLPEGGERPKNIWFGEFIMPDPNAKVLV 437
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 1-172 1.15e-27

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: 112.76  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981    1 MALFYLAAYPQYMGHLRDEVDRVVREH-GWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTY 79
Cdd:pfam00067 283 WALYELAKHPEVQEKLREEIDEVIGDKrSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVI-PGYLIPKGTL 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDmRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGV 151
Cdd:pfam00067 362 VIVNLYALHRDPEVFPNPEEFDPERFLD-ENGKFrksfaflpFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTD 440

                         170       180
                  ....*....|....*....|.
gi 807744981  152 IPTPIMIGHICAPSRKAEILV 172
Cdd:pfam00067 441 PPDIDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 2-143 1.97e-11

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: 64.53  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVvrehgwtkaaldemhkvDSFLREVMRASGmTTGTMSRKAVKDYTFsDGTFIPAGTYLM 81
Cdd:COG2124  249 ALYALLRHPEQLARLRAEPELL-----------------PAAVEETLRLYP-PVPLLPRTATEDVEL-GGVTIPAGDRVL 309

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRfsDMRDQDDFGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:COG2124  310 LSLAAANRDPRVFPDPDRFDPDR--PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP 369
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 46-157 3.29e-10

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 60.91  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  46 EVMRASGMTTGTMsRKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDmRDQDD-----FGHGHHA 120
Cdd:PLN03141 323 ETLRMGNIINGVM-RKAMKDVEIK-GYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQE-KDMNNssftpFGGGQRL 399

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 807744981 121 CPGRFFAVSEMKTILAHIVATYDVKMEQEGVI--PTPIM 157
Cdd:PLN03141 400 CPGLDLARLEASIFLHHLVTRFRWVAEEDTIVnfPTVRM 438
 
Name Accession Description Interval E-value
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 2-172 4.32e-69

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: 222.94  E-value: 4.32e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG-WTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSDGTFIPAGTYL 80
Cdd:cd11041  250 VLLDLAAHPEYIEPLREEIRSVLAEHGgWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSDGLTLPKGTRI 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD----------------FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd11041  330 AVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGqekkhqfvstspdflgFGHGRHACPGRFFASNEIKLILAHLLLNYDF 409

                        170       180
                 ....*....|....*....|....*...
gi 807744981 145 KMEQEGVIPTPIMIGHICAPSRKAEILV 172
Cdd:cd11041  410 KLPEGGERPKNIWFGEFIMPDPNAKVLV 437
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 1-172 1.15e-27

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: 112.76  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981    1 MALFYLAAYPQYMGHLRDEVDRVVREH-GWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTY 79
Cdd:pfam00067 283 WALYELAKHPEVQEKLREEIDEVIGDKrSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVI-PGYLIPKGTL 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDmRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGV 151
Cdd:pfam00067 362 VIVNLYALHRDPEVFPNPEEFDPERFLD-ENGKFrksfaflpFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTD 440

                         170       180
                  ....*....|....*....|.
gi 807744981  152 IPTPIMIGHICAPSRKAEILV 172
Cdd:pfam00067 441 PPDIDETPGLLLPPKPYKLKF 461
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 1-153 3.18e-27

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: 110.68  E-value: 3.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVREHgwTKAALDEMHKVDSFLREVMRASgMTTGTMSRKAVKDYTFsDGTFIPAGTYL 80
Cdd:cd00302  224 WALYLLARHPEVQERLRAEIDAVLGDG--TPEDLSKLPYLEAVVEETLRLY-PPVPLLPRVATEDVEL-GGYTIPAGTLV 299

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-----FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGVIP 153
Cdd:cd00302  300 LLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRyahlpFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELE 377
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 2-157 1.46e-24

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: 103.60  E-value: 1.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHK------VDSFLREVMRASGMTTGTmsRKAVKDYTFSDGTFIP 75
Cdd:cd11040  246 LLAHILSDPELLERIREEIEPAVTPDSGTNAILDLTDLltscplLDSTYLETLRLHSSSTSV--RLVTEDTVLGGGYLLR 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  76 AGTYLMAPTGAIYTDDAVY-PNAVEFNPWRF------SDMRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd11040  324 KGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkdgdKKGRGLPGafrpFGGGASLCPGRHFAKNEILAFVALLLSRFDV 403

                        170
                 ....*....|...
gi 807744981 145 KMEQEGVIPTPIM 157
Cdd:cd11040  404 EPVGGGDWKVPGM 416
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 2-154 7.75e-24

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: 101.52  E-value: 7.75e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG--WTKAALDEMHKVDSFLREVMRasgMTTG--TMSRKAVKDYTFSDGTF-IPA 76
Cdd:cd11042  235 TGLELLRNPEHLEALREEQKEVLGDGDdpLTYDVLKEMPLLHACIKETLR---LHPPihSLMRKARKPFEVEGGGYvIPK 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  77 GTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD---------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKME 147
Cdd:cd11042  312 GHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSkggkfaylpFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELV 391


                 ....*..
gi 807744981 148 QEGVIPT 154
Cdd:cd11042  392 DSPFPEP 398
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 2-156 3.58e-21

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: 93.80  E-value: 3.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGW-TKAALDEMHKVDSFLREVMRasgM--TTGTMSRKAVKDYTFsDGTFIPAGT 78
Cdd:cd11055  249 ASYLLATNPDVQEKLIEEIDEVLPDDGSpTYDTVSKLKYLDMVINETLR---LypPAFFISRECKEDCTI-NGVFIPKGV 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGV 151
Cdd:cd11055  325 DVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRhpyaylpFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETE 404


                 ....*
gi 807744981 152 IPTPI 156
Cdd:cd11055  405 IPLKL 409
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 2-156 1.56e-19

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: 89.25  E-value: 1.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHK---VDSFLREVMR---ASGMTtgtmSRKAVKDyTFSDGTFIP 75
Cdd:cd11069  258 ALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDLDRlpyLNAVCRETLRlypPVPLT----SREATKD-TVIKGVPIP 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  76 AGTYLMAPTGAIYTDDAVY-PNAVEFNPWRFSDMRDQDD------------FGHGHHACPGRFFAVSEMKTILAHIVATY 142
Cdd:cd11069  333 KGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASpggagsnyalltFLHGPRSCIGKKFALAEMKVLLAALVSRF 412

                        170
                 ....*....|....
gi 807744981 143 DVKMEQEGVIPTPI 156
Cdd:cd11069  413 EFELDPDAEVERPI 426
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 4-156 4.21e-19

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: 87.76  E-value: 4.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   4 FYLAAYPQYMGHLRDEVDRVVREHGwTKAALDEMHKVDSFLREVMRasgMTT--GTMSRKAVKDYTFsDGTFIPAGTYLM 81
Cdd:cd11045  236 YFLARHPEWQERLREESLALGKGTL-DYEDLGQLEVTDWVFKEALR---LVPpvPTLPRRAVKDTEV-LGYRIPAGTLVA 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYDV-------KM 146
Cdd:cd11045  311 VSPGVTHYMPEYWPNPERFDPERFSPERAEDKvhryawapFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWwsvpgyyPP 390

                        170
                 ....*....|
gi 807744981 147 EQEGVIPTPI 156
Cdd:cd11045  391 WWQSPLPAPK 400
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 1-145 3.23e-17

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: 82.30  E-value: 3.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVREHGWTKAA-LDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSDgTFIPAGTY 79
Cdd:cd20621  251 MCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEdLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGD-LKIKKGWI 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:cd20621  330 VNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDnpfvfipFSAGPRNCIGQHLALMEAKIILIYILKNFEIE 402
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 1-158 3.51e-17

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: 82.19  E-value: 3.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVRE-HGWTKAALDEMHKVDSFLREVMRASGMTTGTMsRKAVKDYTFSdGTFIPAGTY 79
Cdd:cd11054  253 FLLYHLAKNPEVQEKLYEEIRSVLPDgEPITAEDLKKMPYLKACIKESLRLYPVAPGNG-RILPKDIVLS-GYHIPKGTL 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFsdMRDQDD-----------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ 148
Cdd:cd11054  331 VVLSNYVMGRDEEYFPDPEEFIPERW--LRDDSEnknihpfaslpFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHH 408

                        170
                 ....*....|
gi 807744981 149 EGVIPTPIMI 158
Cdd:cd11054  409 EELKVKTRLI 418
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 2-150 8.92e-17

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: 80.73  E-value: 8.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRV--VREHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSDGTFIPAGTY 79
Cdd:cd11061  239 IFYYLARNPEAYEKLRAELDSTfpSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGLPRETPPGGLTIDGEYIPGGTT 318

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRF----SDMRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEG 150
Cdd:cd11061  319 VSVPIYSIHRDERYFPDPFEFIPERWlsrpEELVRARSafipFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGE 397
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 5-157 4.87e-16

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: 78.77  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   5 YLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYLMAP 83
Cdd:cd11065  249 AMALHPEVQKKAQEELDRVVgPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPHALTEDDEY-EGYFIPKGTTVIPN 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  84 TGAIYTDDAVYPNAVEFNPWRFSDMRDQDD---------FGHGHHACPGRFFAVSEMKTILAHIVATYDVK--MEQEGVI 152
Cdd:cd11065  328 AWAIHHDPEVYPDPEEFDPERYLDDPKGTPdppdpphfaFGFGRRICPGRHLAENSLFIAIARLLWAFDIKkpKDEGGKE 407


                 ....*
gi 807744981 153 PTPIM 157
Cdd:cd11065  408 IPDEP 412
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 1-145 2.35e-15

