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Conserved domains on  [gi|4503211|ref|NP_000775|]
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sterol 26-hydroxylase, mitochondrial precursor [Homo sapiens]

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 ...
89-524 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 cd20646:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 430  Bit Score: 805.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20646   1 KKIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  169 AEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20646  81 KEVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  249 QNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaaGPDGIQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20646 161 KLSEIVTLLPKWTRPYLPFWKRYVDAWDTIFSFGKKLIDKKMEEIEERV---DRGEPVEGEYLTYLLSSGKLSPKEVYGS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRII- 407
Cdd:cd20646 238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIv 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20646 318 EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGG----LKHHPFGSIPFGYGVRACVGRRIAELEMY 393
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503211  488 LLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20646 394 LALSRLIKRFEVRPDPSGGEVKAITRTLLVPNKPINL 430
 
Name Accession Description Interval E-value
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
89-524 0e+00

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: 805.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20646   1 KKIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  169 AEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20646  81 KEVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  249 QNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaaGPDGIQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20646 161 KLSEIVTLLPKWTRPYLPFWKRYVDAWDTIFSFGKKLIDKKMEEIEERV---DRGEPVEGEYLTYLLSSGKLSPKEVYGS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRII- 407
Cdd:cd20646 238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIv 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20646 318 EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGG----LKHHPFGSIPFGYGVRACVGRRIAELEMY 393
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503211  488 LLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20646 394 LALSRLIKRFEVRPDPSGGEVKAITRTLLVPNKPINL 430
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
61-526 4.69e-135

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: 399.35  E-value: 4.69e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211     61 PRLGQLRFFFQLFVQ-GYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQ 139
Cdd:pfam00067   1 PPGPPPLPLFGNLLQlGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    140 HDLTYGPFTTEGHHWYQLRQALNQRLLKPaEAALYTDAFNEVIDDFMTRLDQLRAEsasgNQVSDMAQLFYYFALEAICY 219
Cdd:pfam00067  81 PFLGKGIVFANGPRWRQLRRFLTPTFTSF-GKLSFEPRVEEEARDLVEKLRKTAGE----PGVIDITDLLFRAALNVICS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    220 ILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTrpVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQA 299
Cdd:pfam00067 156 ILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPI--LKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    300 AgpDGIQVSGYLHFLLAS-----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQV 374
Cdd:pfam00067 234 A--KKSPRDFLDALLLAKeeedgSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    375 PQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNS 453
Cdd:pfam00067 312 PTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDEN 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503211    454 QPatprIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLV-PNKKVGLQF 526
Cdd:pfam00067 392 GK----FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLlPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
90-516 1.35e-46

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: 167.38  E-value: 1.35e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   90 AKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYpvRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALnQRLLKPA 169
Cdd:COG2124  29 REYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTF--SSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLV-QPAFTPR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  170 EAALYTDAFNEVIDDFMTRLdqlrAESASGNQVSDMAQLFyyfALEAICYILfekrigclqrSIPEDTVTFVRSIGLMFQ 249
Cdd:COG2124 106 RVAALRPRIREIADELLDRL----AARGPVDLVEEFARPL---PVIVICELL----------GVPEEDRDRLRRWSDALL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  250 NSLyatflpkwTRPVLPFWKRYLDGWNAIFSFGKKLIDEKledmeaqlQAAGPDGIqvsgyLHFLLAS----GQLSPREA 325
Cdd:COG2124 169 DAL--------GPLPPERRRRARRARAELDAYLRELIAER--------RAEPGDDL-----LSALLAArddgERLSDEEL 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  326 MGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVvgvvpagqvpqhkdfahmPLLKAVLKETLRLYPVVPTNSR 405
Cdd:COG2124 228 RDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPR 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  406 IIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatpriqHPFGSVPFGYGVRACLGRRIAELE 485
Cdd:COG2124 290 TATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------------PPNAHLPFGGGPHRCLGAALARLE 356
                       410       420       430
                ....*....|....*....|....*....|.
gi 4503211  486 MQLLLARLIQKYKVVLAPETGELKSVARIVL 516
Cdd:COG2124 357 ARIALATLLRRFPDLRLAPPEELRWRPSLTL 387
PLN02687 PLN02687
flavonoid 3'-monooxygenase
318-502 1.49e-26

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 112.98  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   318 GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLY 397
Cdd:PLN02687 291 GRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLH 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   398 PVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQ-HPFGSVPFGYGVRA 475
Cdd:PLN02687 371 PSTPLSlPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKgSDFELIPFGAGRRI 450
                        170       180
                 ....*....|....*....|....*..
gi 4503211   476 CLGRRIAELEMQLLLARLIQKYKVVLA 502
Cdd:PLN02687 451 CAGLSWGLRMVTLLTATLVHAFDWELA 477
 
Name Accession Description Interval E-value
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
89-524 0e+00

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: 805.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20646   1 KKIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  169 AEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20646  81 KEVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  249 QNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaaGPDGIQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20646 161 KLSEIVTLLPKWTRPYLPFWKRYVDAWDTIFSFGKKLIDKKMEEIEERV---DRGEPVEGEYLTYLLSSGKLSPKEVYGS 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRII- 407
Cdd:cd20646 238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIv 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20646 318 EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGG----LKHHPFGSIPFGYGVRACVGRRIAELEMY 393
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503211  488 LLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20646 394 LALSRLIKRFEVRPDPSGGEVKAITRTLLVPNKPINL 430
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
91-522 1.19e-178

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: 509.38  E-value: 1.19e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd11054   3 KYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRPKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  171 AALYTDAFNEVIDDFMTRLDQLRAESasGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQN 250
Cdd:cd11054  83 VASYLPAINEVADDFVERIRRLRDED--GEEVPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIFES 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  251 SLYATFLPKWTRPV-LPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGPDgiqvSGYLHFLLASGQLSPREAMGSL 329
Cdd:cd11054 161 SAKLMFGPPLWKYFpTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDEEE----DSLLEYLLSKPGLSKKEIVTMA 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  330 PELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEK 409
Cdd:cd11054 237 LDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPK 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  410 EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpaTPRIQHPFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd11054 317 DIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDS--ENKNIHPFASLPFGFGPRMCIGRRFAELEMYLL 394
                       410       420       430
                ....*....|....*....|....*....|...
gi 4503211  490 LARLIQKYKVVlaPETGELKSVARIVLVPNKKV 522
Cdd:cd11054 395 LAKLLQNFKVE--YHHEELKVKTRLILVPDKPL 425
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
89-524 3.54e-152

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: 442.27  E-value: 3.54e-152
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   89 KAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKP 168
Cdd:cd20648   2 KAKYGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSSWKDYRQLRGHAYGLLTAEGEEWQRLRSLLAKHMLKP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  169 AEAALYTDAFNEVIDDFMTRLDQLRAESaSGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF 248
Cdd:cd20648  82 KAVEAYAGVLNAVVTDLIRRLRRQRSRS-SPGVVKDIAGEFYKFGLEGISSVLFESRIGCLEANVPEETETFIQSINTMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  249 QNSLYATFLPKWTRPVLPF-WKRYLDGWNAIFSFGKKLIDEKLEDMEAQLqaagPDGIQVSG-YLHFLLASGQLSPREAM 326
Cdd:cd20648 161 VMTLLTMAMPKWLHRLFPKpWQRFCRSWDQMFAFAKGHIDRRMAEVAAKL----PRGEAIEGkYLTYFLAREKLPMKSIY 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  327 GSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRI 406
Cdd:cd20648 237 GNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARV 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  407 IEK-EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAtpriqHPFGSVPFGYGVRACLGRRIAELE 485
Cdd:cd20648 317 IPDrDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTH-----HPYASLPFGFGKRSCIGRRIAELE 391
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 4503211  486 MQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGL 524
Cdd:cd20648 392 VYLALARILTHFEVRPEPGGSPVKPMTRTLLVPERSINL 430
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
61-526 4.69e-135

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: 399.35  E-value: 4.69e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211     61 PRLGQLRFFFQLFVQ-GYALQLHQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQ 139
Cdd:pfam00067   1 PPGPPPLPLFGNLLQlGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    140 HDLTYGPFTTEGHHWYQLRQALNQRLLKPaEAALYTDAFNEVIDDFMTRLDQLRAEsasgNQVSDMAQLFYYFALEAICY 219
Cdd:pfam00067  81 PFLGKGIVFANGPRWRQLRRFLTPTFTSF-GKLSFEPRVEEEARDLVEKLRKTAGE----PGVIDITDLLFRAALNVICS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    220 ILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTrpVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQA 299
Cdd:pfam00067 156 ILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPI--LKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    300 AgpDGIQVSGYLHFLLAS-----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQV 374
Cdd:pfam00067 234 A--KKSPRDFLDALLLAKeeedgSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    375 PQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNS 453
Cdd:pfam00067 312 PTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDEN 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503211    454 QPatprIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLV-PNKKVGLQF 526
Cdd:pfam00067 392 GK----FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLlPPKPYKLKF 461
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
91-518 2.89e-131

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: 388.89  E-value: 2.89e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd20647   3 EYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWQEYRDLRGRSTGLISAEGEQWLKMRSVLRQKILRPRD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  171 AALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMF-- 248
Cdd:cd20647  83 VAVYSGGVNEVVADLIKRIKTLRSQEDDGETVTNVNDLFFKYSMEGVATILYECRLGCLENEIPKQTVEYIEALELMFsm 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  249 -QNSLYATFLPKWTRPVLPF-WKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQaagpDGIQVSG-YLHFLLASGQLSPREA 325
Cdd:cd20647 163 fKTTMYAGAIPKWLRPFIPKpWEEFCRSWDGLFKFSQIHVDNRLREIQKQMD----RGEEVKGgLLTYLLVSKELTLEEI 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  326 MGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSR 405
Cdd:cd20647 239 YANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNGR 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  406 IIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSqpATPRIQHpFGSVPFGYGVRACLGRRIAELE 485
Cdd:cd20647 319 VTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKD--ALDRVDN-FGSIPFGYGIRSCIGRRIAELE 395
                       410       420       430
                ....*....|....*....|....*....|...
gi 4503211  486 MQLLLARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd20647 396 IHLALIQLLQNFEIKVSPQTTEVHAKTHGLLCP 428
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
91-522 1.55e-99

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: 307.12  E-value: 1.55e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd20645   3 KFGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKPKE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  171 AALYTDAFNEVIDDFMTRLDQLRAESAsgnQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFqn 250
Cdd:cd20645  83 VMKLDGKINEVLADFMGRIDELCDETG---RVEDLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIKTMM-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  251 slyATFLPKWTRPV-------LPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAagpdgiqvsGYLHFLLASGQLSPR 323
Cdd:cd20645 158 ---STFGKMMVTPVelhkrlnTKVWQDHTEAWDNIFKTAKHCIDKRLQRYSQGPAN---------DFLCDIYHDNELSKK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  324 EAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN 403
Cdd:cd20645 226 ELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFT 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  404 SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAtpriqHPFGSVPFGYGVRACLGRRIAE 483
Cdd:cd20645 306 SRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHSI-----NPFAHVPFGIGKRMCIGRRLAE 380
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 4503211  484 LEMQLLLARLIQKYKVVlAPETGELKSVARIVLVPNKKV 522
Cdd:cd20645 381 LQLQLALCWIIQKYQIV-ATDNEPVEMLHSGILVPSREL 418
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
91-520 1.87e-82

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: 263.11  E-value: 1.87e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAE 170
Cdd:cd20643   3 KYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAPKV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  171 AALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQN 250
Cdd:cd20643  83 IDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMFHT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  251 SLYATFLPkwtrPVL------PFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGpdgiQVSGYLHFLLASGQLSPRE 324
Cdd:cd20643 163 TSPMLYIP----PDLlrlintKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKGKNEH----EYPGILANLLLQDKLPIED 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  325 AMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS 404
Cdd:cd20643 235 IKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQ 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  405 RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSqpatprIQHpFGSVPFGYGVRACLGRRIAEL 484
Cdd:cd20643 315 RYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKD------ITH-FRNLGFGFGPRQCLGRRIAET 387
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 4503211  485 EMQLLLARLIQKYKVVLAPETgELKSVARIVLVPNK 520
Cdd:cd20643 388 EMQLFLIHMLENFKIETQRLV-EVKTTFDLILVPEK 422
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
93-526 9.48e-73

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: 237.82  E-value: 9.48e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   93 GPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALNQRLLKPAEAA 172
Cdd:cd20644   5 GPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSPAAVQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  173 LYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSL 252
Cdd:cd20644  85 RFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVMLKTTV 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  253 YATFLP----KWTRPVLpfWKRYLDGWNAIFSFGKKLIDEKLEDMeaqlqAAGPDGiQVSGYLHFLLASGQLSPREAMGS 328
Cdd:cd20644 165 PLLFMPrslsRWISPKL--WKEHFEAWDCIFQYADNCIQKIYQEL-----AFGRPQ-HYTGIVAELLLQAELSLEAIKAN 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVvpAGQVPQH--KDFAHMPLLKAVLKETLRLYPVVPTNSRI 406
Cdd:cd20644 237 ITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAA--AAQISEHpqKALTELPLLKAALKETLRLYPVGITVQRV 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  407 IEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpriqhPFGSVPFGYGVRACLGRRIAELEM 486
Cdd:cd20644 315 PSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGR-----NFKHLAFGFGMRQCLGRRLAEAEM 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 4503211  487 QLLLARLIQKYKV-VLAPEtgELKSVARIVLVPNKKVGLQF 526
Cdd:cd20644 390 LLLLMHVLKNFLVeTLSQE--DIKTVYSFILRPEKPPLLTF 428
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
93-504 1.16e-67

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: 223.16  E-value: 1.16e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   93 GPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYPVRNDMELWKEHRDqhdLTYGPFTTEGHHWYQLRQALnQRLLKPAEAA 172
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDF---LGDGLLTLDGPEHRRLRRLL-APAFTPRALA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  173 LYTDAFNEVIDDFMTRLDQLraesasGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFqnsl 252
Cdd:cd00302  77 ALRPVIREIARELLDRLAAG------GEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRL---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  253 yatflpkWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDmeaqlqaagPDGIQVSGYLHFLLASGQLSPREAMGSLPEL 332
Cdd:cd00302 147 -------LRPLPSPRLRRLRRARARLRDYLEELIARRRAE---------PADDLDLLLLADADDGGGLSDEEIVAELLTL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  333 LMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAgqvPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIE 412
Cdd:cd00302 211 LLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGD---GTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVE 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  413 VDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRnsqpatPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLAR 492
Cdd:cd00302 288 LGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLP------EREEPRYAHLPFGAGPHRCLGARLARLELKLALAT 361
                       410
                ....*....|..
gi 4503211  493 LIQKYKVVLAPE 504
Cdd:cd00302 362 LLRRFDFELVPD 373
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
147-518 1.45e-62

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: 210.84  E-value: 1.45e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  147 FTTEGHHWYQLRQALN----QRLLKPaeaalYTDAFNEVIDDFMTRLDQLraesaSGNQVSDMAQLFYYFALEAICYILF 222
Cdd:cd20628  50 LTSTGEKWRKRRKLLTpafhFKILES-----FVEVFNENSKILVEKLKKK-----AGGGEFDIFPYISLCTLDIICETAM 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  223 EKRIGCLQrsipEDTVTFVRSIglmfqNSLYATFLPKWTRPVL---PFWKRYLDGW------NAIFSFGKKLIDEKLEDM 293
Cdd:cd20628 120 GVKLNAQS----NEDSEYVKAV-----KRILEIILKRIFSPWLrfdFIFRLTSLGKeqrkalKVLHDFTNKVIKERREEL 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  294 EAQLQAAGPDGIQVSG----YLHFLLAS----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEV 365
Cdd:cd20628 191 KAEKRNSEEDDEFGKKkrkaFLDLLLEAhedgGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEEL 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  366 VGVV-PAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESF 444
Cdd:cd20628 271 DEIFgDDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKF 350
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503211  445 QPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd20628 351 DPDRFL----PENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGEDLKLIAEIVLRS 420
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
91-520 6.73e-61

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: 206.28  E-value: 6.73e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLG--PQMHVnlaSAP-LLEQVMRQE-----GKYPVRNDMELWKEHRdqhdltygpFTTEGHHWYQLRQALN 162
Cdd:cd11055   1 KYGKVFGLYFGtiPVIVV---SDPeMIKEILVKEfsnftNRPLFILLDEPFDSSL---------LFLKGERWKRLRTTLS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  163 QRL----LKpaeaaLYTDAFNEVIDDFMTRLDQLraesASGNQVSDMAQLFYYFALEAICYILFEkrIGCLQRSIPEDTv 238
Cdd:cd11055  69 PTFssgkLK-----LMVPIINDCCDELVEKLEKA----AETGKPVDMKDLFQGFTLDVILSTAFG--IDVDSQNNPDDP- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  239 tFVRSIGLMFQNS---LYATFLPKWTRPVLPFWKRYLDGWNAIFSFG---KKLIDEKLEDMEAQ----LQA---AGPDGI 305
Cdd:cd11055 137 -FLKAAKKIFRNSiirLFLLLLLFPLRLFLFLLFPFVFGFKSFSFLEdvvKKIIEQRRKNKSSRrkdlLQLmldAQDSDE 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  306 QVSgylhfllaSGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPL 385
Cdd:cd11055 216 DVS--------KKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKY 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  386 LKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsqPATPRIQHPFG 465
Cdd:cd11055 288 LDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFS----PENKAKRHPYA 363
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4503211  466 SVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET-GELKSVARIVLVPNK 520
Cdd:cd11055 364 YLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETeIPLKLVGGATLSPKN 419
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
99-499 1.58e-58

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: 200.13  E-value: 1.58e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   99 YLGPQMHVNLASAPLLEQVMRQEGKYPV-RNDMELWKEHRDQHDLtygpFTTEGHHWYQLRQ-ALNQ-RLLKpaeaalYT 175
Cdd:cd20617   7 WLGDVPTVVLSDPEIIKEAFVKNGDNFSdRPLLPSFEIISGGKGI----LFSNGDYWKELRRfALSSlTKTK------LK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  176 DAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRsipEDTVTFVRSIGLMFQ--NSLY 253
Cdd:cd20617  77 KKMEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDD---GEFLKLVKPIEEIFKelGSGN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  254 ATFLPKWTRPVLPFWKRYLDGW-NAIFSFGKKLIDEKLEDMEAQlqaagpDGIQVSGYLHFLLASGQLSPREAMGSLP-- 330
Cdd:cd20617 154 PSDFIPILLPFYFLYLKKLKKSyDKIKDFIEKIIEEHLKTIDPN------NPRDLIDDELLLLLKEGDSGLFDDDSIIst 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  331 --ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRII 407
Cdd:cd20617 228 clDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGlPRVT 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpaTPRIQHpfgSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20617 308 TEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDG--NKLSEQ---FIPFGIGKRNCVGENLARDELF 382
                       410
                ....*....|..
gi 4503211  488 LLLARLIQKYKV 499
Cdd:cd20617 383 LFFANLLLNFKF 394
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
156-507 1.28e-55

