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Conserved domains on  [gi|2112896241|ref|XP_044103001|]
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cytochrome P450 11B1, mitochondrial-like isoform X1 [Neogale vison]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 72-488 0e+00

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.


The actual alignment was detected with superfamily member cd20644:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 428  Bit Score: 654.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  72 FQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSP 151
Cdd:cd20644     1 FQELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 152 QAVQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAML 231
Cdd:cd20644    81 AAVQRFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 232 KSTAQLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALGRPQHYSGIVGELLMHADMTLEAVRANSIEL 311
Cdd:cd20644   161 KTTVPLLFMPRSLSRWISPKLWKEHFEAWDCIFQYADNCIQKIYQELAFGRPQHYTGIVAELLLQAELSLEAIKANITEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 312 TAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDVV 391
Cdd:cd20644   241 TAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCLGRRLAETEMLLLLHHVLNHF 471
Cdd:cd20644   321 LQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNF 400

                         410
                  ....*....|....*..
gi 2112896241 472 LVETLTQEDIKMTYQFI 488
Cdd:cd20644   401 LVETLSQEDIKTVYSFI 417
 
Name Accession Description Interval E-value
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 72-488 0e+00

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: 654.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  72 FQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSP 151
Cdd:cd20644     1 FQELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 152 QAVQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAML 231
Cdd:cd20644    81 AAVQRFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 232 KSTAQLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALGRPQHYSGIVGELLMHADMTLEAVRANSIEL 311
Cdd:cd20644   161 KTTVPLLFMPRSLSRWISPKLWKEHFEAWDCIFQYADNCIQKIYQELAFGRPQHYTGIVAELLLQAELSLEAIKANITEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 312 TAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDVV 391
Cdd:cd20644   241 TAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCLGRRLAETEMLLLLHHVLNHF 471
Cdd:cd20644   321 LQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNF 400

                         410
                  ....*....|....*..
gi 2112896241 472 LVETLTQEDIKMTYQFI 488
Cdd:cd20644   401 LVETLSQEDIKTVYSFI 417
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 42-460 1.74e-116

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: 350.81  E-value: 1.74e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  42 PRCPGNKWLRLLQIWKEQGsENLHLEMHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQ 121
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRK-GNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 122 HRGHKCGVFLLNGPEWRVNRLKLNPDVLSPQAvQKYIPMVDGVARDFSKALKARVLQNARgsltLDIQPSILNYTVEASN 201
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGK-LSFEPRVEEEARDLVEKLRKTAGEPGV----IDITDLLFRAALNVIC 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 202 LALFGERLGLLGPSPSPASLQFIRALEAMLKSTAQLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALG 281
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 282 RPQHYSGIVGELLM-----HADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQ 356
Cdd:pfam00067 235 KKSPRDFLDALLLAkeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 357 RATTELPLLRAALKETLRLYP-VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSR-SS 434
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPvVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENgKF 394

                         410       420
                  ....*....|....*....|....*.
gi 2112896241 435 GTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEM 420
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 66-460 1.98e-39

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: 147.35  E-value: 1.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  66 LEMHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRA----ESPQPWRPLLDPWLAYRQhrghkcGVFLLNGPEWRVNR 141
Cdd:COG2124    22 YPFYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDprtfSSDGGLPEVLRPLPLLGD------SLLTLDGPEHTRLR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 142 LKLNPdVLSPQAVQKYIPMVDGVARdfskalkaRVLQNARGSLTLDIQPSILNYTVEASNLALFGerlgllgpSPSPASL 221
Cdd:COG2124    96 RLVQP-AFTPRRVAALRPRIREIAD--------ELLDRLAARGPVDLVEEFARPLPVIVICELLG--------VPEEDRD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 222 QFIRALEAMLKSTAQLmfmprdlsrwtSARVWKEHFESWDYIFQYannaiqkIYQELALGRPQHYSGIVGELLMHAD--- 298
Cdd:COG2124   159 RLRRWSDALLDALGPL-----------PPERRRRARRARAELDAY-------LRELIAERRAEPGDDLLSALLAARDdge 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 -MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvaeagitenpqratteLPLLRAALKETLRLYP 377
Cdd:COG2124   221 rLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYP 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 378 VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAE 457
Cdd:COG2124   283 PVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR--------PPNAHLPFGGGPHRCLGAALAR 354


                  ...
gi 2112896241 458 TEM 460
Cdd:COG2124   355 LEA 357
PLN02655 PLN02655
ent-kaurene oxidase
 315-452 1.60e-19

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 90.96  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 315 SVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENpqrATTELPLLRAALKETLRLY-PVGISLDRQVGSDVV 391
Cdd:PLN02655  274 AADTTLVTTEWAMYELAKNPDKQERLYREirEVCGDERVTEE---DLPNLPYLNAVFHETLRKYsPVPLLPPRFVHEDTT 350

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSR-SSGTRSPSLAFGFGLRQCLG 452
Cdd:PLN02655  351 LGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKyESADMYKTMAFGAGKRVCAG 412
 
Name Accession Description Interval E-value
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 72-488 0e+00

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: 654.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  72 FQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSP 151
Cdd:cd20644     1 FQELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 152 QAVQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAML 231
Cdd:cd20644    81 AAVQRFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVML 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 232 KSTAQLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALGRPQHYSGIVGELLMHADMTLEAVRANSIEL 311
Cdd:cd20644   161 KTTVPLLFMPRSLSRWISPKLWKEHFEAWDCIFQYADNCIQKIYQELAFGRPQHYTGIVAELLLQAELSLEAIKANITEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 312 TAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDVV 391
Cdd:cd20644   241 TAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDLV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCLGRRLAETEMLLLLHHVLNHF 471
Cdd:cd20644   321 LQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNF 400

                         410
                  ....*....|....*..
gi 2112896241 472 LVETLTQEDIKMTYQFI 488
Cdd:cd20644   401 LVETLSQEDIKTVYSFI 417
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 72-488 4.50e-142

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: 414.88  E-value: 4.50e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  72 FQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSP 151
Cdd:cd20643     1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 152 QAVQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAML 231
Cdd:cd20643    81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 232 KSTAQLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALGRPQH--YSGIVGELLMHADMTLEAVRANSI 309
Cdd:cd20643   161 HTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKGKNEheYPGILANLLLQDKLPIEDIKASVT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 310 ELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSD 389
Cdd:cd20643   241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITED 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 390 VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRspSLAFGFGLRQCLGRRLAETEMLLLLHHVLN 469
Cdd:cd20643   321 LVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFR--NLGFGFGPRQCLGRRIAETEMQLFLIHMLE 398

                         410
                  ....*....|....*....
gi 2112896241 470 HFLVETLTQEDIKMTYQFI 488
Cdd:cd20643   399 NFKIETQRLVEVKTTFDLI 417
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 72-488 3.83e-130

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: 384.57  E-value: 3.83e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  72 FQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSP 151
Cdd:cd11054     1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 152 QAVQKYIPMVDGVARDFSKALKArvLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAML 231
Cdd:cd11054    81 KSVASYLPAINEVADDFVERIRR--LRDEDGEEVPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 232 KSTAQLMFMPRdLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELA--LGRPQHYSGIVGELLMHADMTLEAVRANSI 309
Cdd:cd11054   159 ESSAKLMFGPP-LWKYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKkkDEEDEEEDSLLEYLLSKPGLSKKEIVTMAL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 310 ELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAG-ITENpqrATTELPLLRAALKETLRLYPVGISLDRQV 386
Cdd:cd11054   238 DLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEirSVLPDGEpITAE---DLKKMPYLKACIKESLRLYPVAPGNGRIL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 387 GSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWL-DSRSSGTRSP--SLAFGFGLRQCLGRRLAETEMLLL 463
Cdd:cd11054   315 PKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLrDDSENKNIHPfaSLPFGFGPRMCIGRRFAELEMYLL 394

                         410       420
                  ....*....|....*....|....*
gi 2112896241 464 LHHVLNHFLVETlTQEDIKMTYQFI 488
Cdd:cd11054   395 LAKLLQNFKVEY-HHEELKVKTRLI 418
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 42-460 1.74e-116

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: 350.81  E-value: 1.74e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  42 PRCPGNKWLRLLQIWKEQGsENLHLEMHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQ 121
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRK-GNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 122 HRGHKCGVFLLNGPEWRVNRLKLNPDVLSPQAvQKYIPMVDGVARDFSKALKARVLQNARgsltLDIQPSILNYTVEASN 201
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGK-LSFEPRVEEEARDLVEKLRKTAGEPGV----IDITDLLFRAALNVIC 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 202 LALFGERLGLLGPSPSPASLQFIRALEAMLKSTAQLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALG 281
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 282 RPQHYSGIVGELLM-----HADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQ 356
Cdd:pfam00067 235 KKSPRDFLDALLLAkeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 357 RATTELPLLRAALKETLRLYP-VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSR-SS 434
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPvVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENgKF 394

                         410       420
                  ....*....|....*....|....*.
gi 2112896241 435 GTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEM 420
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 73-460 6.78e-72

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


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 234.65  E-value: 6.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  73 QELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSPQ 152
Cdd:cd20648     3 AKYGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSSWKDYRQLRGHAYGLLTAEGEEWQRLRSLLAKHMLKPK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 153 AVQKYIPMVDGVARDFSKALKARVLQNARGsLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAMLK 232
Cdd:cd20648    83 AVEAYAGVLNAVVTDLIRRLRRQRSRSSPG-VVKDIAGEFYKFGLEGISSVLFESRIGCLEANVPEETETFIQSINTMFV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 233 STAQLMFMPRDLSRWTSARvWKEHFESWDYIFQYANNAIQKIYQELA--LGRPQHYSG-IVGELLMHADMTLEAVRANSI 309
Cdd:cd20648   162 MTLLTMAMPKWLHRLFPKP-WQRFCRSWDQMFAFAKGHIDRRMAEVAakLPRGEAIEGkYLTYFLAREKLPMKSIYGNVT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 310 ELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPVgISLDRQVGSD 389
Cdd:cd20648   241 ELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPV-IPGNARVIPD 319

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112896241 390 VVLQ--NYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20648   320 RDIQvgEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTHHPYASLPFGFGKRSCIGRRIAELEV 392
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 76-460 5.51e-68

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: 224.54  E-value: 5.51e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSPQAVQ 155
Cdd:cd20646     5 GPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKPKEVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 156 KYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAMLKSTA 235
Cdd:cd20646    85 LYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMFKLSE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 236 QLMFMPrdlsRWTSARV--WKEHFESWDYIFQYANNAIQK----IYQELALGRPQhysgiVGE----LLMHADMTLEAVR 305
Cdd:cd20646   165 IVTLLP----KWTRPYLpfWKRYVDAWDTIFSFGKKLIDKkmeeIEERVDRGEPV-----EGEyltyLLSSGKLSPKEVY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 306 ANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQ 385
Cdd:cd20646   236 GSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARV 315

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 386 VG-SDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLdsRSSGTR-SP--SLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20646   316 IVeKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWL--RDGGLKhHPfgSIPFGYGVRACVGRRIAELEM 392
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 69-460 7.35e-62

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: 208.12  E-value: 7.35e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  69 HRTFqelGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDV 148
Cdd:cd20645     1 HKKF---GKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 149 LSPQAVQKYIPMVDGVARDFSKalKARVLQNARGSLTlDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALE 228
Cdd:cd20645    78 MKPKEVMKLDGKINEVLADFMG--RIDELCDETGRVE-DLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 229 AMLKSTAQLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALGRPQHYsgiVGELLMHADMTLEAVRANS 308
Cdd:cd20645   155 TMMSTFGKMMVTPVELHKRLNTKVWQDHTEAWDNIFKTAKHCIDKRLQRYSQGPANDF---LCDIYHDNELSKKELYAAI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 309 IELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvAEAGITENpQRATTE----LPLLRAALKETLRLYPVGISLDR 384
Cdd:cd20645   232 TELQIGGVETTANSLLWILYNLSRNPQAQQKLLQE---IQSVLPAN-QTPRAEdlknMPYLKACLKESMRLTPSVPFTSR 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112896241 385 QVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20645   308 TLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHSINPFAHVPFGIGKRMCIGRRLAELQL 383
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 73-460 3.07e-58

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: 198.99  E-value: 3.07e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  73 QELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPDVLSPQ 152
Cdd:cd20647     2 REYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWQEYRDLRGRSTGLISAEGEQWLKMRSVLRQKILRPR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 153 AVQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAMLK 232
Cdd:cd20647    82 DVAVYSGGVNEVVADLIKRIKTLRSQEDDGETVTNVNDLFFKYSMEGVATILYECRLGCLENEIPKQTVEYIEALELMFS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 233 STAQLMF---MPRDLsRWTSARVWKEHFESWDYIFQYA----NNAIQKIYQELALGRpQHYSGIVGELLMHADMTLEAVR 305
Cdd:cd20647   162 MFKTTMYagaIPKWL-RPFIPKPWEEFCRSWDGLFKFSqihvDNRLREIQKQMDRGE-EVKGGLLTYLLVSKELTLEEIY 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 306 ANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRATT-ELPLLRAALKETLRLYPVGISLDR 384
Cdd:cd20647   240 ANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEE-IVRNLGKRVVPTAEDVpKLPLIRALLKETLRLFPVLPGNGR 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112896241 385 QVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWL--DSRSSGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20647   319 VTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLrkDALDRVDNFGSIPFGYGIRSCIGRRIAELEI 396
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 76-460 4.15e-58

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: 197.35  E-value: 4.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESLQRAESpqpWRPLLDPWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNPdVLSPQAVQ 155
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPR---DFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAP-AFTPRALA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 156 KYIPMVDGVARDFSKALKARvlqnarGSLTLDIQPSILNYTVEASNLALFGerlgllgPSPSPASLQFIRALEAMLKSTA 235
Cdd:cd00302    77 ALRPVIREIARELLDRLAAG------GEVGDDVADLAQPLALDVIARLLGG-------PDLGEDLEELAELLEALLKLLG 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 236 QLMFMPRDLSRWTSARvwkehfESWDYIFQYANNAIQKIyqeLALGRPQHYSGIVGELLMHADMTLEAVRANSIELTAGS 315
Cdd:cd00302   144 PRLLRPLPSPRLRRLR------RARARLRDYLEELIARR---RAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAG 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 316 VDTTAYPLLMTLFELARNPDVQQALRQEslvAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNY 395
Cdd:cd00302   215 HETTASLLAWALYLLARHPEVQERLRAE---IDAVLGDGTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGY 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112896241 396 HIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd00302   292 TIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREE-PRYAHLPFGAGPHRCLGARLARLEL 355
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 128-460 4.33e-40

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: 149.68  E-value: 4.33e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 128 GVFLLNGPEWRVNRLKLNPdVLSPQAVQKYIPMVDGVARDFSKALKARVlqnarGSLTLDIQPSILNYTVEASNLALFGE 207
Cdd:cd11057    46 GLFSAPYPIWKLQRKALNP-SFNPKILLSFLPIFNEEAQKLVQRLDTYV-----GGGEFDILPDLSRCTLEMICQTTLGS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 208 RLGllgpSPSPASLQFIRALEAMLKSTAQLMFMP----RDLSRWTSArvWKEHFESWDYIFQYANNAIQKIYQELALGRP 283
Cdd:cd11057   120 DVN----DESDGNEEYLESYERLFELIAKRVLNPwlhpEFIYRLTGD--YKEEQKARKILRAFSEKIIEKKLQEVELESN 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 284 QHYSG---------IVGELLMHA-----DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVA 347
Cdd:cd11057   194 LDSEEdeengrkpqIFIDQLLELarngeEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEimEVFP 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 348 EAGItENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDVVLQN-YHIPAGTVVKVLLYSLGRNPSVF-PRPERYHP 425
Cdd:cd11057   274 DDGQ-FITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNgVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDP 352

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2112896241 426 RRWLDSRSSGtRSPS--LAFGFGLRQCLGRRLAETEM 460
Cdd:cd11057   353 DNFLPERSAQ-RHPYafIPFSAGPRNCIGWRYAMISM 388
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 66-460 1.98e-39

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: 147.35  E-value: 1.98e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  66 LEMHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRA----ESPQPWRPLLDPWLAYRQhrghkcGVFLLNGPEWRVNR 141
Cdd:COG2124    22 YPFYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDprtfSSDGGLPEVLRPLPLLGD------SLLTLDGPEHTRLR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 142 LKLNPdVLSPQAVQKYIPMVDGVARdfskalkaRVLQNARGSLTLDIQPSILNYTVEASNLALFGerlgllgpSPSPASL 221
Cdd:COG2124    96 RLVQP-AFTPRRVAALRPRIREIAD--------ELLDRLAARGPVDLVEEFARPLPVIVICELLG--------VPEEDRD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 222 QFIRALEAMLKSTAQLmfmprdlsrwtSARVWKEHFESWDYIFQYannaiqkIYQELALGRPQHYSGIVGELLMHAD--- 298
Cdd:COG2124   159 RLRRWSDALLDALGPL-----------PPERRRRARRARAELDAY-------LRELIAERRAEPGDDLLSALLAARDdge 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 -MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvaeagitenpqratteLPLLRAALKETLRLYP 377
Cdd:COG2124   221 rLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYP 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 378 VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAE 457
Cdd:COG2124   283 PVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR--------PPNAHLPFGGGPHRCLGAALAR 354