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: 76.79  E-value: 2.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVV--REHGWTKAALDEMHKVDSFLREVMRasgMTTG--TMSRKAVKDYTFsDGTFIPA 76
Cdd:cd20628  251 FTLYLLGLHPEVQEKVYEELDEIFgdDDRRPTLEDLNKMKYLERVIKETLR---LYPSvpFIGRRLTEDIKL-DGYTIPK 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744981  77 GTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:cd20628  327 GTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRhpyayipFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVL 402
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 1-153 3.53e-15

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: 76.04  E-value: 3.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVREHG--WTKAALDEMHKVDSFLREVMRasgM--TTGTMSRKAVKDYTFSDGTF-IP 75
Cdd:cd11056  251 FALYELAKNPEIQEKLREEIDEVLEKHGgeLTYEALQEMKYLDQVVNETLR---KypPLPFLDRVCTKDYTLPGTDVvIE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  76 AGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ 148
Cdd:cd11056  328 KGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRhpytylpFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSS 407


                 ....*
gi 807744981 149 EGVIP 153
Cdd:cd11056  408 KTKIP 412
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 2-148 6.61e-15

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: 75.30  E-value: 6.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRAsgMTTGTM-SRKAVKDYTFSDGTFIPAGTYL 80
Cdd:cd11068  253 ALYYLLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRL--WPTAPAfARKPKEDTVLGGKYPLKKGDPV 330

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744981  81 MAPTGAIYTDDAVY-PNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ 148
Cdd:cd11068  331 LVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKLppnawkpFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDP 406
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 1-153 6.97e-15

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: 75.33  E-value: 6.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTY 79
Cdd:cd20651  247 FAFLYLLLNPEVQRKVQEEIDEVVgRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTTL-GGYRIPKDTT 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSD---MRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMeQEGVI 152
Cdd:cd20651  326 ILASLYSVHMDPEYWGDPEEFRPERFLDedgKLLKDEwflpFGAGKRRCLGESLARNELFLFFTGLLQNFTFSP-PNGSL 404


                 .
gi 807744981 153 P 153
Cdd:cd20651  405 P 405
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 1-157 1.26e-14

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: 74.52  E-value: 1.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPqymghlrDEVDRVVREH-----------GWTKAALDEMHKVDSFLREVMRASGMTTGTMsRKAVKDYTFs 69
Cdd:cd11043  232 LAVKFLAENP-------KVLQELLEEHeeiakrkeegeGLTWEDYKSMKYTWQVINETLRLAPIVPGVF-RKALQDVEY- 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  70 DGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMrDQDD------FGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:cd11043  303 KGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGK-GKGVpytflpFGGGPRLCPGAELAKLEILVFLHHLVTRFR 381

                        170
                 ....*....|....*..
gi 807744981 144 VKMEQEGVI---PTPIM 157
Cdd:cd11043  382 WEVVPDEKIsrfPLPRP 398
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 3-157 2.03e-14

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: 73.78  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFY-LAAYPQYMGHLRDEVDRVVREHGWTKA------ALDEMHKVDSFLREVMR---ASGMTtgtmSRKAVKDYTFSDGT 72
Cdd:cd11064  253 FFWlLSKNPRVEEKIREELKSKLPKLTTDESrvptyeELKKLVYLHAALSESLRlypPVPFD----SKEAVNDDVLPDGT 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  73 FIPAGT------YLMAPTGAIYTDDAVypnavEFNPWRFSD----MRDQDD-----FGHGHHACPGRFFAVSEMKTILAH 137
Cdd:cd11064  329 FVKKGTrivysiYAMGRMESIWGEDAL-----EFKPERWLDedggLRPESPykfpaFNAGPRICLGKDLAYLQMKIVAAA 403

                        170       180
                 ....*....|....*....|
gi 807744981 138 IVATYDVKMEqEGVIPTPIM 157
Cdd:cd11064  404 ILRRFDFKVV-PGHKVEPKM 422
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 2-172 5.47e-14

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: 72.62  E-value: 5.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVreHGWTKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFsDGTFIPAGTYLM 81
Cdd:cd11053  246 AFYWLHRHPEVLARLLAELDALG--GDPDPEDIAKLPYLDAVIKETLRLYPVAP-LVPRRVKEPVEL-GGYTLPAGTTVA 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRFSDMR----DQDDFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGVIPtPIM 157
Cdd:cd11053  322 PSIYLTHHRPDLYPDPERFRPERFLGRKpspyEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPER-PVR 400

                        170
                 ....*....|....*
gi 807744981 158 IGHICAPSRKAEILV 172
Cdd:cd11053  401 RGVTLAPSRGVRMVV 415
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 3-146 2.34e-13

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: 70.52  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMR----ASgmttgTMSRKAVKDYTFSdGTFIPAGT 78
Cdd:cd20640  254 LMLLALHPEWQDRVRAEVLEVCKGGPPDADSLSRMKTVTMVIQETLRlyppAA-----FVSREALRDMKLG-GLVVPKGV 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807744981  79 YLMAPTGAIYTDDAVY-PNAVEFNPWRFSDMRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKM 146
Cdd:cd20640  328 NIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACkpphsympFGAGARTCLGQNFAMAELKVLVSLILSKFSFTL 404
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 2-146 3.97e-13

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 70.09  E-value: 3.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG-----------WTKAALDEMHKVDSFLREVMRasgMTTG-TMSRKAVKDYTF- 68
Cdd:cd20633  247 LLLYLLKHPEAMKAVREEVEQVLKETGqevkpggplinLTRDMLLKTPVLDSAVEETLR---LTAApVLIRAVVQDMTLk 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  69 -SDG---TFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRF--SDMRDQDDF--------------GHGHHACPGRFFAV 128
Cdd:cd20633  324 mANGreyALRKGDRLALFPYLAVQMDPEIHPEPHTFKYDRFlnPDGGKKKDFykngkklkyynmpwGAGVSICPGRFFAV 403

                        170
                 ....*....|....*...
gi 807744981 129 SEMKTILAHIVATYDVKM 146
Cdd:cd20633  404 NEMKQFVFLMLTYFDLEL 421
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 1-143 4.42e-13

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


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 69.62  E-value: 4.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTGTmSRKAVKDYTFsDGTFIPAGTYL 80
Cdd:cd11044  245 SLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGG-FRKVLEDFEL-GGYQIPKGWLV 322

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:cd11044  323 YYSIRDTHRDPELYPDPERFDPERFSPARSEDKkkpfslipFGGGPRECLGKEFAQLEMKILASELLRNYD 393
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 10-143 6.31e-13

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 69.21  E-value: 6.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  10 PQYMGHLRDEVDRVVREHG-WTKAALDEMHKVDSFLREVMRasgmttgtMS-------RKAVKDYT--FSDGTF-IPAGT 78
Cdd:cd11071  257 EELHARLAEEIRSALGSEGgLTLAALEKMPLLKSVVYETLR--------LHppvplqyGRARKDFVieSHDASYkIKKGE 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  79 YLMaptGAIYT---DDAVYPNAVEFNPWRFSDM-------------RDQDDFGHGHHACPGRFFAVSEMKTILAHIVATY 142
Cdd:cd11071  329 LLV---GYQPLatrDPKVFDNPDEFVPDRFMGEegkllkhliwsngPETEEPTPDNKQCPGKDLVVLLARLFVAELFLRY 405


                 .
gi 807744981 143 D 143
Cdd:cd11071  406 D 406
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 2-156 7.98e-13

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 68.94  E-value: 7.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG-----------WTKAALDEMHKVDSFLREVMRASgmTTGTMSRKAVKDYTF-- 68
Cdd:cd20631  250 SLFYLLRCPEAMKAATKEVKRTLEKTGqkvsdggnpivLTREQLDDMPVLGSIIKEALRLS--SASLNIRVAKEDFTLhl 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  69 -SDGTF-IPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD----------------FGHGHHACPGRFFAVSE 130
Cdd:cd20631  328 dSGESYaIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKttfykngrklkyyympFGSGTSKCPGRFFAINE 407

                        170       180
                 ....*....|....*....|....*.
gi 807744981 131 MKTILAHIVATYDVKMEQEGVIPTPI 156
Cdd:cd20631  408 IKQFLSLMLCYFDMELLDGNAKCPPL 433
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 2-148 9.87e-13

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: 68.78  E-value: 9.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG--WTKAALDEMHKVDSFLREVMRAsgMTTGTM-SRKAVKDYTFSDGTFIPAGT 78
Cdd:cd11057  250 TLLLLAMHPEVQEKVYEEIMEVFPDDGqfITYEDLQQLVYLEMVLKETMRL--FPVGPLvGRETTADIQLSNGVVIPKGT 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  79 YLMAPTGAIYTDDAVY-PNAVEFNPWRFSDMRDQD-------DFGHGHHACPGRFFAVSEMKTILAHIVATY----DVKM 146
Cdd:cd11057  328 TIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQrhpyafiPFSAGPRNCIGWRYAMISMKIMLAKILRNYrlktSLRL 407


                 ..
gi 807744981 147 EQ 148
Cdd:cd11057  408 ED 409
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 3-144 1.12e-12

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: 68.37  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFY-LAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMR----ASgmttgTMSRKAVKDYTFsDGTFIPAG 77
Cdd:cd20620  235 TWYlLAQHPEVAARLRAEVDRVLGGRPPTAEDLPQLPYTEMVLQESLRlyppAW-----IIGREAVEDDEI-GGYRIPAG 308

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744981  78 TYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd20620  309 STVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARpryayfpFGGGPRICIGNHFAMMEAVLLLATIAQRFRL 382
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 2-164 5.55e-12

