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Conserved domains on  [gi|315113433|pdb|3MZS|D]
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Chain D, Cholesterol side-chain cleavage enzyme

Protein Classification

cytochrome P450( domain architecture ID 15335005)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
44-469 0e+00

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: 802.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAP 123
Cdd:cd20643   1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      124 EAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMF 203
Cdd:cd20643  81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      204 HTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRK-TEFRNYPGILYCLLKSEKMLLEDVKANIT 282
Cdd:cd20643 161 HTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKgKNEHEYPGILANLLLQDKLPIEDIKASVT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      283 EMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESD 362
Cdd:cd20643 241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITED 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      363 LVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILE 442
Cdd:cd20643 321 LVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLS--KDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLE 398
                       410       420
                ....*....|....*....|....*..
3MZS_D      443 NFKVEMQHIGDVDTIFNLILTPDKPIF 469
Cdd:cd20643 399 NFKIETQRLVEVKTTFDLILVPEKPIN 425
 
Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
44-469 0e+00

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: 802.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAP 123
Cdd:cd20643   1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      124 EAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMF 203
Cdd:cd20643  81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      204 HTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRK-TEFRNYPGILYCLLKSEKMLLEDVKANIT 282
Cdd:cd20643 161 HTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKgKNEHEYPGILANLLLQDKLPIEDIKASVT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      283 EMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESD 362
Cdd:cd20643 241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITED 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      363 LVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILE 442
Cdd:cd20643 321 LVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLS--KDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLE 398
                       410       420
                ....*....|....*....|....*..
3MZS_D      443 NFKVEMQHIGDVDTIFNLILTPDKPIF 469
Cdd:cd20643 399 NFKIETQRLVEVKTTFDLILVPEKPIN 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
14-472 3.14e-150

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: 436.33  E-value: 3.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D         14 PSPGDNGWLNLYHFWREKGsQRIHFRHIENFQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHR 93
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRK-GNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D         94 YYQKPIGVLFKKSGTWKKDRVVLNTEVMAPEaIKNFIPLLNPVSQDFVSLLHKRIKQQGsgkfVGDIKEDLFHFAFESIT 173
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFG-KLSFEPRVEEEARDLVEKLRKTAGEPG----VIDITDLLFRAALNVIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        174 NVMFGERLGMLEETVNPEAQKFIDAVYKMFHTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRrK 253
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLD-S 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        254 TEFRNYPGILYCLLKSE-----KMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDI 328
Cdd:pfam00067 234 AKKSPRDFLDALLLAKEeedgsKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        329 SKMLQMVPLLKASIKETLRLHPISVT-LQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKD 407
Cdd:pfam00067 314 YDDLQNMPYLDAVIKETLRLHPVVPLlLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGK 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3MZS_D        408 LIH-FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDVDTIFNL--ILTPDKPIFLVF 472
Cdd:pfam00067 394 FRKsFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETpgLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-474 5.84e-30

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 121.00  E-value: 5.84e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       61 VYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNtEVMAPEAIKNFIPLL-NPVSQD 139
Cdd:COG2124  51 WVVSRPADVREVLRDPRFFSSALGAGLRPRLLRPVLGDGSLLTLDGPEHTRLRKLLA-PAFTPRALRGYRPLIrEIADRL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      140 FVSLLHKRIkqqgsgkfvgdikEDLFHFAFE---SITNVMFGERLGmleetvnpEAQKFIDAVYKMFHTSVPLLNVPPEl 216
Cdd:COG2124 130 LDDLWQGGA-------------DLVLDFAAEltlRVIAELLGVPLE--------DRPQLLRWSDALLLRLDPDLGPEEP- 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      217 yrlfrtktWRDHVAAWDTIFnkaekyteifyQDLRRK-TEFRNYPG--ILYCLLKSE-----KMLLEDVKANITEMLAGG 288
Cdd:COG2124 188 --------WRRARAARRELD-----------AYLRALiAERRAAPRddLLSLLLSAEddgggRLSDDEIRDELITLLVAG 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      289 VNTTSMTLQWHLYEMARSLNVQEMLREEvlnarrqaegdiskmlQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDY 368
Cdd:COG2124 249 HETTANALAWALYALLRHPDQLAKLRAE----------------PDRPLLEAVVEETLRLYPPVPLARRVATEDVELGGY 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      369 LIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdkdlihfRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVeM 448
Cdd:COG2124 313 RIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN--------AHLPFGGGPHRCLGAALARLELKVALAELLRRFPL-L 383
                       410       420
                ....*....|....*....|....*.
3MZS_D      449 QHIGDVDTIFNLILTPDKPIFLVFRP 474
Cdd:COG2124 384 LLAEPPPLVRRPTLVPRGGERLPVRR 409
PTZ00404 PTZ00404
cytochrome P450; Provisional
45-466 2.92e-26