                  ...
gi 2112896241 458 TEM 460
Cdd:COG2124   355 LEA 357
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 147-460 3.90e-39

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: 147.06  E-value: 3.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 147 DVLSPQAVQKYI--PMVdgvaRDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLG--LLGPSPSPASLQ 222
Cdd:cd11059    64 GVYSKSSLLRAAmePII----RERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGtlLLGDKDSREREL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 223 FIRALEAMLKStaqLMFMPRDLSRWTSARVWKEHFESWDYIFQYA----NNAIQKIYQELALGRPQHYSGIVGELLMHAD 298
Cdd:cd11059   140 LRRLLASLAPW---LRWLPRYLPLATSRLIIGIYFRAFDEIEEWAldlcARAESSLAESSDSESLTVLLLEKLKGLKKQG 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIE-LTAGSvDTTAYPLLMTLFELARNPDVQQALRQEslVAEAGITENPQRATTE---LPLLRAALKETLR 374
Cdd:cd11059   217 LDDLEIASEALDhIVAGH-DTTAVTLTYLIWELSRPPNLQEKLREE--LAGLPGPFRGPPDLEDldkLPYLNAVIRETLR 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 375 LY-PVGISLDRQVGSD-VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS---LAFGFGLRQ 449
Cdd:cd11059   294 LYpPIPGSLPRVVPEGgATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMKrafWPFGSGSRM 373

                         330
                  ....*....|.
gi 2112896241 450 CLGRRLAETEM 460
Cdd:cd11059   374 CIGMNLALMEM 384
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 144-460 1.67e-38

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: 145.47  E-value: 1.67e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 144 LNPdVLSPQAVQKYIPMVDGVARDFSKALKARV-------LQNARGSLTLDIqpsILNYtveasnlaLFGERLGLLGPSP 216
Cdd:cd11062    62 LSP-FFSKRSILRLEPLIQEKVDKLVSRLREAKgtgepvnLDDAFRALTADV---ITEY--------AFGRSYGYLDEPD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 217 SPAslQFIRALEAMLKSTAQLMFMP------RDLSRWTSARVWKeHFESWDYIFQYANNAIQKIYQELALGRPQ-----H 285
Cdd:cd11062   130 FGP--EFLDALRALAEMIHLLRHFPwllkllRSLPESLLKRLNP-GLAVFLDFQESIAKQVDEVLRQVSAGDPPsivtsL 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 286 YSGIVGELLMHADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTE-LPL 364
Cdd:cd11062   207 FHALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSPPSLAELEkLPY 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 365 LRAALKETLRL-YPVGISLDRQVG-SDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSL- 441
Cdd:cd11062   287 LTAVIKEGLRLsYGVPTRLPRVVPdEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGKLDRYLv 366

                         330
                  ....*....|....*....
gi 2112896241 442 AFGFGLRQCLGRRLAETEM 460
Cdd:cd11062   367 PFSKGSRSCLGINLAYAEL 385
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 149-460 1.16e-37

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: 143.13  E-value: 1.16e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 149 LSPQAVQKYIPMVDGVARDFSKALKARvlQNARGSLTLDIQPSILNYTVEA-SNLAlFGERLGLLGpspSPASLQFIRAL 227
Cdd:cd11061    65 FSDKALRGYEPRILSHVEQLCEQLDDR--AGKPVSWPVDMSDWFNYLSFDVmGDLA-FGKSFGMLE---SGKDRYILDLL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 228 EAMLKSTAQLMFMP----RDLSRWTSARVWKEHFESWDYIFQyannAIQKIYQELALGRPQ--HYsgivgelLMHAD--- 298
Cdd:cd11061   139 EKSMVRLGVLGHAPwlrpLLLDLPLFPGATKARKRFLDFVRA----QLKERLKAEEEKRPDifSY-------LLEAKdpe 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 ----MTLEAVRANSIELT-AGSvDTTAYPLLMTLFELARNPDVQQALRQE--SLVA-EAGITENPQRATteLPLLRAALK 370
Cdd:cd11061   208 tgegLDLEELVGEARLLIvAGS-DTTATALSAIFYYLARNPEAYEKLRAEldSTFPsDDEIRLGPKLKS--LPYLRACID 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 371 ETLRLYP-VGISLDRQVGSD-VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGT--RSPSLAFGFG 446
Cdd:cd11061   285 EALRLSPpVPSGLPRETPPGgLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVraRSAFIPFSIG 364

                         330
                  ....*....|....
gi 2112896241 447 LRQCLGRRLAETEM 460
Cdd:cd11061   365 PRGCIGKNLAYMEL 378
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 76-460 7.69e-37

Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; Fusarium verticillioides cytochrome P450 monooxygenase FUM15, is also called fumonisin biosynthesis cluster protein 15. The FUM15 gene is part of the gene cluster that mediates the biosynthesis of fumonisins B1, B2, B3, and B4, which are carcinogenic mycotoxins. This FUM15-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410692 [Multi-domain]  Cd Length: 437  Bit Score: 141.25  E-value: 7.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRY-DVGGTHMVYVMLPEDV-ESLQRAESPQPWRPLLDPWLayRQHRGHkcGVFLLNGPEWRVNRLKLNPdVLSPQA 153
Cdd:cd11069     2 GGLIRYrGLFGSERLLVTDPKALkHILVTNSYDFEKPPAFRRLL--RRILGD--GLLAAEGEEHKRQRKILNP-AFSYRH 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 154 VQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPASLQFIRALEAMLKS 233
Cdd:cd11069    77 VKELYPIFWSKAEELVDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYRRLFEPTLLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 234 TAQLMFMPRDLSRWTSARVWKeHFESWDYIFQYANNAIQKIYQEL--ALGRPQHYSG--IVGeLLMHADMTLEAVRANSI 309
Cdd:cd11069   157 SLLFILLLFLPRWLVRILPWK-ANREIRRAKDVLRRLAREIIREKkaALLEGKDDSGkdILS-ILLRANDFADDERLSDE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 310 EL--------TAGSvDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATT--ELPLLRAALKETLRLYP-V 378
Cdd:cd11069   235 ELidqiltflAAGH-ETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDldRLPYLNAVCRETLRLYPpV 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 379 GISLdRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLD----SRSSGTRSPS--LAFGFGLRQCL 451
Cdd:cd11069   314 PLTS-REATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEpdgaASPGGAGSNYalLTFLHGPRSCI 392


                  ....*....
gi 2112896241 452 GRRLAETEM 460
Cdd:cd11069   393 GKKFALAEM 401
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 76-460 1.22e-36

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: 140.35  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESLQRaeSPQ-----PWRPLLDPWLayrqhrGHkcGVFLLNGPEWRVNRLKLNPdVLS 150
Cdd:cd20628     1 GGVFRLWIGPKPYVVVTNPEDIEVILS--SSKlitksFLYDFLKPWL------GD--GLLTSTGEKWRKRRKLLTP-AFH 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 151 PQAVQKYIPMVDGVARDFSKALKARVlqnarGSLTLDIQPSILNYTVEASNLALFGERLGLLgpspSPASLQFIRALEAM 230
Cdd:cd20628    70 FKILESFVEVFNENSKILVEKLKKKA-----GGGEFDIFPYISLCTLDIICETAMGVKLNAQ----SNEDSEYVKAVKRI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 231 LKSTAQLMFMP--RD--LSRWTSARvwKEHFESWDYIFQYANNAIQKIYQEL-ALGRPQHYSGIVGE----------LLM 295
Cdd:cd20628   141 LEIILKRIFSPwlRFdfIFRLTSLG--KEQRKALKVLHDFTNKVIKERREELkAEKRNSEEDDEFGKkkrkafldllLEA 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 296 HAD---MTLEAVR--ANSIeLTAGSvDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGitENPQRATTE----LPLLR 366
Cdd:cd20628   219 HEDggpLTDEDIReeVDTF-MFAGH-DTTASAISFTLYLLGLHPEVQEKVYEE-LDEIFG--DDDRRPTLEdlnkMKYLE 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 367 AALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGtRSPS--LAFG 444
Cdd:cd20628   294 RVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAK-RHPYayIPFS 372

                         410
                  ....*....|....*.
gi 2112896241 445 FGLRQCLGRRLAETEM 460
Cdd:cd20628   373 AGPRNCIGQKFAMLEM 388
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 128-460 6.87e-35

cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome P450 families 1 (CYP1) and 2 (CYP2), CYP17A1, and CYP21 in vertebrates, as well as insect and crustacean CYPs similar to CYP15A1 and CYP306A1. CYP1 and CYP2 enzymes are involved in the metabolism of endogenous and exogenous compounds such as hormones, xenobiotics, and drugs. CYP17A1 catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products, while CYP21 catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. Members of this group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 135.42  E-value: 6.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 128 GVFLLNGPEWRVNRlKLNPDVLSPQAVQKYI-PMVDGVARDFSKALKArvlqNARGSLTLDIQPSILNYTVEASNLALFG 206
Cdd:cd20617    50 GILFSNGDYWKELR-RFALSSLTKTKLKKKMeELIEEEVNKLIESLKK----HSKSGEPFDPRPYFKKFVLNIINQFLFG 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 207 ERLGLLGpspSPASLQFIRALEAMLKSTAQLMF-----MPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALG 281
Cdd:cd20617   125 KRFPDED---DGEFLKLVKPIEEIFKELGSGNPsdfipILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRD 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 282 RPQHYSGIVGELLMHADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLvaeaGITENPQRATTE 361
Cdd:cd20617   202 LIDDELLLLLKEGDSGLFDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEID----NVVGNDRRVTLS 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 362 ----LPLLRAALKETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGT 436
Cdd:cd20617   278 drskLPYLNAVIKEVLRLRPILpLGLPRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKL 357

                         330       340
                  ....*....|....*....|....
gi 2112896241 437 RSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20617   358 SEQFIPFGIGKRNCVGENLARDEL 381
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 126-460 9.90e-34

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: 131.94  E-value: 9.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 126 KCGVFLLNGPEWRVNRLKLNPdVLSPQAVQKYIPMVDGVARDFSKALKarvlQNARGSLTLDIQPSILNYTVEASNLALF 205
Cdd:cd11055    49 DSSLLFLKGERWKRLRTTLSP-TFSSGKLKLMVPIINDCCDELVEKLE----KAAETGKPVDMKDLFQGFTLDVILSTAF 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 206 GERLGLLGPSPSPaslqFIRALEAMLKS--TAQLMFMPRDLSRWTSAR--VWKEHFESWDYIFQYANNAIQKIYQELALG 281
Cdd:cd11055   124 GIDVDSQNNPDDP----FLKAAKKIFRNsiIRLFLLLLLFPLRLFLFLlfPFVFGFKSFSFLEDVVKKIIEQRRKNKSSR 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 282 RP---QHY--SGIVGELLMHADMTLEAVRANS-IELTAGsVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENP 355
Cdd:cd11055   200 RKdllQLMldAQDSDEDVSKKKLTDDEIVAQSfIFLLAG-YETTSNTLSFASYLLATNPDVQEKLIEE-IDEVLPDDGSP 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 356 QRATT-ELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSS 434
Cdd:cd11055   278 TYDTVsKLKYLDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKA 357

                         330       340
                  ....*....|....*....|....*...
gi 2112896241 435 gTRSPS--LAFGFGLRQCLGRRLAETEM 460
Cdd:cd11055   358 -KRHPYayLPFGAGPRNCIGMRFALLEV 384
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 205-460 2.34e-33

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: 130.78  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 205 FGERLGLLGPS-PSP---ASLQFIR--ALEAMLKSTAQLMFMPRDLSRWTSARVWKEHFEswdyifqyanNAIQKIYQEL 278
Cdd:cd11058   121 FGESFGCLENGeYHPwvaLIFDSIKalTIIQALRRYPWLLRLLRLLIPKSLRKKRKEHFQ----------YTREKVDRRL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 279 ALG--RPQHYSGIVGELLMHADMTLEAVRAN-SIELTAGSvDTTAYPLLMTLFELARNPDVQQALRQE---SLVAEAGIT 352
Cdd:cd11058   191 AKGtdRPDFMSYILRNKDEKKGLTREELEANaSLLIIAGS-ETTATALSGLTYYLLKNPEVLRKLVDEirsAFSSEDDIT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 353 enpQRATTELPLLRAALKETLRLYP-VGISLDRQVGSD-VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLD 430
Cdd:cd11058   270 ---LDSLAQLPYLNAVIQEALRLYPpVPAGLPRVVPAGgATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLG 346

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2112896241 431 SRSSGTRSPSLA----FGFGLRQCLGRRLAETEM 460
Cdd:cd11058   347 DPRFEFDNDKKEafqpFSVGPRNCIGKNLAYAEM 380
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 154-460 2.90e-33

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: 130.78  E-value: 2.90e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 154 VQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQpsilNYTVEA-SNLAlFGERLGLL-------GpspspaslqFIR 225
Cdd:cd11060    73 LLSLEPFVDECIDLLVDLLDEKAVSGKEVDLGKWLQ----YFAFDViGEIT-FGKPFGFLeagtdvdG---------YIA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 226 ALEAMLKSTAQLMFMP--RDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALGRPQHySGIVGELLMH-----AD 298
Cdd:cd11060   139 SIDKLLPYFAVVGQIPwlDRLLLKNPLGPKRKDKTGFGPLMRFALEAVAERLAEDAESAKGR-KDMLDSFLEAglkdpEK 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIE-LTAGSvDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENPQRA-TTELPLLRAALKETLR 374
Cdd:cd11060   218 VTDREVVAEALSnILAGS-DTTAIALRAILYYLLKNPRVYAKLRAEidAAVAEGKLSSPITFAeAQKLPYLQAVIKEALR 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 375 LYP-VGISLDRQVG-SDVVLQNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDS---RSSGTRSPSLAFGFGLR 448
Cdd:cd11060   297 LHPpVGLPLERVVPpGGATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEAdeeQRRMMDRADLTFGAGSR 376

                         330
                  ....*....|..
gi 2112896241 449 QCLGRRLAETEM 460
Cdd:cd11060   377 TCLGKNIALLEL 388
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 76-460 2.07e-32

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: 128.21  E-value: 2.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESLQRaESPQPWRPLLDPWLAYRQHRGHkcGVFLLNGPEWRVNRlKLNPDVLSPQAVQ 155
Cdd:cd11083     1 GSAYRFRLGRQPVLVISDPELIREVLR-RRPDEFRRISSLESVFREMGIN--GVFSAEGDAWRRQR-RLVMPAFSPKHLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 156 KYIPMVDGVARDFSKALKARVLQNArgslTLDIQPSILNYTVEASNLALFGERLGLLGPSPSPaslqFIRALEAMLKSTA 235
Cdd:cd11083    77 YFFPTLRQITERLRERWERAAAEGE----AVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDP----LQEHLERVFPMLN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 236 QLMFMPRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQELALGRPQHYSGIVGELLMHA------DMTLEAVRANSI 309
Cdd:cd11083   149 RRVNAPFPYWRYLRLPADRALDRALVEVRALVLDIIAAARARLAANPALAEAPETLLAMMLAeddpdaRLTDDEIYANVL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 310 ELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRATT--ELPLLRAALKETLRLYPVGISLDRQVG 387
Cdd:cd11083   229 TLLLAGEDTTANTLAWMLYYLASRPDVQARVREE-VDAVLGGARVPPLLEAldRLPYLEAVARETLRLKPVAPLLFLEPN 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112896241 388 SDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSG---TRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11083   308 EDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAephDPSSLLPFGAGPRLCPGRSLALMEM 383
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 68-460 1.52e-31

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: 125.77  E-value: 1.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  68 MHRTFQELGPIFRYDVGGT-HMVYVMLPEDVES--------LQRAESPQPWRPLLDPWlayrqhrghkcGVFLLNGPEWR 138
Cdd:cd11053     4 LERLRARYGDVFTLRVPGLgPVVVLSDPEAIKQiftadpdvLHPGEGNSLLEPLLGPN-----------SLLLLDGDRHR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 139 VNRlKLnpdvLSP----QAVQKYIPMVDGVARdfskalkaRVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGllgp 214
Cdd:cd11053    73 RRR-KL----LMPafhgERLRAYGELIAEITE--------REIDRWPPGQPFDLRELMQEITLEVILRVVFGVDDG---- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 215 spsPASLQFIRALEAMLKSTAQLMFMP----RDLSRWTsarVWKEhfeswdyiFQYANNAIQK-IYQELALGRPQHYSG- 288
Cdd:cd11053   136 ---ERLQELRRLLPRLLDLLSSPLASFpalqRDLGPWS---PWGR--------FLRARRRIDAlIYAEIAERRAEPDAEr 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 289 --IVGeLLMHA------DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvAEAGITENPQRATT 360
Cdd:cd11053   202 ddILS-LLLSArdedgqPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAE---LDALGGDPDPEDIA 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 361 ELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRssgtRSPS 440
Cdd:cd11053   278 KLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRK----PSPY 353

                         410       420
                  ....*....|....*....|..
gi 2112896241 441 --LAFGFGLRQCLGRRLAETEM 460
Cdd:cd11053   354 eyLPFGGGVRRCIGAAFALLEM 375
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 76-460 3.36e-31