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: 66.43  E-value: 5.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRasgMTTG--TMSRKAVKDYTF-----SDGT- 72
Cdd:cd11063  239 LFYELARHPEVWAKLREEVLSLFgPEPTPTYEDLKNMKYLRAVINETLR---LYPPvpLNSRVAVRDTTLprgggPDGKs 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  73 --FIPAGTYLMAPTGAIYTDDAVY-PNAVEFNPWRFSDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYDvK 145
Cdd:cd11063  316 piFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLKRPGweylPFNGGPRICLGQQFALTEASYVLVRLLQTFD-R 394

                        170
                 ....*....|....*....
gi 807744981 146 MEQEGVIPTPIMIGHICAP 164
Cdd:cd11063  395 IESRDVRPPEERLTLTLSN 413
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 2-158 6.37e-12

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: 66.04  E-value: 6.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVreHGWTKAALDEMHKV---DSFLREVMRasgmttgtM-------SRKAVKDYTFsDG 71
Cdd:cd20659  250 TLYSLAKHPEHQQKCREEVDEVL--GDRDDIEWDDLSKLpylTMCIKESLR--------LyppvpfiARTLTKPITI-DG 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  72 TFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSD--MRDQDD-----FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd20659  319 VTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPenIKKRDPfafipFSAGPRNCIGQNFAMNEMKVVLARILRRFEL 398

                        170
                 ....*....|....
gi 807744981 145 KMEQEGVIPTPIMI 158
Cdd:cd20659  399 SVDPNHPVEPKPGL 412
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 2-145 8.19e-12

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: 65.70  E-value: 8.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV---REHGWTKaaLDEMHKVDSFLREVMRASGMTTGTMSRKAVKDyTFSDGTFIPAGT 78
Cdd:cd20617  246 FLLYLANNPEIQEKIYEEIDNVVgndRRVTLSD--RSKLPYLNAVIKEVLRLRPILPLGLPRVTTED-TEIGGYFIPKGT 322

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRF--SDMRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:cd20617  323 QIIINIYSLHRDEKYFEDPEEFNPERFleNDGNKLSEqfipFGIGKRNCVGENLARDELFLFFANLLLNFKFK 395
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 2-139 9.85e-12

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


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 65.81  E-value: 9.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG---WTKAALDEMHKVDSFLREVMR----ASGMTtgtmsRKAVKD---YTFSDG 71
Cdd:cd11070  246 ALYLLAKHPEVQDWLREEIDSVLGDEPddwDYEEDFPKLPYLLAVIYETLRlyppVQLLN-----RKTTEPvvvITGLGQ 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  72 TF-IPAGTYLMAPTGAIYTDDAVY-PNAVEFNPWRFsdMRDQDD----------------FGHGHHACPGRFFAVSEMKT 133
Cdd:cd11070  321 EIvIPKGTYVGYNAYATHRDPTIWgPDADEFDPERW--GSTSGEigaatrftpargafipFSAGPRACLGRKFALVEFVA 398


                 ....*.
gi 807744981 134 ILAHIV 139
Cdd:cd11070  399 ALAELF 404
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 2-143 1.01e-11

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: 65.55  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGW-TKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFSdGTFIPAGTYL 80
Cdd:cd20639  255 TTVLLAMHPEWQERARREVLAVCGKGDVpTKDHLPKLKTLGMILNETLRLYPPAV-ATIRRAKKDVKLG-GLDIPAGTEL 332

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744981  81 MAPTGAIYTDDAVY-PNAVEFNPWRFSDMRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:cd20639  333 LIPIMAIHHDAELWgNDAAEFNPARFADGVARAAkhplafipFGLGPRTCVGQNLAILEAKLTLAVILQRFE 404
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 3-166 1.75e-11

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: 64.74  E-value: 1.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGmTTGTMSRKAVKDYTFsDGTFIPAGTYLM 81
Cdd:cd20650  252 LYELATHPDVQQKLQEEIDAVLpNKAPPTYDTVMQMEYLDMVVNETLRLFP-IAGRLERVCKKDVEI-NGVFIPKGTVVM 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRFS-DMRDQDD------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGVIPT 154
Cdd:cd20650  330 IPTYALHRDPQYWPEPEEFRPERFSkKNKDNIDpyiylpFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPL 409

                        170
                 ....*....|..
gi 807744981 155 PIMIGHICAPSR 166
Cdd:cd20650  410 KLSLQGLLQPEK 421
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 2-150 1.92e-11

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: 64.65  E-value: 1.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG--WTKAALDEMHKVDSFLREVMRASGmTTGTMSRKAVKDyTFSDGTFIPAGTY 79
Cdd:cd11083  245 MLYYLASRPDVQARVREEVDAVLGGARvpPLLEALDRLPYLEAVARETLRLKP-VAPLLFLEPNED-TVVGDIALPAGTP 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD---------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEG 150
Cdd:cd11083  323 VFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEphdpssllpFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPA 402
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 2-143 1.97e-11

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: 64.53  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVvrehgwtkaaldemhkvDSFLREVMRASGmTTGTMSRKAVKDYTFsDGTFIPAGTYLM 81
Cdd:COG2124  249 ALYALLRHPEQLARLRAEPELL-----------------PAAVEETLRLYP-PVPLLPRTATEDVEL-GGVTIPAGDRVL 309

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRfsDMRDQDDFGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:COG2124  310 LSLAAANRDPRVFPDPDRFDPDR--PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP 369
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 38-138 5.39e-11

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 63.13  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  38 HKVDSFLREVMRASGMTTGTMsRKAVKDYTFSDGTF----IPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRfsDMRDQDD 113
Cdd:cd20612  238 ATLRGYVLEALRLNPIAPGLY-RRATTDTTVADGGGrtvsIKAGDRVFVSLASAMRDPRAFPDPERFRLDR--PLESYIH 314

                         90       100
                 ....*....|....*....|....*
gi 807744981 114 FGHGHHACPGRFFAVSEMKTILAHI 138
Cdd:cd20612  315 FGHGPHQCLGEEIARAALTEMLRVV 339
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 1-145 1.17e-10

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: 62.26  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVV--REHGWTKAALDEMHKVDSFLREVMRASgmTTGTM-SRKAVKDYTFSDGTFIPAG 77
Cdd:cd11082  242 WALQLLADHPDVLAKVREEQARLRpnDEPPLTLDLLEEMKYTRQVVKEVLRYR--PPAPMvPHIAKKDFPLTEDYTVPKG 319

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  78 TYLMaPTgaIYtdDAV---YPNAVEFNPWRFSDMRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:cd11082  320 TIVI-PS--IY--DSCfqgFPEPDKFDPDRFSPERQEDRkykknflvFGAGPHQCVGQEYAINHLMLFLALFSTLVDWK 393
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 2-164 2.11e-10

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: 61.46  E-value: 2.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV-REHGWT---KAALDEMHkvdSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAG 77
Cdd:cd11027  252 AIAYLVNYPEVQAKLHAELDDVIgRDRLPTlsdRKRLPYLE---ATIAEVLRLSSVVPLALPHKTTCDTTL-RGYTIPKG 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  78 TYLMAPTGAIYTDDAVYPNAVEFNPWRFSD----MRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQE 149
Cdd:cd11027  328 TTVLVNLWALHHDPKEWDDPDEFRPERFLDengkLVPKPEsflpFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEG 407

                        170
                 ....*....|....*...
gi 807744981 150 GVIP--TPIM-IGHICAP 164
Cdd:cd11027  408 EPPPelEGIPgLVLYPLP 425
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 46-157 3.29e-10

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 60.91  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  46 EVMRASGMTTGTMsRKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDmRDQDD-----FGHGHHA 120
Cdd:PLN03141 323 ETLRMGNIINGVM-RKAMKDVEIK-GYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQE-KDMNNssftpFGGGQRL 399

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 807744981 121 CPGRFFAVSEMKTILAHIVATYDVKMEQEGVI--PTPIM 157
Cdd:PLN03141 400 CPGLDLARLEASIFLHHLVTRFRWVAEEDTIVnfPTVRM 438
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 3-148 8.07e-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: 59.68  E-value: 8.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTGTMsRKAVKDYTFsDGTFIPAGTYLMA 82
Cdd:cd20616  248 LLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVM-RKALEDDVI-DGYPVKKGTNIIL 325

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  83 PTGAIYTDDaVYPNAVEFNPWRFSD---MRDQDDFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ 148
Cdd:cd20616  326 NIGRMHRLE-FFPKPNEFTLENFEKnvpSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQ 393
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 2-153 1.01e-09

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: 59.47  E-value: 1.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAAL-DEMHKVDSFLREVMRASGmTTGTMSRKAVKDYTFSdGTFIPAGTYL 80
Cdd:cd20649  284 ATYLLATHPECQKKLLREVDEFFSKHEMVDYANvQELPYLDMVIAETLRMYP-PAFRFAREAAEDCVVL-GQRIPAGAVL 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQD-------DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGVIP 153
Cdd:cd20649  362 EIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRrhpfvylPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIP 441
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 1-149 1.09e-09

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: 59.24  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFY-LAAYPQYMGHLRDEVdrvvREHGWTKAALDEMHKVDS------FLREVMRASGMTTGTMSRKAVKDYTFSDGTF 73
Cdd:cd11059  242 TYLIWeLSRPPNLQEKLREEL----AGLPGPFRGPPDLEDLDKlpylnaVIRETLRLYPPIPGSLPRVVPEGGATIGGYY 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  74 IPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRF-----SDMRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd11059  318 IPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWldpsgETAREMKRafwpFGSGSRMCIGMNLALMEMKLALAAIYRNYRT 397

                        170
                 ....*....|.
gi 807744981 145 ------KMEQE 149
Cdd:cd11059  398 stttddDMEQE 408
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 2-142 1.24e-09

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: 59.28  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTGTmSRKAVKDYTFSDGTfIPAGTYLM 81
Cdd:cd11052  255 TTMLLAIHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLRLYPPAVFL-TRKAKEDIKLGGLV-IPKGTSIW 332