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: 192.05  E-value: 1.28e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  156 QLRQALNQRLlkpAEAAL--YTDAFNEVIDDFMTRLDQLRAESASGnqVSDMAQLFYYFALEAICYILFEKRIGCLQRS- 232
Cdd:cd11061  56 RRRRVWSHAF---SDKALrgYEPRILSHVEQLCEQLDDRAGKPVSW--PVDMSDWFNYLSFDVMGDLAFGKSFGMLESGk 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  233 ---IPEDTVTFVRSIGLMfqnsLYATFLPKWTRpVLPFWKRYLDGWNAIFSFGKKLIDEKLedmeaQLQAAGPDGIqvsg 309
Cdd:cd11061 131 dryILDLLEKSMVRLGVL----GHAPWLRPLLL-DLPLFPGATKARKRFLDFVRAQLKERL-----KAEEEKRPDI---- 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  310 yLHFLLAS------GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQ-VPQHKDFAH 382
Cdd:cd11061 197 -FSYLLEAkdpetgEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDeIRLGPKLKS 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  383 MPLLKAVLKETLRLYPVVPTN-SRIIEKE-IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpRI 460
Cdd:cd11061 276 LPYLRACIDEALRLSPPVPSGlPRETPPGgLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELV-RA 354
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 4503211  461 QHPFgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP-ETGE 507
Cdd:cd11061 355 RSAF--IPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPgEDGE 400
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
145-520 3.95e-51

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: 180.54  E-value: 3.95e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  145 GPFTTEGHHWYQLRQALNqRLLKPAEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEK 224
Cdd:cd11069  52 GLLAAEGEEHKRQRKILN-PAFSYRHVKELYPIFWSKAEELVDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGY 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  225 RIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVLPFW-----KRYLDGWNAIFSFGKKLIDEKLEDMEAQLQA 299
Cdd:cd11069 131 DFDSLENPDNELAEAYRRLFEPTLLGSLLFILLLFLPRWLVRILpwkanREIRRAKDVLRRLAREIIREKKAALLEGKDD 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  300 AGPDGIQVsgylhfLLASGQ------LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPA-- 371
Cdd:cd11069 211 SGKDILSI------LLRANDfadderLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDpp 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  372 GQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWL 450
Cdd:cd11069 285 DGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWL 364
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503211  451 RNSQPATPRIQHPFGS-VPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKsVARIVLVPNK 520
Cdd:cd11069 365 EPDGAASPGGAGSNYAlLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVER-PIGIITRPPV 434
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
164-499 1.77e-50

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: 178.65  E-value: 1.77e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  164 RLLKPA--EAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDtvtfv 241
Cdd:cd11059  60 RLLSGVysKSSLLRAAMEPIIRERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDS----- 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  242 RSIGLMFqnsLYATFLPKWTRPVLPFWKR---------YLDGWNAIFSFGKKLIDEKLEDmeAQLQAAGPDGIQVSGYLH 312
Cdd:cd11059 135 RERELLR---RLLASLAPWLRWLPRYLPLatsrliigiYFRAFDEIEEWALDLCARAESS--LAESSDSESLTVLLLEKL 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  313 FLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGV-VPAGQVPQHKDFAHMPLLKAVLK 391
Cdd:cd11059 210 KGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLpGPFRGPPDLEDLDKLPYLNAVIR 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  392 ETLRLYPVVP-TNSRII-EKEIEVDGFLFPKNTQfVFCH-YVVSRDPTAFSEPESFQPHRWLrNSQPATPRIQHPFgSVP 468
Cdd:cd11059 290 ETLRLYPPIPgSLPRVVpEGGATIGGYYIPGGTI-VSTQaYSLHRDPEVFPDPEEFDPERWL-DPSGETAREMKRA-FWP 366
                       330       340       350
                ....*....|....*....|....*....|.
gi 4503211  469 FGYGVRACLGRRIAELEMQLLLARLIQKYKV 499
Cdd:cd11059 367 FGSGSRMCIGMNLALMEMKLALAAIYRNYRT 397
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
99-503 2.15e-49

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: 175.07  E-value: 2.15e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   99 YLGPQMHVNLASAPLLEQVMRQE-GKYPVRNDMELWKEHrdqhdLTYGPFTTEGHHWyqLRQalnQRLLKPAEA----AL 173
Cdd:cd20620   7 RLGPRRVYLVTHPDHIQHVLVTNaRNYVKGGVYERLKLL-----LGNGLLTSEGDLW--RRQ---RRLAQPAFHrrriAA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  174 YTDAFNEVIDDFMTRLDQlRAESASGNQVSDMAQLfyyfALEAICYILFEKRIGCLQRSIPEDTVTFVRSIglmfqNSLY 253
Cdd:cd20620  77 YADAMVEATAALLDRWEA-GARRGPVDVHAEMMRL----TLRIVAKTLFGTDVEGEADEIGDALDVALEYA-----ARRM 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  254 ATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAqlqaaGPDGIQVsgylhfLLAS------GQLSPR---- 323
Cdd:cd20620 147 LSPFLLPLWLPTPANRRFRRARRRLDEVIYRLIAERRAAPAD-----GGDLLSM------LLAArdeetgEPMSDQqlrd 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  324 EAMGslpeLLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN 403
Cdd:cd20620 216 EVMT----LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVL-GGRPPTAEDLPQLPYTEMVLQESLRLYPPAWII 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  404 SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRiqhpFGSVPFGYGVRACLGRRIAE 483
Cdd:cd20620 291 GREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPR----YAYFPFGGGPRICIGNHFAM 366
                       410       420
                ....*....|....*....|
gi 4503211  484 LEMQLLLARLIQKYKVVLAP 503
Cdd:cd20620 367 MEAVLLLATIAQRFRLRLVP 386
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
149-503 3.84e-49

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: 175.01  E-value: 3.84e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  149 TEGHH--WYQLRQALNqrllkPAEAALY----TDAFNEVIDDFMTRLDQLraesASGNQVSDMAQLFYYFALEAICYILF 222
Cdd:cd20613  67 TEVDHekWKKRRAILN-----PAFHRKYlknlMDEFNESADLLVEKLSKK----ADGKTEVNMLDEFNRVTLDVIAKVAF 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  223 ekriGCLQRSIPEDTVTFVRSIGLMFQnSLYATFLPKWTRPvLPF-WK---------RYLDGwnaifsFGKKLIDEKLED 292
Cdd:cd20613 138 ----GMDLNSIEDPDSPFPKAISLVLE-GIQESFRNPLLKY-NPSkRKyrrevreaiKFLRE------TGRECIEERLEA 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  293 MEAQLQAagPDGIqvsgyLHFLLASGQLSPREAMGSLPE----LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGV 368
Cdd:cd20613 206 LKRGEEV--PNDI-----LTHILKASEEEPDFDMEELLDdfvtFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEV 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  369 VPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHR 448
Cdd:cd20613 279 LGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPER 358
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 4503211  449 WLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd20613 359 FS----PEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELVP 409
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
200-518 1.13e-48

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: 173.54  E-value: 1.13e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  200 NQVSDMAQLFYYFALEAICYILF----EKRIGCLQRSIPeDTVTFVRSIGLMFqnslyaTFLPKWTRPVLPfWKRYLDGW 275
Cdd:cd11053 108 GQPFDLRELMQEITLEVILRVVFgvddGERLQELRRLLP-RLLDLLSSPLASF------PALQRDLGPWSP-WGRFLRAR 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  276 NAIfsfgKKLIDEKLEDMEAQLQAAGPDgiqvsgYLHFLLASG-----QLSPREAMGSLPELLMAGVDTTSNTLTWALYH 350
Cdd:cd11053 180 RRI----DALIYAEIAERRAEPDAERDD------ILSLLLSARdedgqPLSDEELRDELMTLLFAGHETTATALAWAFYW 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  351 LSKDPEIQEALHEEVVGVvpaGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYV 430
Cdd:cd11053 250 LHRHPEVLARLLAELDAL---GGDPDPEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYL 326
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  431 VSRDPTAFSEPESFQPHRWLrNSQPAtpriqhPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGElKS 510
Cdd:cd11053 327 THHRPDLYPDPERFRPERFL-GRKPS------PYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPE-RP 398

                ....*....
gi 4503211  511 VAR-IVLVP 518
Cdd:cd11053 399 VRRgVTLAP 407
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
179-518 6.14e-48

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: 171.61  E-value: 6.14e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  179 NEVIDDFMTRLDqlraESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSipEDTVTFVRSIGLMFQNSLYATFLP 258
Cdd:cd11060  81 DECIDLLVDLLD----EKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLEAG--TDVDGYIASIDKLLPYFAVVGQIP 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  259 KWTRPV----LPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAqlqaagpDGIQVSGYLHFLLASGQ-----LSPREAMGSL 329
Cdd:cd11060 155 WLDRLLlknpLGPKRKDKTGFGPLMRFALEAVAERLAEDAE-------SAKGRKDMLDSFLEAGLkdpekVTDREVVAEA 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  330 PELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFA---HMPLLKAVLKETLRLYPVVPTN-SR 405
Cdd:cd11060 228 LSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKLSSPITFAeaqKLPYLQAVIKEALRLHPPVGLPlER 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  406 IIEKE-IEVDGFLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRnSQPATPRIQHPFgSVPFGYGVRACLGRRIAE 483
Cdd:cd11060 308 VVPPGgATICGRFIPGGTIVGVNPWVIHRDKEVFGEdADVFRPERWLE-ADEEQRRMMDRA-DLTFGAGSRTCLGKNIAL 385
                       330       340       350
                ....*....|....*....|....*....|....*
gi 4503211  484 LEMQLLLARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd11060 386 LELYKVIPELLRRFDFELVDPEKEWKTRNYWFVKQ 420
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
93-498 2.70e-47

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: 170.09  E-value: 2.70e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   93 GPMWMSYLGPQMHVNLASAPLLEQVMrqegkypvrNDMElWKEHRDQHD---LTYGPFTTEGHHWYQLRQALN----QRL 165
Cdd:cd11057   1 GSPFRAWLGPRPFVITSDPEIVQVVL---------NSPH-CLNKSFFYDffrLGRGLFSAPYPIWKLQRKALNpsfnPKI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  166 LKPaeaalYTDAFNEVIDDFMTRLDQLraesASGNQVsDMAQLFYYFALEAICYILF-----------EKRIGCLQRSIp 234
Cdd:cd11057  71 LLS-----FLPIFNEEAQKLVQRLDTY----VGGGEF-DILPDLSRCTLEMICQTTLgsdvndesdgnEEYLESYERLF- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  235 edTVTFVRsiglMFQNSLYATFLPKWTrpvlPFWKRYLDGWNAIFSFGKKLIDEKL-EDMEAQLQAAGPDGIQVSGYLHF 313
Cdd:cd11057 140 --ELIAKR----VLNPWLHPEFIYRLT----GDYKEEQKARKILRAFSEKIIEKKLqEVELESNLDSEEDEENGRKPQIF 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  314 L-------LASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVP-AGQVPQHKDFAHMPL 385
Cdd:cd11057 210 IdqllelaRNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPdDGQFITYEDLQQLVY 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  386 LKAVLKETLRLYPVVPTNSRIIEKEIEVD-GFLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWLrnsqpaTPRIQ-- 461
Cdd:cd11057 290 LEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFL------PERSAqr 363
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503211  462 HPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYK 498
Cdd:cd11057 364 HPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYR 400
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
90-516 1.35e-46

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: 167.38  E-value: 1.35e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   90 AKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYpvRNDMELWKEHRDQHDLTYGPFTTEGHHWYQLRQALnQRLLKPA 169
Cdd:COG2124  29 REYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTF--SSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLV-QPAFTPR 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  170 EAALYTDAFNEVIDDFMTRLdqlrAESASGNQVSDMAQLFyyfALEAICYILfekrigclqrSIPEDTVTFVRSIGLMFQ 249
Cdd:COG2124 106 RVAALRPRIREIADELLDRL----AARGPVDLVEEFARPL---PVIVICELL----------GVPEEDRDRLRRWSDALL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  250 NSLyatflpkwTRPVLPFWKRYLDGWNAIFSFGKKLIDEKledmeaqlQAAGPDGIqvsgyLHFLLAS----GQLSPREA 325
Cdd:COG2124 169 DAL--------GPLPPERRRRARRARAELDAYLRELIAER--------RAEPGDDL-----LSALLAArddgERLSDEEL 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  326 MGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVvgvvpagqvpqhkdfahmPLLKAVLKETLRLYPVVPTNSR 405
Cdd:COG2124 228 RDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPR 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  406 IIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatpriqHPFGSVPFGYGVRACLGRRIAELE 485
Cdd:COG2124 290 TATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------------PPNAHLPFGGGPHRCLGAALARLE 356
                       410       420       430
                ....*....|....*....|....*....|.
gi 4503211  486 MQLLLARLIQKYKVVLAPETGELKSVARIVL 516
Cdd:COG2124 357 ARIALATLLRRFPDLRLAPPEELRWRPSLTL 387
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
91-507 2.22e-46

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: 167.81  E-value: 2.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQegKYPVRNDMELWKE-----HRDQHDLTYGPFtteGHHWYQLRQALNQRL 165
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQ--KGSSFASRPPANPlrvlfSSNKHMVNSSPY---GPLWRTLRRNLVSEV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  166 LKPAEAALYTDAFNEVIDDFMTRLdqlRAESASGNQVSDMAQLFYYfaleAICYILFekrIGCLQRSIPEDTVTFVRSIG 245
Cdd:cd11075  76 LSPSRLKQFRPARRRALDNLVERL---REEAKENPGPVNVRDHFRH----ALFSLLL---YMCFGERLDEETVRELERVQ 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  246 LMFQNSLYAT----FLPKWTRpvLPFWKRyldgWNAIFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFLLAS---- 317
Cdd:cd11075 146 RELLLSFTDFdvrdFFPALTW--LLNRRR----WKKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFLLLDLldlk 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  318 -----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKE 392
Cdd:cd11075 220 eeggeRKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLE 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  393 TLRLY-PVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATprIQHPFGSV---P 468
Cdd:cd11075 300 TLRRHpPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAAD--IDTGSKEIkmmP 377
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 4503211  469 FGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd11075 378 FGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEGEEV 416
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
148-516 2.31e-45

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: 164.65  E-value: 2.31e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  148 TTEGHHWYQlrqalNQRLLKPA--EAAL--YTDAFNEVIDDFMTRLDQLraesASGNQVSDMAQLFYYFALEAICYILFE 223
Cdd:cd20659  51 LSNGKKWKR-----NRRLLTPAfhFDILkpYVPVYNECTDILLEKWSKL----AETGESVEVFEDISLLTLDIILRCAFS 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  224 KRIGCLQRSIPEDTVTFVRSIGLM----FQNSLY-ATFLPKWTrPVLPFWKRYLDGwnaIFSFGKKLIDEKLEdmeaQLQ 298
Cdd:cd20659 122 YKSNCQQTGKNHPYVAAVHELSRLvmerFLNPLLhFDWIYYLT-PEGRRFKKACDY---VHKFAEEIIKKRRK----ELE 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  299 AAGPDGIQVSGYLHFL----LA---SGQ-LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVP 370
Cdd:cd20659 194 DNKDEALSKRKYLDFLdillTArdeDGKgLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLG 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  371 AGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWL 450
Cdd:cd20659 274 DRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL 353
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503211  451 R-NSQPatpriQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETgELKSVARIVL 516
Cdd:cd20659 354 PeNIKK-----RDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNH-PVEPKPGLVL 414
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
145-519 1.66e-44

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: 162.34  E-value: 1.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  145 GPFTTEGHHWYQLRQalnqrLLKPAEAALY---TDAFNEVIDDFMTRLDqlraesaSGNQVSDMAQLFYYFALEAICYIL 221
Cdd:cd11063  51 GIFTSDGEEWKHSRA-----LLRPQFSRDQisdLELFERHVQNLIKLLP-------RDGSTVDLQDLFFRLTLDSATEFL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  222 FEKRIGCLQ-RSIPEDTVTFVRSiglmFQNSLyaTFLPKWTR--PVLPFW--KRYLDGWNAIFSFGKKLIDEKLEDMEAQ 296
Cdd:cd11063 119 FGESVDSLKpGGDSPPAARFAEA----FDYAQ--KYLAKRLRlgKLLWLLrdKKFREACKVVHRFVDPYVDKALARKEES 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  297 LQAAGPDGIqvsGYLHFLLASGQlSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQ 376
Cdd:cd11063 193 KDEESSDRY---VFLDELAKETR-DPKELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPT 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  377 HKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKeievDGFL------------F-PKNTQFVFCHYVVSRDPTAFSE-PE 442
Cdd:cd11063 269 YEDLKNMKYLRAVINETLRLYPPVPLNSRVAVR----DTTLprgggpdgkspiFvPKGTRVLYSVYAMHRRKDIWGPdAE 344
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503211  443 SFQPHRWLRNSQPatpriqhPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPN 519
Cdd:cd11063 345 EFRPERWEDLKRP-------GWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFDRIESRDVRPPEERLTLTLSNA 414
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
147-507 2.41e-44

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: 162.04  E-value: 2.41e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  147 FTTEGHHWYQLRQALnqrlLKPAEAALYTDAFNEVIDDFMTRL-DQLRAESASGNQVsDMAQLFYYFALEAICYILFEKR 225
Cdd:cd11062  47 FSTVDHDLHRLRRKA----LSPFFSKRSILRLEPLIQEKVDKLvSRLREAKGTGEPV-NLDDAFRALTADVITEYAFGRS 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  226 IGCL-QRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLD----GWNAIFSFGKKLIDEKLEDMEAQLQAA 300
Cdd:cd11062 122 YGYLdEPDFGPEFLDALRALAEMIHLLRHFPWLLKLLRSLPESLLKRLNpglaVFLDFQESIAKQVDEVLRQVSAGDPPS 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  301 GPDGIQVSGYLHFLLASGqLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVP-AGQVPQHKD 379
Cdd:cd11062 202 IVTSLFHALLNSDLPPSE-KTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPdPDSPPSLAE 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  380 FAHMPLLKAVLKETLRLYPVVPTNS-RIIEKE-IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNsqPAT 457
Cdd:cd11062 281 LEKLPYLTAVIKEGLRLSYGVPTRLpRVVPDEgLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGA--AEK 358
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 4503211  458 PRIQHPFgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd11062 359 GKLDRYL--VPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYETTEE 406
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
91-526 3.93e-44

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: 161.73  E-value: 3.93e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGP-QMHVNLASAplLEQVMRQEGKYPVRNDMElwkehrdQHDLTYGP--FTTEGHHWYQLR----QALNQ 163
Cdd:cd11070   1 KLGAVKILFVSRwNILVTKPEY--LTQIFRRRDDFPKPGNQY-------KIPAFYGPnvISSEGEDWKRYRkivaPAFNE 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  164 RLLK--PAEAALYTDAFNEVIddfmtrldqLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQ--RSIPEDTVT 239
Cdd:cd11070  72 RNNAlvWEESIRQAQRLIRYL---------LEEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDeeESSLHDTLN 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  240 FVRS-----IGLMFqnslyaTFLPKWTRPVLPFWKRYLDgwnAIFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFL 314
Cdd:cd11070 143 AIKLaifppLFLNF------PFLDRLPWVLFPSRKRAFK---DVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRA 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  315 LASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEV--VGVVPAGQVPQHKDFAHMPLLKAVLKE 392
Cdd:cd11070 214 RRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIdsVLGDEPDDWDYEEDFPKLPYLLAVIYE 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  393 TLRLYPVVPTNSRIIEKEIEV-----DGFLFPKNTQFVFCHYVVSRDPTA-FSEPESFQPHRWLRNSQP--ATPRIQHPF 464
Cdd:cd11070 294 TLRLYPPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWGSTSGEigAATRFTPAR 373
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503211  465 GS-VPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQF 526
Cdd:cd11070 374 GAfIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRVDPEWEEGETPAGATRDSPAKLRLRF 436
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
164-503 7.11e-43