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: 124.61  E-value: 3.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVE--------SLQRAESPQPWRPLLdpwlayrqhrGHkcGVFLLNGPEWRVNRLKLNPd 147
Cdd:cd20620     1 GDVVRLRLGPRRVYLVTHPDHIQhvlvtnarNYVKGGVYERLKLLL----------GN--GLLTSEGDLWRRQRRLAQP- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 148 VLSPQAVQKYIPMVDGVARDFSKALKARvlqnaRGSLTLDIQPSILNYTVEASNLALFGERLgllgpspSPASLQFIRAL 227
Cdd:cd20620    68 AFHRRRIAAYADAMVEATAALLDRWEAG-----ARRGPVDVHAEMMRLTLRIVAKTLFGTDV-------EGEADEIGDAL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 228 EAMLKSTAQLMFMPRDLSRW----TSARVWKEhfeswdyiFQYANNAIQKIYQElALGRPQHYSGIVGELLMHAD----- 298
Cdd:cd20620   136 DVALEYAARRMLSPFLLPLWlptpANRRFRRA--------RRRLDEVIYRLIAE-RRAAPADGGDLLSMLLAARDeetge 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 -MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRqeslvAEAGITENPQRATTE----LPLLRAALKETL 373
Cdd:cd20620   207 pMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLR-----AEVDRVLGGRPPTAEdlpqLPYTEMVLQESL 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 374 RLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSgtRSPSLA---FGFGLRQC 450
Cdd:cd20620   282 RLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREA--ARPRYAyfpFGGGPRIC 359

                         410
                  ....*....|
gi 2112896241 451 LGRRLAETEM 460
Cdd:cd20620   360 IGNHFAMMEA 369
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 130-460 6.23e-31

cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome P450s from insects and crustaceans, including the CYP6, CYP9 and CYP310 subfamilies, which are involved in the metabolism of insect hormones and xenobiotic detoxification. The CYP6-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 124.19  E-value: 6.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 130 FLLNGPEWRVNRLKLNPdVLSPQAVQKYIPMVDGVARDFSKALKARVLQNArgslTLDIQPSILNYTVE--ASnlALFGE 207
Cdd:cd11056    54 FSLDGEKWKELRQKLTP-AFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGK----ELEIKDLMARYTTDviAS--CAFGL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 208 RLGLLGPSPSPA--------SLQFIRALEAMLkstaqLMFMPRdLSRWTSARVWKEHFEswDYIFQYANNAIQK------ 273
Cdd:cd11056   127 DANSLNDPENEFremgrrlfEPSRLRGLKFML-----LFFFPK-LARLLRLKFFPKEVE--DFFRKLVRDTIEYreknni 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 274 -------IYQELALGRPQHYSGIVGELLMHaDMTLEAVransIELTAGSvDTTAYPLLMTLFELARNPDVQQALRQEslV 346
Cdd:cd11056   199 vrndfidLLLELKKKGKIEDDKSEKELTDE-ELAAQAF----VFFLAGF-ETSSSTLSFALYELAKNPEIQEKLREE--I 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 347 AEAGITENPQ---RATTELPLLRAALKETLRLYPVGISLDRQVGSDVVL--QNYHIPAGTVVKVLLYSLGRNPSVFPRPE 421
Cdd:cd11056   271 DEVLEKHGGEltyEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLpgTDVVIEKGTPVIIPVYALHHDPKYYPEPE 350

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2112896241 422 RYHPRRWLDSRSSGTRSPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd11056   351 KFDPERFSPENKKKRHPYTyLPFGDGPRNCIGMRFGLLQV 390
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 203-460 5.52e-28

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: 115.89  E-value: 5.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 203 ALFGERLGLLGPSPSPAsLQFIRALEAMLKSTAQLMFMPRDLSRWTSARVWKEHFESwdyIFQYANNAIQKIYQELALGR 282
Cdd:cd11070   121 VGFGFDLPALDEEESSL-HDTLNAIKLAIFPPLFLNFPFLDRLPWVLFPSRKRAFKD---VDEFLSELLDEVEAELSADS 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 283 P--QHYSGIVGELLMHAD----MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQ 356
Cdd:cd11070   197 KgkQGTESVVASRLKRARrsggLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREE-IDSVLGDEPDDW 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 357 RATT---ELPLLRAALKETLRLYPVGISLDRQVGSDVVL-----QNYHIPAGTVVKVLLYSLGRNPSV-FPRPERYHPRR 427
Cdd:cd11070   276 DYEEdfpKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPER 355

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2112896241 428 WLDS--------RSSGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11070   356 WGSTsgeigaatRFTPARGAFIPFSAGPRACLGRKFALVEF 396
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 72-460 1.46e-27

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: 114.30  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  72 FQELGPIFRYDVGGTHMVYVMLPEDVESL--QRAESPQPWRPLldpwlAYRQHRGHKCgVFLLNGPEWRVNRlKLNPDVL 149
Cdd:cd11044    18 YQKYGPVFKTHLLGRPTVFVIGAEAVRFIlsGEGKLVRYGWPR-----SVRRLLGENS-LSLQDGEEHRRRR-KLLAPAF 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 150 SPQAVQKYIPMVDGVARDFSKAL--KARVLQNAR-GSLTLDIqpsilnytveASNLalfgerlgLLGPSPSPASLQFIRA 226
Cdd:cd11044    91 SREALESYVPTIQAIVQSYLRKWlkAGEVALYPElRRLTFDV----------AARL--------LLGLDPEVEAEALSQD 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 227 LEAMLKStaqLMFMPRDL--SRWTSARVWKEHfeswdyIFQYANNAIQKIYQELALGrpqhYSGIVGELLMHAD-----M 299
Cdd:cd11044   153 FETWTDG---LFSLPVPLpfTPFGRAIRARNK------LLARLEQAIRERQEEENAE----AKDALGLLLEAKDedgepL 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 300 TLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRATTELPLLRAALKETLRLYPVG 379
Cdd:cd11044   220 SMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQE-QDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPV 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 380 ISLDRQVGSDVVLQNYHIPAGTVVkvlLYSLG---RNPSVFPRPERYHPRRWLDSRSSGTRSPS--LAFGFGLRQCLGRR 454
Cdd:cd11044   299 GGGFRKVLEDFELGGYQIPKGWLV---YYSIRdthRDPELYPDPERFDPERFSPARSEDKKKPFslIPFGGGPRECLGKE 375


                  ....*.
gi 2112896241 455 LAETEM 460
Cdd:cd11044   376 FAQLEM 381
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 76-460 1.87e-27

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: 114.21  E-value: 1.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESL--QRAE--SPQPWRPLLDPWLAYRQHRghkcgVFLLNGPEWRVNRlKLNPDVLSP 151
Cdd:cd11065     2 GPIISLKVGGQTIIVLNSPKAAKDLleKRSAiySSRPRMPMAGELMGWGMRL-----LLMPYGPRWRLHR-RLFHQLLNP 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 152 QAVQKYIPMVDgvarDFSKALKARVLQNARgsltlDIQPSILNYtveASNLAL---FGERLGLLGPSPSPASLQFIRALE 228
Cdd:cd11065    76 SAVRKYRPLQE----LESKQLLRDLLESPD-----DFLDHIRRY---AASIILrlaYGYRVPSYDDPLLRDAEEAMEGFS 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 229 AMLKSTAQLM-FMP--RDLSRWTSA---RVWKEHFESWDYIF-QYANNAIQKIYQELAlgrpqhYSGIVGELLMH----A 297
Cdd:cd11065   144 EAGSPGAYLVdFFPflRYLPSWLGApwkRKARELRELTRRLYeGPFEAAKERMASGTA------TPSFVKDLLEEldkeG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 298 DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVaeagiteNPQRATT-----ELPLLRAALK 370
Cdd:cd11065   218 GLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEEldRVV-------GPDRLPTfedrpNLPYVNAIVK 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 371 ETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLD---SRSSGTRSPSLAFGFG 446
Cdd:cd11065   291 EVLRWRPVApLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDdpkGTPDPPDPPHFAFGFG 370

                         410
                  ....*....|....
gi 2112896241 447 LRQCLGRRLAETEM 460
Cdd:cd11065   371 RRICPGRHLAENSL 384
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 128-460 2.28e-27

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: 113.81  E-value: 2.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 128 GVFLLNGPEWRVNRlklnpDVLSPQAVQKYIPMVDGVARDFSKALKarvLQNARGSlTLDIQPSILNYTVEASNLALFGE 207
Cdd:cd11063    51 GIFTSDGEEWKHSR-----ALLRPQFSRDQISDLELFERHVQNLIK---LLPRDGS-TVDLQDLFFRLTLDSATEFLFGE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 208 RLGLLGP-SPSPASLQFIRALEAMLKSTAQLMFMpRDLSRWTSARVWKE-----HfeswDYIFQYANNAIQKIYQELALG 281
Cdd:cd11063   122 SVDSLKPgGDSPPAARFAEAFDYAQKYLAKRLRL-GKLLWLLRDKKFREackvvH----RFVDPYVDKALARKEESKDEE 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 282 RPQHYSGIVGelLMHADMTLEAVRAN--SIeLTAGsVDTTAYPLLMTLFELARNPDVQQALRQESLvAEAGITENPQRAT 359
Cdd:cd11063   197 SSDRYVFLDE--LAKETRDPKELRDQllNI-LLAG-RDTTASLLSFLFYELARHPEVWAKLREEVL-SLFGPEPTPTYED 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 360 -TELPLLRAALKETLRLYPVGISLDRQVGSDVVL---------QNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRW 428
Cdd:cd11063   272 lKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLprgggpdgkSPIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERW 351

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2112896241 429 LDsrssGTRSP--SLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11063   352 ED----LKRPGweYLPFNGGPRICLGQQFALTEA 381
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 298-456 2.08e-26

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: 111.11  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 298 DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--------SLVAEAGItenPQratteLPLLRAAL 369
Cdd:cd20618   224 KLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEEldsvvgreRLVEESDL---PK-----LPYLQAVV 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 370 KETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS---LAFGF 445
Cdd:cd20618   296 KETLRLHPPGpLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDfelLPFGS 375

                         170
                  ....*....|.
gi 2112896241 446 GLRQCLGRRLA 456
Cdd:cd20618   376 GRRMCPGMPLG 386
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 293-460 7.27e-26

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: 109.27  E-value: 7.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 293 LLMHAD------MTLEAVRANSIE-LTAGSvDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRaTTELPLL 365
Cdd:cd11049   204 LLLAARdeegrpLSDEELRDQVITlLTAGT-ETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPATFED-LPRLTYT 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 366 RAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSG-TRSPSLAFG 444
Cdd:cd11049   282 RRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAvPRGAFIPFG 361

                         170
                  ....*....|....*.
gi 2112896241 445 FGLRQCLGRRLAETEM 460
Cdd:cd11049   362 AGARKCIGDTFALTEL 377
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 326-460 1.99e-25

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: 108.07  E-value: 1.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 326 TLFELARNPDVQQALRQESLVAEAGITENPQR-ATTELPLLRAALKETLRLYPVGISLDRQVGSDVVLQN--YHIPAGTV 402
Cdd:cd11042   235 TGLELLRNPEHLEALREEQKEVLGDGDDPLTYdVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEGggYVIPKGHI 314

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 403 VKVLLYSLGRNPSVFPRPERYHPRRWLDSR---SSGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11042   315 VLASPAVSHRDPEIFKNPDEFDPERFLKGRaedSKGGKFAYLPFGAGRHRCIGENFAYLQI 375
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 66-459 3.51e-25

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: 107.40  E-value: 3.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  66 LEMHRTFqelGPIFRYDVGGTHMVYVMLPEDVESL-----QRAESPQPWRPLLDPWlayrQHRGhkcgVFLLNGPEWRVN 140
Cdd:cd11045     4 RQRYRRY---GPVSWTGMLGLRVVALLGPDANQLVlrnrdKAFSSKQGWDPVIGPF----FHRG----LMLLDFDEHRAH 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 141 RLKLNPdVLSPQAVQKYipmVDGVARDFSKALKARVLQNArgsltLDIQPSILNYTVEASNLALFGERLGllgpspsPAS 220
Cdd:cd11045    73 RRIMQQ-AFTRSALAGY---LDRMTPGIERALARWPTGAG-----FQFYPAIKELTLDLATRVFLGVDLG-------PEA 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 221 LQFIRALEAMLKSTAQLMFMPRDLSRWTSA----RVWKEHFESwdyifqyannaiqKIYQELALGRPQHYSgivgeLLMH 296
Cdd:cd11045   137 DKVNKAFIDTVRASTAIIRTPIPGTRWWRGlrgrRYLEEYFRR-------------RIPERRAGGGDDLFS-----ALCR 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 297 AD------MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESL-VAEAGITENpqrATTELPLLRAAL 369
Cdd:cd11045   199 AEdedgdrFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLaLGKGTLDYE---DLGQLEVTDWVF 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 370 KETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS--LAFGFGL 447
Cdd:cd11045   276 KEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYawAPFGGGA 355

                         410
                  ....*....|..
gi 2112896241 448 RQCLGRRLAETE 459
Cdd:cd11045   356 HKCIGLHFAGME 367
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 63-460 8.47e-25

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: 106.45  E-value: 8.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  63 NLHLEMHrtfQELGPIFRYDVGGTHMVYVMLPEDV-ESLQRAESPQPWRPlldpwlaYRQhRGHKCGV-FLLNG------ 134
Cdd:cd20613     2 DLLLEWA---KEYGPVFVFWILHRPIVVVSDPEAVkEVLITLNLPKPPRV-------YSR-LAFLFGErFLGNGlvtevd 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 135 -PEWRVNRLKLNP------------------DVLspqaVQKYIPMVDGvardfskalKARV-LQNARGSLTLDIqpsIln 194
Cdd:cd20613    71 hEKWKKRRAILNPafhrkylknlmdefnesaDLL----VEKLSKKADG---------KTEVnMLDEFNRVTLDV---I-- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 195 YTVeasnlaLFGERLGLLGPSPSPASLQFIRALEAMLKSTAQLMFMPRdlsrwtsarVWKehfesWDYIFQYANnAIQKI 274
Cdd:cd20613   133 AKV------AFGMDLNSIEDPDSPFPKAISLVLEGIQESFRNPLLKYN---------PSK-----RKYRREVRE-AIKFL 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 275 YQE---------LALGRPQH-----YSGIVGELLMHADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQAL 340
Cdd:cd20613   192 RETgrecieerlEALKRGEEvpndiLTHILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRL 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 341 RQEslvAEAGItENPQRATTE----LPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSV 416
Cdd:cd20613   272 QAE---VDEVL-GSKQYVEYEdlgkLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEY 347

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 2112896241 417 FPRPERYHPRRWldSRSSGTRSPSLA---FGFGLRQCLGRRLAETEM 460
Cdd:cd20613   348 FEDPLKFDPERF--SPEAPEKIPSYAyfpFSLGPRSCIGQQFAQIEA 392
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 68-460 4.82e-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: 104.37  E-value: 4.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  68 MHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPwlAYRQHRGHKCGVFLLNGPEWRVNRLKLNPD 147
Cdd:cd11040     4 NGKKYFSGGPIFTIRLGGQKIYVITDPELISAVFRNPKTLSFDPIVIV--VVGRVFGSPESAKKKEGEPGGKGLIRLLHD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 148 VLSPQAVQkyIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSIL----NYTVEASNLALFGERLGLLGPspspaslQF 223
Cdd:cd11040    82 LHKKALSG--GEGLDRLNEAMLENLSKLLDELSLSGGTSTVEVDLYewlrDVLTRATTEALFGPKLPELDP-------DL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 224 IRALEAMLKSTAQLMFmprDLSRWTSARVWKehfeSWDYIFQyannAIQKIYQELALGRPqHYSGIVGE---LLMHADMT 300
Cdd:cd11040   153 VEDFWTFDRGLPKLLL---GLPRLLARKAYA----ARDRLLK----ALEKYYQAAREERD-DGSELIRArakVLREAGLS 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 301 LEAVRANSIELTAGSVDTTaYPLLM-TLFELARNPDVQQALRQEslVAEAGITENPQRAT-------TELPLLRAALKET 372
Cdd:cd11040   221 EEDIARAELALLWAINANT-IPAAFwLLAHILSDPELLERIREE--IEPAVTPDSGTNAIldltdllTSCPLLDSTYLET 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 373 LRLYPVGISLdRQVGSDVVL-QNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRSS----GTRSPSLAFGFG 446
Cdd:cd11040   298 LRLHSSSTSV-RLVTEDTVLgGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDkkgrGLPGAFRPFGGG 376

                         410
                  ....*....|....
gi 2112896241 447 LRQCLGRRLAETEM 460
Cdd:cd11040   377 ASLCPGRHFAKNEI 390
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 128-460 4.29e-23

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 101.51  E-value: 4.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 128 GVFLLNGPEWRVNRlKLNPDVLSPQAVQKYipMVDGVARDFSKALKaRVLQNA-RGSLTLDIQPSILNYTVEASNLALFG 206
Cdd:cd11064    50 GIFNVDGELWKFQR-KTASHEFSSRALREF--MESVVREKVEKLLV-PLLDHAaESGKVVDLQDVLQRFTFDVICKIAFG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 207 ERLGLLGPS-PSPASLQ-FIRALEAMLKSTAQLMFMPRdLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQEL--ALGR 282
Cdd:cd11064   126 VDPGSLSPSlPEVPFAKaFDDASEAVAKRFIVPPWLWK-LKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELnsREEE 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 283 PQHYSGIVGELLM-----HADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQR 357
Cdd:cd11064   205 NNVREDLLSRFLAseeeeGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESR 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 358 ATT-----ELPLLRAALKETLRLYPVgISLD-RQVGSDVVLQNYH-IPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWL 429
Cdd:cd11064   285 VPTyeelkKLVYLHAALSESLRLYPP-VPFDsKEAVNDDVLPDGTfVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWL 363