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  82 APTGAIYTDDAVYPN-AVEFNPWRFSD----MRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATY 142
Cdd:cd11052  333 IPVLALHHDEEIWGEdANEFNPERFADgvakAAKHPMaflpFGLGPRNCIGQNFATMEAKIVLAMILQRF 402
PLN02774 PLN02774
brassinosteroid-6-oxidase
 1-150 1.83e-09

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 58.63  E-value: 1.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEvDRVVREHGWTKAALD-EMHKVDSFLR----EVMRASGMTTGTMsRKAVKDYTFsDGTFIP 75
Cdd:PLN02774 286 MAVKYLHDHPKALQELRKE-HLAIRERKRPEDPIDwNDYKSMRFTRavifETSRLATIVNGVL-RKTTQDMEL-NGYVIP 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  76 AGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSD--MRDQDD---FGHGHHACPGRFFAVSEMKTILAHIVATYdvKMEQEG 150
Cdd:PLN02774 363 KGWRIYVYTREINYDPFLYPDPMTFNPWRWLDksLESHNYfflFGGGTRLCPGKELGIVEISTFLHYFVTRY--RWEEVG 440
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 2-145 2.22e-09

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 58.57  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVR-----EHGWTKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFsDGTFIPA 76
Cdd:PLN02302 310 ATIFLQEHPEVLQKAKAEQEEIAKkrppgQKGLTLKDVRKMEYLSQVIDETLRLINISL-TVFREAKTDVEV-NGYTIPK 387

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744981  77 GTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:PLN02302 388 GWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPKAgtflPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLE 460
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 2-146 2.55e-09

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: 58.30  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHgwTKAALDEMHK---VDSFLREVMRASGMTTGTmSRKAVKDYTFsDGTFIPAGT 78
Cdd:cd20613  257 TLLELGRHPEILKRLQAEVDEVLGSK--QYVEYEDLGKleyLSQVLKETLRLYPPVPGT-SRELTKDIEL-GGYKIPAGT 332

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSDmrDQDD---------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKM 146
Cdd:cd20613  333 TVLVSTYVMGRMEEYFEDPLKFDPERFSP--EAPEkipsyayfpFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFEL 407
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 2-138 4.33e-09

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: 57.46  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVdrvVREHGWTK-------AALDEMHKVdsfLREVMRASGMTTgTMSRKAVKDYTFSdGTFI 74
Cdd:cd20641  258 TMFLLSLHPDWQEKLREEV---FRECGKDKipdadtlSKLKLMNMV---LMETLRLYGPVI-NIARRASEDMKLG-GLEI 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744981  75 PAGTYLMAPTGAIYTDDAVY-PNAVEFNPWRFSD--MRDQDD------FGHGHHACPGRFFAVSEMKTILAHI 138
Cdd:cd20641  330 PKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANgvSRAATHpnallsFSLGPRACIGQNFAMIEAKTVLAMI 402
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 2-147 5.16e-09

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: 57.37  E-value: 5.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMsRKAVKDYTFSDGT-FIPAGTY 79
Cdd:cd11046  263 TLYELSQNPELMAKVQAEVDAVLgDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLI-RRAVEDDKLPGGGvKVPAGTD 341

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQ------DD-----FGHGHHACPGRFFAVSEMKTILAHIVATYDVKME 147
Cdd:cd11046  342 IFISVYNLHRSPELWEDPEEFDPERFLDPFINppneviDDfaflpFGGGPRKCLGDQFALLEATVALAMLLRRFDFELD 420
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 2-158 9.52e-09

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: 56.50  E-value: 9.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV--REHGWTKAALDEMHKVDSFLREVMR---ASGMttgtMSRKAVKDYTFsDGTFIPA 76
Cdd:cd20660  255 ALYLIGSHPEVQEKVHEELDRIFgdSDRPATMDDLKEMKYLECVIKEALRlfpSVPM----FGRTLSEDIEI-GGYTIPK 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  77 GTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQD-------DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ- 148
Cdd:cd20660  330 GTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGrhpyayiPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQk 409

                        170
                 ....*....|.
gi 807744981 149 -EGVIPTPIMI 158
Cdd:cd20660  410 rEDLKPAGELI 420
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 2-144 1.24e-08

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: 56.17  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKA--ALDEMHKVDSFLREVM-----RASGMTTgtmsRKAVKDYTFSDGTfI 74
Cdd:cd20635  233 TLAFILSHPSVYKKVMEEISSVLGKAGKDKIkiSEDDLKKMPYIKRCVLeairlRSPGAIT----RKVVKPIKIKNYT-I 307

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  75 PAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDmRDQDD---------FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd20635  308 PAGDMLMLSPYWAHRNPKYFPDPELFKPERWKK-ADLEKnvflegfvaFGGGRYQCPGRWFALMEIQMFVAMFLYKYDF 385
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 70-150 1.48e-08

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: 55.76  E-value: 1.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  70 DGTFIPAGTYLMAPTGAIYTDDAVY-PNAVEFNPWRFSDMRDQD------DFGHGHHACPGRFFAVSEMKTILAHIVATY 142
Cdd:cd20615  307 GGYRIPANTPVVVDTYALNINNPFWgPDGEAYRPERFLGISPTDlrynfwRFGFGPRKCLGQHVADVILKALLAHLLEQY 386


                 ....*...
gi 807744981 143 DVKMEQEG 150
Cdd:cd20615  387 ELKLPDQG 394
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 29-153 2.04e-08

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: 55.40  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  29 WTKAALDE-MHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSD 107
Cdd:cd11066  282 WEDCAAEEkCPYVVALVKETLRYFTVLPLGLPRKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLD 360

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 807744981 108 MRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGVIP 153
Cdd:cd11066  361 ASGDLIpgpphfsFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEEPM 413
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 3-136 2.27e-08

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: 55.47  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEV-----DRVVREHGWTKaaLDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFSDGTFIPAG 77
Cdd:cd20679  268 LYNLARHPEYQERCRQEVqellkDREPEEIEWDD--LAQLPFLTMCIKESLRLHPPVT-AISRCCTQDIVLPDGRVIPKG 344

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744981  78 TYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQD-------DFGHGHHACPGRFFAVSEMKTILA 136
Cdd:cd20679  345 IICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGrsplafiPFSAGPRNCIGQTFAMAEMKVVLA 410
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 1-144 2.28e-08

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: 55.23  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVRE-HGWTKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFSDgTFIPAGTY 79
Cdd:cd20644  254 FTLFELARNPDVQQILRQESLAAAAQiSEHPQKALTELPLLKAALKETLRLYPVGI-TVQRVPSSDLVLQN-YHIPAGTL 331

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD------FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd20644  332 VQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRnfkhlaFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLV 402
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 2-144 3.40e-08

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: 54.57  E-value: 3.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMR---ASGMttgtMSRKAVKDYTFsDGTFIPAGT 78
Cdd:cd11049  243 AFHLLARHPEVERRLHAELDAVLGGRPATFEDLPRLTYTRRVVTEALRlypPVWL----LTRRTTADVEL-GGHRLPAGT 317

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDV 144
Cdd:cd11049  318 EVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVprgafipFGAGARKCIGDTFALTELTLALATIASRWRL 390
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 3-164 4.01e-08

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 54.56  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVVR----EHGWTKAALDEMHKVDSFLREVMRASGMTTGTMsRKAVKDYTFsDGTFIPAGT 78
Cdd:PLN02196 288 LKYLAENPSVLEAVTEEQMAIRKdkeeGESLTWEDTKKMPLTSRVIQETLRVASILSFTF-REAVEDVEY-EGYLIPKGW 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDDF---GHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGvipTP 155
Cdd:PLN02196 366 KVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNTFmpfGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTS---NG 442


                 ....*....
gi 807744981 156 IMIGHICAP 164
Cdd:PLN02196 443 IQYGPFALP 451
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 2-156 8.19e-08

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 53.93  E-value: 8.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGW-TKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGTYL 80
Cdd:PLN03234 311 AMTYLIKYPEAMKKAQDEVRNVIGDKGYvSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIG-GYDIPAKTII 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVY-PNAVEFNPWRFS------DMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQe 149
Cdd:PLN03234 390 QVNAWAVSRDTAAWgDNPNEFIPERFMkehkgvDFKGQDfellPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPK- 468


                 ....*..
gi 807744981 150 GVIPTPI 156
Cdd:PLN03234 469 GIKPEDI 475
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 2-167 1.03e-07

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: 53.27  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAA-LDEMHKVDSFLREVMRASG---MTTGTMSRKAV-KDYTfsdgtfIPA 76
Cdd:cd20645  249 ILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEdLKNMPYLKACLKESMRLTPsvpFTSRTLDKDTVlGDYL------LPK 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  77 GTYLMAPTGAIYTDDAVYPNAVEFNPWRFsdMRDQDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ 148
Cdd:cd20645  323 GTVLMINSQALGSSEEYFEDGRQFKPERW--LQEKHSinpfahvpFGIGKRMCIGRRLAELQLQLALCWIIQKYQIVATD 400

                        170
                 ....*....|....*....
gi 807744981 149 EGviPTPIMIGHICAPSRK 167
Cdd:cd20645  401 NE--PVEMLHSGILVPSRE 417
PLN02500 PLN02500
cytochrome P450 90B1
 1-161 1.11e-07

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 53.33  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDE---VDRVVREHGWTKAALDEMHKVD---SFLREVMRAsGMTTGTMSRKAVKDYTFSdGTFI 74
Cdd:PLN02500 301 LAIFFLQGCPKAVQELREEhleIARAKKQSGESELNWEDYKKMEftqCVINETLRL-GNVVRFLHRKALKDVRYK-GYDI 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  75 PAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD--------------FGHGHHACPGRFFAVSEMKTILAHIVA 140
Cdd:PLN02500 379 PSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGssgsssattnnfmpFGGGPRLCAGSELAKLEMAVFIHHLVL 458