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: 157.81  E-value: 7.11e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  164 RLLKPA----EAALYTDAfneviddfMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGclqrsiPEDTVT 239
Cdd:cd11049  75 RLMQPAfhrsRIPAYAEV--------MREEAEALAGSWRPGRVVDVDAEMHRLTLRVVARTLFSTDLG------PEAAAE 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  240 FVRSIGLMFQNSLYATFLPKWTRPV-LPFWKRYLDGWNAIFSfgkkLIDEkledMEAQLQAAGPDGiqvSGYLHFLLAS- 317
Cdd:cd11049 141 LRQALPVVLAGMLRRAVPPKFLERLpTPGNRRFDRALARLRE----LVDE----IIAEYRASGTDR---DDLLSLLLAAr 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  318 ----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKET 393
Cdd:cd11049 210 deegRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVL-GGRPATFEDLPRLTYTRRVVTEA 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  394 LRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRiqHPFgsVPFGYGV 473
Cdd:cd11049 289 LRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPR--GAF--IPFGAGA 364
                       330       340       350
                ....*....|....*....|....*....|
gi 4503211  474 RACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11049 365 RKCIGDTFALTELTLALATIASRWRLRPVP 394
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
138-507 4.67e-40

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: 150.40  E-value: 4.67e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  138 DQHDLTYGPFtteGHHWYQLRQALNQRLLKPAEAALYTDAFNEVIDDFMTRLdqlRAESASGNQVsDMAQLFYYFALEAI 217
Cdd:cd20618  48 NGQDIVFAPY---GPHWRHLRKICTLELFSAKRLESFQGVRKEELSHLVKSL---LEESESGKPV-NLREHLSDLTLNNI 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  218 CYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSL---YATFLPkWTRPVLPFW-KRYLDGWNAIF-SFGKKLIDEKLEd 292
Cdd:cd20618 121 TRMLFGKRYFGESEKESEEAREFKELIDEAFELAGafnIGDYIP-WLRWLDLQGyEKRMKKLHAKLdRFLQKIIEEHRE- 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  293 mEAQLQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAG 372
Cdd:cd20618 199 -KRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRE 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  373 QVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLr 451
Cdd:cd20618 278 RLVEESDLPKLPYLQAVVKETLRLHPPGPLLLpHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFL- 356
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 4503211  452 NSQPATPRIQHpFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd20618 357 ESDIDDVKGQD-FELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFDWSLPGPKPE 411
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
139-503 4.81e-39

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: 147.74  E-value: 4.81e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  139 QHD-LTYGPFTTEGHHWYQlrqalnQRllKPAEAALYTDAFNevidDFMT---------RLDQLRAESASGNQVSDMAQL 208
Cdd:cd11064  43 FFDlLGDGIFNVDGELWKF------QR--KTASHEFSSRALR----EFMEsvvrekvekLLVPLLDHAAESGKVVDLQDV 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  209 FYYFALEAICYILFEKRIGCLQRSIPEdtVTFVRSIGLMFQNSLYATFLPKWtrpvlpFWK--RYL---------DGWNA 277
Cdd:cd11064 111 LQRFTFDVICKIAFGVDPGSLSPSLPE--VPFAKAFDDASEAVAKRFIVPPW------LWKlkRWLnigsekklrEAIRV 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  278 IFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFLLASGQLSPRE-----AMGslpeLLMAGVDTTSNTLTWALYHLS 352
Cdd:cd11064 183 IDDFVYEVISRRREELNSREEENNVREDLLSRFLASEEEEGEPVSDKflrdiVLN----FILAGRDTTAAALTWFFWLLS 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  353 KDPEIQEALHEEVVGVVPA-----GQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSR-IIEKEIEVDGFLFPKNTQFVF 426
Cdd:cd11064 259 KNPRVEEKIREELKSKLPKlttdeSRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKeAVNDDVLPDGTFVKKGTRIVY 338
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  427 CHYVVSRDPTAFSE-PESFQPHRWLRNSqpatPRIQH--PFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11064 339 SIYAMGRMESIWGEdALEFKPERWLDED----GGLRPesPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVP 414
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
332-518 1.03e-38

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: 146.31  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQ-HKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKE 410
Cdd:cd11083 230 LLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKPVAPLLFLEPNED 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPriQHPFGSVPFGYGVRACLGRRIAELEMQLLL 490
Cdd:cd11083 310 TVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEP--HDPSSLLPFGAGPRLCPGRSLALMEMKLVF 387
                       170       180
                ....*....|....*....|....*...
gi 4503211  491 ARLIQKYKVVLAPETGELKSVARIVLVP 518
Cdd:cd11083 388 AMLCRNFDIELPEPAPAVGEEFAFTMSP 415
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
135-518 2.13e-38

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: 145.76  E-value: 2.13e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  135 EHRDqhDLTYGPFTTEGHHWYQLRQALnqrllkpaeAALYTDA--------FNEVIDDFMtrlDQLRAESASGNQVsDMA 206
Cdd:cd11056  44 EKDD--PLSANLFSLDGEKWKELRQKL---------TPAFTSGklknmfplMVEVGDELV---DYLKKQAEKGKEL-EIK 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  207 QLFYYFALEAICYILFEKRIGCLQRSIPEdtvtFVRSIGLMFQNSLYATFLpKWTRPVLPFWKRYLdgwnaifsfGKKLI 286
Cdd:cd11056 109 DLMARYTTDVIASCAFGLDANSLNDPENE----FREMGRRLFEPSRLRGLK-FMLLFFFPKLARLL---------RLKFF 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  287 DEKLED-----MEAQLQAAGPDGIQVSGYLHFLL---ASGQLSPREAMGSLPE---------LLMAGVDTTSNTLTWALY 349
Cdd:cd11056 175 PKEVEDffrklVRDTIEYREKNNIVRNDFIDLLLelkKKGKIEDDKSEKELTDeelaaqafvFFLAGFETSSSTLSFALY 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  350 HLSKDPEIQEALHEEVVGVVPA--GQVpQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDG--FLFPKNTQFV 425
Cdd:cd11056 255 ELAKNPEIQEKLREEIDEVLEKhgGEL-TYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPVI 333
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  426 FCHYVVSRDPTAFSEPESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:cd11056 334 IPVYALHHDPKYYPEPEKFDPERFS----PENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKT 409
                       410
                ....*....|....*
gi 4503211  506 G-ELK-SVARIVLVP 518
Cdd:cd11056 410 KiPLKlSPKSFVLSP 424
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
88-515 3.15e-38

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: 145.59  E-value: 3.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   88 YKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGKYpvrndmelwkehRDQHDLTY---------GPFTTEGHHWYQLR 158
Cdd:cd11046   6 WFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFS------------YDKKGLLAeilepimgkGLIPADGEIWKKRR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  159 QALNQRLLKPAEAALyTDAFNEVIDDFMTRLDqlraESASGNQVSDMAQLFYYFALEAICYILFEKRIGclqrSIPEDTV 238
Cdd:cd11046  74 RALVPALHKDYLEMM-VRVFGRCSERLMEKLD----AAAETGESVDMEEEFSSLTLDIIGLAVFNYDFG----SVTEESP 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  239 TFVRSIGLMFQNSLYATF-LPKWTRP----VLPFWKRYLDGWNAIFSFGKKLIDEKLEDM-EAQLQAAGPDGIQV--SGY 310
Cdd:cd11046 145 VIKAVYLPLVEAEHRSVWePPYWDIPaalfIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRqEEDIELQQEDYLNEddPSL 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  311 LHFLLASG--QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKA 388
Cdd:cd11046 225 LRFLVDMRdeDVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRR 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  389 VLKETLRLYPVVPTNSRIIEKEIEVDGFLF--PKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGS 466
Cdd:cd11046 305 VLNESLRLYPQPPVLIRRAVEDDKLPGGGVkvPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEVIDDFAF 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 4503211  467 VPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLA--PETGELKSVARIV 515
Cdd:cd11046 385 LPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDvgPRHVGMTTGATIH 435
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
164-507 2.99e-37

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: 142.34  E-value: 2.99e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  164 RLLKPA--EAALYT--DAFNEVIDDFMtrlDQLRAESASGNQVsDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTV- 238
Cdd:cd11058  63 RLLAHAfsEKALREqePIIQRYVDLLV---SRLRERAGSGTPV-DMVKWFNFTTFDIIGDLAFGESFGCLENGEYHPWVa 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  239 ---TFVRSIGLMfQNSLYATFLPKWTRPVLP--FWKRYLDGWnaifsfgkKLIDEKLeDMEAQLQAAGPDgiqvsgYLHF 313
Cdd:cd11058 139 lifDSIKALTII-QALRRYPWLLRLLRLLIPksLRKKRKEHF--------QYTREKV-DRRLAKGTDRPD------FMSY 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  314 LLAS----GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVvgvvpAGQVPQHKD-----FAHMP 384
Cdd:cd11058 203 ILRNkdekKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEI-----RSAFSSEDDitldsLAQLP 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  385 LLKAVLKETLRLYPVVPTN-SRIIEKE-IEVDGFLFPKNTQfVFC-HYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQ 461
Cdd:cd11058 278 YLNAVIQEALRLYPPVPAGlPRVVPAGgATIDGQFVPGGTS-VSVsQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNDK 356
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4503211  462 HPfGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:cd11058 357 KE-AFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESED 401
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
256-522 3.69e-37

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: 142.43  E-value: 3.69e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  256 FLPKWTRPV----LPFWKRYldgwNAIFSFGKKLIDEKLEDMEAQlqAAGPDGIQVSGYLHFLL----ASGQLSPREAMG 327
Cdd:cd11041 157 LFPPFLRPLvapfLPEPRRL----RRLLRRARPLIIPEIERRRKL--KKGPKEDKPNDLLQWLIeaakGEGERTPYDLAD 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  328 SLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRI 406
Cdd:cd11041 231 RQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSlRRK 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  407 IEKEIEV-DGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSV-----PFGYGVRACLGRR 480
Cdd:cd11041 311 VLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKHQFVSTspdflGFGHGRHACPGRF 390
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 4503211  481 IAELEMQLLLARLIQKYKVVLAPETGELKSV---ARIVLVPNKKV 522
Cdd:cd11041 391 FASNEIKLILAHLLLNYDFKLPEGGERPKNIwfgEFIMPDPNAKV 435
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
336-520 4.07e-37

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: 142.02  E-value: 4.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  336 GVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAG-QVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD 414
Cdd:cd20660 244 GHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSdRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIG 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  415 GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd20660 324 GYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFL----PENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSIL 399
                       170       180
                ....*....|....*....|....*.
gi 4503211  495 QKYKVVLAPETGELKSVARIVLVPNK 520
Cdd:cd20660 400 RNFRIESVQKREDLKPAGELILRPVD 425
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
256-494 5.93e-37

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: 141.56  E-value: 5.93e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  256 FLPKWtrpVLPFWKRYLDGWNAIFsfgKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMA 335
Cdd:cd11065 161 YLPSW---LGAPWKRKARELRELT---RRLYEGPFEAAKERMASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEA 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  336 GVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEKEIEVD 414
Cdd:cd11065 235 GSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIpHALTEDDEYE 314
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  415 GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGSvpFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd11065 315 GYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPPHFA--FGFGRRICPGRHLAENSLFIAIARLL 392
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
276-503 1.15e-35

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: 137.80  E-value: 1.15e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  276 NAIFSFGKKLIDEKLEdmeaQLQAAGPDGIQVsgYLHFLLASGQ-LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKD 354
Cdd:cd11044 180 NKLLARLEQAIRERQE----EENAEAKDALGL--LLEAKDEDGEpLSMDELKDQALLLLFAGHETTASALTSLCFELAQH 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  355 PEIQEALHEEVVGVVPAGQVPQhKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRD 434
Cdd:cd11044 254 PDVLEKLRQEQDALGLEEPLTL-ESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRD 332
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503211  435 PTAFSEPESFQPHRWlrnSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11044 333 PELYPDPERFDPERF---SPARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLP 398
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
91-505 2.83e-35

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: 136.54  E-value: 2.83e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYL-GPQMHVnLASAPLLEQVMRQEGK-----YPvrndmelwkehRDQHDL--TYGPFTTEGHHWYQLRQALn 162
Cdd:cd11043   4 RYGPVFKTSLfGRPTVV-SADPEANRFILQNEGKlfvswYP-----------KSVRKLlgKSSLLTVSGEEHKRLRGLL- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  163 QRLLKPaEAAlyTDAFNEVIDDFMtrLDQLRAESASGNQ-VSDMAQLFyyfALEAICYILFekrigclqrSIpeDTVTFV 241
Cdd:cd11043  71 LSFLGP-EAL--KDRLLGDIDELV--RQHLDSWWRGKSVvVLELAKKM---TFELICKLLL---------GI--DPEEVV 131
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  242 RSIGLMFQNSLYATF-----LPkWTRpvlpFWkRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAagpdgiqvSGYLHFLLA 316
Cdd:cd11043 132 EELRKEFQAFLEGLLsfplnLP-GTT----FH-RALKARKRIRKELKKIIEERRAELEKASPK--------GDLLDVLLE 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  317 SGQ-----LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEAL---HEEVVGVVPAGQVPQHKDFAHMPLLKA 388
Cdd:cd11043 198 EKDedgdsLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELleeHEEIAKRKEEGEGLTWEDYKSMKYTWQ 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  389 VLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAtpriqhPFGSVP 468
Cdd:cd11043 278 VINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV------PYTFLP 351
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 4503211  469 FGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:cd11043 352 FGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPDE 388
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
262-504 3.83e-35

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: 136.29  E-value: 3.83e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  262 RPVLPF--WKRYLDGWNAIFSFGKKLIDEKLE----DMEAQL-QAAGPDGiqvsgylhfllasGQLSPREAMGSLPELLM 334
Cdd:cd11045 155 RTPIPGtrWWRGLRGRRYLEEYFRRRIPERRAgggdDLFSALcRAEDEDG-------------DRFSDDDIVNHMIFLMM 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVvpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD 414
Cdd:cd11045 222 AAHDTTTSTLTSMAYFLARHPEWQERLREESLAL--GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVL 299
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  415 GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWlrnSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd11045 300 GYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERF---SPERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQML 376
                       250
                ....*....|
gi 4503211  495 QKYKVVLAPE 504
Cdd:cd11045 377 RRFRWWSVPG 386
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
332-505 6.38e-35

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: 135.81  E-value: 6.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpaGQVPQHKDFAH---MPLLKAVLKETLRLYPVVPTNSRIIE 408
Cdd:cd11042 220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVL--GDGDDPLTYDVlkeMPLLHACIKETLRLHPPIHSLMRKAR 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  409 KEIEVD--GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFgsVPFGYGVRACLGRRIAELEM 486
Cdd:cd11042 298 KPFEVEggGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGGKFAY--LPFGAGRHRCIGENFAYLQI 375
                       170
                ....*....|....*....
gi 4503211  487 QLLLARLIQKYKVVLAPET 505
Cdd:cd11042 376 KTILSTLLRNFDFELVDSP 394
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
326-520 1.01e-34

cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 135.42  E-value: 1.01e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  326 MGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-S 404
Cdd:cd11027 231 VMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLAlP 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  405 RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsQPATPRIQHPFGSVPFGYGVRACLGRRIAEL 484
Cdd:cd11027 311 HKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFL---DENGKLVPKPESFLPFSAGRRVCLGESLAKA 387
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4503211  485 EMQLLLARLIQKYKVVLAPETG--ELKSVARIVLVPNK 520
Cdd:cd11027 388 ELFLFLARLLQKFRFSPPEGEPppELEGIPGLVLYPLP 425
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
228-499 9.94e-34

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: 132.76  E-value: 9.94e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  228 CLQRSIPEDTVTFVRSIGLMFQNSLY----ATFL--PKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAG 301
Cdd:cd20621 126 INGKEIQVELVEILIESFLYRFSSPYfqlkRLIFgrKSWKLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKNKDEIK 205
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  302 PDGIQVSGYLhflLASGQLSPREamgSLPELL-------MAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQV 374
Cdd:cd20621 206 DIIIDLDLYL---LQKKKLEQEI---TKEEIIqqfitffFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDD 279
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  375 PQHKDFAHMPLLKAVLKETLRLYPVVP-TNSRIIEKEIEVDGFLFPKNTqFVFCHY-VVSRDPTAFSEPESFQPHRWLrN 452
Cdd:cd20621 280 ITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQIGDLKIKKGW-IVNVGYiYNHFNPKYFENPDEFNPERWL-N 357
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 4503211  453 SQPATpriQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKV 499
Cdd:cd20621 358 QNNIE---DNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEI 401
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
213-520 2.09e-33

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 131.81  E-value: 2.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  213 ALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKLIDEKLED 292
Cdd:cd20680 121 ALDIICETAMGKKIGAQSNKDSEYVQAVYRMSDIIQRRQKMPWLWLDLWYLMFKEGKEHNKNLKILHTFTDNVIAERAEE 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  293 MEAQLQAAGPDGIQVSG------YLHFLL-----ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEAL 361
Cdd:cd20680 201 MKAEEDKTGDSDGESPSkkkrkaFLDMLLsvtdeEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKV 280
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  362 HEEVVGVVPAGQVP-QHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSE 440
Cdd:cd20680 281 HKELDEVFGKSDRPvTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPE 360
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  441 PESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGELKSVARIVLVPNK 520
Cdd:cd20680 361 PEEFRPERFF----PENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQKREELGLVGELILRPQN 436
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
331-495 6.77e-33

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: 130.41  E-value: 6.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKE 410
Cdd:cd20655 235 DLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEG 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPAT---PRIQHpFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:cd20655 315 CKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQeldVRGQH-FKLLPFGSGRRGCPGASLAYQVVG 393

                ....*...
gi 4503211  488 LLLARLIQ 495
Cdd:cd20655 394 TAIAAMVQ 401
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
333-525 9.61e-33

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: 129.84  E-value: 9.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  333 LMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIE 412
Cdd:cd20650 237 IFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVE 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  413 VDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLR-NSQPATPRIQHPFGSVPfgygvRACLGRRIAELEMQLLLA 491
Cdd:cd20650 317 INGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKkNKDNIDPYIYLPFGSGP-----RNCIGMRFALMNMKLALV 391
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4503211  492 RLIQKYKVVLAPETG-ELKSVARIVLVPNKKVGLQ 525
Cdd:cd20650 392 RVLQNFSFKPCKETQiPLKLSLQGLLQPEKPIVLK 426
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
278-505 1.30e-32

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: 129.51  E-value: 1.30e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  278 IFSFGKKLIdeklEDMEAQLQAAGP-DGIQVsgylhFLLASGQLSPREAMGSLPE---------LLMAGVDTTSNTLTWA 347
Cdd:cd20666 181 ITAFLKKII----ADHRETLDPANPrDFIDM-----YLLHIEEEQKNNAESSFNEdylfyiigdLFIAGTDTTTNTLLWC 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  348 LYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVP-TNSRIIEKEIEVDGFLFPKNTQFVF 426
Cdd:cd20666 252 LLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPlSIPHMASENTVLQGYTIPKGTVIVP 331
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  427 CHYVVSRDPTAFSEPESFQPHRWL-RNSQpatprIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:cd20666 332 NLWSVHRDPAIWEKPDDFMPSRFLdENGQ-----LIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNA 406
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
319-503 2.06e-31