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2112896241 430 DSrSSGTRSPS----LAFGFGLRQCLGRRLAETEM 460
Cdd:cd11064   364 DE-DGGLRPESpykfPAFNAGPRICLGKDLAYLQM 397
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 317-459 7.15e-23

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: 100.80  E-value: 7.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQESlvaeAGITENPQRATT-----ELPLLRAALKETLRLYPVGISLDRQVGSDVV 391
Cdd:cd20660   246 DTTAAAINWALYLIGSHPEVQEKVHEEL----DRIFGDSDRPATmddlkEMKYLECVIKEALRLFPSVPMFGRTLSEDIE 321

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGtRSPS--LAFGFGLRQCLGRRLAETE 459
Cdd:cd20660   322 IGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAG-RHPYayIPFSAGPRNCIGQKFALME 390
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 267-460 2.41e-22

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: 99.41  E-value: 2.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 267 ANNAIQKIYQELALGRPQHYSGIVGELLMhADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLV 346
Cdd:cd20652   199 PENPRDAEDFELCELEKAKKEGEDRDLFD-GFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDE 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 347 AEAGITENPQRATTELPLLRAALKETLRL---YPVGISldRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERY 423
Cdd:cd20652   278 VVGRPDLVTLEDLSSLPYLQACISESQRIrsvVPLGIP--HGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEF 355

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2112896241 424 HPRRWLDSRSSGTRSPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20652   356 RPERFLDTDGKYLKPEAfIPFQTGKRMCLGDELARMIL 393
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 85-460 2.78e-22

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: 99.17  E-value: 2.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  85 GTHMVYVML--PEDVESLQRAESPQP-WR-PLLDPWLayrqhrGHkcGVFLLNGPEWRVNRLKLNP----DVLSPqavqk 156
Cdd:cd20659     9 GPFRPILVLnhPDTIKAVLKTSEPKDrDSyRFLKPWL------GD--GLLLSNGKKWKRNRRLLTPafhfDILKP----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 157 YIPMVDGVARDFSKALKARVLQNAR-------GSLTLDIqpsILN--YTVEaSNLALFGERlgllgpspSPaslqFIRAL 227
Cdd:cd20659    76 YVPVYNECTDILLEKWSKLAETGESvevfediSLLTLDI---ILRcaFSYK-SNCQQTGKN--------HP----YVAAV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 228 EAMLKSTAQLMFMPR---D-LSRWTSARvwKEHFESWDYIFQYANNAIQKIYQELALGRPQHYSG--------IvgeLLM 295
Cdd:cd20659   140 HELSRLVMERFLNPLlhfDwIYYLTPEG--RRFKKACDYVHKFAEEIIKKRRKELEDNKDEALSKrkyldfldI---LLT 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 296 HAD-----MTLEAVRAnsiE----LTAGSvDTTAYPLLMTLFELARNPDVQQALRQE--SLVAeagitenpQRATTE--- 361
Cdd:cd20659   215 ARDedgkgLTDEEIRD---EvdtfLFAGH-DTTASGISWTLYSLAKHPEHQQKCREEvdEVLG--------DRDDIEwdd 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 362 ---LPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGtRS 438
Cdd:cd20659   283 lskLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKK-RD 361

                         410       420
                  ....*....|....*....|....
gi 2112896241 439 PS--LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20659   362 PFafIPFSAGPRNCIGQNFAMNEM 385
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 143-460 3.30e-22

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: 98.90  E-value: 3.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 143 KLNPDVLSPQAVQKYI-----PMVDGVARDFSKALKaRVLQNARGSLTLDIQPSILNYTVEASNLALFGERLG----LLG 213
Cdd:cd11041    61 VVLDSPLHVDVVRKDLtpnlpKLLPDLQEELRAALD-EELGSCTEWTEVNLYDTVLRIVARVSARVFVGPPLCrneeWLD 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 214 pspspASLQFIralEAMLKSTAQLMFMP---RDLSRWTSARVWKEHfeswdYIFQYANNAIQKIYQELALGRPQHYSGIV 290
Cdd:cd11041   140 -----LTINYT---IDVFAAAAALRLFPpflRPLVAPFLPEPRRLR-----RLLRRARPLIIPEIERRRKLKKGPKEDKP 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 291 GELLmhaDMTLEAVRANSIE-----------LTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGitENPQR 357
Cdd:cd11041   207 NDLL---QWLIEAAKGEGERtpydladrqlaLSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEirSVLAEHG--GWTKA 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 358 ATTELPLLRAALKETLRLYPVGI-SLDRQVGSDVVLQN-YHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSG 435
Cdd:cd11041   282 ALNKLKKLDSFMKESQRLNPLSLvSLRRKVLKDVTLSDgLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQP 361

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 2112896241 436 ---------TRSP-SLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11041   362 gqekkhqfvSTSPdFLGFGHGRHACPGRFFASNEI 396
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 88-460 3.89e-22

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: 98.48  E-value: 3.89e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  88 MVYVMLPEDVESLQRaESPQPWRPLLDPWLayrQHRGHKCGVFLLNGPEWRVNRLKLNPDvLSPQAVQKYIP-MVDGVAR 166
Cdd:cd11051    12 LLVVTDPELAEQITQ-VTNLPKPPPLRKFL---TPLTGGSSLISMEGEEWKRLRKRFNPG-FSPQHLMTLVPtILDEVEI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 167 dfskaLKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERL--GLLGPSPSPASLQFIRALEAMLkSTAQLMFMPRDL 244
Cdd:cd11051    87 -----FAAILRELAESGEVFSLEELTTNLTFDVIGRVTLDIDLhaQTGDNSLLTALRLLLALYRSLL-NPFKRLNPLRPL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 245 SRWTSARVwkehfeswdyIFQYANNAIQKIYQelalgrpqhysgivgellmhADMTLEAVRansIELTAGSvDTTAYPLL 324
Cdd:cd11051   161 RRWRNGRR----------LDRYLKPEVRKRFE--------------------LERAIDQIK---TFLFAGH-DTTSSTLC 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 325 MTLFELARNPDVQQALRQE---------SLVAEAgITENPQRaTTELPLLRAALKETLRLYPVGISLdRQV--GSDVVLQ 393
Cdd:cd11051   207 WAFYLLSKHPEVLAKVRAEhdevfgpdpSAAAEL-LREGPEL-LNQLPYTTAVIKETLRLFPPAGTA-RRGppGVGLTDR 283

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112896241 394 NYHIP--AGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLA---FGFGLRQCLGRRLAETEM 460
Cdd:cd11051   284 DGKEYptDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYPPKSAwrpFERGPRNCIGQELAMLEL 355
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 310-456 4.80e-21

cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 95.39  E-value: 4.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 310 ELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLY-PVGISLDRQVGS 388
Cdd:cd11075   238 EFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHpPGHFLLPHAVTE 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2112896241 389 DVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSR-----SSGTRSPS-LAFGFGLRQCLGRRLA 456
Cdd:cd11075   318 DTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGeaadiDTGSKEIKmMPFGAGRRICPGLGLA 391
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 311-459 4.86e-21

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: 95.20  E-value: 4.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQEslVAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDV 390
Cdd:cd20614   217 VLAGH-ETTASIMAWMVIMLAEHPAVWDALCDE--AAAAGDVPRTPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEI 293

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 391 VLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCLGRRLAETE 459
Cdd:cd20614   294 ELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPNPVELLQFGGGPHFCLGYHVACVE 362
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 298-460 5.61e-21

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: 95.01  E-value: 5.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 298 DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslVAEAGITENPQRAT--TELPLLRAALKETLRL 375
Cdd:cd20621   224 EITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQE--IKSVVGNDDDITFEdlQKLNYLNAFIKEVLRL 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 376 YPVGISL-DRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQCLGR 453
Cdd:cd20621   302 YNPAPFLfPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVfIPFSAGPRNCIGQ 381


                  ....*..
gi 2112896241 454 RLAETEM 460
Cdd:cd20621   382 HLALMEA 388
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 311-460 5.95e-21

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 94.97  E-value: 5.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQE--------SLVAEAGITEnpqratteLPLLRAALKETLRLYPVGISL 382
Cdd:cd20655   237 FIAGT-DTSAATTEWAMAELINNPEVLEKAREEidsvvgktRLVQESDLPN--------LPYLQAVVKETLRLHPPGPLL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 383 DRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-------LAFGFGLRQCLGRRL 455
Cdd:cd20655   308 VRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQELDVrgqhfklLPFGSGRRGCPGASL 387


                  ....*
gi 2112896241 456 AETEM 460
Cdd:cd20655   388 AYQVV 392
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 76-460 7.40e-21

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: 94.55  E-value: 7.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESLQRAESP--QPWRP-----LLdpwlayrqhrgHKCGVFLLNGPEWR-VNRLKLNPd 147
Cdd:cd11043     6 GPVFKTSLFGRPTVVSADPEANRFILQNEGKlfVSWYPksvrkLL-----------GKSSLLTVSGEEHKrLRGLLLSF- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 148 vLSPQAVQ-KYIPMVDGVARdfskalkaRVLQNARGSLTLDIQPSILNYTVEASNLALFGErlgllgpSPSPASLQFIRA 226
Cdd:cd11043    74 -LGPEALKdRLLGDIDELVR--------QHLDSWWRGKSVVVLELAKKMTFELICKLLLGI-------DPEEVVEELRKE 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 227 LEAMLKStaqLMFMPRDLSRWTSARVWKEHfeswdyifQYANNAIQKIYQE--LALGRPQHYSGIVGELLMHAD-----M 299
Cdd:cd11043   138 FQAFLEG---LLSFPLNLPGTTFHRALKAR--------KRIRKELKKIIEErrAELEKASPKGDLLDVLLEEKDedgdsL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 300 TLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLvaeaGITEN---PQRATTE----LPLLRAALKET 372
Cdd:cd11043   207 TDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHE----EIAKRkeeGEGLTWEdyksMKYTWQVINET 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 373 LRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSpSLAFGFGLRQCLG 452
Cdd:cd11043   283 LRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPYT-FLPFGGGPRLCPG 361


                  ....*...
gi 2112896241 453 RRLAETEM 460
Cdd:cd11043   362 AELAKLEI 369
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 239-460 7.92e-21

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: 94.67  E-value: 7.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 239 FMP--RDLSRWTsarvwkehFESWDYIFQYANNAIQKIYQE-LALGRPQHYSGIVGELLMHAD-----------MTLEAV 304
Cdd:cd11028   161 VMPwlRYLTRRK--------LQKFKELLNRLNSFILKKVKEhLDTYDKGHIRDITDALIKASEekpeeekpevgLTDEHI 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 305 RANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRA-TTELPLLRAALKETLR---LYPVgi 380
Cdd:cd11028   233 ISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAE-LDRVIGRERLPRLSdRPNLPYTEAFILETMRhssFVPF-- 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 381 SLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS---LAFGFGLRQCLGRRLAE 457
Cdd:cd11028   310 TIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTKVdkfLPFGAGRRRCLGEELAR 389


                  ...
gi 2112896241 458 TEM 460
Cdd:cd11028   390 MEL 392
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 313-459 9.69e-21

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: 94.58  E-value: 9.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 313 AGSvDTTAYPLLMTLFELARNPDVQQALRQEslvaeagITEN--PQRATT-----ELPLLRAALKETLRLYPVG-ISLDR 384
Cdd:cd11027   240 AGT-ETTATTLRWAIAYLVNYPEVQAKLHAE-------LDDVigRDRLPTlsdrkRLPYLEATIAEVLRLSSVVpLALPH 311

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 385 QVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDsrSSGTRSPS----LAFGFGLRQCLGRRLAETE 459
Cdd:cd11027   312 KTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLD--ENGKLVPKpesfLPFSAGRRVCLGESLAKAE 388
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 73-460 1.11e-20

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: 94.17  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  73 QELGPIFRYDVGGTHMVYVmlpEDVESLQRAESPQPWRPLLDPWLAYRQHRGHKcGVFLLNG--PEWRV-NRLkLNPdVL 149
Cdd:cd11068    10 DELGPIFKLTLPGRRVVVV---SSHDLIAELCDESRFDKKVSGPLEELRDFAGD-GLFTAYThePNWGKaHRI-LMP-AF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 150 SPQAVQKYIP-MVD------------------GVARDFSKalkarvlqnargsLTLDiqpsilnyTVeasNLALFGERLG 210
Cdd:cd11068    84 GPLAMRGYFPmMLDiaeqlvlkwerlgpdepiDVPDDMTR-------------LTLD--------TI---ALCGFGYRFN 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 211 LLgpsPSPASLQFIRALEAMLK---STAQLMFMPRDLSRWTSARVWKEhfeswdyiFQYANNAIQKIYQELALGRPQHYS 287
Cdd:cd11068   140 SF---YRDEPHPFVEAMVRALTeagRRANRPPILNKLRRRAKRQFRED--------IALMRDLVDEIIAERRANPDGSPD 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 288 GIVGELLMHAD------MTLEAVRANSIE-LTAGSvDTTAYPLLMTLFELARNPDVQQALRQEslVAEA-GITENPQRAT 359
Cdd:cd11068   209 DLLNLMLNGKDpetgekLSDENIRYQMITfLIAGH-ETTSGLLSFALYYLLKNPEVLAKARAE--VDEVlGDDPPPYEQV 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 360 TELPLLRAALKETLRLYPVGISLDRQVGSDVVLQN-YHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRSSgtR 437
Cdd:cd11068   286 AKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFR--K 363

                         410       420
                  ....*....|....*....|....*.
gi 2112896241 438 SPSLA---FGFGLRQCLGRRLAETEM 460
Cdd:cd11068   364 LPPNAwkpFGNGQRACIGRQFALQEA 389
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 309-456 3.61e-20

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: 92.86  E-value: 3.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 309 IELTAGSV-------DTTAYPLLMTLFELARNPDVQQALRQE---SLVAEAGITENpqrATTELPLLRAALKETLRLYPV 378
Cdd:cd20650   227 LEILAQSIififagyETTSSTLSFLLYELATHPDVQQKLQEEidaVLPNKAPPTYD---TVMQMEYLDMVVNETLRLFPI 303

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 379 GISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWL-DSRSSGTRSPSLAFGFGLRQCLGRRLA 456
Cdd:cd20650   304 AGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSkKNKDNIDPYIYLPFGSGPRNCIGMRFA 382
PLN02655 PLN02655
ent-kaurene oxidase
 315-452 1.60e-19

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 90.96  E-value: 1.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 315 SVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENpqrATTELPLLRAALKETLRLY-PVGISLDRQVGSDVV 391
Cdd:PLN02655  274 AADTTLVTTEWAMYELAKNPDKQERLYREirEVCGDERVTEE---DLPNLPYLNAVFHETLRKYsPVPLLPPRFVHEDTT 350

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSR-SSGTRSPSLAFGFGLRQCLG 452
Cdd:PLN02655  351 LGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKyESADMYKTMAFGAGKRVCAG 412
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 66-459 1.75e-19

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: 90.89  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  66 LEMHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRaESPQPWRP------LLDPWLAYrqhrghkcGVFLLNGPEWRV 139
Cdd:cd11046     1 LDLYKWFLEYGPIYKLAFGPKSFLVISDPAIAKHVLR-SNAFSYDKkgllaeILEPIMGK--------GLIPADGEIWKK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 140 NRLKLnpdvlSPQAVQKYIPMVDGVARDFSKALKARVLQNARG-----------SLTLD-IQPSILNY----------TV 197
Cdd:cd11046    72 RRRAL-----VPALHKDYLEMMVRVFGRCSERLMEKLDAAAETgesvdmeeefsSLTLDiIGLAVFNYdfgsvteespVI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 198 EASNLALFgerlgllgpspspaslqfiralEAMLKSTAQLMFMPRDLSRWTSARvWKEHFESWDYIFQYANNAIQK---I 274
Cdd:cd11046   147 KAVYLPLV----------------------EAEHRSVWEPPYWDIPAALFIVPR-QRKFLRDLKLLNDTLDDLIRKrkeM 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 275 YQELALGRPQH-YSGI--VGELLMHADMTLEAVRANSIE------LTAGSvDTTAYPLLMTLFELARNPDVQQALRQE-- 343
Cdd:cd11046   204 RQEEDIELQQEdYLNEddPSLLRFLVDMRDEDVDSKQLRddlmtmLIAGH-ETTAAVLTWTLYELSQNPELMAKVQAEvd 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 344 SLVAEAGITENPQRAttELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYH--IPAGTVVKVLLYSLGRNPSVFPRPE 421
Cdd:cd11046   283 AVLGDRLPPTYEDLK--KLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGGvkVPAGTDIFISVYNLHRSPELWEDPE 360

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2112896241 422 RYHPRRWLDSRSSGTRSPS-----LAFGFGLRQCLGRRLAETE 459
Cdd:cd11046   361 EFDPERFLDPFINPPNEVIddfafLPFGGGPRKCLGDQFALLE 403
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 302-460 3.28e-19

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: 90.14  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 302 EAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENPQRATTELPLLRAALKETLRLYPVG 379
Cdd:cd20679   243 EDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEvqELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHPPV 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 380 ISLDRQVGSDVVLQNYH-IPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWlDSRSSGTRSPsLA---FGFGLRQCLGRRL 455
Cdd:cd20679   323 TAISRCCTQDIVLPDGRvIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF-DPENSQGRSP-LAfipFSAGPRNCIGQTF 400