                        170       180       190
                 ....*....|....*....|....*....|.
gi 807744981 141 TYD---VKMEQEGVIP-------TPIMIGHI 161
Cdd:PLN02500 459 NFNwelAEADQAFAFPfvdfpkgLPIRVRRI 489
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 2-159 1.32e-07

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: 52.86  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV---REHGWTKAAldEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGT 78
Cdd:cd20666  251 CLLYMSLYPEVQEKVQAEIDTVIgpdRAPSLTDKA--QMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQ-GYTIPKGT 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQ-------DDFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGv 151
Cdd:cd20666  328 VIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQlikkeafIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNA- 406


                 ....*...
gi 807744981 152 iPTPIMIG 159
Cdd:cd20666  407 -PKPSMEG 413
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 60-172 1.65e-07

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: 52.62  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  60 RKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRF------SDMRDQD----DFGHGHHACPGRFFAVS 129
Cdd:cd20654  323 REATEDCTVG-GYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFltthkdIDVRGQNfeliPFGSGRRSCPGVSFGLQ 401

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 807744981 130 EMKTILAHIVATYDVKMEQEGVIPTPIMIGHICAPSRKAEILV 172
Cdd:cd20654  402 VMHLTLARLLHGFDIKTPSNEPVDMTEGPGLTNPKATPLEVLL 444
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 2-144 1.73e-07

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 52.69  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG----------WTKAALDEMHKVDSFLREVMRasgMTTGTMS-RKAVKDYTFSd 70
Cdd:cd20632  238 AMYYLLRHPEALAAVRDEIDHVLQSTGqelgpdfdihLTREQLDSLVYLESAINESLR---LSSASMNiRVVQEDFTLK- 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  71 gtFIPAGTY---------LMAPTgaIYTDDAVYPNAVEFNPWRF--SDMRDQDD-------------FGHGHHACPGRFF 126
Cdd:cd20632  314 --LESDGSVnlrkgdivaLYPQS--LHMDPEIYEDPEVFKFDRFveDGKKKTTFykrgqklkyylmpFGSGSSKCPGRFF 389

                        170
                 ....*....|....*...
gi 807744981 127 AVSEMKTILAHIVATYDV 144
Cdd:cd20632  390 AVNEIKQFLSLLLLYFDL 407
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 2-149 1.77e-07

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: 52.58  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEV-DRVVREHGWTKAALDEMHKVDSFLREVMRasgM---TTGTMSRKAVKDYTFSDGTFIPAG 77
Cdd:cd11058  240 LTYYLLKNPEVLRKLVDEIrSAFSSEDDITLDSLAQLPYLNAVIQEALR---LyppVPAGLPRVVPAGGATIDGQFVPGG 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  78 TYLMAPTGAIYTDDAVYPNAVEFNPWRF---SDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKME 147
Cdd:cd11058  317 TSVSVSQWAAYRSPRNFHDPDEFIPERWlgdPRFEFDNDkkeafqpFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELD 396


                 ..
gi 807744981 148 QE 149
Cdd:cd11058  397 PE 398
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 1-146 2.27e-07

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: 52.20  E-value: 2.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVREHGW----TKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSDGTFIPA 76
Cdd:cd11060  244 AILYYLLKNPRVYAKLRAEIDAAVAEGKLsspiTFAEAQKLPYLQAVIKEALRLHPPVGLPLERVVPPGGATICGRFIPG 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  77 GTYLMAPTGAIYTDDAVY-PNAVEFNPWRF-------SDMRDQDD--FGHGHHACPGRFFAVSEMKTILAHIVATYDVKM 146
Cdd:cd11060  324 GTIVGVNPWVIHRDKEVFgEDADVFRPERWleadeeqRRMMDRADltFGAGSRTCLGKNIALLELYKVIPELLRRFDFEL 403
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 9-143 2.69e-07

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: 51.79  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   9 YPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMR---ASGMTTGTMSRKAVK--DYTfsdgtfIPAGTYLMA 82
Cdd:cd20618  259 HPEVMRKAQEELDSVVgRERLVEESDLPKLPYLQAVVKETLRlhpPGPLLLPHESTEDCKvaGYD------IPAGTRVLV 332

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  83 PTGAIYTDDAVYPNAVEFNPWRF-----SDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:cd20618  333 NVWAIGRDPKVWEDPLEFKPERFlesdiDDVKGQDfellPFGSGRRMCPGMPLGLRMVQLTLANLLHGFD 402
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 3-162 2.83e-07

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: 52.03  E-value: 2.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVVREHgwTKAALDEMHKVdSFLR----EVMRAS-----GMTTGTMSRKAVKDYtfsdgtF 73
Cdd:cd20652  258 LLYMALFPKEQRRIQRELDEVVGRP--DLVTLEDLSSL-PYLQacisESQRIRsvvplGIPHGCTEDAVLAGY------R 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  74 IPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQ-------DDFGHGHHACPGRFFAVSEMKTILAHIVATYDVKM 146
Cdd:cd20652  329 IPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKylkpeafIPFQTGKRMCLGDELARMILFLFTARILRKFRIAL 408

                        170
                 ....*....|....*.
gi 807744981 147 EQEgvIPTPiMIGHIC 162
Cdd:cd20652  409 PDG--QPVD-SEGGNV 421
PTZ00404 PTZ00404
cytochrome P450; Provisional
 6-145 3.11e-07

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 52.03  E-value: 3.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   6 LAAYPQYMGHLRDEVDRVVRehGWTKAALDEMHK---VDSFLREVMRASGMTTGTMSRKAVKDYTFSDGTFIPAGTYLMA 82
Cdd:PTZ00404 310 LCNYPEIQEKAYNEIKSTVN--GRNKVLLSDRQStpyTVAIIKETLRYKPVSPFGLPRSTSNDIIIGGGHFIPKDAQILI 387

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744981  83 PTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD---FGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:PTZ00404 388 NYYSLGRNEKYFENPEQFDPSRFLNPDSNDAfmpFSIGPRNCVGQQFAQDELYLAFSNIILNFKLK 453
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 2-131 3.14e-07

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: 51.72  E-value: 3.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHgwTKAALDE---MHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGT 78
Cdd:cd20662  248 ALLYMALYPEIQEKVQAEIDRVIGQK--RQPSLADresMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLA-GFHLPKGT 324

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSD---MRDQDD---FGHGHHACPGRFFAVSEM 131
Cdd:cd20662  325 MILTNLTALHRDPKEWATPDTFNPGHFLEngqFKKREAflpFSMGKRACLGEQLARSEL 383
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 6-159 4.36e-07

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


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 51.34  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   6 LAAYPQYMGHLRDEVDRVV---REHGWTKAAldEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSDgTFIPAGTYLMA 82
Cdd:cd20668  253 LMKHPEVEAKVHEEIDRVIgrnRQPKFEDRA--KMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRD-FFLPKGTEVFP 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  83 PTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ--EGVIP 153
Cdd:cd20668  330 MLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKksdafvpFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQspEDIDV 409


                 ....*.
gi 807744981 154 TPIMIG 159
Cdd:cd20668  410 SPKHVG 415
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 2-131 5.63e-07

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


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 51.14  E-value: 5.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYL 80
Cdd:cd11028  254 SLLYMIRYPEIQEKVQAELDRVIgRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIPHATTRDTTL-NGYFIPKGTVV 332

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD---------FGHGHHACPGRFFAVSEM 131
Cdd:cd11028  333 FVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDktkvdkflpFGAGRRRCLGEELARMEL 392
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 3-136 6.31e-07

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 50.74  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFY-LAAYPQYMGHLRDEVDRVVR-------EHgwtkaaLDEMHKVDSFLREVMRASGMTTGtMSRKAVKDYTFSDGTFI 74
Cdd:cd20678  262 ILYcLALHPEHQQRCREEIREILGdgdsitwEH------LDQMPYTTMCIKEALRLYPPVPG-ISRELSKPVTFPDGRSL 334

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 807744981  75 PAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSdmRDQDDFGHGH---------HACPGRFFAVSEMKTILA 136
Cdd:cd20678  335 PAGITVSLSIYGLHHNPAVWPNPEVFDPLRFS--PENSSKRHSHaflpfsagpRNCIGQQFAMNEMKVAVA 403
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 10-139 1.01e-06

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: 50.18  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  10 PQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGTYLMAPTGAIY 88
Cdd:cd20656  261 PRVQEKAQEELDRVVgSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIG-GYDIPKGANVHVNVWAIA 339

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  89 TDDAVYPNAVEFNPWRF----SDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIV 139
Cdd:cd20656  340 RDPAVWKNPLEFRPERFleedVDIKGHDfrllPFGAGRRVCPGAQLGINLVTLMLGHLL 398
PLN02290 PLN02290
cytokinin trans-hydroxylase
 2-149 1.18e-06

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 50.20  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFSDGTfIPAGTYLM 81
Cdd:PLN02290 339 TLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRLYPPAT-LLPRMAFEDIKLGDLH-IPKGLSIW 416

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 807744981  82 APTGAIYTDDAVY-PNAVEFNPWRFSDM-----RDQDDFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQE 149
Cdd:PLN02290 417 IPVLAIHHSEELWgKDANEFNPDRFAGRpfapgRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDN 490
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 2-131 2.24e-06

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 49.03  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGTYLM 81
Cdd:cd20664  248 GLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFR-GYFIPKGTYVI 326

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRFSD------MRDQ-DDFGHGHHACPGRFFAVSEM 131
Cdd:cd20664  327 PLLTSVLQDKTEWEKPEEFNPEHFLDsqgkfvKRDAfMPFSAGRRVCIGETLAKMEL 383
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 1-149 2.37e-06