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: 126.15  E-value: 2.06e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  319 QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYP 398
Cdd:cd11068 225 KLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVL-GDDPPPYEQVAKLRYIRRVLDETLRLWP 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  399 VVPTNSRIIEKEIEVDG-FLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRNSQPATPRiqHPFGsvPFGYGVRAC 476
Cdd:cd11068 304 TAPAFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWGEdAEEFRPERFLPEEFRKLPP--NAWK--PFGNGQRAC 379
                       170       180
                ....*....|....*....|....*..
gi 4503211  477 LGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11068 380 IGRQFALQEATLVLAMLLQRFDFEDDP 406
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
253-504 2.19e-31

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: 125.79  E-value: 2.19e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  253 YATFLPkWTRPVLPFWKRY---LDGWNAIFSFGKKLIDEKLEDMEaqlqaagPDGIQ--VSGYLHFLLASGQLSP---RE 324
Cdd:cd20651 153 LLNQFP-WLRFIAPEFSGYnllVELNQKLIEFLKEEIKEHKKTYD-------EDNPRdlIDAYLREMKKKEPPSSsftDD 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  325 --AMGSLpELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVP- 401
Cdd:cd20651 225 qlVMICL-DLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPi 303
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  402 TNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNsqpaTPRIQHPFGSVPFGYGVRACLGRRI 481
Cdd:cd20651 304 GIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDE----DGKLLKDEWFLPFGAGKRRCLGESL 379
                       250       260
                ....*....|....*....|...
gi 4503211  482 AELEMQLLLARLIQKYKVVLAPE 504
Cdd:cd20651 380 ARNELFLFFTGLLQNFTFSPPNG 402
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
283-497 9.54e-31

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: 124.46  E-value: 9.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  283 KKL---IDEKLEDMEAQLQAAGPDGIQVSGYLHFLLAS-------GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLS 352
Cdd:cd20657 177 KRLhkrFDALLTKILEEHKATAQERKGKPDFLDFVLLEnddngegERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELI 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  353 KDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVV 431
Cdd:cd20657 257 RHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNlPRIASEACEVDGYYIPKGTRLLVNIWAI 336
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503211  432 SRDPTAFSEPESFQPHRWL--RNSQpATPRIQHpFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKY 497
Cdd:cd20657 337 GRDPDVWENPLEFKPERFLpgRNAK-VDVRGND-FELIPFGAGRRICAGTRMGIRMVEYILATLVHSF 402
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
278-495 1.97e-30

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: 123.41  E-value: 1.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  278 IFSFGKKLIDEKLEDMEAQlQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEI 357
Cdd:cd11073 186 LFDIFDGFIDERLAEREAG-GDKKKDDDLLLLLDLELDSESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEK 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  358 QEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPT 436
Cdd:cd11073 265 MAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLpRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPS 344
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503211  437 AFSEPESFQPHRWLRNSqpatprIQ---HPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQ 495
Cdd:cd11073 345 VWEDPLEFKPERFLGSE------IDfkgRDFELIPFGSGRRICPGLPLAERMVHLVLASLLH 400
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
92-516 3.53e-30

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: 122.52  E-value: 3.53e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   92 YGPMWMSYLGPQMHVNLASAPLLEQVM-RQEGKYPVRNDMELWK-EHRDQHDLTYGPFTTEghhWYQLRQALNQRLLKpa 169
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALvRKWADFAGRPHSYTGKlVSQGGQDLSLGDYSLL---WKAHRKLTRSALQL-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  170 eaalytdAFNEVIDDFMTRLDQLRAE--SASGNQVSDMAQLFYYFALEAICYILFEKRigclqrsipEDTVTFVRSIGLM 247
Cdd:cd20674  76 -------GIRNSLEPVVEQLTQELCErmRAQAGTPVDIQEEFSLLTCSIICCLTFGDK---------EDKDTLVQAFHDC 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  248 FQNslyatFLPKWTRP------VLPFWKRYLdgwNAIFSFGKKLIDEKLEDMEAQLQA------AGPDGIQVSGYLHFLL 315
Cdd:cd20674 140 VQE-----LLKTWGHWsiqaldSIPFLRFFP---NPGLRRLKQAVENRDHIVESQLRQhkeslvAGQWRDMTDYMLQGLG 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  316 ASGQLSPREAMG------SLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAV 389
Cdd:cd20674 212 QPRGEKGMGQLLeghvhmAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNAT 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  390 LKETLRLYPVVPTN--SRIIeKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpATPRIqhpfgsV 467
Cdd:cd20674 292 IAEVLRLRPVVPLAlpHRTT-RDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGA-ANRAL------L 363
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 4503211  468 PFGYGVRACLGRRIAELEMQLLLARLIQKYKvVLAPETGELKS---VARIVL 516
Cdd:cd20674 364 PFGCGARVCLGEPLARLELFVFLARLLQAFT-LLPPSDGALPSlqpVAGINL 414
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
158-506 5.05e-30

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: 122.04  E-value: 5.05e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  158 RQALNQRLLKPAEAAlYTDAFNEVIDDFMTrldQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGC-----LQRS 232
Cdd:cd11066  68 RKAAASALNRPAVQS-YAPIIDLESKSFIR---ELLRDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCvdddsLLLE 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  233 I--PEDTVTFVRSiglmfQNSLYATFLPkwtrpVLpfwkRYLDGWNAIFSFGKKLIDEKLEDME---AQLQAAGPDGIQV 307
Cdd:cd11066 144 IieVESAISKFRS-----TSSNLQDYIP-----IL----RYFPKMSKFRERADEYRNRRDKYLKkllAKLKEEIEDGTDK 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  308 SGYLHFLL--ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDP--EIQEALHEEVVGVVPAGQVPQHKDFAHM 383
Cdd:cd11066 210 PCIVGNILkdKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAEE 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  384 --PLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRI 460
Cdd:cd11066 290 kcPYVVALVKETLRYFTVLPLGlPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGP 369
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 4503211  461 QHpFGsvpFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETG 506
Cdd:cd11066 370 PH-FS---FGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEE 411
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
144-508 1.17e-29

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: 120.74  E-value: 1.17e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  144 YGPFTTEGHHWYQLRQ--------------ALNQRLLkpAEAALYTDAFNEviddfmtrldqlraesaSGNQVSDMAQLF 209
Cdd:cd11026  50 YGVVFSNGERWKQLRRfslttlrnfgmgkrSIEERIQ--EEAKFLVEAFRK-----------------TKGKPFDPTFLL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  210 YYFALEAICYILFEKRIGC-------LQRSIPEdTVTFVRSIGLMfqnsLYATFlPKWTRPVLPFWKRYLDGWNAIFSFG 282
Cdd:cd11026 111 SNAVSNVICSIVFGSRFDYedkeflkLLDLINE-NLRLLSSPWGQ----LYNMF-PPLLKHLPGPHQKLFRNVEEIKSFI 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  283 KKLIDEKLEDMEAQ----------LQAAGPDGIQVSGYlhfllasgqlSPREAMGSLPELLMAGVDTTSNTLTWALYHLS 352
Cdd:cd11026 185 RELVEEHRETLDPSsprdfidcflLKMEKEKDNPNSEF----------HEENLVMTVLDLFFAGTETTSTTLRWALLLLM 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  353 KDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVV 431
Cdd:cd11026 255 KYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGvPHAVTRDTKFRGYTIPKGTTVIPNLTSV 334
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503211  432 SRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGEL 508
Cdd:cd11026 335 LRDPKQWETPEEFNPGHFLDEQG----KFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKDP 407
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
92-503 2.15e-28

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


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 117.44  E-value: 2.15e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   92 YGPMWMSYLGPQMHVNLASAPLLEQVMRQ----EGKYPVRNDMELWkehrdqhdLTYGPFTTEGHHWYQLRqalnqRLLK 167
Cdd:cd11052  11 YGKNFLYWYGTDPRLYVTEPELIKELLSKkegyFGKSPLQPGLKKL--------LGRGLVMSNGEKWAKHR-----RIAN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  168 PAEAA----LYTDAfneVIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKrigclqrSIPEDTVTF--V 241
Cdd:cd11052  78 PAFHGeklkGMVPA---MVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGS-------SYEEGKEVFklL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  242 RSIGLMFQNSLYATFLPKW----TRPVLPFWKryLDgwNAIFSFGKKLIDEKLEDMEAqlqaaGPDGIQVSGYLHFLLAS 317
Cdd:cd11052 148 RELQKICAQANRDVGIPGSrflpTKGNKKIKK--LD--KEIEDSLLEIIKKREDSLKM-----GRGDDYGDDLLGLLLEA 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  318 GQLSPREAMGSLPELL-------MAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKdFAHMPLLKAVL 390
Cdd:cd11052 219 NQSDDQNKNMTVQEIVdecktffFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDS-LSKLKTVSMVI 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  391 KETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRNSQPATpriQHPFGSVPF 469
Cdd:cd11052 298 NESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKAA---KHPMAFLPF 374
                       410       420       430
                ....*....|....*....|....*....|....
gi 4503211  470 GYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11052 375 GLGPRNCIGQNFATMEAKIVLAMILQRFSFTLSP 408
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
147-502 2.36e-28

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: 116.97  E-value: 2.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  147 FTTEGHHWYQLRQALNqrllkPAEAALY----TDAFNEVIDDFMTRLDQLrAESasgNQVSDMAQLFYYFALEAICYILF 222
Cdd:cd11051  50 ISMEGEEWKRLRKRFN-----PGFSPQHlmtlVPTILDEVEIFAAILREL-AES---GEVFSLEELTTNLTFDVIGRVTL 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  223 EKRIGClQRSIPEDTvTFVRSIGLMFQNSLyatFLPKWTRPVLPfWKRYLDGwNAIFSFGKKLIDEKLEdMEaqlqaagp 302
Cdd:cd11051 121 DIDLHA-QTGDNSLL-TALRLLLALYRSLL---NPFKRLNPLRP-LRRWRNG-RRLDRYLKPEVRKRFE-LE-------- 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  303 dgiqvsgylhfllasgqlsprEAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEAL---HEEVVGVVP---AGQVPQ 376
Cdd:cd11051 185 ---------------------RAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVraeHDEVFGPDPsaaAELLRE 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  377 HKDFAH-MPLLKAVLKETLRLYPVVPTnSRIIEKEIEV---DGFLFPKNTQFVF-CHYVVSRDPTAFSEPESFQPHRWLR 451
Cdd:cd11051 244 GPELLNqLPYTTAVIKETLRLFPPAGT-ARRGPPGVGLtdrDGKEYPTDGCIVYvCHHAIHRDPEYWPRPDEFIPERWLV 322
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 4503211  452 nsQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLA 502
Cdd:cd11051 323 --DEGHELYPPKSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFEKA 371
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
233-526 3.96e-28

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: 116.39  E-value: 3.96e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  233 IPEDTV-TFVRSIGLMFQNSLyatfLPKWTRPVLPFWK-RYLDGWnaifsfgkklIDEKLEDMEAQLQAAGPDGIQVSGY 310
Cdd:cd20614 128 VPTDDLpEWRRQYRELFLGVL----PPPVDLPGMPARRsRRARAW----------IDARLSQLVATARANGARTGLVAAL 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  311 LHFLLASGQ-LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGvvpAGQVP-QHKDFAHMPLLKA 388
Cdd:cd20614 194 IRARDDNGAgLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAA---AGDVPrTPAELRRFPLAEA 270
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  389 VLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpriqhPFGSVP 468
Cdd:cd20614 271 LFRETLRLHPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPN-----PVELLQ 345
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503211  469 FGYGVRACLGRRIAELEM---QLLLARLIQKYKVVLAPETGELKSVARIVLVPNKKVGLQF 526
Cdd:cd20614 346 FGGGPHFCLGYHVACVELvqfIVALARELGAAGIRPLLVGVLPGRRYFPTLHPSNKTRVAF 406
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
92-497 4.04e-28

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: 116.43  E-value: 4.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   92 YGPMWMSYLGPQMHVNLASAPLLEQVMRQegkypvrNDMELWKEHR---------DQHDLT---YGPftteghHWYQLRQ 159
Cdd:cd20656   1 YGPIISVWIGSTLNVVVSSSELAKEVLKE-------KDQQLADRHRtrsaarfsrNGQDLIwadYGP------HYVKVRK 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  160 ALNQRL--------LKPAEAALYTDAFNEVIDDFMTRlDQLRAESASGNQVSDMAqlfyyfaLEAICYILFEKRIGCLQR 231
Cdd:cd20656  68 LCTLELftpkrlesLRPIREDEVTAMVESIFNDCMSP-ENEGKPVVLRKYLSAVA-------FNNITRLAFGKRFVNAEG 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  232 SIPEDTVTFvRSI---GLMFQNSL-YATFLPkwtrpvlpfWKRYLDGWNAIfSFGK------KLIDEKLEDMEAQLQAAG 301
Cdd:cd20656 140 VMDEQGVEF-KAIvsnGLKLGASLtMAEHIP---------WLRWMFPLSEK-AFAKhgarrdRLTKAIMEEHTLARQKSG 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  302 PdGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFA 381
Cdd:cd20656 209 G-GQQHFVALLTLKEQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFP 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  382 HMPLLKAVLKETLRLYPvvPTNSRIIEK---EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsQPATP 458
Cdd:cd20656 288 QLPYLQCVVKEALRLHP--PTPLMLPHKaseNVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFL---EEDVD 362
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 4503211  459 RIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKY 497
Cdd:cd20656 363 IKGHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHF 401
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
107-499 4.07e-28

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 116.70  E-value: 4.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  107 NLASAPLLEQVMRQEGKYPvRNDMELWKEHRDQHdltYGPFTTEGHHWYqlrqalnqrlLKPAEaalYTDAFNE-VIDDF 185
Cdd:cd11040  42 TLSFDPIVIVVVGRVFGSP-ESAKKKEGEPGGKG---LIRLLHDLHKKA----------LSGGE---GLDRLNEaMLENL 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  186 MTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLMFQNslyatfLPKWTRPvl 265
Cdd:cd11040 105 SKLLDELSLSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPELDPDLVEDFWTFDRGLPKLLLG------LPRLLAR-- 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  266 pfwkrylDGWNAIfsfgKKLIDEkledMEAQLQAAGPDGIQVSGYLH---FLLASGQLSPREaMGSLpELLM--AGVDTT 340
Cdd:cd11040 177 -------KAYAAR----DRLLKA----LEKYYQAAREERDDGSELIRaraKVLREAGLSEED-IARA-ELALlwAINANT 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  341 SNTLTWALYHLSKDPEIQEALHEEVVGVV-PAGQVPQHKD----FAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDG 415
Cdd:cd11040 240 IPAAFWLLAHILSDPELLERIREEIEPAVtPDSGTNAILDltdlLTSCPLLDSTYLETLRLHSSSTSVRLVTEDTVLGGG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  416 FLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWLRNSQPATPRiQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd11040 320 YLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKKGR-GLPGAFRPFGGGASLCPGRHFAKNEILAFVALLL 398

                ....*
gi 4503211  495 QKYKV 499
Cdd:cd11040 399 SRFDV 403
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
91-512 1.19e-27

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: 115.71  E-value: 1.19e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQE-GKYPvrNDMELWKEHRDQHDltyGPFTTEGHHWYQLRQALNQRLlKPA 169
Cdd:cd20649   1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKDfNNFT--NRMKANLITKPMSD---SLLCLRDERWKRVRSILTPAF-SAA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  170 EAALYTDAFNEVIDdfmTRLDQLRAESASGNQVsDMAQLFYYFALEAICYILFEKRIGCLQRsiPEDTvtFVRSIGLMFQ 249
Cdd:cd20649  75 KMKEMVPLINQACD---VLLRNLKSYAESGNAF-NIQRCYGCFTMDVVASVAFGTQVDSQKN--PDDP--FVKNCKRFFE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  250 NSLYATFL------PKWTRP---VLPFWKRyldgwNAIFSFGKKLIDEKLEDMEAQ---------LQ-------AAGPDG 304
Cdd:cd20649 147 FSFFRPILilflafPFIMIPlarILPNKSR-----DELNSFFTQCIRNMIAFRDQQspeerrrdfLQlmldartSAKFLS 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  305 IQvsgylHF----------------LLASGQLSPREAMGSLPE---------LLMAGVDTTSNTLTWALYHLSKDPEIQE 359
Cdd:cd20649 222 VE-----HFdivndadesaydghpnSPANEQTKPSKQKRMLTEdeivgqafiFLIAGYETTTNTLSFATYLLATHPECQK 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  360 ALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPK----NTQFVFCHYvvsrDP 435
Cdd:cd20649 297 KLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAgavlEIPVGFLHH----DP 372
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  436 TAFSEPESFQPHRWlrnsQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETG---ELKSVA 512
Cdd:cd20649 373 EHWPEPEKFIPERF----TAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEiplQLKSKS 448
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
151-504 2.49e-27

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: 113.92  E-value: 2.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  151 GHHWYQLRQALNQRLLKPAeAALYTDAFNEVIDDFMTRLDQLRAESASGnqVSDMAQLFYYFALEAICYILFEKrigclq 230
Cdd:cd20615  57 GTDWKRVRKVFDPAFSHSA-AVYYIPQFSREARKWVQNLPTNSGDGRRF--VIDPAQALKFLPFRVIAEILYGE------ 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  231 rsIPEDTVTFVRSIGLMFQNSLYATFLPKWTRPVlpfWKRYLD--GWNAIFSFGKKLIDEKLEDMEAQLQAaGPDGIQVS 308
Cdd:cd20615 128 --LSPEEKEELWDLAPLREELFKYVIKGGLYRFK---ISRYLPtaANRRLREFQTRWRAFNLKIYNRARQR-GQSTPIVK 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  309 GYLHFLlaSGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVgvvpagqvpQHKDFAHMP---- 384
Cdd:cd20615 202 LYEAVE--KGDITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEIS---------AAREQSGYPmedy 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  385 ------LLKAVLKETLRLYPVVP-TNSRIIEKEIEVDGFLFPKNTQFVFCHYVVS-RDPTAFSEPESFQPHRWLRNSQPA 456
Cdd:cd20615 271 ilstdtLLAYCVLESLRLRPLLAfSVPESSPTDKIIGGYRIPANTPVVVDTYALNiNNPFWGPDGEAYRPERFLGISPTD 350
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 4503211  457 TpRiqhpFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPE 504
Cdd:cd20615 351 L-R----YNFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPDQ 393
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
88-503 6.62e-27

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: 112.93  E-value: 6.62e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   88 YKAKYGPMWMSYLGPQMHVNLASAPLLEQVM-------RQEGKYPVRNDMElwkehrdqhdlTYGPFTTEGHHWyqlrqA 160
Cdd:cd20639   7 WRKIYGKTFLYWFGPTPRLTVADPELIREILltradhfDRYEAHPLVRQLE-----------GDGLVSLRGEKW-----A 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  161 LNQRLLKPAeaaLYTDAFN----EVIDDFMTRLDQLRAESASGNQVS-DMAQLFYYFALEAICYILFekrigclQRSIPE 235
Cdd:cd20639  71 HHRRVITPA---FHMENLKrlvpHVVKSVADMLDKWEAMAEAGGEGEvDVAEWFQNLTEDVISRTAF-------GSSYED 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  236 DTVTFvrsiGLMFQNSLYATflpkwtrpvLPFWKRYLDGWNAIFSFGKKL---IDEKLEDMEAQL----QAAGPDGIQVS 308
Cdd:cd20639 141 GKAVF----RLQAQQMLLAA---------EAFRKVYIPGYRFLPTKKNRKswrLDKEIRKSLLKLierrQTAADDEKDDE 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  309 GY---LHFLLASGQLSPREAMGsLPELL-------MAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHK 378
Cdd:cd20639 208 DSkdlLGLMISAKNARNGEKMT-VEEIIeecktffFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKD 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  379 DFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFS-EPESFQPHRWlrnSQPAT 457
Cdd:cd20639 287 HLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWGnDAAEFNPARF---ADGVA 363
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 4503211  458 PRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd20639 364 RAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLSP 409
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
286-518 1.18e-26