                  ....*
gi 2112896241 456 AETEM 460
Cdd:cd20679   401 AMAEM 405
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 317-459 7.20e-19

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: 89.05  E-value: 7.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPqrATTE----LPLLRAALKETLRLYPVGISLDRQVGSDVVL 392
Cdd:cd20680   257 DTTAAAMNWSLYLLGSHPEVQRKVHKE-LDEVFGKSDRP--VTMEdlkkLRYLECVIKESLRLFPSVPLFARSLCEDCEI 333

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 393 QNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGtRSPS--LAFGFGLRQCLGRRLAETE 459
Cdd:cd20680   334 RGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSG-RHPYayIPFSAGPRNCIGQRFALME 401
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 311-460 1.40e-18

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: 88.04  E-value: 1.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQEslvaeagITENPQRAT-------TELPLLRAALKETLRLYP-VGISL 382
Cdd:cd20651   234 FIAGS-ETTSNTLGFAFLYLLLNPEVQRKVQEE-------IDEVVGRDRlptlddrSKLPYTEAVILEVLRIFTlVPIGI 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 383 DRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDsrSSGTRSP---SLAFGFGLRQCLGRRLAETE 459
Cdd:cd20651   306 PHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLD--EDGKLLKdewFLPFGAGKRRCLGESLARNE 383


                  .
gi 2112896241 460 M 460
Cdd:cd20651   384 L 384
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 239-452 2.77e-18

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: 87.13  E-value: 2.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 239 FMPR----DLSRWTSARVWKeHFESWDYIFQyannaiqKIYQE-LALGRPQHYSGIVGELLmhaDMTLEAVRANSIELT- 312
Cdd:cd11072   158 YFPSlgwiDLLTGLDRKLEK-VFKELDAFLE-------KIIDEhLDKKRSKDEDDDDDDLL---DLRLQKEGDLEFPLTr 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 313 -----------AGSVDTTAYPLLMTLFELARNPDV----QQALRqESLVAEAGITENpqrATTELPLLRAALKETLRLYP 377
Cdd:cd11072   227 dnikaiildmfLAGTDTSATTLEWAMTELIRNPRVmkkaQEEVR-EVVGGKGKVTEE---DLEKLKYLKAVIKETLRLHP 302

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112896241 378 VG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRS--SGTRSPSLAFGFGLRQCLG 452
Cdd:cd11072   303 PApLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIdfKGQDFELIPFGAGRRICPG 380
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 298-460 6.16e-18

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: 85.04  E-value: 6.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 298 DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQeslvaeagitenpQRAttelpLLRAALKETLRLYP 377
Cdd:cd20629   187 KLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRR-------------DRS-----LIPAAIEEGLRWEP 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 378 VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAE 457
Cdd:cd20629   249 PVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR--------KPKPHLVFGGGAHRCLGEHLAR 320


                  ...
gi 2112896241 458 TEM 460
Cdd:cd20629   321 VEL 323
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 313-460 1.52e-17

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


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 84.68  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 313 AGsVDTTAYPLLMTLFELARNPDVQQALrQESLVAEAGITENPQRAT-TELPLLRAALKETLRLYPVGISLDRQVG-SDV 390
Cdd:cd20673   243 AG-VETTTTVLKWIIAFLLHNPEVQKKI-QEEIDQNIGFSRTPTLSDrNHLPLLEATIREVLRIRPVAPLLIPHVAlQDS 320

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112896241 391 VLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS---LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20673   321 SIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQLISPSlsyLPFGAGPRVCLGEALARQEL 393
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 297-457 3.43e-17

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: 83.74  E-value: 3.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 297 ADMTLEAVRANSIEL-TAGSvDTTAYPLLMTLFELARNPDVQQALRQE--------SLVAEAGITEnpqratteLPLLRA 367
Cdd:cd11073   225 SELTRNHIKALLLDLfVAGT-DTTSSTIEWAMAELLRNPEKMAKARAEldevigkdKIVEESDISK--------LPYLQA 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 368 ALKETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSS-GTRSPSLA-FG 444
Cdd:cd11073   296 VVKETLRLHPPApLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDfKGRDFELIpFG 375

                         170
                  ....*....|...
gi 2112896241 445 FGLRQCLGRRLAE 457
Cdd:cd11073   376 SGRRICPGLPLAE 388
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 76-460 3.68e-17

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: 83.49  E-value: 3.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDP-WLAYrQHRGHkcGVFLLNGPEWRVNRLKLNPDVLSPQAV 154
Cdd:cd20615     1 GPIYRIWSGPTPEIVLTTPEHVKEFYRDSNKHHKAPNNNSgWLFG-QLLGQ--CVGLLSGTDWKRVRKVFDPAFSHSAAV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 155 QkYIPMVDGVARDFSKALKarvlQNARGSLTLDIQP----SILNYTVEAsnLALFGErlglLGPSPSPASLQFIRALEAM 230
Cdd:cd20615    78 Y-YIPQFSREARKWVQNLP----TNSGDGRRFVIDPaqalKFLPFRVIA--EILYGE----LSPEEKEELWDLAPLREEL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 231 LK---STAQLMFMprdLSRW--TSARVWKEHFESwdyifQYAN-NaiQKIYQelaLGRPQHYSGIVGELLMHA---DMTL 301
Cdd:cd20615   147 FKyviKGGLYRFK---ISRYlpTAANRRLREFQT-----RWRAfN--LKIYN---RARQRGQSTPIVKLYEAVekgDITF 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 302 EAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvaeagITENPQRATTELP--------LLRAALKETL 373
Cdd:cd20615   214 EELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREE-------ISAAREQSGYPMEdyilstdtLLAYCVLESL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 374 RLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLG-RNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCL 451
Cdd:cd20615   287 RLRPLLaFSVPESSPTDKIIGGYRIPANTPVVVDTYALNiNNPFWGPDGEAYRPERFLGISPTDLRYNFWRFGFGPRKCL 366


                  ....*....
gi 2112896241 452 GRRLAETEM 460
Cdd:cd20615   367 GQHVADVIL 375
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 309-459 5.43e-17

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: 83.35  E-value: 5.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 309 IELTAGsVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGS 388
Cdd:cd20649   268 IFLIAG-YETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAE 346

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112896241 389 DVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWlDSRSSGTRSP--SLAFGFGLRQCLGRRLAETE 459
Cdd:cd20649   347 DCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERF-TAEAKQRRHPfvYLPFGAGPRSCIGMRLALLE 418
PTZ00404 PTZ00404
cytochrome P450; Provisional
 313-460 5.98e-17

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 83.23  E-value: 5.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 313 AGsVDTTAYPLLMTLFELARNPDVQQALRQE---SLVAEAGITENPQRATtelPLLRAALKETLRLYPVG-ISLDRQVGS 388
Cdd:PTZ00404  294 AG-VDTSATSLEWMVLMLCNYPEIQEKAYNEiksTVNGRNKVLLSDRQST---PYTVAIIKETLRYKPVSpFGLPRSTSN 369

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112896241 389 DVVLQNYH-IPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPslaFGFGLRQCLGRRLAETEM 460
Cdd:PTZ00404  370 DIIIGGGHfIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSNDAFMP---FSIGPRNCVGQQFAQDEL 439
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 67-460 7.14e-17

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: 82.77  E-value: 7.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  67 EMHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQPWRPLLDPWLayRQHRGHkcGVFLLNGPEWRVNRLKLNP 146
Cdd:cd11052     3 HYYHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPGL--KKLLGR--GLVMSNGEKWAKHRRIANP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 147 dVLSPQAVQKYIP-MVDGVARDFSKALKarvlQNARGSLTLDIQPSILNYTVEASNLALFG-------ERLGLLgpspsp 218
Cdd:cd11052    79 -AFHGEKLKGMVPaMVESVSDMLERWKK----QMGEEGEEVDVFEEFKALTADIISRTAFGssyeegkEVFKLL------ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 219 ASLQFIRAleamlKSTAQLMFmprDLSRWTSAR----VWKEHFESWDYIfqyaNNAIQKIYQELALGRPQHY-SGIVGEL 293
Cdd:cd11052   148 RELQKICA-----QANRDVGI---PGSRFLPTKgnkkIKKLDKEIEDSL----LEIIKKREDSLKMGRGDDYgDDLLGLL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 294 LMHADMTLEAVRANSIELT--------AGSvDTTAYPLLMTLFELARNPDVQQALRQEslVAEAGITENPQRAT-TELPL 364
Cdd:cd11052   216 LEANQSDDQNKNMTVQEIVdecktfffAGH-ETTALLLTWTTMLLAIHPEWQEKAREE--VLEVCGKDKPPSDSlSKLKT 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 365 LRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPR-PERYHPRRWLDSRSSGTRSPS--L 441
Cdd:cd11052   293 VSMVINESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKAAKHPMafL 372

                         410
                  ....*....|....*....
gi 2112896241 442 AFGFGLRQCLGRRLAETEM 460
Cdd:cd11052   373 PFGLGPRNCIGQNFATMEA 391
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 149-460 7.23e-17

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: 82.75  E-value: 7.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 149 LSPQAVQKYIPMVDGVARDFSKALKARvlqNARGSLTLDIQPSILNYtveASNLAL---FGERLGLLGPSP--------- 216
Cdd:cd11066    75 LNRPAVQSYAPIIDLESKSFIRELLRD---SAEGKGDIDPLIYFQRF---SLNLSLtlnYGIRLDCVDDDSllleiieve 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 217 -------SPAS-LQ----FIRALEAMLKSTAQLMFMPRDLSRWTSARVwkehfeswdyifqyaNNAIQKIYQELAlgRPq 284
Cdd:cd11066   149 saiskfrSTSSnLQdyipILRYFPKMSKFRERADEYRNRRDKYLKKLL---------------AKLKEEIEDGTD--KP- 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 285 hysGIVGELLMHADMTLEAVRANSIELT--AGSVDTTAYPLLMTLFELARNP--DVQQALRQESLVAEAGITENPQRATT 360
Cdd:cd11066   211 ---CIVGNILKDKESKLTDAELQSICLTmvSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAA 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 361 E--LPLLRAALKETLRLYPV-GISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTR 437
Cdd:cd11066   288 EekCPYVVALVKETLRYFTVlPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIP 367

                         330       340
                  ....*....|....*....|....
gi 2112896241 438 SPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd11066   368 GPPhFSFGAGSRMCAGSHLANREL 391
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 295-452 1.16e-16

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 82.28  E-value: 1.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 295 MHADMTleaVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--------SLVAEAGITEnpqratteLPLLR 366
Cdd:cd20654   236 YDADTV---IKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEEldthvgkdRWVEESDIKN--------LVYLQ 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 367 AALKETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSS----GTRSPSL 441
Cdd:cd20654   305 AIVKETLRLYPPGpLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKDidvrGQNFELI 384

                         170
                  ....*....|.
gi 2112896241 442 AFGFGLRQCLG 452
Cdd:cd20654   385 PFGSGRRSCPG 395
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 317-460 1.75e-16

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 81.96  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGiTENPQR-----ATTELPLLRAALKETLRLYPVGISLDRQVGSD 389
Cdd:cd20622   276 DTTSTALSWGLKYLTANQDVQSKLRKAlySAHPEAV-AEGRLPtaqeiAQARIPYLDAVIEEILRCANTAPILSREATVD 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 390 VVLQNYHIPAGTVVkvllYSLGRNPSVF-PRPE--------------------------RYHPRRWL-DSRSSGTRS--- 438
Cdd:cd20622   355 TQVLGYSIPKGTNV----FLLNNGPSYLsPPIEidesrrssssaakgkkagvwdskdiaDFDPERWLvTDEETGETVfdp 430

                         170       180
                  ....*....|....*....|....*
gi 2112896241 439 ---PSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20622   431 sagPTLAFGLGPRGCFGRRLAYLEM 455
PLN02966 PLN02966
cytochrome P450 83A1
 73-456 3.56e-16

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 80.95  E-value: 3.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  73 QELGPIFRYDVGGTHMVYVMLPEDVESLQRAEspqpwrpllDPWLAYRQ-HRGHKCGVF-----LLN--GPEWR-VNRLK 143
Cdd:PLN02966   60 KKYGPILSYRIGSRTMVVISSAELAKELLKTQ---------DVNFADRPpHRGHEFISYgrrdmALNhyTPYYReIRKMG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 144 LNpDVLSPQAVQKYIPMVDGVARdfskALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGERLGLLGPSpSPASLQF 223
Cdd:PLN02966  131 MN-HLFSPTRVATFKHVREEEAR----RMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGEE-MKRFIKI 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 224 IRALEAMLKSTAQLMFMP-----RDLSRWTSarVWKEHFESWD-YIFQYANNAIQ-KIYQELALGRPQHYSGIVGELLMH 296
Cdd:PLN02966  205 LYGTQSVLGKIFFSDFFPycgflDDLSGLTA--YMKECFERQDtYIQEVVNETLDpKRVKPETESMIDLLMEIYKEQPFA 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 297 ADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENPQRATTELPLLRAALKETLR 374
Cdd:PLN02966  283 SEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEvrEYMKEKGSTFVTEDDVKNLPYFRALVKETLR 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 375 LYPV-GISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRS--SGTRSPSLAFGFGLRQC 450
Cdd:PLN02966  363 IEPViPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVdfKGTDYEFIPFGSGRRMC 442


                  ....*.
gi 2112896241 451 LGRRLA 456
Cdd:PLN02966  443 PGMRLG 448
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 298-458 4.11e-16

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 80.64  E-value: 4.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 298 DMTLEAVRANSIeltAGSVDTTAYPLLMTLFELARNPDVQQALrQESLVAEAGITENPQRAT-TELPLLRAALKETLRLY 376
Cdd:PLN03112  294 DVEIKALMQDMI---AAATDTSAVTNEWAMAEVIKNPRVLRKI-QEELDSVVGRNRMVQESDlVHLNYLRCVVRETFRMH 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 377 PVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHP-RRWLD--SRSSGTRSPS---LAFGFGLRQ 449
Cdd:PLN03112  370 PAGpFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPeRHWPAegSRVEISHGPDfkiLPFSAGKRK 449


                  ....*....
gi 2112896241 450 CLGRRLAET 458
Cdd:PLN03112  450 CPGAPLGVT 458
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 300-460 4.21e-16

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: 80.30  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 300 TLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE-SLVAEAGitenpQRATTE----LPLLRAALKETLR 374
Cdd:cd11026   223 HEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEiDRVIGRN-----RTPSLEdrakMPYTDAVIHEVQR 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 375 LYP-VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQCLG 452
Cdd:cd11026   298 FGDiVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAfMPFSAGKRVCLG 377


                  ....*...
gi 2112896241 453 RRLAETEM 460
Cdd:cd11026   378 EGLARMEL 385
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 316-456 4.28e-16

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: 80.45  E-value: 4.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 316 VDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGitenPQRATTE-----LPLLRAALKETLRLYPVG--ISLDRQVGS 388
Cdd:cd11076   237 TDTVAILTEWIMARMVLHPDIQSKAQAE-IDAAVG----GSRRVADsdvakLPYLQAVVKETLRLHPPGplLSWARLAIH 311

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112896241 389 DVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWL--------DSRSSGTRspsLA-FGFGLRQCLGRRLA 456
Cdd:cd11076   312 DVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVaaeggadvSVLGSDLR---LApFGAGRRVCPGKALG 385
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 313-460 4.48e-16

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: 80.21  E-value: 4.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 313 AGSvDTTAYPLLMTLFELARNPDVQQALrQESLVAEAGITENPQ-RATTELPLLRAALKETLRLYPV-GISLDRQVGSDV 390
Cdd:cd20666   239 AGT-DTTTNTLLWCLLYMSLYPEVQEKV-QAEIDTVIGPDRAPSlTDKAQMPFTEATIMEVQRMTVVvPLSIPHMASENT 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 391 VLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSL-AFGFGLRQCLGRRLAETEM 460
Cdd:cd20666   317 VLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFiPFGIGRRVCMGEQLAKMEL 387
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 311-455 5.99e-16

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 79.84  E-value: 5.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGsVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEagitenpQRATTE-----LPLLRAALKETLRLYP-VGISL 382
Cdd:cd20656   239 ITAG-MDTTAISVEWAMAEMIRNPRVQEKAQEEldRVVGS-------DRVMTEadfpqLPYLQCVVKEALRLHPpTPLML 310

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112896241 383 DRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWL--DSRSSGTRSPSLAFGFGLRQCLGRRL 455
Cdd:cd20656   311 PHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLeeDVDIKGHDFRLLPFGAGRRVCPGAQL 385
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 311-460 6.04e-16

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: 79.57  E-value: 6.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRqeslvaeagitENPQrattelpLLRAALKETLRLYPVGISLDRQVGSDV 390
Cdd:cd11078   218 LVAGH-ETTTNLLGNAVKLLLEHPDQWRRLR-----------ADPS-------LIPNAVEETLRYDSPVQGLRRTATRDV 278

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 391 VLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11078   279 EIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR-------PNARKHLTFGHGIHFCLGAALARMEA 341
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 312-460 6.40e-16

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: 79.85  E-value: 6.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 312 TAGSvDTTAYPLLMTLFELARNPDVQQALRQEslvAEAGITENPQRAT--TELPLLRAALKETLRLYPVG-ISLDRQVGS 388
Cdd:cd20664   235 GAGT-DTTGTTLRWGLLLMMKYPEIQKKVQEE---IDRVIGSRQPQVEhrKNMPYTDAVIHEIQRFANIVpMNLPHATTR 310