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: 49.00  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MAlfYLAAYPQYMGHLRDEVDRVVREHGW-TKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTY 79
Cdd:cd11072  252 MT--ELIRNPRVMKKAQEEVREVVGGKGKvTEEDLEKLKYLKAVIKETLRLHPPAPLLLPRECREDCKI-NGYDIPAKTR 328

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRF----SDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQE 149
Cdd:cd11072  329 VIVNAWAIGRDPKYWEDPEEFRPERFldssIDFKGQDfeliPFGAGRRICPGITFGLANVELALANLLYHFDWKLPDG 406
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 2-138 2.54e-06

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


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 48.94  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVrehGWTKAALDE----MHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAG 77
Cdd:cd20677  259 SLLYLIKYPEIQDKIQEEIDEKI---GLSRLPRFEdrksLHYTEAFINEVFRHSSFVPFTIPHCTTADTTL-NGYFIPKD 334

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  78 TYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD---------FGHGHHACPGRFFAVSEMKTILAHI 138
Cdd:cd20677  335 TCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNkslvekvliFGMGVRKCLGEDVARNEIFVFLTTI 404
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 2-145 3.04e-06

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: 48.76  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTmSRKAVKDYTFSdGTFIPAGTYL 80
Cdd:cd20647  260 ATYLLARHPEVQQQVYEEIVRNLgKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGN-GRVTQDDLIVG-GYLIPKGTQL 337

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNP--WRFSDMRDQDD------FGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:cd20647  338 ALCHYSTSYDEENFPRAEEFRPerWLRKDALDRVDnfgsipFGYGIRSCIGRRIAELEIHLALIQLLQNFEIK 410
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 1-155 3.24e-06

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 48.82  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVREHG------WTKaaLDEMHKVDSFLREVMRASGMTTG----TMSRKAVKDYTfsd 70
Cdd:PLN02987 289 LAVKFLTETPLALAQLKEEHEKIRAMKSdsysleWSD--YKSMPFTQCVVNETLRVANIIGGifrrAMTDIEVKGYT--- 363

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  71 gtfIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFsdmrdQDD------------FGHGHHACPGRFFAVSEMKTILAHI 138
Cdd:PLN02987 364 ---IPKGWKVFASFRAVHLDHEYFKDARTFNPWRW-----QSNsgttvpsnvftpFGGGPRLCPGYELARVALSVFLHRL 435

                        170
                 ....*....|....*...
gi 807744981 139 VATYD-VKMEQEGVIPTP 155
Cdd:PLN02987 436 VTRFSwVPAEQDKLVFFP 453
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 40-135 3.71e-06

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 48.37  E-value: 3.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  40 VDSFLREVMRASGMTTGtMSRKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRfSDMRDQDDFGHGHH 119
Cdd:cd11078  253 IPNAVEETLRYDSPVQG-LRRTATRDVEIG-GVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR-PNARKHLTFGHGIH 329

                         90
                 ....*....|....*.
gi 807744981 120 ACPGRFFAVSEMKTIL 135
Cdd:cd11078  330 FCLGAALARMEARIAL 345
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 3-153 4.15e-06

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 48.22  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVVREHGWTKAA--------LDEMHKVDSFLREVMRasgMTTGT-MSRKAVKDYT--FSDG 71
Cdd:cd20634  245 LLFLLKHPEAMAAVRGEIQRIKHQRGQPVSQtltinqelLDNTPVFDSVLSETLR---LTAAPfITREVLQDMKlrLADG 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  72 T-----------FIPAGTYLMAPTgaIYTDdavyPNAVEFNPWRFSDMRDQDDF--------------GHGHHACPGRFF 126
Cdd:cd20634  322 QeynlrrgdrlcLFPFLSPQMDPE--IHQE----PEVFKYDRFLNADGTEKKDFykngkrlkyynmpwGAGDNVCIGRHF 395

                        170       180
                 ....*....|....*....|....*...
gi 807744981 127 AVSEMKTILAHIVATYDVKM-EQEGVIP 153
Cdd:cd20634  396 AVNSIKQFVFLILTHFDVELkDPEAEIP 423
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 2-146 5.80e-06

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: 47.80  E-value: 5.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYL 80
Cdd:cd20657  251 ALAELIRHPDILKKAQEEMDQVIgRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEV-DGYYIPKGTRL 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRF-------SDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKM 146
Cdd:cd20657  330 LVNIWAIGRDPDVWENPLEFKPERFlpgrnakVDVRGNDfeliPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKL 406
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 1-135 8.33e-06

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 47.20  E-value: 8.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVrehgwtkAALDEMhkvdsflrevMRASGMTTgtMSRKAVKDYTFsDGTFIPAGTYL 80
Cdd:cd11035  212 FIFRHLARHPEDRRRLREDPELIP-------AAVEEL----------LRRYPLVN--VARIVTRDVEF-HGVQLKAGDMV 271

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWR-----FSdmrdqddFGHGHHACPGRFFAVSEMKTIL 135
Cdd:cd11035  272 LLPLALANRDPREFPDPDTVDFDRkpnrhLA-------FGAGPHRCLGSHLARLELRIAL 324
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 5-153 1.01e-05

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 46.96  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   5 YLAAYPQYMGHLRDEVDRVvrehgwtKAALDEMHKVDSFLRevmrasgmttgTMSRKAVKDYTFSdGTFIPAGTYLMAPT 84
Cdd:cd11079  209 YLARHPELQARLRANPALL-------PAAIDEILRLDDPFV-----------ANRRITTRDVELG-GRTIPAGSRVTLNW 269

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 807744981  85 GAIYTDDAVYPNAVEFNPwrfsdMRDQDD---FGHGHHACPGRFFAVSEMKTILAHIVA-TYDVKMEQEGVIP 153
Cdd:cd11079  270 ASANRDERVFGDPDEFDP-----DRHAADnlvYGRGIHVCPGAPLARLELRILLEELLAqTEAITLAAGGPPE 337
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 10-152 1.10e-05

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: 46.82  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  10 PQYMGHLRDEVDRVVrehGWTK----AALDEMHKVDSFLREVMR---ASGMTTgtmsRKAVKDYTFsDGTFIPAGTYLMA 82
Cdd:cd20655  259 PEVLEKAREEIDSVV---GKTRlvqeSDLPNLPYLQAVVKETLRlhpPGPLLV----RESTEGCKI-NGYDIPEKTTLFV 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  83 PTGAIYTDDAVYPNAVEFNPWRF---SDMRDQDD----------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQE 149
Cdd:cd20655  331 NVYAIMRDPNYWEDPLEFKPERFlasSRSGQELDvrgqhfkllpFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDG 410


                 ...
gi 807744981 150 GVI 152
Cdd:cd20655  411 EKV 413
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 16-124 1.14e-05

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


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 46.94  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  16 LRDEVDRVVREHGW-TKAALDEMHKVDSFLREVMRASgmTTGTM---SRKAVKDYTFsDGTFIPAGTYLMAPTGAIYTDD 91
Cdd:cd11076  261 AQAEIDAAVGGSRRvADSDVAKLPYLQAVVKETLRLH--PPGPLlswARLAIHDVTV-GGHVVPAGTTAMVNMWAITHDP 337

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 807744981  92 AVYPNAVEFNPWRF-------------SDMRdQDDFGHGHHACPGR 124
Cdd:cd11076  338 HVWEDPLEFKPERFvaaeggadvsvlgSDLR-LAPFGAGRRVCPGK 382
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 6-138 1.62e-05

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: 46.50  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   6 LAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTGtMSRKAVKDYTFSDGTfIPAGTYLMAPTG 85
Cdd:cd20642  261 LSQHPDWQERAREEVLQVFGNNKPDFEGLNHLKVVTMILYEVLRLYPPVIQ-LTRAIHKDTKLGDLT-LPAGVQVSLPIL 338

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744981  86 AIYTDDAVYPN-AVEFNPWRFSD-----MRDQDD---FGHGHHACPGRFFAVSEMKTILAHI 138
Cdd:cd20642  339 LVHRDPELWGDdAKEFNPERFAEgiskaTKGQVSyfpFGWGPRICIGQNFALLEAKMALALI 400
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 2-137 2.24e-05

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


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 45.91  E-value: 2.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVrEHGWTKAALD--EMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGTY 79
Cdd:cd20669  249 GFLILMKYPKVAARVQEEIDRVV-GRNRLPTLEDraRMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFR-GFLIPKGTD 326

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-------FGHGHHACPGRFFAVSEM----KTILAH 137
Cdd:cd20669  327 VIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKkndafmpFSAGKRICLGESLARMELflylTAILQN 395
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 2-164 2.32e-05

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 46.10  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGwTKAALDEMHK--VDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGTY 79
Cdd:cd20665  249 GLLLLLKHPEVTAKVQEEIDRVIGRHR-SPCMQDRSHMpyTDAVIHEIQRYIDLVPNNLPHAVTCDTKFR-NYLIPKGTT 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSD----MRDQD---DFGHGHHACPGRFFAVSEMKTILAHIVATYDVK--MEQEG 150
Cdd:cd20665  327 VITSLTSVLHDDKEFPNPEKFDPGHFLDengnFKKSDyfmPFSAGKRICAGEGLARMELFLFLTTILQNFNLKslVDPKD 406

                        170
                 ....*....|....
gi 807744981 151 VIPTPIMIGHICAP 164
Cdd:cd20665  407 IDTTPVVNGFASVP 420
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 3-107 2.43e-05

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


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 45.77  E-value: 2.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDyTFSDGTFIPAGTYLM 81
Cdd:cd20675  259 LLLLVRYPDVQARLQEELDRVVgRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVTIPHATTAD-TSILGYHIPKDTVVF 337