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: 112.50  E-value: 1.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  286 IDEKLEDMEAQLQAAGPDGIQVSGY-LHFLLAsgqlspreamgslpELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEE 364
Cdd:cd20652 209 ELCELEKAKKEGEDRDLFDGFYTDEqLHHLLA--------------DLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRE 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  365 VVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVP---TNSRIieKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEP 441
Cdd:cd20652 275 LDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPlgiPHGCT--EDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEP 352
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503211  442 ESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP--ETGELKSVARIVLVP 518
Cdd:cd20652 353 EEFRPERFLDTDG----KYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIALPDgqPVDSEGGNVGITLTP 427
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
316-504 1.39e-26

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


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 112.01  E-value: 1.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  316 ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLR 395
Cdd:cd11028 223 PEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMR 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  396 LYPVVP-TNSRIIEKEIEVDGFLFPKNTqFVFCH-YVVSRDPTAFSEPESFQPHRWL-RNS---QPATPRIqhpfgsVPF 469
Cdd:cd11028 303 HSSFVPfTIPHATTRDTTLNGYFIPKGT-VVFVNlWSVNHDEKLWPDPSVFRPERFLdDNGlldKTKVDKF------LPF 375
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4503211  470 GYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPE 504
Cdd:cd11028 376 GAGRRRCLGEELARMELFLFFATLLQQCEFSVKPG 410
PLN02687 PLN02687
flavonoid 3'-monooxygenase
318-502 1.49e-26

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 112.98  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   318 GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLY 397
Cdd:PLN02687 291 GRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLH 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   398 PVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQ-HPFGSVPFGYGVRA 475
Cdd:PLN02687 371 PSTPLSlPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKgSDFELIPFGAGRRI 450
                        170       180
                 ....*....|....*....|....*..
gi 4503211   476 CLGRRIAELEMQLLLARLIQKYKVVLA 502
Cdd:PLN02687 451 CAGLSWGLRMVTLLTATLVHAFDWELA 477
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
181-503 3.41e-26

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 111.80  E-value: 3.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   181 VIDDFMTRLDQLRAESASGNQVSDMAQLFYYFALEAICYILFEKRIGCLQRSIPEdtVTFVRSiglmFQNSLYATFLpkw 260
Cdd:PLN03195 146 VFREYSLKLSSILSQASFANQVVDMQDLFMRMTLDSICKVGFGVEIGTLSPSLPE--NPFAQA----FDTANIIVTL--- 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   261 tRPVLPFW--KRYLD-GWNAIFSFGKKLIDE----KLEDMEAQLQAAGPDGIQVSGYL--HFLLASGQLSPREAMGSLPE 331
Cdd:PLN03195 217 -RFIDPLWklKKFLNiGSEALLSKSIKVVDDftysVIRRRKAEMDEARKSGKKVKHDIlsRFIELGEDPDSNFTDKSLRD 295
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   332 LLM----AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVG--------------------VVPAGQVPQHKDFAHMPLLK 387
Cdd:PLN03195 296 IVLnfviAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKAlekerakeedpedsqsfnqrVTQFAGLLTYDSLGKLQYLH 375
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   388 AVLKETLRLYPVVPTNSR-IIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWLRNS--QPATPriqhp 463
Cdd:PLN03195 376 AVITETLRLYPAVPQDPKgILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGvfQNASP----- 450
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 4503211   464 FGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:PLN03195 451 FKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQLVP 490
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
195-518 3.61e-26

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: 110.67  E-value: 3.61e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  195 ESASGNQVsDMAQLFYYFALEAICYILFEKRIgclqrsipEDT-VTFVRSIGLMFQN---------SLYATFlpkwtrPV 264
Cdd:cd20664  97 EKHKGKPF-ETTLSMNVAVSNIIASIVLGHRF--------EYTdPTLLRMVDRINENmkltgspsvQLYNMF------PW 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  265 LPFWKryldGW-NAIFSFGKKLIDEKLEDMEAQLQAAGPDGIQvsGYLHFLLASgQLSPREAMGS----------LPELL 333
Cdd:cd20664 162 LGPFP----GDiNKLLRNTKELNDFLMETFMKHLDVLEPNDQR--GFIDAFLVK-QQEEEESSDSffhddnltcsVGNLF 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  334 MAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQvPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIE 412
Cdd:cd20664 235 GAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQ-PQVEHRKNMPYTDAVIHEIQRFANIVPMNlPHATTRDVT 313
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  413 VDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrNSQPATPRiQHPFgsVPFGYGVRACLGRRIAELEMQLLLAR 492
Cdd:cd20664 314 FRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFL-DSQGKFVK-RDAF--MPFSAGRRVCIGETLAKMELFLFFTS 389
                       330       340       350
                ....*....|....*....|....*....|
gi 4503211  493 LIQKYKVVLAPETGE----LKSVARIVLVP 518
Cdd:cd20664 390 LLQRFRFQPPPGVSEddldLTPGLGFTLNP 419
PLN02655 PLN02655
ent-kaurene oxidase
310-507 6.40e-26

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 110.60  E-value: 6.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   310 YLHFLLA-SGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQhKDFAHMPLLKA 388
Cdd:PLN02655 247 YLDFLLSeATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTE-EDLPNLPYLNA 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   389 VLKETLRLY---PVVPtnSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRiqhpFG 465
Cdd:PLN02655 326 VFHETLRKYspvPLLP--PRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADM----YK 399
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4503211   466 SVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGE 507
Cdd:PLN02655 400 TMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREGDEE 441
PTZ00404 PTZ00404
cytochrome P450; Provisional
331-499 7.12e-26

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 110.58  E-value: 7.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEK 409
Cdd:PTZ00404 290 DFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGlPRSTSN 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   410 EIEVDGFLF-PKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpriqhpFgsVPFGYGVRACLGRRIAELEMQL 488
Cdd:PTZ00404 370 DIIIGGGHFiPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSNDA------F--MPFSIGPRNCVGQQFAQDELYL 441
                        170
                 ....*....|.
gi 4503211   489 LLARLIQKYKV 499
Cdd:PTZ00404 442 AFSNIILNFKL 452
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
287-516 1.21e-25

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 109.29  E-value: 1.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  287 DEKLEDMEAQLQAAGP-DGIQVSGYLHFL--LASGQ------LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEI 357
Cdd:cd20678 193 DKVIQQRKEQLQDEGElEKIKKKRHLDFLdiLLFAKdengksLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEH 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  358 QEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIE-VDGFLFPKNTQFVFCHYVVSRDPT 436
Cdd:cd20678 273 QQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTfPDGRSLPAGITVSLSIYGLHHNPA 352
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  437 AFSEPESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPeTGELKSVARIVL 516
Cdd:cd20678 353 VWPNPEVFDPLRFS----PENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLPDP-TRIPIPIPQLVL 427
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
331-527 1.60e-25

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: 109.24  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEK 409
Cdd:cd20654 248 ELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPLLGpREATE 327
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  410 EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHpFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd20654 328 DCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKDIDVRGQN-FELIPFGSGRRSCPGVSFGLQVMHLT 406
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 4503211  490 LARLIQKYKvVLAPETGELKSVARIVLVPNKKVGLQFL 527
Cdd:cd20654 407 LARLLHGFD-IKTPSNEPVDMTEGPGLTNPKATPLEVL 443
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
335-522 3.96e-25

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: 107.79  E-value: 3.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTnsrIIEKEIEVD 414
Cdd:cd20673 243 AGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPL---LIPHVALQD 319
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  415 ----GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnsQPATPRIQHPFGS-VPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd20673 320 ssigEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFL---DPTGSQLISPSLSyLPFGAGPRVCLGEALARQELFLF 396
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 4503211  490 LARLIQKYKVVLAPETG--ELKSVARIVLVPNK-KV 522
Cdd:cd20673 397 MAWLLQRFDLEVPDGGQlpSLEGKFGVVLQIDPfKV 432
PLN02738 PLN02738
carotene beta-ring hydroxylase
111-503 4.89e-25

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 109.23  E-value: 4.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   111 APLLEQVMrqeGKYPVRNDMELWKEHRdqhdltygpftteghhwyqlrqalnqRLLKPAEAALYTDAFNEVIDDFMTRL- 189
Cdd:PLN02738 203 AEILEFVM---GKGLIPADGEIWRVRR--------------------------RAIVPALHQKYVAAMISLFGQASDRLc 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   190 DQLRAESASGNQVsDMAQLFYYFALEAICYILFEKRIGclqrSIPEDTvtfvrsiGLMfqNSLYATFLPKWTRPV--LPF 267
Cdd:PLN02738 254 QKLDAAASDGEDV-EMESLFSRLTLDIIGKAVFNYDFD----SLSNDT-------GIV--EAVYTVLREAEDRSVspIPV 319
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   268 WKryLDGWNAIFSFGKK------LIDEKLEDM---------EAQLQAAGPD-GIQVSGYLHFLLASG-QLSPREAMGSLP 330
Cdd:PLN02738 320 WE--IPIWKDISPRQRKvaealkLINDTLDDLiaickrmveEEELQFHEEYmNERDPSILHFLLASGdDVSSKQLRDDLM 397
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTnsrIIEKE 410
Cdd:PLN02738 398 TMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVL-GDRFPTIEDMKKLKYTTRVINESLRLYPQPPV---LIRRS 473
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   411 IEVD---GFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQ 487
Cdd:PLN02738 474 LENDmlgGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPLDG-PNPNETNQNFSYLPFGGGPRKCVGDMFASFENV 552
                        410
                 ....*....|....*.
gi 4503211   488 LLLARLIQKYKVVLAP 503
Cdd:PLN02738 553 VATAMLVRRFDFQLAP 568
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
329-497 5.23e-25

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 108.40  E-value: 5.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   329 LPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRII 407
Cdd:PLN00110 294 LLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNlPRVS 373
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   408 EKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWL--RNSQpATPRiQHPFGSVPFGYGVRACLGRRIAELE 485
Cdd:PLN00110 374 TQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLseKNAK-IDPR-GNDFELIPFGAGRRICAGTRMGIVL 451
                        170
                 ....*....|..
gi 4503211   486 MQLLLARLIQKY 497
Cdd:PLN00110 452 VEYILGTLVHSF 463
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
331-518 7.49e-25

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: 106.81  E-value: 7.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEK 409
Cdd:cd20662 232 DLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNvPREVAV 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  410 EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatPRIQHPFgsVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd20662 312 DTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQ---FKKREAF--LPFSMGKRACLGEQLARSELFIF 386
                       170       180       190
                ....*....|....*....|....*....|..
gi 4503211  490 LARLIQKYkvVLAPETGE---LKSVARIVLVP 518
Cdd:cd20662 387 FTSLLQKF--TFKPPPNEklsLKFRMGITLSP 416
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
91-493 7.96e-25

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: 106.78  E-value: 7.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMwmsylgpqMHVNLASAPLL--------EQVMRqegkypvRNDME------------LWkehRDQHDLTYGPFtte 150
Cdd:cd11072   1 KYGPL--------MLLRLGSVPTVvvsspeaaKEVLK-------THDLVfasrpkllaariLS---YGGKDIAFAPY--- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  151 GHHWYQLRQALNQRLLKPAEAALYTDAFNEVIDDFMTRLdqlrAESASGNQVSDMAQLFYYFALEAICYILFEKRIGClq 230
Cdd:cd11072  60 GEYWRQMRKICVLELLSAKRVQSFRSIREEEVSLLVKKI----RESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEG-- 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  231 rsipEDTVTFvrsIGLMFQNSLYAT------FLP--KWTRpVLPFWKRYLD----GWNAIFsfgKKLIDEKLEDMEAQLQ 298
Cdd:cd11072 134 ----KDQDKF---KELVKEALELLGgfsvgdYFPslGWID-LLTGLDRKLEkvfkELDAFL---EKIIDEHLDKKRSKDE 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  299 AAGPDG-----IQVSGYLHFLLASGQLsprEAMgsLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQ 373
Cdd:cd11072 203 DDDDDDlldlrLQKEGDLEFPLTRDNI---KAI--ILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKG 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  374 VPQHKDFAHMPLLKAVLKETLRLYPVVP-TNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRN 452
Cdd:cd11072 278 KVTEEDLEKLKYLKAVIKETLRLHPPAPlLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDS 357
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 4503211  453 SqpATPRIQHpFGSVPFGYGVRAC----LGrrIAELEmqLLLARL 493
Cdd:cd11072 358 S--IDFKGQD-FELIPFGAGRRICpgitFG--LANVE--LALANL 395
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
284-503 3.32e-24

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: 104.88  E-value: 3.32e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  284 KLIDEKLEDMEA----QLQAAGP--DGIQVSGYLHFLLASGQL-SPREAM-------GSLPELLMAGVDTTSNTLTWALY 349
Cdd:cd20671 169 KPILDKVEEVCMilrtLIEARRPtiDGNPLHSYIEALIQKQEEdDPKETLfhdanvlACTLDLVMAGTETTSTTLQWAVL 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  350 HLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHY 429
Cdd:cd20671 249 LMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLS 328
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503211  430 VVSRDPTAFSEPESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd20671 329 SVLLDKTQWETPYQFNPNHFL----DAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPP 398
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
263-520 5.51e-24

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: 104.76  E-value: 5.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  263 PVLPFW------KRYLDGWNAIFSFGKKLIDEKLEdmeaqlQAAGPDGIQVSGYLHFLL----ASGQ--LSPREAMGSLP 330
Cdd:cd20658 170 PFLRGLdldgheKIVREAMRIIRKYHDPIIDERIK------QWREGKKKEEEDWLDVFItlkdENGNplLTPDEIKAQIK 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEK 409
Cdd:cd20658 244 ELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNvPHVAMS 323
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  410 EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpRIQHPFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd20658 324 DTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVT-LTEPDLRFISFSTGRRGCPGVKLGTAMTVML 402
                       250       260       270
                ....*....|....*....|....*....|.
gi 4503211  490 LARLIQKYKVVLAPetgelkSVARIVLVPNK 520
Cdd:cd20658 403 LARLLQGFTWTLPP------NVSSVDLSESK 427
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
331-497 6.34e-24

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: 104.39  E-value: 6.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEK 409
Cdd:cd20663 237 DLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGvPHMTSR 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  410 EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRnsqpATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd20663 317 DIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLD----AQGHFVKPEAFMPFSAGRRACLGEPLARMELFLF 392

                ....*...
gi 4503211  490 LARLIQKY 497
Cdd:cd20663 393 FTCLLQRF 400
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
328-505 3.17e-23

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: 102.20  E-value: 3.17e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  328 SLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RI 406
Cdd:cd20661 242 SVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIfHA 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  407 IEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRiqHPFgsVPFGYGVRACLGRRIAELEM 486
Cdd:cd20661 322 TSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKK--EAF--VPFSLGRRHCLGEQLARMEM 397
                       170
                ....*....|....*....
gi 4503211  487 QLLLARLIQKYKVVLAPET 505
Cdd:cd20661 398 FLFFTALLQRFHLHFPHGL 416
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
280-506 5.15e-23

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: 101.64  E-value: 5.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  280 SFGKKLIDEKledmEAQLQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQE 359
Cdd:cd11076 184 TFVGKIIEEH----RAKRSNRARDDEDDVDVLLSLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQS 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  360 ALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS--RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTA 437
Cdd:cd11076 260 KAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLLSwaRLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHV 339
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503211  438 FSEPESFQPHRWLRNSQPATPRIqhpFGS----VPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETG 506
Cdd:cd11076 340 WEDPLEFKPERFVAAEGGADVSV---LGSdlrlAPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDAKP 409
PLN02183 PLN02183
ferulate 5-hydroxylase
144-494 6.74e-23

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 101.85  E-value: 6.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   144 YGPFtteghhWYQLRQALNQRLLKPAEAALYTDAFNEVidDFMtrldqLRAESASGNQVSDMAQLFYYFALEaicyILFE 223
Cdd:PLN02183 125 YGPF------WRQMRKLCVMKLFSRKRAESWASVRDEV--DSM-----VRSVSSNIGKPVNIGELIFTLTRN----ITYR 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   224 KRIGCLQRSIPEDTVTFVRSIGLMFQNSLYATFLP--KWTRPVlPFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAG 301
Cdd:PLN02183 188 AAFGSSSNEGQDEFIKILQEFSKLFGAFNVADFIPwlGWIDPQ-GLNKRLVKARKSLDGFIDDIIDDHIQKRKNQNADND 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   302 PDGIQ---VSGYLHFLLASGQLSPREAMGSLPEL------------LMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVV 366
Cdd:PLN02183 267 SEEAEtdmVDDLLAFYSEEAKVNESDDLQNSIKLtrdnikaiimdvMFGGTETVASAIEWAMAELMKSPEDLKRVQQELA 346
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   367 GVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQP 446
Cdd:PLN02183 347 DVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKP 426
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 4503211   447 HRWLrnsQPATPRIQ-HPFGSVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:PLN02183 427 SRFL---KPGVPDFKgSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLL 472
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
319-516 1.47e-22

cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4F subfamily show diverse specificities among its members: CYP4F2 and CYP4F3 metabolize pro- and anti-inflammatory leukotrienes; CYP4F8 and CYP4F12 metabolize prostaglandins, endoperoxides and arachidonic acid; CYP4F11 and CYP4F12 metabolize VLFA and are unique in the CYP4F subfamily since they also hydroxylate xenobiotics such as benzphetamine, ethylmorphine, erythromycin, and ebastine. CYP4F belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 100.15  E-value: 1.47e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  319 QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQH---KDFAHMPLLKAVLKETLR 395
Cdd:cd20679 239 ELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELL-KDREPEEiewDDLAQLPFLTMCIKESLR 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  396 LYPVVPTNSRIIEKEIEV-DGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWlrnsQPATPRIQHPFGSVPFGYGVR 474
Cdd:cd20679 318 LHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF----DPENSQGRSPLAFIPFSAGPR 393
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 4503211  475 ACLGRRIAELEMQLLLARLIQKYKVVlaPETGELKSVARIVL 516
Cdd:cd20679 394 NCIGQTFAMAEMKVVLALTLLRFRVL--PDDKEPRRKPELIL 433
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
332-495 1.52e-22

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: 99.99  E-value: 1.52e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKE 410
Cdd:cd20653 235 MLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLvPHESSED 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  411 IEVDGFLFPKNTqFVFCH-YVVSRDPTAFSEPESFQPHRWLRNSqpatpriQHPFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd20653 315 CKIGGYDIPRGT-MLLVNaWAIHRDPKLWEDPTKFKPERFEGEE-------REGYKLIPFGLGRRACPGAGLAQRVVGLA 386

                ....*.
gi 4503211  490 LARLIQ 495
Cdd:cd20653 387 LGSLIQ 392
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
317-504 1.89e-22