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2112896241 389 DVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20664   311 DVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAfMPFSAGRRVCIGETLAKMEL 383
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 299-460 7.55e-16

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 79.72  E-value: 7.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDV-QQALRQ-------ESLVAEAGITEnpqratteLPLLRAALK 370
Cdd:cd20658   233 LTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEIlRKATEEldrvvgkERLVQESDIPN--------LNYVKACAR 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 371 ETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRS-PSL---AFGF 445
Cdd:cd20658   305 EAFRLHPVApFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTLTePDLrfiSFST 384

                         170
                  ....*....|....*
gi 2112896241 446 GLRQCLGRRLAETEM 460
Cdd:cd20658   385 GRRGCPGVKLGTAMT 399
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 312-455 1.69e-15

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: 78.62  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 312 TAGSvDTTAYPLLMTLFELARNPDV----QQALRQ----ESLVAEAGItenPQratteLPLLRAALKETLRLYP-VGISL 382
Cdd:cd20657   238 TAGT-DTSSSTVEWALAELIRHPDIlkkaQEEMDQvigrDRRLLESDI---PN-----LPYLQAICKETFRLHPsTPLNL 308

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112896241 383 DRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSS-----GTRSPSLAFGFGLRQCLGRRL 455
Cdd:cd20657   309 PRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAkvdvrGNDFELIPFGAGRRICAGTRM 386
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 313-460 1.71e-15

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 78.01  E-value: 1.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 313 AGSVDTTAYPLLMTLFELARNPDVQQALRqeslvaeagitENPQrattelpLLRAALKETLRLYPVGISLDRQVGSDVVL 392
Cdd:cd11037   212 SAGLDTTISAIGNALWLLARHPDQWERLR-----------ADPS-------LAPNAFEEAVRLESPVQTFSRTTTRDTEL 273

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 393 QNYHIPAGTVVKVLLYSLGRNPSVFPRPERYhprrwlDSrssgTRSPS--LAFGFGLRQCLGRRLAETEM 460
Cdd:cd11037   274 AGVTIPAGSRVLVFLGSANRDPRKWDDPDRF------DI----TRNPSghVGFGHGVHACVGQHLARLEG 333
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 317-460 3.86e-15

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: 77.32  E-value: 3.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQE--SLVAE-AGITENpqrATTELPLLRAALKETLRLYPVGISLDRQVGSDVVLQ 393
Cdd:cd20678   253 DTTASGISWILYCLALHPEHQQRCREEirEILGDgDSITWE---HLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFP 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 394 NYH-IPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLdSRSSGTRSPS--LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20678   330 DGRsLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFS-PENSSKRHSHafLPFSAGPRNCIGQQFAMNEM 398
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 309-460 4.18e-15

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 77.07  E-value: 4.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 309 IELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRAT-TELPLLRAALKETLRLYPVG-ISLDRQV 386
Cdd:cd20674   232 VDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEE-LDRVLGPGASPSYKDrARLPLLNATIAEVLRLRPVVpLALPHRT 310

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112896241 387 GSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSrssGTRSPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20674   311 TRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEP---GAANRAlLPFGCGARVCLGEPLARLEL 382
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 311-460 7.07e-15

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: 76.10  E-value: 7.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSVDTTAypLLMTLFE-LARNPDVQQALRqeslvaeagitENPQrattelpLLRAALKETLRLYPVGISLDRQVGSD 389
Cdd:cd11032   207 LIAGHETTTN--LLGNAVLcLDEDPEVAARLR-----------ADPS-------LIPGAIEEVLRYRPPVQRTARVTTED 266

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 390 VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11032   267 VELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR--------NPNPHLSFGHGIHFCLGAPLARLEA 329
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 76-460 8.99e-15

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: 76.30  E-value: 8.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  76 GPIFRYDVGGTHMVYVMLPEDVESLQRAESpqpwrplLDPWLAYRQHRGHKC----GVFLLNGPEWRVNRLKLNPDvLSP 151
Cdd:cd20640    12 GPIFTYSTGNKQFLYVSRPEMVKEINLCVS-------LDLGKPSYLKKTLKPlfggGILTSNGPHWAHQRKIIAPE-FFL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 152 QAVQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLALFGErlgllgpspspaslQFIRALEAML 231
Cdd:cd20640    84 DKVKGMVDLMVDSAQPLLSSWEERIDRAGGMAADIVVDEDLRAFSADVISRACFGS--------------SYSKGKEIFS 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 232 KStaqlmfmpRDLSRWTSARVWKEHFESWDYIFQYANNAIQKIYQE-----LALGRPQHYSGIVGELLMHAdmTLEAVRA 306
Cdd:cd20640   150 KL--------RELQKAVSKQSVLFSIPGLRHLPTKSNRKIWELEGEirsliLEIVKEREEECDHEKDLLQA--ILEGARS 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 307 NSIELTA--------------GSVDTTAYPLLMTLFELARNPDVQQALRQESL-VAEAGITENPqrATTELPLLRAALKE 371
Cdd:cd20640   220 SCDKKAEaedfivdnckniyfAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLeVCKGGPPDAD--SLSRMKTVTMVIQE 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 372 TLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRSSGTRSPS--LAFGFGLR 448
Cdd:cd20640   298 TLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPPHsyMPFGAGAR 377

                         410
                  ....*....|..
gi 2112896241 449 QCLGRRLAETEM 460
Cdd:cd20640   378 TCLGQNFAMAEL 389
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 293-460 2.16e-14

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


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 74.49  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 293 LLMHAD-----MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRqeslvaeagitENPQrattelpLLRA 367
Cdd:cd11033   194 VLANAEvdgepLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLR-----------ADPS-------LLPT 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 368 ALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVkVLLYSLG-RNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFG 446
Cdd:cd11033   256 AVEEILRWASPVIHFRRTATRDTELGGQRIRAGDKV-VLWYASAnRDEEVFDDPDRFDITR--------SPNPHLAFGGG 326

                         170
                  ....*....|....
gi 2112896241 447 LRQCLGRRLAETEM 460
Cdd:cd11033   327 PHFCLGAHLARLEL 340
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 73-460 2.57e-14

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: 74.65  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  73 QELGPIFRYDVGGTHMVYVMLPEDVEslqraespqpwrplldpwlayrqhrghkcgVFLLNgpewrvnrlklnPDVLSPQ 152
Cdd:cd20635    10 QKLGPVFTVKAAGERMTFVTDEEDFH------------------------------VFFKS------------KDVDFQK 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 153 AVQKYIPMVDGVARDFSKALKARVLQNARGSLTldiqPSILNYTVEASNLAlFGERLGLLGPSPSPASLQFIRalEAMLK 232
Cdd:cd20635    48 AVQDPVQNTASISKESFFEYHTKIHDMMKGKLA----SSNLAPLSDKLCEE-FKEQLELLGSEGTGDLNDLVR--HVMYP 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 233 STAQLMFMPRDLSrwTSARVWKE---HFESWDYIFQYAN------------------NAIQKIYQELALGRP-------- 283
Cdd:cd20635   121 AVVNNLFGKGLLP--TSEEEIKEfeeHFVKFDEQFEYGSqlpefflrdwssskqwllSLFEKVVPDAEKTKPlennsktl 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 284 -QHYSGIVGE-------LLMhadmtLEAVRANSIELTagsvdttayplLMTLFELARNPDVQQALRQE--SLVAEAG--- 350
Cdd:cd20635   199 lQHLLDTVDKenapnysLLL-----LWASLANAIPIT-----------FWTLAFILSHPSVYKKVMEEisSVLGKAGkdk 262

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 351 --ITENPQRattELPLLRAALKETLRLYPVGIsLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRW 428
Cdd:cd20635   263 ikISEDDLK---KMPYIKRCVLEAIRLRSPGA-ITRKVVKPIKIKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERW 338

                         410       420       430
                  ....*....|....*....|....*....|....
gi 2112896241 429 LDSRSSGTRSPS--LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20635   339 KKADLEKNVFLEgfVAFGGGRYQCPGRWFALMEI 372
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 132-460 3.87e-14

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: 73.91  E-value: 3.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 132 LNGPEWRVNRLKLNPdVLSPQAVQKYIPMVDGVARDfskaLKARVLQNARGSL--TLDIQPSILnytveasnlaLFGERL 209
Cdd:cd11034    56 TDPPEHKKYRKLLNP-FFTPEAVEAFRPRVRQLTND----LIDAFIERGECDLvtELANPLPAR----------LTLRLL 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 210 GLlgpsPSPASLQFIRALEAMLKStaqlmfmpRDLSRWTSArvwkehfesWDYIFQYANNAIQKIYQElalGRPQHYSGI 289
Cdd:cd11034   121 GL----PDEDGERLRDWVHAILHD--------EDPEEGAAA---------FAELFGHLRDLIAERRAN---PRDDLISRL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 290 V-----GELLMHADMTleavrANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLvaeagitenpqrattelpL 364
Cdd:cd11034   177 IegeidGKPLSDGEVI-----GFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLIADPS------------------L 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 365 LRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWldsrssgtRSPSLAFG 444
Cdd:cd11034   234 IPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRT--------PNRHLAFG 305

                         330
                  ....*....|....*.
gi 2112896241 445 FGLRQCLGRRLAETEM 460
Cdd:cd11034   306 SGVHRCLGSHLARVEA 321
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 318-459 6.68e-14

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: 73.64  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 318 TTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQR-ATTELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYH 396
Cdd:cd20639   247 TTSNLLTWTTVLLAMHPEWQERARRE-VLAVCGKGDVPTKdHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKLGGLD 325

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112896241 397 IPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRSSGTRSPS--LAFGFGLRQCLGRRLAETE 459
Cdd:cd20639   326 IPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKHPLafIPFGLGPRTCVGQNLAILE 391
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 317-459 7.81e-14

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: 73.25  E-value: 7.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRAT-TELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNY 395
Cdd:cd20641   249 ETTSNLLTWTMFLLSLHPDWQEKLREE-VFRECGKDKIPDADTlSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGGL 327

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112896241 396 HIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRSSGTRSPS--LAFGFGLRQCLGRRLAETE 459
Cdd:cd20641   328 EIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPNalLSFSLGPRACIGQNFAMIE 394
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 315-457 1.22e-13

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: 72.66  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 315 SVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGiteNPQRATTEL----PLLRAALKETLRLYPVGISLDRQVGSDV 390
Cdd:cd11082   232 SQDASTSSLVWALQLLADHPDVLAKVREEQARLRPN---DEPPLTLDLleemKYTRQVVKEVLRYRPPAPMVPHIAKKDF 308

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 391 VL-QNYHIPAGTVVKVLLYSLGRNPsvFPRPERYHPRRWLDSRSSGTRSPS--LAFGFGLRQCLGRRLAE 457
Cdd:cd11082   309 PLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRKYKKnfLVFGAGPHQCVGQEYAI 376
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 311-460 1.77e-13

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: 71.83  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGsVDTTAYPLLMTLFELARNPDVQQALRqeslvaeagitENPQrattelpLLRAALKETLRLYPVGISLD--RQVGS 388
Cdd:cd11031   215 LVAG-HETTASQIGNGVLLLLRHPEQLARLR-----------ADPE-------LVPAAVEELLRYIPLGAGGGfpRYATE 275

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2112896241 389 DVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11031   276 DVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR--------EPNPHLAFGHGPHHCLGAPLARLEL 339
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 299-460 2.44e-13

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: 71.35  E-value: 2.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESlvaeagitenpqrattelPLLRAALKETLRLYPV 378
Cdd:cd11080   189 LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRADR------------------SLVPRAIAETLRYHPP 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 379 GISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRW-LDSRSSGTRSPS-LAFGFGLRQCLGRRLA 456
Cdd:cd11080   251 VQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREdLGIRSAFSGAADhLAFGSGRHFCVGAALA 330


                  ....
gi 2112896241 457 ETEM 460
Cdd:cd11080   331 KREI 334
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 45-450 4.19e-13

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 71.26  E-value: 4.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  45 PGNKWLRLLQIWKEQGSENLHLEMHRTFQELGPIFRYDVGGTHMVYVMLPEDVESLQRAESPQ-PWRPLLDPWLAYrQHR 123
Cdd:PLN03234   31 PGPKGLPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNfTARPLLKGQQTM-SYQ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 124 GHKCGvFLLNGPEWRVNRLKLNPDVLSPQAVQKYIPmvdgVARDFSKALKARVLQNARGSLTLDIQPSILNYTVEASNLA 203
Cdd:PLN03234  110 GRELG-FGQYTAYYREMRKMCMVNLFSPNRVASFRP----VREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQ 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 204 LFGERLGLLGpSPSPASLQFIRALEAMLKSTAQLMFMPR----DLSRWTSARVwKEHFESWDYIFQyannaiQKIYQELA 279
Cdd:PLN03234  185 AFGKRYNEYG-TEMKRFIDILYETQALLGTLFFSDLFPYfgflDNLTGLSARL-KKAFKELDTYLQ------ELLDETLD 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 280 LGRPQHYSGIVGELLMHA--------DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEA 349
Cdd:PLN03234  257 PNRPKQETESFIDLLMQIykdqpfsiKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEvrNVIGDK 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 350 GITEnpQRATTELPLLRAALKETLRLYPV-GISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRR 427
Cdd:PLN03234  337 GYVS--EEDIPNLPYLKAVIKESLRLEPViPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPER 414

                         410       420
                  ....*....|....*....|....*..
gi 2112896241 428 WLDSRS----SGTRSPSLAFGFGLRQC 450
Cdd:PLN03234  415 FMKEHKgvdfKGQDFELLPFGSGRRMC 441
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 312-452 4.48e-13

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 71.38  E-value: 4.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 312 TAGSvDTTAYPLLMTLFELARNPDVQQALRQE--------SLVAEAGItenPQratteLPLLRAALKETLRLYP-VGISL 382
Cdd:PLN02687  307 TAGT-DTTSSTVEWAIAELIRHPDILKKAQEEldavvgrdRLVSESDL---PQ-----LTYLQAVIKETFRLHPsTPLSL 377

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112896241 383 DRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRS------SGTRSPSLAFGFGLRQCLG 452
Cdd:PLN02687  378 PRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEhagvdvKGSDFELIPFGAGRRICAG 453
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 297-460 7.20e-13

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 70.35  E-value: 7.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 297 ADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLVAEAGITENPQRA---TTELPLLRAALKETL 373
Cdd:PLN02196  258 EGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGESLTwedTKKMPLTSRVIQETL 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 374 RLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPslaFGFGLRQCLGR 453
Cdd:PLN02196  338 RVASILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNTFMP---FGNGTHSCPGN 414


                  ....*..
gi 2112896241 454 RLAETEM 460
Cdd:PLN02196  415 ELAKLEI 421
PLN02183 PLN02183
ferulate 5-hydroxylase
 299-455 8.43e-13

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 70.65  E-value: 8.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRATTE-LPLLRAALKETLRLYP 377
Cdd:PLN02183  300 LTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQE-LADVVGLNRRVEESDLEkLTYLKCTLKETLRLHP 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 378 VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRS---SGTRSPSLAFGFGLRQCLGRR 454
Cdd:PLN02183  379 PIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVpdfKGSHFEFIPFGSGRRSCPGMQ 458


                  .
gi 2112896241 455 L 455
Cdd:PLN02183  459 L 459
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 287-460 1.28e-12

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: 69.09  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 287 SGIVGELLMHADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRqeslvaeagitENPQrattelpLLR 366
Cdd:cd11030   192 SRLVAEHGAPGELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALR-----------ADPS-------LVP 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 367 AALKETLR-LYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGF 445
Cdd:cd11030   254 GAVEELLRyLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR--------PARRHLAFGH 325

                         170
                  ....*....|....*
gi 2112896241 446 GLRQCLGRRLAETEM 460
Cdd:cd11030   326 GVHQCLGQNLARLEL 340
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 311-456 1.62e-12

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 69.17  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENPQraTTELPLLRAALKETLRLYPVG-ISLDRQVG 387
Cdd:cd20653   236 LLAGT-DTSAVTLEWAMSNLLNHPEVLKKAREEidTQVGQDRLIEESD--LPKLPYLQNIISETLRLYPAApLLVPHESS 312

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 388 SDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRspSLAFGFGLRQCLGRRLA 456
Cdd:cd20653   313 EDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREGYK--LIPFGLGRRACPGAGLA 379
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 314-460 1.65e-12

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


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 69.02  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 314 GSVDTTAYPLLMTLFELARNPDVQQALrQESLVAEAGITENPQRAT-TELPLLRAALKETLRLYPV-GISLDRQVGSDVV 391
Cdd:cd20669   237 GGTETVSTTLRYGFLILMKYPKVAARV-QEEIDRVVGRNRLPTLEDrARMPYTDAVIHEIQRFADIiPMSLPHAVTRDTN 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSL-AFGFGLRQCLGRRLAETEM 460
Cdd:cd20669   316 FRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFmPFSAGKRICLGESLARMEL 385
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 314-460 2.54e-12

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: 68.16  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 314 GSVDTTAYPLLMTLFELARNPDVQQALRqeslvaeagitENPQrattelpLLRAALKETLRLYPVGISLDRQVGSDVVLQ 393
Cdd:cd11038   225 AGVDTTRNQLGLAMLTFAEHPDQWRALR-----------EDPE-------LAPAAVEEVLRWCPTTTWATREAVEDVEYN 286