                         90       100
                 ....*....|....*....|....*.
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRFSD 107
Cdd:cd20675  338 VNQWSVNHDPQKWPNPEVFDPTRFLD 363
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 1-146 4.25e-05

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: 44.94  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRV--VREHGWTKAALDEMHKVDSFLREVMRasgMTTGTMSRKA---------VKDYtfs 69
Cdd:cd11062  246 VATFHLLSNPEILERLREELKTAmpDPDSPPSLAELEKLPYLTAVIKEGLR---LSYGVPTRLPrvvpdeglyYKGW--- 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  70 dgtFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRF---SDMRDQDD----FGHGHHACPGRFFAVSEMKTILAHIVATY 142
Cdd:cd11062  320 ---VIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWlgaAEKGKLDRylvpFSKGSRSCLGINLAYAELYLALAALFRRF 396


                 ....
gi 807744981 143 DVKM 146
Cdd:cd11062  397 DLEL 400
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 2-154 5.03e-05

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: 44.71  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVRE-HGWTKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFSDgTFIPAGTYL 80
Cdd:cd20643  257 TLYELARNPNVQEMLRAEVLAARQEaQGDMVKMLKSVPLLKAAIKETLRLHPVAV-SLQRYITEDLVLQN-YHIPAGTLV 334

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQEGVIPT 154
Cdd:cd20643  335 QVGLYAMGRDPTVFPKPEKYDPERWLSKDITHfrnlGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIETQRLVEVKT 412
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 17-136 7.01e-05

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


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 44.21  E-value: 7.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  17 RDEVDRVVREHGWTKAALDEMHKVDSFLrevmrasgmttGTMSRKAVKDYTFsDGTFIPAGTYLMAPTGAIYTDDAVYPN 96
Cdd:cd20629  223 PEQLERVRRDRSLIPAAIEEGLRWEPPV-----------ASVPRMALRDVEL-DGVTIPAGSLLDLSVGSANRDEDVYPD 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 807744981  97 AVEFNPWRfSDMRdQDDFGHGHHACPGRFFAVSEMKTILA 136
Cdd:cd20629  291 PDVFDIDR-KPKP-HLVFGGGAHRCLGEHLARVELREALN 328
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 2-123 7.91e-05

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: 44.09  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGwtKAALDE---MHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGT 78
Cdd:cd11026  249 ALLLLMKYPHIQEKVQEEIDRVIGRNR--TPSLEDrakMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFR-GYTIPKGT 325

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSDmrdqDD-----------FGHGHHACPG 123
Cdd:cd11026  326 TVIPNLTSVLRDPKQWETPEEFNPGHFLD----EQgkfkkneafmpFSAGKRVCLG 377
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 2-136 1.08e-04

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 43.73  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPqymghlrDEVDRVVREHGWTKAALDEMHKVDSFLRevmrasgmttgTMSRKAVKDYTFsDGTFIPAGTYLM 81
Cdd:cd11037  225 ALWLLARHP-------DQWERLRADPSLAPNAFEEAVRLESPVQ-----------TFSRTTTRDTEL-AGVTIPAGSRVL 285

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRfsDMRDQDDFGHGHHACPGRFFAVSEMKTILA 136
Cdd:cd11037  286 VFLGSANRDPRKWDDPDRFDITR--NPSGHVGFGHGVHACVGQHLARLEGEALLT 338
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
 1-164 1.11e-04

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 43.57  E-value: 1.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDyTFSDGTFIPAGTYL 80
Cdd:cd20619  195 ILVFYAVGHMAIGYLIASGIELFARRPEVFTAFRNDESARAAIINEMVRMDPPQL-SFLRFPTED-VEIGGVLIEAGSPI 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDDFGHGHHACPGRFFAVSEMKTILAHIV--ATYDVKMEQEGVIPTPIMI 158
Cdd:cd20619  273 RFMIGAANRDPEVFDDPDVFDHTRPPAASRNLSFGLGPHSCAGQIISRAEATTVFAVLAerYERIELAEEPTVAHNDFAR 352


                 ....*.
gi 807744981 159 GHICAP 164
Cdd:cd20619  353 RYRKLP 358
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 2-153 1.39e-04

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 43.65  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGwtKAALDE---MHKVDSFLREVMRASGMTTGTMSRKAVKDyTFSDGTFIPAGT 78
Cdd:cd20661  261 AILFMALYPNIQGQVQKEIDLVVGPNG--MPSFEDkckMPYTEAVLHEVLRFCNIVPLGIFHATSKD-AVVRGYSIPKGT 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  79 YLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQ-------DDFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQeGV 151
Cdd:cd20661  338 TVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQfakkeafVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPH-GL 416


                 ..
gi 807744981 152 IP 153
Cdd:cd20661  417 IP 418
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 46-131 1.48e-04

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: 43.12  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  46 EVMRASGMTTgTMSRKAVKDYTFsDGTFIPAGTYLMAPTGAIYTDDAVypnaveFNPWRFSDMRDQD---DFGHGHHACP 122
Cdd:cd11038  264 EVLRWCPTTT-WATREAVEDVEY-NGVTIPAGTVVHLCSHAANRDPRV------FDADRFDITAKRAphlGFGGGVHHCL 335


                 ....*....
gi 807744981 123 GRFFAVSEM 131
Cdd:cd11038  336 GAFLARAEL 344
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 2-150 1.69e-04

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: 43.39  E-value: 1.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHG-WTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYL 80
Cdd:cd11075  254 AMAELVKNPEIQEKLYEEIKEVVGDEAvVTEEDLPKMPYLKAVVLETLRRHPPGHFLLPHAVTEDTVL-GGYDIPAGAEV 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD------------FGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ 148
Cdd:cd11075  333 NFNVAAIGRDPKVWEDPEEFKPERFLAGGEAADidtgskeikmmpFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVE 412


                 ..
gi 807744981 149 EG 150
Cdd:cd11075  413 GE 414
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 32-143 2.31e-04

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: 42.90  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  32 AALDEMHKVDSFLREVMRASGMTTGTMsRKAVKdyTFS-DGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDMRD 110
Cdd:cd20636  287 EKLSRLRYLDCVVKEVLRLLPPVSGGY-RTALQ--TFElDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVERE 363

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 807744981 111 QDD--------FGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:cd20636  364 ESKsgrfnyipFGGGVRSCIGKELAQVILKTLAVELVTTAR 404
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 1-135 2.48e-04

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


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 42.55  E-value: 2.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   1 MALFYLAAYPQYMGHLRDEVDRVVrehgwtkAALDEMhkvdsfLREVMRASGmttGTMSRKAVKDYTFSDGTfIPAGTYL 80
Cdd:cd11031  228 NGVLLLLRHPEQLARLRADPELVP-------AAVEEL------LRYIPLGAG---GGFPRYATEDVELGGVT-IRAGEAV 290

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPwrfsdmrDQDD-----FGHGHHACPGRFFAVSEMKTIL 135
Cdd:cd11031  291 LVSLNAANRDPEVFPDPDRLDL-------DREPnphlaFGHGPHHCLGAPLARLELQVAL 343
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 3-145 2.76e-04

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: 42.63  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFY-LAAYPQYMGHLRDEVDRVVREhGWTKAA---------LDEMHKVDSFLREVMR----ASGMTtgtMSRKAVKdYTF 68
Cdd:cd11051  208 AFYlLSKHPEVLAKVRAEHDEVFGP-DPSAAAellregpelLNQLPYTTAVIKETLRlfppAGTAR---RGPPGVG-LTD 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  69 SDGTFIP-AGTYLMAPTGAIYTDDAVYPNAVEFNPWRFSDmrdQDD------------FGHGHHACPGRFFAVSEMKTIL 135
Cdd:cd11051  283 RDGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLV---DEGhelyppksawrpFERGPRNCIGQELAMLELKIIL 359

                        170
                 ....*....|
gi 807744981 136 AHIVATYDVK 145
Cdd:cd11051  360 AMTVRRFDFE 369
PLN02936 PLN02936
epsilon-ring hydroxylase
 3-154 2.98e-04

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 42.47  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTgTMSRKAVKDYTFSDGTFIPAGTYLMA 82
Cdd:PLN02936 302 LYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPP-VLIRRAQVEDVLPGGYKVNAGQDIMI 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  83 PTGAIYTDDAVYPNAVEFNPWRF-----------SDMRdQDDFGHGHHACPGRFFAVSEMKTILA--------HIVATYD 143
Cdd:PLN02936 381 SVYNIHRSPEVWERAEEFVPERFdldgpvpnetnTDFR-YIPFSGGPRKCVGDQFALLEAIVALAvllqrldlELVPDQD 459

                        170
                 ....*....|.
gi 807744981 144 VKMEQEGVIPT 154
Cdd:PLN02936 460 IVMTTGATIHT 470
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 2-145 3.12e-04

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 42.37  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFY-LAAYPQYMGHLRDEVDRVV--REHGWTKAALDEMHKVDSFLREVMRASGMTTGTmSRKAVKDYTFSDGTFIPAGT 78
Cdd:PLN02426 315 SFFWlLSKHPEVASAIREEADRVMgpNQEAASFEEMKEMHYLHAALYESMRLFPPVQFD-SKFAAEDDVLPDGTFVAKGT 393

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744981  79 YLMAPTGAIYTDDAVY-PNAVEFNPWRFSD---MRDQDDFGH-----GHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:PLN02426 394 RVTYHPYAMGRMERIWgPDCLEFKPERWLKngvFVPENPFKYpvfqaGLRVCLGKEMALMEMKSVAVAVVRRFDIE 469
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 2-143 3.49e-04