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: 99.79  E-value: 1.89e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  317 SGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRL 396
Cdd:cd20677 229 SAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRH 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  397 YPVVP-TNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWL-RNSQPATPRIQHpfgSVPFGYGVR 474
Cdd:cd20677 309 SSFVPfTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLdENGQLNKSLVEK---VLIFGMGVR 385
                       170       180       190
                ....*....|....*....|....*....|
gi 4503211  475 ACLGRRIAELEMQLLLARLIQKYKVVLAPE 504
Cdd:cd20677 386 KCLGEDVARNEIFVFLTTILQQLKLEKPPG 415
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
91-498 2.49e-22

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 100.28  E-value: 2.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    91 KYGPMWMSYLGPQMHVNLASAPLLEQVM-RQEGKYPVRNDMeLWKEH--RDQHDLTYGPFtteGHHWYQLRQALNQRLLK 167
Cdd:PLN03112  63 KYGPLVYLRLGSVDAITTDDPELIREILlRQDDVFASRPRT-LAAVHlaYGCGDVALAPL---GPHWKRMRRICMEHLLT 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   168 PAEAALYTdafNEVIDDFMTRLDQLRAESASGNQVsDMAQLFYYFALEAICYILFEKRIGCLQRSIPEDTVTFVRSIGLM 247
Cdd:PLN03112 139 TKRLESFA---KHRAEEARHLIQDVWEAAQTGKPV-NLREVLGAFSMNNVTRMLLGKQYFGAESAGPKEAMEFMHITHEL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   248 FQ--NSLY-ATFLPKWtRPVLP--FWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGP-DGIQVSGYLHFLLASGQLS 321
Cdd:PLN03112 215 FRllGVIYlGDYLPAW-RWLDPygCEKKMREVEKRVDEFHDKIIDEHRRARSGKLPGGKDmDFVDVLLSLPGENGKEHMD 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   322 PREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVP 401
Cdd:PLN03112 294 DVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGP 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   402 TnsrIIEKE----IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHP-FGSVPFGYGVRAC 476
Cdd:PLN03112 374 F---LIPHEslraTTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGSRVEISHGPdFKILPFSAGKRKC 450
                        410       420
                 ....*....|....*....|..
gi 4503211   477 LGRRIAELEMQLLLARLIQKYK 498
Cdd:PLN03112 451 PGAPLGVTMVLMALARLFHCFD 472
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
335-504 3.34e-22

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: 99.06  E-value: 3.34e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD 414
Cdd:cd20641 246 AGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLG 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  415 GFLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWlRN--SQPATpriqHPFGSVPFGYGVRACLGRRIAELEMQLLLA 491
Cdd:cd20641 326 GLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRF-ANgvSRAAT----HPNALLSFSLGPRACIGQNFAMIEAKTVLA 400
                       170
                ....*....|...
gi 4503211  492 RLIQKYKVVLAPE 504
Cdd:cd20641 401 MILQRFSFSLSPE 413
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
332-509 3.93e-22

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: 98.68  E-value: 3.93e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKE 410
Cdd:cd20669 234 LLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSlPHAVTRD 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWL--RNSQPATPRIqhpfgsVPFGYGVRACLGRRIAELEMQL 488
Cdd:cd20669 314 TNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLddNGSFKKNDAF------MPFSAGKRICLGESLARMELFL 387
                       170       180
                ....*....|....*....|...
gi 4503211  489 LLARLIQKY--KVVLAPETGELK 509
Cdd:cd20669 388 YLTAILQNFslQPLGAPEDIDLT 410
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
335-504 4.57e-22

cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP714 enzymes are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels. They contribute to the production of diverse GA compounds through various oxidations of C and D rings in both monocots and eudicots. CYP714B1 and CYP714B2 encode the enzyme GA 13-oxidase, which is required for GA1 biosynthesis, while CYP714D1 encodes GA 16a,17-epoxidase, which inactivates the non-13-hydroxy GAs in rice. Arabidopsis CYP714A1 is an inactivation enzyme that catalyzes the conversion of GA12 to 16-carboxylated GA12 (16-carboxy-16beta,17-dihydro GA12). CYP714 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 98.64  E-value: 4.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD 414
Cdd:cd20640 241 AGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVC-KGGPPDADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLG 319
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  415 GFLFPKNTQFVFCHYVVSRDPTAF-SEPESFQPHRWlRNSQPATPRIQHPFgsVPFGYGVRACLGRRIAELEMQLLLARL 493
Cdd:cd20640 320 GLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERF-SNGVAAACKPPHSY--MPFGAGARTCLGQNFAMAELKVLVSLI 396
                       170
                ....*....|.
gi 4503211  494 IQKYKVVLAPE 504
Cdd:cd20640 397 LSKFSFTLSPE 407
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
287-505 7.57e-22

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 98.51  E-value: 7.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   287 DEKLEDMEAQLQAAGpDGIQVSGYLHFLLAsgqlspreamgslpeLLMAGVDTTSNTLTWALYHLSKDP----EIQEAlH 362
Cdd:PLN02987 246 AEKKKDMLAALLASD-DGFSDEEIVDFLVA---------------LLVAGYETTSTIMTLAVKFLTETPlalaQLKEE-H 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   363 EEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPE 442
Cdd:PLN02987 309 EKIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDAR 388
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503211   443 SFQPHRWLRNSQPATPriqhpfGSV--PFGYGVRACLGRRIAELEMQLLLARLIQKY--------KVVLAPET 505
Cdd:PLN02987 389 TFNPWRWQSNSGTTVP------SNVftPFGGGPRLCPGYELARVALSVFLHRLVTRFswvpaeqdKLVFFPTT 455
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
145-505 1.52e-21

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 97.84  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   145 GPFTTEGHHWyqlrqaLNQRLLKPAE---AALYTDAFNEVIDDFMTRLDQLRAESASGN--QVSDMAQLFYYFALEAICY 219
Cdd:PLN02426 122 GIFNVDGDSW------RFQRKMASLElgsVSIRSYAFEIVASEIESRLLPLLSSAADDGegAVLDLQDVFRRFSFDNICK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   220 ILFEKRIGCLQRSIP--EDTVTFVRSIGLMFQNSLYATflpkwtrPVLPFWKRYLDgwnaIFSFGK-----KLIDEKLED 292
Cdd:PLN02426 196 FSFGLDPGCLELSLPisEFADAFDTASKLSAERAMAAS-------PLLWKIKRLLN----IGSERKlkeaiKLVDELAAE 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   293 MEAQLQAAGpdgiqvsgylhfLLASGQLSPReAMGSLPE----------LLMAGVDTTSNTLTWALYHLSKDPEIQEALH 362
Cdd:PLN02426 265 VIRQRRKLG------------FSASKDLLSR-FMASINDdkylrdivvsFLLAGRDTVASALTSFFWLLSKHPEVASAIR 331
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   363 EEVVGVVPAGQVPqhKDFAH---MPLLKAVLKETLRLYPVVPTNSRI-IEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAF 438
Cdd:PLN02426 332 EEADRVMGPNQEA--ASFEEmkeMHYLHAALYESMRLFPPVQFDSKFaAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIW 409
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503211   439 -SEPESFQPHRWLRNsqpATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:PLN02426 410 gPDCLEFKPERWLKN---GVFVPENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVGRS 474
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
332-497 1.70e-21

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: 96.92  E-value: 1.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKE 410
Cdd:cd20670 234 LFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGvPHNVIRD 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQLLL 490
Cdd:cd20670 314 TQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQG----RFKKNEAFVPFSSGKRVCLGEAMARMELFLYF 389

                ....*..
gi 4503211  491 ARLIQKY 497
Cdd:cd20670 390 TSILQNF 396
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
332-498 2.79e-21

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: 96.18  E-value: 2.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEKE 410
Cdd:cd20665 234 LFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLpHAVTCD 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSqpatpriqhpfGS-------VPFGYGVRACLGRRIAE 483
Cdd:cd20665 314 TKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDEN-----------GNfkksdyfMPFSAGKRICAGEGLAR 382
                       170
                ....*....|....*
gi 4503211  484 LEMQLLLARLIQKYK 498
Cdd:cd20665 383 MELFLFLTTILQNFN 397
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
324-504 3.88e-21

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: 96.60  E-value: 3.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  324 EAMGslpeLLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPA----GQVPQHKDFAHM--PLLKAVLKETLRLY 397
Cdd:cd20622 266 ELFG----YLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEavaeGRLPTAQEIAQAriPYLDAVIEEILRCA 341
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  398 PVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPES-----------------------FQPHRWLRNSQ 454
Cdd:cd20622 342 NTAPILSREATVDTQVLGYSIPKGTNVFLLNNGPSYLSPPIEIDESrrssssaakgkkagvwdskdiadFDPERWLVTDE 421
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 4503211  455 PATPRIQHP--FGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPE 504
Cdd:cd20622 422 ETGETVFDPsaGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPE 473
PLN02936 PLN02936
epsilon-ring hydroxylase
283-503 5.13e-21

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 96.01  E-value: 5.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   283 KKLIDEKLEDMEAQ--LQAAGPDgiqvsgYLHFLLASgqlspREAMGS------LPELLMAGVDTTSNTLTWALYHLSKD 354
Cdd:PLN02936 240 KEIVEAEGEVIEGEeyVNDSDPS------VLRFLLAS-----REEVSSvqlrddLLSMLVAGHETTGSVLTWTLYLLSKN 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   355 PEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPT-NSRIIEKEIEVDGFLFPKNTQFVFCHYVVSR 433
Cdd:PLN02936 309 PEALRKAQEELDRVL-QGRPPTYEDIKELKYLTRCINESMRLYPHPPVlIRRAQVEDVLPGGYKVNAGQDIMISVYNIHR 387
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503211   434 DPTAFSEPESFQPHRW-LRNSQPATPRIQHPFgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:PLN02936 388 SPEVWERAEEFVPERFdLDGPVPNETNTDFRY--IPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVP 456
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
316-506 1.58e-20

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: 93.93  E-value: 1.58e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  316 ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLR 395
Cdd:cd20676 229 ANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFR 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  396 LYPVVP-TNSRIIEKEIEVDGFLFPKNTqfvfCHYV----VSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPfGSVPFG 470
Cdd:cd20676 309 HSSFVPfTIPHCTTRDTSLNGYYIPKDT----CVFInqwqVNHDEKLWKDPSSFRPERFLTADGTEINKTESE-KVMLFG 383
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 4503211  471 YGVRACLGRRIAELEMQLLLARLIQKY--------KVVLAPETG 506
Cdd:cd20676 384 LGKRRCIGESIARWEVFLFLAILLQQLefsvppgvKVDMTPEYG 427
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
332-504 2.04e-20

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: 93.71  E-value: 2.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKE 410
Cdd:cd20668 234 LFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGlARRVTKD 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQpatpRIQHPFGSVPFGYGVRACLGRRIAELEMQLLL 490
Cdd:cd20668 314 TKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKG----QFKKSDAFVPFSIGKRYCFGEGLARMELFLFF 389
                       170
                ....*....|....*.
gi 4503211  491 ARLIQ--KYKVVLAPE 504
Cdd:cd20668 390 TTIMQnfRFKSPQSPE 405
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
332-498 2.08e-20

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 93.85  E-value: 2.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPA---GQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIE 408
Cdd:PLN02196 272 VIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDkeeGESLTWEDTKKMPLTSRVIQETLRVASILSFTFREAV 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   409 KEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpriqhpfgSVPFGYGVRACLGRRIAELEMQL 488
Cdd:PLN02196 352 EDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNT--------FMPFGNGTHSCPGNELAKLEISV 423
                        170
                 ....*....|
gi 4503211   489 LLARLIQKYK 498
Cdd:PLN02196 424 LIHHLTTKYR 433
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
283-499 2.43e-20

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: 93.19  E-value: 2.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  283 KKLIDEK---LEDMEAQLqaagpDGIQVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQE 359
Cdd:cd20616 185 EILIEQKrrrISTAEKLE-----DHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEE 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  360 ALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTaFS 439
Cdd:cd20616 260 AILKEIQTVL-GERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEF-FP 337
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  440 EPESFQphrwLRNSQPATPRIQHPfgsvPFGYGVRACLGRRIAELEMQLLLARLIQKYKV 499
Cdd:cd20616 338 KPNEFT----LENFEKNVPSRYFQ----PFGFGPRSCVGKYIAMVMMKAILVTLLRRFQV 389
PLN02971 PLN02971
tryptophan N-hydroxylase
314-502 4.63e-20

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 93.56  E-value: 4.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   314 LLASGQLSPreamgSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKET 393
Cdd:PLN02971 322 LLTADEIKP-----TIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREA 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   394 LRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATpRIQHPFGSVPFGYG 472
Cdd:PLN02971 397 FRLHPVAAFNlPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVT-LTENDLRFISFSTG 475
                        170       180       190
                 ....*....|....*....|....*....|
gi 4503211   473 VRACLGRRIAELEMQLLLARLIQKYKVVLA 502
Cdd:PLN02971 476 KRGCAAPALGTAITTMMLARLLQGFKWKLA 505
PLN00168 PLN00168
Cytochrome P450; Provisional
60-498 5.88e-20

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 93.09  E-value: 5.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    60 IPRLGQLrfffqLFVQGYALQLHQLQVLYKAKYGPMWMSYLGPQMHV-----NLASAPLLEQVMRQEGKYPVRNDMELWK 134
Cdd:PLN00168  43 VPLLGSL-----VWLTNSSADVEPLLRRLIARYGPVVSLRVGSRLSVfvadrRLAHAALVERGAALADRPAVASSRLLGE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   135 EHRDQHDLTYGPFtteghhWYQLRQALNQRLLKPAEAALYTDAFNEVIDDFMTRLDQlRAESASGNQVSDMAQLFYYFAL 214
Cdd:PLN00168 118 SDNTITRSSYGPV------WRLLRRNLVAETLHPSRVRLFAPARAWVRRVLVDKLRR-EAEDAAAPRVVETFQYAMFCLL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   215 EAICY--ILFE---KRIGCLQRsipeDTVTFVRSIGLMFqnslyaTFLPKWTRPVlpfWKRYLDGWNAIFSFGKK----L 285
Cdd:PLN00168 191 VLMCFgeRLDEpavRAIAAAQR----DWLLYVSKKMSVF------AFFPAVTKHL---FRGRLQKALALRRRQKElfvpL 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   286 IDEKLEDMEAQLQAAGPDGIQVS---GYLHFLL-------ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDP 355
Cdd:PLN00168 258 IDARREYKNHLGQGGEPPKKETTfehSYVDTLLdirlpedGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNP 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   356 EIQEALHEEVVGVVPAGQVP-QHKDFAHMPLLKAVLKETLRLYP----VVPTNSriiEKEIEVDGFLFPKNTQFVFCHYV 430
Cdd:PLN00168 338 SIQSKLHDEIKAKTGDDQEEvSEEDVHKMPYLKAVVLEGLRKHPpahfVLPHKA---AEDMEVGGYLIPKGATVNFMVAE 414
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503211   431 VSRDPTAFSEPESFQPHRWLRNSQ------PATPRIQhpfgSVPFGYGVRACLGRRIAELEMQLLLARLIQKYK 498
Cdd:PLN00168 415 MGRDEREWERPMEFVPERFLAGGDgegvdvTGSREIR----MMPFGVGRRICAGLGIAMLHLEYFVANMVREFE 484
PLN02302 PLN02302
ent-kaurenoic acid oxidase
332-499 7.03e-20

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 92.47  E-value: 7.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   332 LLM---AGVDTTSNTLTWALYHLSKDPEIQE---ALHEEVVGVVPAGQVPQH-KDFAHMPLLKAVLKETLRLYPVVPTNS 404
Cdd:PLN02302 292 LLMylnAGHESSGHLTMWATIFLQEHPEVLQkakAEQEEIAKKRPPGQKGLTlKDVRKMEYLSQVIDETLRLINISLTVF 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   405 RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNsqpaTPRiqhPFGSVPFGYGVRACLGRRIAEL 484
Cdd:PLN02302 372 REAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNY----TPK---AGTFLPFGLGSRLCPGNDLAKL 444
                        170
                 ....*....|....*
gi 4503211   485 EMQLLLARLIQKYKV 499
Cdd:PLN02302 445 EISIFLHHFLLGYRL 459
PLN03018 PLN03018
homomethionine N-hydroxylase
269-508 9.42e-20

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 92.38  E-value: 9.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   269 KRYLDGWNA-------------IFSFGKKLIDEKLED-MEAQLQAAGPDGIQVSGYLHFLLASGQLSPREAMGSLPELLM 334
Cdd:PLN03018 245 ERWLRGWNIdgqeerakvnvnlVRSYNNPIIDERVELwREKGGKAAVEDWLDTFITLKDQNGKYLVTPDEIKAQCVEFCI 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYP---VVPtnSRIIEKEI 411
Cdd:PLN03018 325 AAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPsahYVP--PHVARQDT 402
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   412 EVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNS--QPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:PLN03018 403 TLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDgiTKEVTLVETEMRFVSFSTGRRGCVGVKVGTIMMVMM 482
                        250
                 ....*....|....*....
gi 4503211   490 LARLIQKYKVVLAPETGEL 508
Cdd:PLN03018 483 LARFLQGFNWKLHQDFGPL 501
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
208-508 2.72e-19

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 90.22  E-value: 2.72e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  208 LFYYFALEAICYILFEKRIGCLQRSipedtvtFVRSIGLMFQN-SLYATFLPKWTRPVLPFWKRYLDGWNAIFSFGKKL- 285
Cdd:cd20672 109 LFQSITANIICSIVFGERFDYKDPQ-------FLRLLDLFYQTfSLISSFSSQVFELFSGFLKYFPGAHRQIYKNLQEIl 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  286 --IDEKLEDMEAQLQAAGP-DGIQVsgylhFLL--------ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKD 354
Cdd:cd20672 182 dyIGHSVEKHRATLDPSAPrDFIDT-----YLLrmekeksnHHTEFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKY 256
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  355 PEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSR 433
Cdd:cd20672 257 PHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGvPHRVTKDTLFRGYLLPKNTEVYPILSSALH 336
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503211  434 DPTAFSEPESFQPHRWLrnsqPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVV--LAPETGEL 508
Cdd:cd20672 337 DPQYFEQPDTFNPDHFL----DANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVAspVAPEDIDL 409
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
320-490 3.01e-19

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: 89.19  E-value: 3.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  320 LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvPAgqvpqhkdfahmpLLKAVLKETLRLYPV 399
Cdd:cd11035 186 LTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRED-----PE-------------LIPAAVEELLRRYPL 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  400 VPTNsRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatPRIQHpfgsVPFGYGVRACLGR 479
Cdd:cd11035 248 VNVA-RIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR---------KPNRH----LAFGAGPHRCLGS 313
                       170
                ....*....|.
gi 4503211  480 RIAELEMQLLL 490
Cdd:cd11035 314 HLARLELRIAL 324
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
60-497 3.12e-19