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112896241 394 NYHIPAGTVVKVLLYSLGRNPSVFPrPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11038   287 GVTIPAGTVVHLCSHAANRDPRVFD-ADRFDITA--------KRAPHLGFGGGVHHCLGAFLARAEL 344
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 115-460 2.90e-12

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: 68.14  E-value: 2.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 115 PWLAYRQHRGHKCGVFLLNGPEWRVNRLKLNP-DVLSPQAVQKYIPMVDGVARdfsKALKARVLQNARGSLTLDIQPSIL 193
Cdd:cd20612    35 PWGPAMEDLTKGGPFFLLGGDTPANDRQRELMrKALYSPDLAKDVVFFYELQT---RALLVESSRLGGSGGQVDIVRDVA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 194 NytveasnlalfgerlgllgpspsPASLQFIR---ALEAMLKSTAQLMFMPRDLSRWTSArvwkehfeswdyIFQYANNA 270
Cdd:cd20612   112 N-----------------------LVPARFCAdlfGLPLKTKENPRGGYTEAELYRALAA------------IFAYIFFD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 271 IQKIyQELALGR-PQHYSGIVGELLmhaDMTL-EAVRANSIELTAGSVDTTAypllmTLFELArnpdVQQALRQESLVAE 348
Cdd:cd20612   157 LDPA-KSFQLRRaAQAAAARLGALL---DAAVaDEVRDNVLGTAVGGVPTQS-----QAFAQI----LDFYLRRPGAAHL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 349 AGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDVVLQ-----NYHIPAGTVVKVLLYSLGRNPSVFPRPERY 423
Cdd:cd20612   224 AEIQALARENDEADATLRGYVLEALRLNPIAPGLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERF 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2112896241 424 HPRRWLDSrssgtrspSLAFGFGLRQCLGRRLAE---TEM 460
Cdd:cd20612   304 RLDRPLES--------YIHFGHGPHQCLGEEIARaalTEM 335
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 315-456 3.19e-12

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 68.27  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 315 SVDTTAYPLLMTLFELARNPDVQQALRQE-SLVAEAGITEnPQRATTELPLLRAALKETLRLY-PVGISLDRQVGSDVVL 392
Cdd:cd11074   245 AIETTLWSIEWGIAELVNHPEIQKKLRDElDTVLGPGVQI-TEPDLHKLPYLQAVVKETLRLRmAIPLLVPHMNLHDAKL 323

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112896241 393 QNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRS----SGTRSPSLAFGFGLRQCLGRRLA 456
Cdd:cd11074   324 GGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESkveaNGNDFRYLPFGVGRRSCPGIILA 391
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 315-460 5.86e-12

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


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 67.34  E-value: 5.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 315 SVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEA---GITENPQratteLPLLRAALKETLR---LYPVGISldRQV 386
Cdd:cd20675   247 SQDTLSTALQWILLLLVRYPDVQARLQEEldRVVGRDrlpCIEDQPN-----LPYVMAFLYEAMRfssFVPVTIP--HAT 319

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112896241 387 GSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTR---SPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20675   320 TADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKdlaSSVMIFSVGKRRCIGEELSKMQL 396
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 310-460 6.38e-12

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: 67.53  E-value: 6.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 310 ELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENPQRAttELPLLRAALKETLRL---YPVGISldR 384
Cdd:cd20661   245 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEidLVVGPNGMPSFEDKC--KMPYTEAVLHEVLRFcniVPLGIF--H 320

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112896241 385 QVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20661   321 ATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAfVPFSLGRRHCLGEQLARMEM 397
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 315-456 1.08e-11

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 67.06  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 315 SVDTTAYPLLMTLFELARNPDVQQALRQE-SLVAEAG--ITENpqrATTELPLLRAALKETLRLY-PVGISLDRQVGSDV 390
Cdd:PLN02394  305 AIETTLWSIEWGIAELVNHPEIQKKLRDElDTVLGPGnqVTEP---DTHKLPYLQAVVKETLRLHmAIPLLVPHMNLEDA 381

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 391 VLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRS----SGTRSPSLAFGFGLRQCLGRRLA 456
Cdd:PLN02394  382 KLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAkveaNGNDFRFLPFGVGRRSCPGIILA 451
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 257-460 1.75e-11

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: 65.97  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 257 FESWDYIFQYANNAIQKIYQELALGRPQHY-SGIVGELLMHADMT----LEAVRANSIELTAGSVDTTAYPLLMTLFELA 331
Cdd:cd20662   174 FSNWKKLKLFVSDMIDKHREDWNPDEPRDFiDAYLKEMAKYPDPTtsfnEENLICSTLDLFFAGTETTSTTLRWALLYMA 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 332 RNPDVQQALRQEslvAEAGITENPQRATTE---LPLLRAALKETLR---LYPVGISldRQVGSDVVLQNYHIPAGTVVKV 405
Cdd:cd20662   254 LYPEIQEKVQAE---IDRVIGQKRQPSLADresMPYTNAVIHEVQRmgnIIPLNVP--REVAVDTKLAGFHLPKGTMILT 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2112896241 406 LLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20662   329 NLTALHRDPKEWATPDTFNPGHFLENGQFKKREAFLPFSMGKRACLGEQLARSEL 383
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 311-460 3.19e-11

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: 64.75  E-value: 3.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvaeagitenPQrattelpLLRAALKETLRLYPVG-ISLDRQVGSD 389
Cdd:cd20630   211 LIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE-----------PE-------LLRNALEEVLRWDNFGkMGTARYATED 272

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 390 VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20630   273 VELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR--------DPNANIAFGYGPHFCIGAALARLEL 335
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 304-460 3.35e-11

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


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 65.20  E-value: 3.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 304 VRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE-SLVAEAGITENP--QRAtteLPLLRAALKETLRLYPVGI 380
Cdd:cd20671   224 VLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEiDRVLGPGCLPNYedRKA---LPYTSAVIHEVQRFITLLP 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 381 SLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGT-RSPSLAFGFGLRQCLGRRLAETE 459
Cdd:cd20671   301 HVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVkKEAFLPFSAGRRVCVGESLARTE 380


                  .
gi 2112896241 460 M 460
Cdd:cd20671   381 L 381
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 299-456 3.40e-11

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 65.26  E-value: 3.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvAEAGITENPQRATTE---LPLLRAALKETLRL 375
Cdd:PLN00110  285 LTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEE---MDQVIGRNRRLVESDlpkLPYLQAICKESFRK 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 376 YP-VGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSS-----GTRSPSLAFGFGLRQ 449
Cdd:PLN00110  362 HPsTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAkidprGNDFELIPFGAGRRI 441


                  ....*..
gi 2112896241 450 CLGRRLA 456
Cdd:PLN00110  442 CAGTRMG 448
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 313-456 4.52e-11

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: 64.61  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 313 AGSvDTTAYPLLMTLFELARNPDVQQALRQESLVAeAGITENPQRATTELPLLRAALKETLRLYPVGISLDRQVGSDVVL 392
Cdd:cd20642   245 AGQ-ETTSVLLVWTMVLLSQHPDWQERAREEVLQV-FGNNKPDFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKL 322

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112896241 393 QNYHIPAGTVVKVLLYSLGRNPSVFPR-PERYHPRRWLDSRSSGTRSPS--LAFGFGLRQCLGRRLA 456
Cdd:cd20642   323 GDLTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERFAEGISKATKGQVsyFPFGWGPRICIGQNFA 389
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 314-460 4.56e-11

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: 64.15  E-value: 4.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 314 GSVDTTAYPLLMTLFELARNPDVQQALRqeslvaeagitENPQrattelpLLRAALKETLRLYPVgISLDRQVGSDVVLQ 393
Cdd:cd11035   201 AGLDTVASALGFIFRHLARHPEDRRRLR-----------EDPE-------LIPAAVEELLRRYPL-VNVARIVTRDVEFH 261

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2112896241 394 NYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11035   262 GVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR--------KPNRHLAFGAGPHRCLGSHLARLEL 320
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 311-460 5.98e-11

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 64.71  E-value: 5.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQEslvAEAGITENPQRATTE----LPLLRAALKETLRLYPvGISLDRQ- 385
Cdd:PLN02426  302 LLAGR-DTVASALTSFFWLLSKHPEVASAIREE---ADRVMGPNQEAASFEemkeMHYLHAALYESMRLFP-PVQFDSKf 376

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 386 -VGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRSSGTRSPSL--AFGFGLRQCLGRRLAETEM 460
Cdd:PLN02426  377 aAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVFVPENPFKypVFQAGLRVCLGKEMALMEM 455
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 311-459 6.33e-11

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 64.35  E-value: 6.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALR--QESLVAEAGITENPQ--RATTELPLLRAALKETLRLYPVGISLDRQV 386
Cdd:PLN02302  296 LNAGH-ESSGHLTMWATIFLQEHPEVLQKAKaeQEEIAKKRPPGQKGLtlKDVRKMEYLSQVIDETLRLINISLTVFREA 374

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2112896241 387 GSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLD-SRSSGTrspSLAFGFGLRQCLGRRLAETE 459
Cdd:PLN02302  375 KTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNyTPKAGT---FLPFGLGSRLCPGNDLAKLE 445
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 330-460 9.17e-11

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


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 63.34  E-value: 9.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 330 LARNPDVQQALRQESlvaeagitenpqrattelPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYS 409
Cdd:cd20625   228 LLRHPEQLALLRADP------------------ELIPAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGA 289

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 410 LGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20625   290 ANRDPAVFPDPDRFDITR--------APNRHLAFGAGIHFCLGAPLARLEA 332
PLN02500 PLN02500
cytochrome P450 90B1
 289-460 9.25e-11

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 64.11  E-value: 9.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 289 IVGELLMHADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQESLV-----AEAGITENPQRATTELP 363
Cdd:PLN02500  265 LLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEiarakKQSGESELNWEDYKKME 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 364 LLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS--- 440
Cdd:PLN02500  345 FTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGSSGSssa 424

                         170       180
                  ....*....|....*....|....*
gi 2112896241 441 -----LAFGFGLRQCLGRRLAETEM 460
Cdd:PLN02500  425 ttnnfMPFGGGPRLCAGSELAKLEM 449
PLN03018 PLN03018
homomethionine N-hydroxylase
 299-460 1.14e-10

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 63.88  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDV-QQALRQ-------ESLVAEAGITEnpqratteLPLLRAALK 370
Cdd:PLN03018  310 VTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEIlRKALKEldevvgkDRLVQESDIPN--------LNYLKACCR 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 371 ETLRLYPVGISLDRQVG-SDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSgTRSPSL-------- 441
Cdd:PLN03018  382 ETFRIHPSAHYVPPHVArQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDGI-TKEVTLvetemrfv 460

                         170
                  ....*....|....*....
gi 2112896241 442 AFGFGLRQCLGRRLAETEM 460
Cdd:PLN03018  461 SFSTGRRGCVGVKVGTIMM 479
PLN02774 PLN02774
brassinosteroid-6-oxidase
 315-460 1.72e-10

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 62.87  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 315 SVDTTAyplLMTLFELARNPDVQQALRQESLVAEAGitENPQRATT-----ELPLLRAALKETLRLYPVGISLDRQVGSD 389
Cdd:PLN02774  279 TVSTTS---MMAVKYLHDHPKALQELRKEHLAIRER--KRPEDPIDwndykSMRFTRAVIFETSRLATIVNGVLRKTTQD 353

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 390 VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDsRSSGTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:PLN02774  354 MELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLD-KSLESHNYFFLFGGGTRLCPGKELGIVEI 423
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 318-460 2.60e-10

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: 62.51  E-value: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 318 TTAYPLLMtlfeLARNPDVQQALRQEslvAEAGITENPQ---RATTELPLLRAALKETLR---LYPVGISldRQVGSDVV 391
Cdd:cd20668   245 TLRYGFLL----LMKHPEVEAKVHEE---IDRVIGRNRQpkfEDRAKMPYTEAVIHEIQRfgdVIPMGLA--RRVTKDTK 315

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 392 LQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20668   316 FRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAfVPFSIGKRYCFGEGLARMEL 385
PLN02936 PLN02936
epsilon-ring hydroxylase
 311-484 3.04e-10

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 62.50  E-value: 3.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQEslVAEAGITENPQRA-TTELPLLRAALKETLRLYP-VGISLDRQVGS 388
Cdd:PLN02936  287 LVAGH-ETTGSVLTWTLYLLSKNPEALRKAQEE--LDRVLQGRPPTYEdIKELKYLTRCINESMRLYPhPPVLIRRAQVE 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 389 DVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRW-LDS---RSSGTRSPSLAFGFGLRQCLGRRLAETEMLLLL 464
Cdd:PLN02936  364 DVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdLDGpvpNETNTDFRYIPFSGGPRKCVGDQFALLEAIVAL 443

                         170       180
                  ....*....|....*....|
gi 2112896241 465 HHVLNHFLVETLTQEDIKMT 484
Cdd:PLN02936  444 AVLLQRLDLELVPDQDIVMT 463
PLN00168 PLN00168
Cytochrome P450; Provisional
 134-456 8.43e-10

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 61.12  E-value: 8.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 134 GPEWRVNRLKLNPDVLSPQAVQKYIPMVDGVARDFSKALKARVLQNARGSLTLDIQPSILNYTVeasnLALFGERL---- 209
Cdd:PLN00168  128 GPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLV----LMCFGERLdepa 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 210 -------------------GLLGPSPSPASLQFIRALEAMLKSTAQL--MFMPRDLSRwtsaRVWKEHfeswdyifqyAN 268
Cdd:PLN00168  204 vraiaaaqrdwllyvskkmSVFAFFPAVTKHLFRGRLQKALALRRRQkeLFVPLIDAR----REYKNH----------LG 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 269 NAIQKIYQELALgrPQHYSGIVGELLMHADMTL-----EAVRANSIELTAGSvDTTAYPLLMTLFELARNPDVQQALRQE 343
Cdd:PLN00168  270 QGGEPPKKETTF--EHSYVDTLLDIRLPEDGDRaltddEIVNLCSEFLNAGT-DTTSTALQWIMAELVKNPSIQSKLHDE 346

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 344 SLVAeagiTENPQRATTE-----LPLLRAALKETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF 417
Cdd:PLN00168  347 IKAK----TGDDQEEVSEedvhkMPYLKAVVLEGLRKHPPAhFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREW 422

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2112896241 418 PRPERYHPRRWL------DSRSSGTRSPS-LAFGFGLRQCLGRRLA 456
Cdd:PLN00168  423 ERPMEFVPERFLaggdgeGVDVTGSREIRmMPFGVGRRICAGLGIA 468
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 317-460 1.56e-09

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


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 60.11  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQ-RATTELPLLRAALKETLR---LYPVGISldRQVGSDVVL 392
Cdd:cd20677   250 DTISTALQWSLLYLIKYPEIQDKIQEE-IDEKIGLSRLPRfEDRKSLHYTEAFINEVFRhssFVPFTIP--HCTTADTTL 326

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 393 QNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS---LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20677   327 NGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVekvLIFGMGVRKCLGEDVARNEI 397
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 110-460 2.00e-09

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: 59.47  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 110 RPLlDPWlaYRQHRGHKcGVFLLNGPEWRVNR----LKLNPDVLSPQAVQKYIpmvdgvarDFSKALKARVLQNARGSlT 185
Cdd:cd20667    37 RPL-TPF--FRDLFGEK-GIICTNGLTWKQQRrfcmTTLRELGLGKQALESQI--------QHEAAELVKVFAQENGR-P 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 186 LDIQPSILNYTVEASNLALFGERLGllgpSPSPASLQFIRALEAMLkstaqlMFMprdlsrwtsARVWKEHFESWDYIFQ 265
Cdd:cd20667   104 FDPQDPIVHATANVIGAVVFGHRFS----SEDPIFLELIRAINLGL------AFA---------STIWGRLYDAFPWLMR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 266 YANNAIQKIYQELALGRpqhySGIVGELLMHADMTLEAVR-----------------------ANSI----ELTAGSVDT 318
Cdd:cd20667   165 YLPGPHQKIFAYHDAVR----SFIKKEVIRHELRTNEAPQdfidcylaqitktkddpvstfseENMIqvviDLFLGGTET 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 319 TAYPLLMTLFELARNPDVQQALRQE--SLV--AEAGITENPQRatteLPLLRAALKETLRLYPV-GISLDRQVGSDVVLQ 393
Cdd:cd20667   241 TATTLHWALLYMVHHPEIQEKVQQEldEVLgaSQLICYEDRKR----LPYTNAVIHEVQRLSNVvSVGAVRQCVTSTTMH 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112896241 394 NYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSS-GTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20667   317 GYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNfVMNEAFLPFSAGHRVCLGEQLARMEL 384
PLN02971 PLN02971
tryptophan N-hydroxylase
 299-450 3.38e-09

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 59.28  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDV--------QQALRQESLVAEAGITEnpqratteLPLLRAALK 370
Cdd:PLN02971  323 LTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEIlhkameeiDRVVGKERFVQESDIPK--------LNYVKAIIR 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 371 ETLRLYPVG-ISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS----LAFGF 445
Cdd:PLN02971  395 EAFRLHPVAaFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENdlrfISFST 474


                  ....*
gi 2112896241 446 GLRQC 450
Cdd:PLN02971  475 GKRGC 479
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 311-460 4.23e-09

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: 58.31  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQESLvaeagitenpqrattelpLLRAALKETLRLY-PVGISLDRQVGSD 389
Cdd:cd11029   220 LVAGH-ETTVNLIGNGVLALLTHPDQLALLRADPE------------------LWPAAVEELLRYDgPVALATLRFATED 280