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 42.49  E-value: 3.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV-REHGWTKAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYL 80
Cdd:PLN02687 320 AIAELIRHPDILKKAQEELDAVVgRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEI-NGYHIPKGATL 398

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRF--------SDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:PLN02687 399 LVNVWAIARDPEQWPDPLEFRPDRFlpggehagVDVKGSDfeliPFGAGRRICAGLSWGLRMVTLLTATLVHAFD 473
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 2-151 3.76e-04

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: 42.13  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVrehGWTKAALDEMHKV----DSFLREVMRASGMTTGTMSRKAVKDyTFSDGTFIPAG 77
Cdd:cd20667  248 ALLYMVHHPEIQEKVQQELDEVL---GASQLICYEDRKRlpytNAVIHEVQRLSNVVSVGAVRQCVTS-TTMHGYYVEKG 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  78 TYLMAPTGAIYTDDAVYPNAVEFNPWRFSDmRDQD--------DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEqE 149
Cdd:cd20667  324 TIILPNLASVLYDPECWETPHKFNPGHFLD-KDGNfvmneaflPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQLP-E 401


                 ..
gi 807744981 150 GV 151
Cdd:cd20667  402 GV 403
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 60-140 5.27e-04

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


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 41.69  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  60 RKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWR--------FSDMRDQDDFGHGHHACPGRFFAVSEM 131
Cdd:cd11080  256 RQASQDVVVS-GMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHRedlgirsaFSGAADHLAFGSGRHFCVGAALAKREI 334


                 ....*....
gi 807744981 132 KTILAHIVA 140
Cdd:cd11080  335 EIVANQVLD 343
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 31-123 7.32e-04

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


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 40.98  E-value: 7.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  31 KAALDEMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRfsDMRD 110
Cdd:cd11029  246 ALLRADPELWPAAVEELLRYDGPVALATLRFATEDVEV-GGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR--DANG 322

                         90
                 ....*....|...
gi 807744981 111 QDDFGHGHHACPG 123
Cdd:cd11029  323 HLAFGHGIHYCLG 335
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 70-146 9.30e-04

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 40.99  E-value: 9.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  70 DGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRF-------SDMRDQD----DFGHGHHACPGRFFAVSEMKTILAHI 138
Cdd:PLN00110 380 NGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFlseknakIDPRGNDfeliPFGAGRRICAGTRMGIVLVEYILGTL 459


                 ....*...
gi 807744981 139 VATYDVKM 146
Cdd:PLN00110 460 VHSFDWKL 467
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 2-148 1.03e-03

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: 40.90  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVV--REHGWTKAALDEMHKVDSFLREVMRAsgMTTGTMSRKAVKDYTFSDGTFIPAGTY 79
Cdd:cd20680  266 SLYLLGSHPEVQRKVHKELDEVFgkSDRPVTMEDLKKLRYLECVIKESLRL--FPSVPLFARSLCEDCEIRGFKVPKGVN 343

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 807744981  80 LMAPTGAIYTDDAVYPNAVEFNPWRFSDMRDQD-------DFGHGHHACPGRFFAVSEMKTILAHIVATYDVKMEQ 148
Cdd:cd20680  344 AVIIPYALHRDPRYFPEPEEFRPERFFPENSSGrhpyayiPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQ 419
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 18-131 1.09e-03

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: 40.49  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  18 DEVDRVVREHGWTKAALDEMHKVDSFLRevmrasgmtTGTMsRKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNA 97
Cdd:cd20630  235 EALRKVKAEPELLRNALEEVLRWDNFGK---------MGTA-RYATEDVELC-GVTIRKGQMVLLLLPSALRDEKVFSDP 303

                         90       100       110
                 ....*....|....*....|....*....|....
gi 807744981  98 VEFNPWRfsDMRDQDDFGHGHHACPGRFFAVSEM 131
Cdd:cd20630  304 DRFDVRR--DPNANIAFGYGPHFCIGAALARLEL 335
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 63-156 2.08e-03

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: 39.64  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  63 VKDYTFSDGTFIPAGTYlmaptgAIYTDDAVYPNAVEFNPWRFsdMRDQD---------DFGHGHHACPGRFFAVSEMKT 133
Cdd:cd20646  323 VGDYLFPKNTLFHLCHY------AVSHDETNFPEPERFKPERW--LRDGGlkhhpfgsiPFGYGVRACVGRRIAELEMYL 394

                         90       100
                 ....*....|....*....|...
gi 807744981 134 ILAHIVATYDVKMEQEGVIPTPI 156
Cdd:cd20646  395 ALSRLIKRFEVRPDPSGGEVKAI 417
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 60-147 2.27e-03

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: 39.82  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  60 RKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRF----SDMRDQD----DFGHGHHACPGRFFAVSEM 131
Cdd:cd11073  313 RKAEEDVEVM-GYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFlgseIDFKGRDfeliPFGSGRRICPGLPLAERMV 391

                         90
                 ....*....|....*.
gi 807744981 132 KTILAHIVATYDVKME 147
Cdd:cd11073  392 HLVLASLLHSFDWKLP 407
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 3-145 3.27e-03

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: 39.14  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   3 LFYLAAYPQYMGHLRDEVDRVVREHGwTKAALD--EMHKVDSFLREVMRASGMTTGTMSRKAVKDYTFSdGTFIPAGTYL 80
Cdd:cd20670  250 FLLLMKYPEVEAKIHEEINQVIGPHR-LPSVDDrvKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFR-GYLLPKGTDV 327

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744981  81 MAPTGAIYTDDAVYPNAVEFNPWRFSDMR---DQDD----FGHGHHACPGRFFAVSEMKTILAHIVATYDVK 145
Cdd:cd20670  328 FPLLGSVLKDPKYFRYPEAFYPQHFLDEQgrfKKNEafvpFSSGKRVCLGEAMARMELFLYFTSILQNFSLR 399
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 2-140 3.35e-03

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


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 38.86  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRvvrehgWTKAaldemhkVDSFLRevmrASGMTTGtMSRKAVKDYTFSDGTFIPAGTYLM 81
Cdd:cd11034  213 ALLWLAQHPEDRRRLIADPSL------IPNA-------VEEFLR----FYSPVAG-LARTVTQEVEVGGCRLKPGDRVLL 274

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 807744981  82 ApTGAIYTDDAVYPNAVEFNPWRFSdmRDQDDFGHGHHACPGRFFAVSEMKTILAHIVA 140
Cdd:cd11034  275 A-FASANRDEEKFEDPDRIDIDRTP--NRHLAFGSGVHRCLGSHLARVEARVALTEVLK 330
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 43-159 3.68e-03

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 38.73  E-value: 3.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  43 FLREVMRASGMTTGTMsRKAVKDYTFsDGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRfsDMRDQDDFGHGHHACP 122
Cdd:cd11032  245 AIEEVLRYRPPVQRTA-RVTTEDVEL-GGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR--NPNPHLSFGHGIHFCL 320

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 807744981 123 GRFFAVSEMKTILAHIVATYDVKMEQEGV----IPTPIMIG 159
Cdd:cd11032  321 GAPLARLEARIALEALLDRFPRIRVDPDVplelIDSPVVFG 361
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 38-136 3.96e-03

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 38.66  E-value: 3.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981  38 HKVDSFLREVMRASGMTTGTMSRKAVKDYTFsDGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRfsDMRDQDDFGHG 117
Cdd:cd11030  250 SLVPGAVEELLRYLSIVQDGLPRVATEDVEI-GGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR--PARRHLAFGHG 326

                         90
                 ....*....|....*....
gi 807744981 118 HHACPGRFFAVSEMKTILA 136
Cdd:cd11030  327 VHQCLGQNLARLELEIALP 345
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 2-143 7.27e-03

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: 37.83  E-value: 7.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   2 ALFYLAAYPQYMGHLRDEVDRVVREHGWtkaaldemHKVDSFLREVMRASGmTTGTMSRKAVKDyTFSDGTFIPAGTYLM 81
Cdd:cd20624  214 ALALLAAHPEQAARAREEAAVPPGPLAR--------PYLRACVLDAVRLWP-TTPAVLRESTED-TVWGGRTVPAGTGFL 283

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 807744981  82 APTGAIYTDDAVYPNAVEFNPWRFSDMRDQDD-----FGHGHHACPGRFFAVSEMKTILAHIVATYD 143
Cdd:cd20624  284 IFAPFFHRDDEALPFADRFVPEIWLDGRAQPDeglvpFSAGPARCPGENLVLLVASTALAALLRRAE 350
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 5-130 8.27e-03

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: 37.81  E-value: 8.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 807744981   5 YLAAYPQYMGHLRDEVdRVVREHGWTKAALDEMHKVDSFLREVMRASGMTTGTMsRKAVKDYTFsDGTFIPAGTYLMAPT 84
Cdd:cd20614  234 MLAEHPAVWDALCDEA-AAAGDVPRTPAELRRFPLAEALFRETLRLHPPVPFVF-RRVLEEIEL-GGRRIPAGTHLGIPL 310

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 807744981  85 GAIYTDDAVYPNAVEFNPWRFSDMR------DQDDFGHGHHACPGRFFAVSE 130
Cdd:cd20614  311 LLFSRDPELYPDPDRFRPERWLGRDrapnpvELLQFGGGPHFCLGYHVACVE 362
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 56-127 9.64e-03

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 37.48  E-value: 9.64e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 807744981  56 GTMSRKAVKDYTFSdGTFIPAGTYLMAPTGAIYTDDAVYPNAVEFNPWRfsDMRDQDDFGHGHHACPGRFFA 127
Cdd:cd11039  261 GMSPRRVAEDFEIR-GVTLPAGDRVFLMFGSANRDEARFENPDRFDVFR--PKSPHVSFGAGPHFCAGAWAS 329
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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