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 90.52  E-value: 3.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    60 IPRLGQLRFFFQLFVQGYALQLHQLqvlykakYGPMWMSYLGPQMHVNLASAPLLEQVMR-QEGKYPVRNDMELWKEHRD 138
Cdd:PLN03234  36 LPIIGNLHQMEKFNPQHFLFRLSKL-------YGPIFTMKIGGRRLAVISSAELAKELLKtQDLNFTARPLLKGQQTMSY 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   139 Q-HDLTYGPFTTeghHWYQLRQALNQRLLKPAEAALYTDAFNEVIDDFMTRLdqLRAESASGNqvSDMAQLFYYFALEAI 217
Cdd:PLN03234 109 QgRELGFGQYTA---YYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKI--YKAADQSGT--VDLSELLLSFTNCVV 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   218 CYILFEKRIGclqrsipEDTVTFVRSIGLMFQ-NSLYATFLPKWTRPVLPFWKRyLDGWNAIFSFGKKLIDEKLEDMEAQ 296
Cdd:PLN03234 182 CRQAFGKRYN-------EYGTEMKRFIDILYEtQALLGTLFFSDLFPYFGFLDN-LTGLSARLKKAFKELDTYLQELLDE 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   297 LQAAGPDGIQVSGYLHFLLA-------SGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVV 369
Cdd:PLN03234 254 TLDPNRPKQETESFIDLLMQiykdqpfSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVI 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   370 PAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTnsrIIEKEIEVD----GFLFPKNTQFVFCHYVVSRDPTAFSE-PESF 444
Cdd:PLN03234 334 GDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPI---LLHRETIADakigGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEF 410
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4503211   445 QPHRWLrNSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKY 497
Cdd:PLN03234 411 IPERFM-KEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKF 462
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
82-508 4.48e-19

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 90.18  E-value: 4.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    82 HQLQVLYKAKYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGkypvrndMELWKEHRDQ-HDLTYGP-----FTTEGHHWY 155
Cdd:PLN02394  53 HRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQG-------VEFGSRTRNVvFDIFTGKgqdmvFTVYGDHWR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   156 QLRQALNQRLLKPAEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYfaleAICY-ILFEKRIGclqrsiP 234
Cdd:PLN02394 126 KMRRIMTVPFFTNKVVQQYRYGWEEEADLVVEDVRANPEAATEGVVIRRRLQLMMY----NIMYrMMFDRRFE------S 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   235 EDTVTFVRSIGLMFQNSL--------YATFLPkWTRpvlPFWKRYLDGWNAIFS-----FGKKLIDEKLEDMEAQLQAAG 301
Cdd:PLN02394 196 EDDPLFLKLKALNGERSRlaqsfeynYGDFIP-ILR---PFLRGYLKICQDVKErrlalFKDYFVDERKKLMSAKGMDKE 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   302 PDGIQVSgylHFLLA--SGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKD 379
Cdd:PLN02394 272 GLKCAID---HILEAqkKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPD 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   380 FAHMPLLKAVLKETLRLYPVVP-----TNSRiiekEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQ 454
Cdd:PLN02394 349 THKLPYLQAVVKETLRLHMAIPllvphMNLE----DAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEA 424
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 4503211   455 pATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAPETGEL 508
Cdd:PLN02394 425 -KVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQSKI 477
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
145-494 1.56e-18

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: 87.01  E-value: 1.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  145 GPFTTEGHHWYQLRQALNQRLlKPAEAALYTDAFNEVIDDFMTRldqlRAESASGNQVSDMAQLFyyfaleaiCYILFEK 224
Cdd:cd11034  52 MPIETDPPEHKKYRKLLNPFF-TPEAVEAFRPRVRQLTNDLIDA----FIERGECDLVTELANPL--------PARLTLR 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  225 RIGClqrsIPEDTVTFVRsiglmfqnslyatflpkWTRPVL--PFWKRYLDGWNAIFSFGKKLIDEKledmeaqlQAAGP 302
Cdd:cd11034 119 LLGL----PDEDGERLRD-----------------WVHAILhdEDPEEGAAAFAELFGHLRDLIAER--------RANPR 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  303 DGIqVSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALheevvgvvpagqvpqhkdFAH 382
Cdd:cd11034 170 DDL-ISRLIEGEIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRL------------------IAD 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  383 MPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFpKNTQFVFCHY-VVSRDPTAFSEPESFQPHRWlRNSQpatpriq 461
Cdd:cd11034 231 PSLIPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRL-KPGDRVLLAFaSANRDEEKFEDPDRIDIDRT-PNRH------- 301
                       330       340       350
                ....*....|....*....|....*....|...
gi 4503211  462 hpfgsVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd11034 302 -----LAFGSGVHRCLGSHLARVEARVALTEVL 329
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
317-503 1.80e-18

cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Characterized members, among others, include: Catharanthus roseus cytochrome P450 72A1 (CYP72A1), also called secologanin synthase (EC 1.3.3.9), that catalyzes the conversion of loganin into secologanin, the precursor of monoterpenoid indole alkaloids and ipecac alkaloids; Medicago truncatula CYP72A67 that catalyzes a key oxidative step in hemolytic sapogenin biosynthesis; and Arabidopsis thaliana CYP72C1, an atypical CYP that acts on brassinolide precursors and functions as a brassinosteroid-inactivating enzyme. This family also includes Panax ginseng CYP716A47 that catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis. CYP72 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 87.72  E-value: 1.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  317 SGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRL 396
Cdd:cd20642 227 NGGMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVF-GNNKPDFEGLNHLKVVTMILYEVLRL 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  397 YPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRNSQPATPRIQHPFgsvPFGYGVRA 475
Cdd:cd20642 306 YPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERFAEGISKATKGQVSYF---PFGWGPRI 382
                       170       180
                ....*....|....*....|....*...
gi 4503211  476 CLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd20642 383 CIGQNFALLEAKMALALILQRFSFELSP 410
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
307-493 5.06e-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: 85.43  E-value: 5.06e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  307 VSGYLHFLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHeevvgvvpagqvpqhKDFAhmpLL 386
Cdd:cd20629 175 ISRLLRAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVR---------------RDRS---LI 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  387 KAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatPRIQHpFGs 466
Cdd:cd20629 237 PAAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR---------KPKPH-LV- 305
                       170       180       190
                ....*....|....*....|....*....|.
gi 4503211  467 vpFGYGVRACLGRRIAELEMQ----LLLARL 493
Cdd:cd20629 306 --FGGGAHRCLGEHLARVELRealnALLDRL 334
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
319-519 1.70e-17

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: 84.19  E-value: 1.70e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  319 QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHeevvgvvpagqvpqhkdfAHMPLLKAVLKETLRLYP 398
Cdd:cd11032 193 RLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLR------------------ADPSLIPGAIEEVLRYRP 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  399 VVPTNSRIIEKEIEVDGFLFPKNtQFVFChYVVS--RDPTAFSEPESFQPHRwlrnsqpatpriqHPFGSVPFGYGVRAC 476
Cdd:cd11032 255 PVQRTARVTTEDVELGGVTIPAG-QLVIA-WLASanRDERQFEDPDTFDIDR-------------NPNPHLSFGHGIHFC 319
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 4503211  477 LGRRIAELEMQLLLARLIQKYKVVlapetgELKSVARIVLVPN 519
Cdd:cd11032 320 LGAPLARLEARIALEALLDRFPRI------RVDPDVPLELIDS 356
PLN02500 PLN02500
cytochrome P450 90B1
263-502 2.47e-17

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 84.53  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   263 PVLPFWKRyLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGPDGIqvsgyLHFLLASGQLSPREAMGSLPELLMAGVDTTSN 342
Cdd:PLN02500 224 PGTAYRKA-LKSRATILKFIERKMEERIEKLKEEDESVEEDDL-----LGWVLKHSNLSTEQILDLILSLLFAGHETSSV 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   343 TLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQH-----KDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFL 417
Cdd:PLN02500 298 AIALAIFFLQGCPKAVQELREEHLEIARAKKQSGEselnwEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYD 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   418 FPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATPRIQHPFGS---VPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:PLN02500 378 IPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGSSGSSSATTnnfMPFGGGPRLCAGSELAKLEMAVFIHHLV 457

                 ....*...
gi 4503211   495 QKYKVVLA 502
Cdd:PLN02500 458 LNFNWELA 465
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
91-503 6.54e-17

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: 82.91  E-value: 6.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   91 KYGPMWMSYLGPQMHVNLASAPLLEQVMRQEGkypvrndMELWKEHRDQ-HDLTYGP-----FTTEGHHWYQLRQALNQR 164
Cdd:cd11074   2 KFGDIFLLRMGQRNLVVVSSPELAKEVLHTQG-------VEFGSRTRNVvFDIFTGKgqdmvFTVYGEHWRKMRRIMTVP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  165 LLKPAEAALYTDAFNEVIDDFMTRLDQLRAESASGNQVSDMAQLFYYfaleAICY-ILFEKRIGclqrsiPEDTVTFVRS 243
Cdd:cd11074  75 FFTNKVVQQYRYGWEEEAARVVEDVKKNPEAATEGIVIRRRLQLMMY----NNMYrIMFDRRFE------SEDDPLFVKL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  244 IGLMFQNSL--------YATFLPkwtrpVL-PFWKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGP---DGIQVSgYL 311
Cdd:cd11074 145 KALNGERSRlaqsfeynYGDFIP-----ILrPFLRGYLKICKEVKERRLQLFKDYFVDERKKLGSTKStknEGLKCA-ID 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  312 HFLLAS--GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAV 389
Cdd:cd11074 219 HILDAQkkGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAV 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  390 LKETLRLYPVVP-----TNSRiiekEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrNSQPATPRIQHPF 464
Cdd:cd11074 299 VKETLRLRMAIPllvphMNLH----DAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFL-EEESKVEANGNDF 373
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 4503211  465 GSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVLAP 503
Cdd:cd11074 374 RYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPPP 412
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
331-510 7.11e-17

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: 82.96  E-value: 7.11e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  331 ELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNS-RIIEK 409
Cdd:cd20667 232 DLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAvRQCVT 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  410 EIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLrnSQPATPRIQHPFgsVPFGYGVRACLGRRIAELEMQLL 489
Cdd:cd20667 312 STTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFL--DKDGNFVMNEAF--LPFSAGHRVCLGEQLARMELFIF 387
                       170       180
                ....*....|....*....|.
gi 4503211  490 LARLIQKYKVVLAPETGELKS 510
Cdd:cd20667 388 FTTLLRTFNFQLPEGVQELNL 408
PLN02966 PLN02966
cytochrome P450 83A1
88-501 8.44e-17

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 83.26  E-value: 8.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211    88 YKAKYGPMWMSYLGPQMHVNLASAPLLEQVMR-QEGKYPVRndmelwKEHRDQHDLTYGPFTTEGHHWY----QLRQALN 162
Cdd:PLN02966  58 WAKKYGPILSYRIGSRTMVVISSAELAKELLKtQDVNFADR------PPHRGHEFISYGRRDMALNHYTpyyrEIRKMGM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   163 QRLLKPAEAALYTDAFNEVIDDFMTRLDQlraeSASGNQVSDMAQLFYYFALEAICYILFEKRIGclqrsipEDTVTFVR 242
Cdd:PLN02966 132 NHLFSPTRVATFKHVREEEARRMMDKINK----AADKSEVVDISELMLTFTNSVVCRQAFGKKYN-------EDGEEMKR 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   243 SIGLMFQ------NSLYATFLPkwtrpvlpfWKRYLDGWNAIFSFGKK-----------LIDEKLEDMEAQLQAAGPDGI 305
Cdd:PLN02966 201 FIKILYGtqsvlgKIFFSDFFP---------YCGFLDDLSGLTAYMKEcferqdtyiqeVVNETLDPKRVKPETESMIDL 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   306 QVSGYLHFLLASgQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVP--AGQVPQHKDFAHM 383
Cdd:PLN02966 272 LMEIYKEQPFAS-EFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKekGSTFVTEDDVKNL 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   384 PLLKAVLKETLRLYPVVP-TNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFS-EPESFQPHRWLRNsQPATPRIQ 461
Cdd:PLN02966 351 PYFRALVKETLRIEPVIPlLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWGpNPDEFRPERFLEK-EVDFKGTD 429
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 4503211   462 HPFgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVVL 501
Cdd:PLN02966 430 YEF--IPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKL 467
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
269-496 1.55e-16

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 81.40  E-value: 1.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  269 KRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGPD----GIQVSGYLHFLLaSGQLSPREAMGSLPELLMAGVDTTSNTL 344
Cdd:cd20627 144 KGFLDGSLEKSTTRKKQYEDALMEMESVLKKVIKErkgkNFSQHVFIDSLL-QGNLSEQQVLEDSMIFSLAGCVITANLC 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  345 TWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKdFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQF 424
Cdd:cd20627 223 TWAIYFLTTSEEVQKKLYKEVDQVLGKGPITLEK-IEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLV 301
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503211  425 VFCHYVVSRDPTAFSEPESFQPHRWlrNSQPAtpriQHPFGSVPFGyGVRACLGRRIAELEMQLLLARLIQK 496
Cdd:cd20627 302 LYALGVVLQDNTTWPLPYRFDPDRF--DDESV----MKSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRK 366
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
332-497 1.64e-16

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 82.36  E-value: 1.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVvgvvpaGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEK-E 410
Cdd:PLN02169 309 LVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKpD 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   411 IEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPES-FQPHRWLrnSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLL 489
Cdd:PLN02169 383 VLPSGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWI--SDNGGLRHEPSYKFMAFNSGPRTCLGKHLALLQMKIV 460

                 ....*...
gi 4503211   490 LARLIQKY 497
Cdd:PLN02169 461 ALEIIKNY 468
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
318-496 1.69e-16

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: 81.07  E-value: 1.69e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  318 GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvPAgqvpqhkdfahmpLLKAVLKETLRLY 397
Cdd:cd11031 200 DRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRAD-----PE-------------LVPAAVEELLRYI 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  398 PVVPTNS--RIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatPRIQHpfgsVPFGYGVRA 475
Cdd:cd11031 262 PLGAGGGfpRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR---------EPNPH----LAFGHGPHH 328
                       170       180
                ....*....|....*....|.
gi 4503211  476 CLGRRIAELEMQLLLARLIQK 496
Cdd:cd11031 329 CLGAPLARLELQVALGALLRR 349
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
318-517 2.85e-16

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: 80.32  E-value: 2.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  318 GQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvpagqvPQhkdfahmpLLKAVLKETLRLY 397
Cdd:cd11037 196 GEITEDEAPLLMRDYLSAGLDTTISAIGNALWLLARHPDQWERLRAD----------PS--------LAPNAFEEAVRLE 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  398 PVVPTNSRIIEKEIEVDGFLFPKNTQfVFCHY-VVSRDPTAFSEPESFQPHRwlrnsqpatpriqHPFGSVPFGYGVRAC 476
Cdd:cd11037 258 SPVQTFSRTTTRDTELAGVTIPAGSR-VLVFLgSANRDPRKWDDPDRFDITR-------------NPSGHVGFGHGVHAC 323
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 4503211  477 LGRRIAELEMQLLLARLIQKykvvlapetgelksVARIVLV 517
Cdd:cd11037 324 VGQHLARLEGEALLTALARR--------------VDRIELA 350
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
335-493 5.38e-16

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: 80.05  E-value: 5.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVP-TNSRIIEKEIEV 413
Cdd:cd20675 246 ASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPvTIPHATTADTSI 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  414 DGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLR-----NSQPAtpriqhpfGSV-PFGYGVRACLGRRIAELEMQ 487
Cdd:cd20675 326 LGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDengflNKDLA--------SSVmIFSVGKRRCIGEELSKMQLF 397

                ....*.
gi 4503211  488 LLLARL 493
Cdd:cd20675 398 LFTSIL 403
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
319-495 6.66e-16

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: 79.86  E-value: 6.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  319 QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLK------AVLKE 392
Cdd:cd20638 225 PLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKELSMEVLEqlkytgCVIKE 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  393 TLRLYPVVPTNSRIIEKEIEVDGFLFPK--NTQFVFC--HYVVSrdptAFSEPESFQPHRWLRNSqpatPRIQHPFGSVP 468
Cdd:cd20638 305 TLRLSPPVPGGFRVALKTFELNGYQIPKgwNVIYSICdtHDVAD----IFPNKDEFNPDRFMSPL----PEDSSRFSFIP 376
                       170       180
                ....*....|....*....|....*..
gi 4503211  469 FGYGVRACLGRRIAELEMQLLLARLIQ 495
Cdd:cd20638 377 FGGGSRSCVGKEFAKVLLKIFTVELAR 403
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
265-518 2.01e-15

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: 78.35  E-value: 2.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  265 LPF--WKRYLDGWNAIFSFGKKLIDEKLEDMEAQLQAAGPDGIQVSGYLHfllaSGQLSPREAMGSLPELLMAGVDTTSN 342
Cdd:cd20637 169 LPFsgYRRGIRARDSLQKSLEKAIREKLQGTQGKDYADALDILIESAKEH----GKELTMQELKDSTIELIFAAFATTAS 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  343 TLTWALYHLSKDPEIQEALHEEV--VGVVPAGQVPQH----KDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGF 416
Cdd:cd20637 245 ASTSLIMQLLKHPGVLEKLREELrsNGILHNGCLCEGtlrlDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGF 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  417 LFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWlrnSQPATPRIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQK 496
Cdd:cd20637 325 QIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRF---GQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELAST 401
                       250       260
                ....*....|....*....|..
gi 4503211  497 YKVVLAPETgelksVARIVLVP 518
Cdd:cd20637 402 SRFELATRT-----FPRMTTVP 418
PLN02774 PLN02774
brassinosteroid-6-oxidase
282-498 3.26e-15

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 77.89  E-value: 3.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   282 GKKLIDEKLEDMEAQLQAAGPDGIQVSGYLhfLLASGQ---LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQ 358
Cdd:PLN02774 221 ARKNIVRMLRQLIQERRASGETHTDMLGYL--MRKEGNrykLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKAL 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   359 EALHEEVVGVvPAGQVPQH----KDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFvfchYVVSR- 433
Cdd:PLN02774 299 QELRKEHLAI-RERKRPEDpidwNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRI----YVYTRe 373
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503211   434 ---DPTAFSEPESFQPHRWLRNSQPAtpriqHPFGSVpFGYGVRACLGRRIAELEMQLLLARLIQKYK 498
Cdd:PLN02774 374 inyDPFLYPDPMTFNPWRWLDKSLES-----HNYFFL-FGGGTRLCPGKELGIVEISTFLHYFVTRYR 435
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
276-494 9.29e-15

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: 76.03  E-value: 9.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  276 NAIFSFGKKLIDEKL----EDMEAQLQAAGPDGiqvsgylhfllasGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHL 351
Cdd:cd11033 170 AELFAYFRELAEERRanpgDDLISVLANAEVDG-------------EPLTDEEFASFFILLAVAGNETTRNSISGGVLAL 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  352 SKDPEIQEALHEevvgvvpagqvpqhkDFAHMPllKAVlKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVV 431
Cdd:cd11033 237 AEHPDQWERLRA---------------DPSLLP--TAV-EEILRWASPVIHFRRTATRDTELGGQRIRAGDKVVLWYASA 298
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503211  432 SRDPTAFSEPESFQPHRwlrnsqpaTPRiQHpfgsVPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd11033 299 NRDEEVFDDPDRFDITR--------SPN-PH----LAFGGGPHFCLGAHLARLELRVLFEELL 348
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
320-493 9.81e-14

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: 72.64  E-value: 9.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  320 LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvpAGQVPQhkdfahmpllkAVlKETLRLYPV 399
Cdd:cd11078 205 LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRAD------PSLIPN-----------AV-EETLRYDSP 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  400 VPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpaTPRIQHpfgsVPFGYGVRACLGR 479
Cdd:cd11078 267 VQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR--------PNARKH----LTFGHGIHFCLGA 334
                       170
                ....*....|....*...
gi 4503211  480 RIAELEMQL----LLARL 493
Cdd:cd11078 335 ALARMEARIaleeLLRRL 352
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
346-501 1.98e-13