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 390 VVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11029   281 VEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR--------DANGHLAFGHGIHYCLGAPLARLEA 343
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 296-460 4.53e-09

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: 58.43  E-value: 4.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 296 HADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALrQESLVAEAGITENP-QRATTELPLLRAALKETLR 374
Cdd:cd20665   219 QSEFTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKV-QEEIDRVIGRHRSPcMQDRSHMPYTDAVIHEIQR 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 375 ---LYPVGisLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQC 450
Cdd:cd20665   298 yidLVPNN--LPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYfMPFSAGKRIC 375

                         170
                  ....*....|
gi 2112896241 451 LGRRLAETEM 460
Cdd:cd20665   376 AGEGLARMEL 385
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 311-460 5.80e-09

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


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 58.17  E-value: 5.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSVdTTAYPLLMTLFELARNPDVQQALRQEsLVAEAGITENPQRA-TTELPLLRAALKETLR---LYPVGisLDRQV 386
Cdd:cd20663   239 FSAGMV-TTSTTLSWALLLMILHPDVQRRVQQE-IDEVIGQVRRPEMAdQARMPYTNAVIHEVQRfgdIVPLG--VPHMT 314

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112896241 387 GSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20663   315 SRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAfMPFSAGRRACLGEPLARMEL 389
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 317-460 8.86e-09

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 57.87  E-value: 8.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENP-------QRAT-----------TELPLLRAALKETLRLY 376
Cdd:PLN03195  306 DTTATTLSWFVYMIMMNPHVAEKLYSElkALEKERAKEEDPedsqsfnQRVTqfaglltydslGKLQYLHAVITETLRLY 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 377 PvGISLDRQ--VGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF-PRPERYHPRRWLDSRSSGTRSP--SLAFGFGLRQCL 451
Cdd:PLN03195  386 P-AVPQDPKgiLEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVFQNASPfkFTAFQAGPRICL 464


                  ....*....
gi 2112896241 452 GRRLAETEM 460
Cdd:PLN03195  465 GKDSAYLQM 473
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 317-460 1.65e-08

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 56.94  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQESlvaeagITENPQRATTELPLLRAALKETLRLYP-VGISLDRQVGSDVVLQNY 395
Cdd:PLN02169  315 DTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPpLPFNHKAPAKPDVLPSGH 388

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 396 HIPAGTVVKVLLYSLGRNPSVFPR-PERYHPRRWLDSRSSGTRSPS---LAFGFGLRQCLGRRLAETEM 460
Cdd:PLN02169  389 KVDAESKIVICIYALGRMRSVWGEdALDFKPERWISDNGGLRHEPSykfMAFNSGPRTCLGKHLALLQM 457
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 296-460 1.73e-08

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


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 56.60  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 296 HADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENPqraTTELPLLRAALKETL 373
Cdd:cd20616   217 RGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEiqTVLGERDIQNDD---LQKLKVLENFINESM 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 374 RLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPsVFPRPERYHPRRWLDSRSSGTRSPslaFGFGLRQCLGR 453
Cdd:cd20616   294 RYQPVVDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEKNVPSRYFQP---FGFGPRSCVGK 369


                  ....*..
gi 2112896241 454 RLAETEM 460
Cdd:cd20616   370 YIAMVMM 376
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 296-460 1.96e-08

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: 56.47  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 296 HADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGITENPQRAttELPLLRAALKETL 373
Cdd:cd20670   219 HTEFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEinQVIGPHRLPSVDDRV--KMPYTDAVIHEIQ 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 374 RL---YPVGISldRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS-LAFGFGLRQ 449
Cdd:cd20670   297 RLtdiVPLGVP--HNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAfVPFSSGKRV 374

                         170
                  ....*....|.
gi 2112896241 450 CLGRRLAETEM 460
Cdd:cd20670   375 CLGEAMARMEL 385
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 330-460 2.07e-08

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: 56.21  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 330 LARNPDVQQALRQeslvaeagitenpqrATTELPllrAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYS 409
Cdd:cd11079   210 LARHPELQARLRA---------------NPALLP---AAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWAS 271

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 410 LGRNPSVFPRPERYHPRRWLDSrssgtrspSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd11079   272 ANRDERVFGDPDEFDPDRHAAD--------NLVYGRGIHVCPGAPLARLEL 314
PLN02290 PLN02290
cytokinin trans-hydroxylase
 317-459 2.34e-08

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 56.36  E-value: 2.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDVQQALRQEslVAEAGITENPQ-RATTELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNY 395
Cdd:PLN02290  330 ETTALLLTWTLMLLASNPTWQDKVRAE--VAEVCGGETPSvDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDL 407

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2112896241 396 HIPAGTVVKVLLYSL-------GRNPSVFpRPERYHPRRWLDSRSsgtrspSLAFGFGLRQCLGRRLAETE 459
Cdd:PLN02290  408 HIPKGLSIWIPVLAIhhseelwGKDANEF-NPDRFAGRPFAPGRH------FIPFAAGPRNCIGQAFAMME 471
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 302-456 4.34e-08

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 54.80  E-value: 4.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 302 EAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQeslvaeagiteNPQRAttelpllRAALKETLRLYPVGIS 381
Cdd:cd11036   176 GDLVANAILLAVQGAEAAAGLVGNAVLALLRRPAQWARLRP-----------DPELA-------AAAVAETLRYDPPVRL 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2112896241 382 LDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQCLGRRLA 456
Cdd:cd11036   238 ERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR--------PTARSAHFGLGRHACLGAALA 304
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 140-457 7.66e-08

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 54.47  E-value: 7.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 140 NRLKLNPDVLSPQAVQKYIPMVDGVARDFSKALKArvlqnargsltldiQPSILNYTVEASNLALFGERLGLLGPSPSPA 219
Cdd:cd20637    81 HKRKVFSKLFSHEALESYLPKIQQVIQDTLRVWSS--------------NPEPINVYQEAQKLTFRMAIRVLLGFRVSEE 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 220 SLQFIraLEAMLKSTAQLMFMPRDL-----SRWTSARvwkehfeswDYIFQYANNAIQkiyQELALGRPQHYSGIVGELL 294
Cdd:cd20637   147 ELSHL--FSVFQQFVENVFSLPLDLpfsgyRRGIRAR---------DSLQKSLEKAIR---EKLQGTQGKDYADALDILI 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 295 MHA-----DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQE----SLVAEAGITENPQRATT--ELP 363
Cdd:cd20637   213 ESAkehgkELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREElrsnGILHNGCLCEGTLRLDTisSLK 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 364 LLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVkvlLYSL---GRNPSVFPRPERYHPRRWLDSRSS--GTRS 438
Cdd:cd20637   293 YLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSV---LYSIrdtHDTAPVFKDVDAFDPDRFGQERSEdkDGRF 369

                         330
                  ....*....|....*....
gi 2112896241 439 PSLAFGFGLRQCLGRRLAE 457
Cdd:cd20637   370 HYLPFGGGVRTCLGKQLAK 388
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 317-456 8.11e-08

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: 54.39  E-value: 8.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 317 DTTAYPLLMTLFELARNPDvqqalRQESLVAEAGITENPQrattELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYH 396
Cdd:cd20624   205 DAAGMALLRALALLAAHPE-----QAARAREEAAVPPGPL----ARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRT 275

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 397 IPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTrSPSLAFGFGLRQCLGRRLA 456
Cdd:cd20624   276 VPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQPD-EGLVPFSAGPARCPGENLV 334
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 66-457 1.10e-07

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 54.05  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241  66 LEMHRtfQELGPIFRYDVGGTHMVYVMLPEDVESLQRAES-------PQPWRPLLDPWLAYRQHRG-HKcgvfllngpew 137
Cdd:cd20638    14 LQMKR--QKYGYIYKTHLFGRPTVRVMGAENVRQILLGEHklvsvqwPASVRTILGSGCLSNLHDSqHK----------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 138 rvNRLKLNPDVLSPQAVQKYIPMVdgvardfSKALKARVLQnargslTLDIQPSILNYTVEASNLALFGERLgLLGPSPS 217
Cdd:cd20638    81 --HRKKVIMRAFSREALENYVPVI-------QEEVRSSVNQ------WLQSGPCVLVYPEVKRLMFRIAMRI-LLGFEPQ 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 218 PAS----LQFIRALEAMLKStaqLMFMPRD-----LSRWTSARvwkehfeswDYIFQYANNAIQKIYQELALGrpQHYSG 288
Cdd:cd20638   145 QTDreqeQQLVEAFEEMIRN---LFSLPIDvpfsgLYRGLRAR---------NLIHAKIEENIRAKIQREDTE--QQCKD 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 289 IVGELLMHAD-----MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslVAEAGI-----TENPQRA 358
Cdd:cd20638   211 ALQLLIEHSRrngepLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKE--LQEKGLlstkpNENKELS 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 359 TTELPLLR---AALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVkvlLYSLGRNPSV---FPRPERYHPRRWLDSR 432
Cdd:cd20638   289 MEVLEQLKytgCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNV---IYSICDTHDVadiFPNKDEFNPDRFMSPL 365

                         410       420
                  ....*....|....*....|....*.
gi 2112896241 433 -SSGTRSPSLAFGFGLRQCLGRRLAE 457
Cdd:cd20638   366 pEDSSRFSFIPFGGGSRSCVGKEFAK 391
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 261-457 5.30e-07

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: 51.76  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 261 DYIFQYANNAIQkiyQELALGRPQHYSGIVGELLMHA-----DMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPD 335
Cdd:cd20636   183 DILHEYMEKAIE---EKLQRQQAAEYCDALDYMIHSArengkELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPS 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 336 VQQALRQEsLVAEaGITENPQRATTELPL--------LRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVkvlL 407
Cdd:cd20636   260 AIEKIRQE-LVSH-GLIDQCQCCPGALSLeklsrlryLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGWSV---M 334

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2112896241 408 YSLG---------RNPSVFPrPERYHPRRwldSRSSGTRSPSLAFGFGLRQCLGRRLAE 457
Cdd:cd20636   335 YSIRdthetaavyQNPEGFD-PDRFGVER---EESKSGRFNYIPFGGGVRSCIGKELAQ 389
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
 258-458 1.20e-06

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 50.51  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 258 ESWDYIFQYANNAIQKIYQELALGrPQhysGIVGELLMHADMTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQ 337
Cdd:cd20619   149 VAFGYLSARVAEMLEDKRVNPGDG-LA---DSLLDAARAGEITESEAIATILVFYAVGHMAIGYLIASGIELFARRPEVF 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 338 QALRqeslvaeagiTENPQRattelpllRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVF 417
Cdd:cd20619   225 TAFR----------NDESAR--------AAIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVF 286

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2112896241 418 PRPERYHPRRWLDSrssgtrSPSLAFGFGLRQCLGRRLAET 458
Cdd:cd20619   287 DDPDVFDHTRPPAA------SRNLSFGLGPHSCAGQIISRA 321
PLN02738 PLN02738
carotene beta-ring hydroxylase
 311-459 1.81e-06

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 50.68  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGSvDTTAYPLLMTLFELARNPDVQQALRQE--SLVAEAGIT-ENPQ--RATTELpllraaLKETLRLYPVGISLDRQ 385
Cdd:PLN02738  400 LIAGH-ETSAAVLTWTFYLLSKEPSVVAKLQEEvdSVLGDRFPTiEDMKklKYTTRV------INESLRLYPQPPVLIRR 472

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112896241 386 VGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRW-LDS---RSSGTRSPSLAFGFGLRQCLGRRLAETE 459
Cdd:PLN02738  473 SLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpLDGpnpNETNQNFSYLPFGGGPRKCVGDMFASFE 550
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 294-452 2.10e-06

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: 49.81  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 294 LMHAD--MTLEAVRANSIELTAGSVDTTAYPLLMTLFELARNPDVQQALRQEslvaeagitenpqrattELPLLRAaLKE 371
Cdd:cd11039   191 MLNAGmpMSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAEVMAG-----------------DVHWLRA-FEE 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 372 TLR-LYPVGISlDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRwldsrssgTRSPSLAFGFGLRQC 450
Cdd:cd11039   253 GLRwISPIGMS-PRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFR--------PKSPHVSFGAGPHFC 323


                  ..
gi 2112896241 451 LG 452
Cdd:cd11039   324 AG 325
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 299-459 5.50e-06

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 48.58  E-value: 5.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 299 MTLEAVRANSIELTAGSVDTTayPLLMTL---FeLARNPDVQQALRQESLVAEAGITENPQRAT----TELPLLRAALKE 371
Cdd:PLN03141  247 LTDDLISDNMIDMMIPGEDSV--PVLMTLavkF-LSDCPVALQQLTEENMKLKRLKADTGEPLYwtdyMSLPFTQNVITE 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 372 TLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLD-SRSSGTRSPslaFGFGLRQC 450
Cdd:PLN03141  324 TLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEkDMNNSSFTP---FGGGQRLC 400


                  ....*....
gi 2112896241 451 LGRRLAETE 459
Cdd:PLN03141  401 PGLDLARLE 409
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 327-460 5.88e-06

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: 48.52  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 327 LFELARNPDVQQALRQE--SLVAEAGITENP--------QRATTELPLLRAALKETLRLyPVGISLDRQVGSDVVL---- 392
Cdd:cd20633   248 LLYLLKHPEAMKAVREEveQVLKETGQEVKPggplinltRDMLLKTPVLDSAVEETLRL-TAAPVLIRAVVQDMTLkman 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 393 -QNYHIPAGTVVKVLLY-SLGRNPSVFPRPERYHPRRWLDSRSS----------GTRSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20633   327 gREYALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFLNPDGGkkkdfykngkKLKYYNMPWGAGVSICPGRFFAVNEM 406
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 311-460 2.57e-05

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 46.51  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 311 LTAGsVDTTAYPLLMTLFELARNPDVQQALRQE-----SLVAEAGITENPQRATteLPLLRAALKETLRLYPVGISLDRQ 385
Cdd:PLN02987  276 LVAG-YETTSTIMTLAVKFLTETPLALAQLKEEhekirAMKSDSYSLEWSDYKS--MPFTQCVVNETLRVANIIGGIFRR 352

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2112896241 386 VGSDVVLQNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDsrSSGTRSPS---LAFGFGLRQCLGRRLAETEM 460
Cdd:PLN02987  353 AMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQS--NSGTTVPSnvfTPFGGGPRLCPGYELARVAL 428
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 323-458 5.46e-05

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: 45.71  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 323 LLMTLF-ELAR-NPDVQQALRQESLVAEAGITENPQRATTELPLLRAALKETLRLYPvGISL-------DRQVGSDVvlQ 393
Cdd:cd11071   244 LLPSLLaRLGLaGEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHP-PVPLqygrarkDFVIESHD--A 320

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2112896241 394 NYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLD-----------SRSSGTRSPSLafgfGLRQCLGRRLAET 458
Cdd:cd11071   321 SYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGeegkllkhliwSNGPETEEPTP----DNKQCPGKDLVVL 392
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 268-460 9.82e-05

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 44.62  E-value: 9.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 268 NNAIQKIYQElalgrpqHYSG--------IVGELLMHA-DMTLEAVRANSI----------ELTAGSVDTTAYPLLMTLF 328
Cdd:cd20676   190 NSFLQKIVKE-------HYQTfdkdnirdITDSLIEHCqDKKLDENANIQLsdekivnivnDLFGAGFDTVTTALSWSLM 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 329 ELARNPDVQQALrQESLVAEAGITENPQ---RAttELPLLRAALKETLR---LYPVGI--SLDRqvgsDVVLQNYHIPAG 400
Cdd:cd20676   263 YLVTYPEIQKKI-QEELDEVIGRERRPRlsdRP--QLPYLEAFILETFRhssFVPFTIphCTTR----DTSLNGYYIPKD 335

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2112896241 401 TVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGTRSPS----LAFGFGLRQCLGRRLAETEM 460
Cdd:cd20676   336 TCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKTEsekvMLFGLGKRRCIGESIARWEV 399
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 326-460 3.68e-04

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: 43.14  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 326 TLFELARNPDVQQALRQE--SLVAEAGITENP--------QRATTELPLLRAALKETLRLYPVGISLdRQVGSDVVL--- 392
Cdd:cd20631   250 SLFYLLRCPEAMKAATKEvkRTLEKTGQKVSDggnpivltREQLDDMPVLGSIIKEALRLSSASLNI-RVAKEDFTLhld 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 393 --QNYHIPAGTVVKVLLYSLGRNPSVFPRPERYHPRRWLDSRSSGT----------RSPSLAFGFGLRQCLGRRLAETEM 460
Cdd:cd20631   329 sgESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKttfykngrklKYYYMPFGSGTSKCPGRFFAINEI 408
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 330-430 3.22e-03

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 39.82  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2112896241 330 LARNPDVQQALRQEslvaeagitenpqrattELPLLRAALKETLRLYPVGISLDRQVGSDVVLQNYHIPAGTVVkVL-LY 408
Cdd:cd11067   247 LHEHPEWRERLRSG-----------------DEDYAEAFVQEVRRFYPFFPFVGARARRDFEWQGYRFPKGQRV-LLdLY 308

                          90       100
                  ....*....|....*....|..
gi 2112896241 409 SLGRNPSVFPRPERYHPRRWLD 430
Cdd:cd11067   309 GTNHDPRLWEDPDRFRPERFLG 330
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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