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: 71.96  E-value: 1.98e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  346 WALYHLSKDPEIQEALHEEVVGVVPAGQVPQHK----DFAHMPLLKAVLKETLRLYP--VVPtnsRIIEKEIEVDGFLFP 419
Cdd:cd20635 232 WTLAFILSHPSVYKKVMEEISSVLGKAGKDKIKisedDLKKMPYIKRCVLEAIRLRSpgAIT---RKVVKPIKIKNYTIP 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  420 KNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRnsqpATP-RIQHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYK 498
Cdd:cd20635 309 AGDMLMLSPYWAHRNPKYFPDPELFKPERWKK----ADLeKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYD 384

                ...
gi 4503211  499 VVL 501
Cdd:cd20635 385 FTL 387
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
319-491 5.09e-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: 70.74  E-value: 5.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  319 QLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKD-FAHMPLLKAVLKETLRLY 397
Cdd:cd11082 215 HSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPLTLDlLEEMKYTRQVVKEVLRYR 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  398 PVVPTNSRIIEKEIEV-DGFLFPKNTQFVFCHYVVSRDPtaFSEPESFQPHRWlrnSQPATPRIQHPFGSVPFGYGVRAC 476
Cdd:cd11082 295 PPAPMVPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRF---SPERQEDRKYKKNFLVFGAGPHQC 369
                       170
                ....*....|....*
gi 4503211  477 LGRRIAELEMQLLLA 491
Cdd:cd11082 370 VGQEYAINHLMLFLA 384
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
276-505 5.86e-13

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: 70.63  E-value: 5.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  276 NAIFSFGKKLIDEKLEdmeAQLQAAGPDGiqvsgyLHFLLASG-----QLSPREAMGSLPELLMAGVDTTSNTLTWALYH 350
Cdd:cd20636 183 DILHEYMEKAIEEKLQ---RQQAAEYCDA------LDYMIHSArengkELTMQELKESAVELIFAAFSTTASASTSLVLL 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  351 LSKDPEIQEALHEEVVGvvpAGQVPQHKdfaHMP------------LLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLF 418
Cdd:cd20636 254 LLQHPSAIEKIRQELVS---HGLIDQCQ---CCPgalsleklsrlrYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQI 327
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  419 PKNTQFVFCHYVVSRDPTAFSEPESFQPHRW-LRNSQPATPRiqhpFGSVPFGYGVRACLGRRIAELEMQLLLARLIQKY 497
Cdd:cd20636 328 PKGWSVMYSIRDTHETAAVYQNPEGFDPDRFgVEREESKSGR----FNYIPFGGGVRSCIGKELAQVILKTLAVELVTTA 403

                ....*...
gi 4503211  498 KVVLAPET 505
Cdd:cd20636 404 RWELATPT 411
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
291-516 6.19e-13

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: 70.27  E-value: 6.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  291 EDMEAQLQAAGPDGiqvsgylhfllasGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALheevvgvvp 370
Cdd:cd20625 181 DDLISALVAAEEDG-------------DRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALL--------- 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  371 agqvpqhkdFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwl 450
Cdd:cd20625 239 ---------RADPELIPAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR-- 307
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503211  451 rnsqpatPRIQHpfgsVPFGYGVRACLGRRIAELEMQLLLARLIQKYkVVLAPETGELKSVARIVL 516
Cdd:cd20625 308 -------APNRH----LAFGAGIHFCLGAPLARLEAEIALRALLRRF-PDLRLLAGEPEWRPSLVL 361
PLN02290 PLN02290
cytokinin trans-hydroxylase
335-498 9.18e-13

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 70.61  E-value: 9.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   335 AGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVpAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD 414
Cdd:PLN02290 327 AGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVC-GGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLG 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   415 GFLFPKNTQFVFCHYVVSRDPTAFSE-PESFQPHRWLRNSQPATPRIqhpfgsVPFGYGVRACLGRRIAELEMQLLLARL 493
Cdd:PLN02290 406 DLHIPKGLSIWIPVLAIHHSEELWGKdANEFNPDRFAGRPFAPGRHF------IPFAAGPRNCIGQAFAMMEAKIILAML 479

                 ....*
gi 4503211   494 IQKYK 498
Cdd:PLN02290 480 ISKFS 484
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
291-496 1.27e-12

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: 69.42  E-value: 1.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  291 EDMEAQLQAAGPDGIQVSGylhfllasgqlspREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvP 370
Cdd:cd11080 173 SDLISILCTAEYEGEALSD-------------EDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRAD-----R 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  371 AgqvpqhkdfahmpLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQfVFCHY-VVSRDPTAFSEPESFQPHRW 449
Cdd:cd11080 235 S-------------LVPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTT-VFCLIgAANRDPAAFEDPDTFNIHRE 300
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 4503211  450 LRNSQPA-TPRIQHpfgsVPFGYGVRACLGRRIAELEMQLLLARLIQK 496
Cdd:cd11080 301 DLGIRSAfSGAADH----LAFGSGRHFCVGAALAKREIEIVANQVLDA 344
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
332-493 1.99e-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: 68.93  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEevvgvvpagqvpqhkdfaHMPLLKAVLKETLRLYPVVPTNSRIIEKEI 411
Cdd:cd11038 222 LLFAGVDTTRNQLGLAMLTFAEHPDQWRALRE------------------DPELAPAAVEEVLRWCPTTTWATREAVEDV 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  412 EVDGFLFPKNTQFVFCHYVVSRDPTAFsEPESFQphrwlrnsqpATPRIQHPFGsvpFGYGVRACLGRRIAELEMQLLLA 491
Cdd:cd11038 284 EYNGVTIPAGTVVHLCSHAANRDPRVF-DADRFD----------ITAKRAPHLG---FGGGVHHCLGAFLARAELAEALT 349

                ..
gi 4503211  492 RL 493
Cdd:cd11038 350 VL 351
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
355-498 2.95e-12

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: 68.44  E-value: 2.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  355 PEIQEALHEEVVGVVPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVD----GFLFPKNtQFVFCH-Y 429
Cdd:cd11071 257 EELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIEshdaSYKIKKG-ELLVGYqP 335
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503211  430 VVSRDPTAFSEPESFQPhrwLRNSQPATPRIQHPFGS-----VPFGYGVRACLGRRIAELEMQLLLARLIQKYK 498
Cdd:cd11071 336 LATRDPKVFDNPDEFVP---DRFMGEEGKLLKHLIWSngpetEEPTPDNKQCPGKDLVVLLARLFVAELFLRYD 406
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
315-495 3.38e-11

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: 64.85  E-value: 3.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  315 LASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvPAgqvpqhkdfahmpLLKAVLKETL 394
Cdd:cd11030 199 GAPGELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALRAD-----PS-------------LVPGAVEELL 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  395 RLYPVVPTN-SRIIEKEIEVDGFLFPKNtQFVFCH-YVVSRDPTAFSEPESFQPHRwlrnsqpatPRIQHpfgsVPFGYG 472
Cdd:cd11030 261 RYLSIVQDGlPRVATEDVEIGGVTIRAG-EGVIVSlPAANRDPAVFPDPDRLDITR---------PARRH----LAFGHG 326
                       170       180
                ....*....|....*....|...
gi 4503211  473 VRACLGRRIAELEMQLLLARLIQ 495
Cdd:cd11030 327 VHQCLGQNLARLELEIALPTLFR 349
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
317-509 6.59e-11

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: 64.09  E-value: 6.59e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  317 SGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvPAgqvpqhkdfahmpLLKAVLKETLRL 396
Cdd:cd11029 204 GDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRAD-----PE-------------LWPAAVEELLRY 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  397 Y-PVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatPRIQHpfgsVPFGYGVRA 475
Cdd:cd11029 266 DgPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR---------DANGH----LAFGHGIHY 332
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4503211  476 CLGRRIAELEMQLLLARLIQKY-KVVLAPETGELK 509
Cdd:cd11029 333 CLGAPLARLEAEIALGALLTRFpDLRLAVPPDELR 367
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
320-497 1.69e-10

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: 62.83  E-value: 1.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  320 LSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvpagqvPQhkdfahmpLLKAVLKETLRLYPV 399
Cdd:cd20630 199 LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE----------PE--------LLRNALEEVLRWDNF 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  400 VPTN-SRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatpriqHPFGSVPFGYGVRACLG 478
Cdd:cd20630 261 GKMGtARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR-------------DPNANIAFGYGPHFCIG 327
                       170
                ....*....|....*....
gi 4503211  479 RRIAELEMQLLLARLIQKY 497
Cdd:cd20630 328 AALARLELELAVSTLLRRF 346
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
312-505 2.19e-10

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: 62.48  E-value: 2.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  312 HFLLASGQLSPREAMGSLPELLMAgVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPqhkdfahmpLLKAVLK 391
Cdd:cd20624 180 GELSRLPEGDEVDPEGQVPQWLFA-FDAAGMALLRALALLAAHPEQAARAREEAAVPPGPLARP---------YLRACVL 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  392 ETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWLRNsqpatpRIQHPFGSVPFGY 471
Cdd:cd20624 250 DAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDG------RAQPDEGLVPFSA 323
                       170       180       190
                ....*....|....*....|....*....|....
gi 4503211  472 GVRACLGRRIAELEMQLLLARLIQKYKVVLAPET 505
Cdd:cd20624 324 GPARCPGENLVLLVASTALAALLRRAEIDPLESP 357
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
283-500 1.07e-09

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 60.52  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   283 KKLIDEKLEDMEA---QLQAAGPDGIQVsgylhfLL--ASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEI 357
Cdd:PLN03141 211 KKIIEEKRRAMKNkeeDETGIPKDVVDV------LLrdGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVA 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   358 QEALHEEVVGV----VPAGQVPQHKDFAHMPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSR 433
Cdd:PLN03141 285 LQQLTEENMKLkrlkADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHL 364
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503211   434 DPTAFSEPESFQPHRWLRNSQPATpriqhpfGSVPFGYGVRACLGRRIAELEMQLLLARLIQKYKVV 500
Cdd:PLN03141 365 DEENYDNPYQFNPWRWQEKDMNNS-------SFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFRWV 424
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
332-514 1.81e-09

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: 59.66  E-value: 1.81e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEiQEALHEevvgvvpAGQVPQHKDFAHMPLLKAVLkETLRLYPVVPTNSRIIEKEI 411
Cdd:cd20612 195 TAVGGVPTQSQAFAQILDFYLRRPG-AAHLAE-------IQALARENDEADATLRGYVL-EALRLNPIAPGLYRRATTDT 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  412 EVD-----GFLFPKNTQfVFCHYV-VSRDPTAFSEPESFQPHRwlrnsqPATPRIQhpfgsvpFGYGVRACLGRRIAELE 485
Cdd:cd20612 266 TVAdgggrTVSIKAGDR-VFVSLAsAMRDPRAFPDPERFRLDR------PLESYIH-------FGHGPHQCLGEEIARAA 331
                       170       180       190
                ....*....|....*....|....*....|
gi 4503211  486 MQLLLARLIQKYKVVLAP-ETGELKSVARI 514
Cdd:cd20612 332 LTEMLRVVLRLPNLRRAPgPQGELKKIPRG 361
PLN02648 PLN02648
allene oxide synthase
348-450 6.91e-09

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 58.02  E-value: 6.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211   348 LYHLSKD-PEIQEALHEEVVGVVPAGqvPQHKDFA---HMPLLKAVLKETLRLYPVVPTNSRIIEKEIEV---DGFLFPK 420
Cdd:PLN02648 296 LKWVGRAgEELQARLAEEVRSAVKAG--GGGVTFAaleKMPLVKSVVYEALRIEPPVPFQYGRAREDFVIeshDAAFEIK 373
                         90       100       110
                 ....*....|....*....|....*....|.
gi 4503211   421 NTQFVFCH-YVVSRDPTAFSEPESFQPHRWL 450
Cdd:PLN02648 374 KGEMLFGYqPLVTRDPKVFDRPEEFVPDRFM 404
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
350-496 8.33e-09

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: 57.37  E-value: 8.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  350 HLSKDPEIQEALHEEVvgvvpagqvpqhkdfahmPLLKAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQfVFCHY 429
Cdd:cd11079 209 YLARHPELQARLRANP------------------ALLPAAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSR-VTLNW 269
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503211  430 V-VSRDPTAFSEPESFQPHRwlrnsqpatpriqHPFGSVPFGYGVRACLGRRIAELEMQLLLARLIQK 496
Cdd:cd11079 270 AsANRDERVFGDPDEFDPDR-------------HAADNLVYGRGIHVCPGAPLARLELRILLEELLAQ 324
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
332-494 2.45e-08

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 56.15  E-value: 2.45e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVVPAGQVPQHKDFAH---------MPLLKAVLKETLRLyPVVPT 402
Cdd:cd20632 223 FLWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQSTGQELGPDFDIhltreqldsLVYLESAINESLRL-SSASM 301
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  403 NSRIIEKEI----EVDG----------FLFPKNTqfvfcHYvvsrDPTAFSEPESFQPHRWLRNSQPATpriqhPFGS-- 466
Cdd:cd20632 302 NIRVVQEDFtlklESDGsvnlrkgdivALYPQSL-----HM----DPEIYEDPEVFKFDRFVEDGKKKT-----TFYKrg 367
                       170       180       190
                ....*....|....*....|....*....|....*
gi 4503211  467 -------VPFGYGVRACLGRRIAELEMQLLLARLI 494
Cdd:cd20632 368 qklkyylMPFGSGSSKCPGRFFAVNEIKQFLSLLL 402
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
346-482 3.49e-07

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 52.84  E-value: 3.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  346 WALYHLSKDPEIQEALHEEVVGVVP-AGQVPQH------KDFAHMPLLKAVLKETLRLypvvpTNSRIIEKEIEVDGFLF 418
Cdd:cd20634 243 WLLLFLLKHPEAMAAVRGEIQRIKHqRGQPVSQtltinqELLDNTPVFDSVLSETLRL-----TAAPFITREVLQDMKLR 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  419 PKNTQ----------FVFCHYVVSRDPTAFSEPESFQPHRWLRNSQPATP-------RIQHPfgSVPFGYGVRACLGRRI 481
Cdd:cd20634 318 LADGQeynlrrgdrlCLFPFLSPQMDPEIHQEPEVFKYDRFLNADGTEKKdfykngkRLKYY--NMPWGAGDNVCIGRHF 395

                .
gi 4503211  482 A 482
Cdd:cd20634 396 A 396
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
341-528 1.24e-06

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: 50.84  E-value: 1.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  341 SNTLT---WALYHLSKDPEIQEALHEEVVGVV-PAGQVPQ---------HKDFAHMPLLKAVLKETLRLyPVVPTNSRII 407
Cdd:cd20631 241 ANTLPatfWSLFYLLRCPEAMKAATKEVKRTLeKTGQKVSdggnpivltREQLDDMPVLGSIIKEALRL-SSASLNIRVA 319
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  408 EKE--IEVDG---FLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRWL-RNSQPAT------PRIQHPFgsVPFGYGVRA 475
Cdd:cd20631 320 KEDftLHLDSgesYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLdENGKEKTtfykngRKLKYYY--MPFGSGTSK 397
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 4503211  476 CLGRRIAELEMQLLLARLIQKYKVVLapetgeLKSVARIVLVPNKKVGLQFLQ 528
Cdd:cd20631 398 CPGRFFAINEIKQFLSLMLCYFDMEL------LDGNAKCPPLDQSRAGLGILP 444
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
332-488 1.47e-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: 50.83  E-value: 1.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  332 LLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVGVV-PAGQVPQHKD---------FAHMPLLKAVLKETLRLyPVVP 401
Cdd:cd20633 232 LLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVEQVLkETGQEVKPGGplinltrdmLLKTPVLDSAVEETLRL-TAAP 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  402 TNSRIIEKEIEV---DG--FLFPKNTQF-VFCHYVVSRDPTAFSEPESFQPHRWLrNSQPATPRIQHPFG------SVPF 469
Cdd:cd20633 311 VLIRAVVQDMTLkmaNGreYALRKGDRLaLFPYLAVQMDPEIHPEPHTFKYDRFL-NPDGGKKKDFYKNGkklkyyNMPW 389
                       170
                ....*....|....*....
gi 4503211  470 GYGVRACLGRRIAELEMQL 488
Cdd:cd20633 390 GAGVSICPGRFFAVNEMKQ 408
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
301-506 1.50e-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: 1.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  301 GPDGIQVSgylhfLLASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEvvgvvpagqvPQHKDf 380
Cdd:cd20619 172 GLADSLLD-----AARAGEITESEAIATILVFYAVGHMAIGYLIASGIELFARRPEVFTAFRND----------ESARA- 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  381 ahmpllkAVLKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsQPATPRi 460
Cdd:cd20619 236 -------AIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTR-----PPAASR- 302
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4503211  461 qhpfgSVPFGYGVRACLGRRIAELEMQLLLARLIQK-YKVVLAPETG 506
Cdd:cd20619 303 -----NLSFGLGPHSCAGQIISRAEATTVFAVLAERyERIELAEEPT 344
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
344-496 4.18e-06

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: 49.06  E-value: 4.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  344 LTWALYHLSKDPEIQEALHEEVVGVVpagqvpqhKDFAHmpllkavlkETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQ 423
Cdd:cd11067 240 VTFAALALHEHPEWRERLRSGDEDYA--------EAFVQ---------EVRRFYPFFPFVGARARRDFEWQGYRFPKGQR 302
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503211  424 FVFCHYVVSRDPTAFSEPESFQPHRWLRnsqpatpRIQHPFGSVPFGYGVRA----CLGRRIAELEMQLLLARLIQK 496
Cdd:cd11067 303 VLLDLYGTNHDPRLWEDPDRFRPERFLG-------WEGDPFDFIPQGGGDHAtghrCPGEWITIALMKEALRLLARR 372
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
293-493 1.46e-03

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.95  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  293 MEAQLQAAGPDGI-QVSGYLHFLLASGQLSPREAMGslpellmagvdttsnTLTWALyhLSkDPEIQEAlheevvgvVPA 371
Cdd:cd11039 188 LSVMLNAGMPMSLeQIRANIKVAIGGGLNEPRDAIA---------------GTCWGL--LS-NPEQLAE--------VMA 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  372 GQVPQHKDFahmpllkavlKETLRLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlr 451
Cdd:cd11039 242 GDVHWLRAF----------EEGLRWISPIGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFR--- 308
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 4503211  452 nsqpatPRIQHpfgsVPFGYGVRACLG-----RRIAELEMQLLLARL 493
Cdd:cd11039 309 ------PKSPH----VSFGAGPHFCAGawasrQMVGEIALPELFRRL 345
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
315-493 2.71e-03

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: 40.17  E-value: 2.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  315 LASGQLSPREAMGSLPELLMAGVDTTSNTLTWALYHLSKDPEIQEALHEEVVgvvpagqvpqhkdfahmpLLKAVLKETL 394
Cdd:cd11036 168 DALALSAPGDLVANAILLAVQGAEAAAGLVGNAVLALLRRPAQWARLRPDPE------------------LAAAAVAETL 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503211  395 RLYPVVPTNSRIIEKEIEVDGFLFPKNTQFVFCHYVVSRDPTAFSEPESFQPHRwlrnsqpatpriqHPFGSVPFGYGVR 474
Cdd:cd11036 230 RYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR-------------PTARSAHFGLGRH 296
                       170       180
                ....*....|....*....|...
gi 4503211  475 ACLG----RRIAELEMQLLLARL 493
Cdd:cd11036 297 ACLGaalaRAAAAAALRALAARF 319
 
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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