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 111.35  E-value: 2.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        45 QKYGPIYREKLGNLESVYIIHPEDVAHLF--KFEgSYPERYDIPPwLAYHRYYQkpiGVLFKKSGTWKKDRVVLNtEVMA 122
Cdd:PTZ00404  59 KKYGGIFRIWFADLYTVVLSDPILIREMFvdNFD-NFSDRPKIPS-IKHGTFYH---GIVTSSGEYWKRNREIVG-KAMR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       123 PEAIKNFIPLLNpvsqDFVSLLHKRIKQ-QGSGKfVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYK 201
Cdd:PTZ00404 133 KTNLKHIYDLLD----DQVDVLIESMKKiESSGE-TFEPRYYLTKFTMSAMFKYIFNEDISFDEDIHNGKLAELMGPMEQ 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       202 MFHT-----SVPLLNVPPELYRLFRTKTwrdhvaawDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKS------E 270
Cdd:PTZ00404 208 VFKDlgsgsLFDVIEITQPLYYQYLEHT--------DKNFKKIKKFIKEKYHEHLKTIDPEVPRDLLDLLIKEygtntdD 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       271 KMLleDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlnarRQAEGDISKML----QMVPLLKASIKETL 346
Cdd:PTZ00404 280 DIL--SILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEI----KSTVNGRNKVLlsdrQSTPYTVAIIKETL 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       347 RLHPISV-TLQRYPESDLVLQD-YLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRnlgFGWGVRQCV 424
Cdd:PTZ00404 354 RYKPVSPfGLPRSTSNDIIIGGgHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSNDAFMP---FSIGPRNCV 430
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
3MZS_D       425 GRRIAELEMTLFLIHILENFK---VEMQHIGDVDtIFNLILTPDK 466
Cdd:PTZ00404 431 GQQFAQDELYLAFSNIILNFKlksIDGKKIDETE-EYGLTLKPNK 474
 
Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
44-469 0e+00

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: 802.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAP 123
Cdd:cd20643   1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      124 EAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMF 203
Cdd:cd20643  81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      204 HTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRK-TEFRNYPGILYCLLKSEKMLLEDVKANIT 282
Cdd:cd20643 161 HTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKgKNEHEYPGILANLLLQDKLPIEDIKASVT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      283 EMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESD 362
Cdd:cd20643 241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITED 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      363 LVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILE 442
Cdd:cd20643 321 LVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLS--KDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLE 398
                       410       420
                ....*....|....*....|....*..
3MZS_D      443 NFKVEMQHIGDVDTIFNLILTPDKPIF 469
Cdd:cd20643 399 NFKIETQRLVEVKTTFDLILVPEKPIN 425
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
44-472 2.03e-167

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: 478.95  E-value: 2.03e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAP 123
Cdd:cd20644   1 FQELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      124 EAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMF 203
Cdd:cd20644  81 AAVQRFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVML 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      204 HTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEfRNYPGILYCLLKSEKMLLEDVKANITE 283
Cdd:cd20644 161 KTTVPLLFMPRSLSRWISPKLWKEHFEAWDCIFQYADNCIQKIYQELAFGRP-QHYTGIVAELLLQAELSLEAIKANITE 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESDL 363
Cdd:cd20644 240 LTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      364 VLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILEN 443
Cdd:cd20644 320 VLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKN 399
                       410       420
                ....*....|....*....|....*....
3MZS_D      444 FKVEMQHIGDVDTIFNLILTPDKPIFLVF 472
Cdd:cd20644 400 FLVETLSQEDIKTVYSFILRPEKPPLLTF 428
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
44-468 2.20e-158

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: 455.83  E-value: 2.20e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAP 123
Cdd:cd11054   1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      124 EAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGkfVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMF 203
Cdd:cd11054  81 KSVASYLPAINEVADDFVERIRRLRDEDGEE--VPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      204 HTSVPLLNVPPeLYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFR-NYPGILYCLLKSEKMLLEDVKANIT 282
Cdd:cd11054 159 ESSAKLMFGPP-LWKYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDeEEDSLLEYLLSKPGLSKKEIVTMAL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      283 EMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESD 362
Cdd:cd11054 238 DLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKD 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      363 LVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDL--IH-FRNLGFGWGVRQCVGRRIAELEMTLFLIH 439
Cdd:cd11054 318 IVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENknIHpFASLPFGFGPRMCIGRRFAELEMYLLLAK 397
                       410       420
                ....*....|....*....|....*....
3MZS_D      440 ILENFKVEMQHiGDVDTIFNLILTPDKPI 468
Cdd:cd11054 398 LLQNFKVEYHH-EELKVKTRLILVPDKPL 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
14-472 3.14e-150

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: 436.33  E-value: 3.14e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D         14 PSPGDNGWLNLYHFWREKGsQRIHFRHIENFQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHR 93
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRK-GNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D         94 YYQKPIGVLFKKSGTWKKDRVVLNTEVMAPEaIKNFIPLLNPVSQDFVSLLHKRIKQQGsgkfVGDIKEDLFHFAFESIT 173
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFG-KLSFEPRVEEEARDLVEKLRKTAGEPG----VIDITDLLFRAALNVIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        174 NVMFGERLGMLEETVNPEAQKFIDAVYKMFHTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRrK 253
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLD-S 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        254 TEFRNYPGILYCLLKSE-----KMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDI 328
Cdd:pfam00067 234 AKKSPRDFLDALLLAKEeedgsKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        329 SKMLQMVPLLKASIKETLRLHPISVT-LQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKD 407
Cdd:pfam00067 314 YDDLQNMPYLDAVIKETLRLHPVVPLlLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGK 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3MZS_D        408 LIH-FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDVDTIFNL--ILTPDKPIFLVF 472
Cdd:pfam00067 394 FRKsFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETpgLLLPPKPYKLKF 461
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
45-470 5.90e-101

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: 309.28  E-value: 5.90e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       45 QKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAPE 124
Cdd:cd20646   2 KIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKPK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      125 AIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMFH 204
Cdd:cd20646  82 EVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMFK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      205 TSVPLLNVPPELYRLFrtKTWRDHVAAWDTIFNKA-----EKYTEIFYQDLRRKTEFRNYpgiLYCLLKSEKMLLEDVKA 279
Cdd:cd20646 162 LSEIVTLLPKWTRPYL--PFWKRYVDAWDTIFSFGkklidKKMEEIEERVDRGEPVEGEY---LTYLLSSGKLSPKEVYG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      280 NITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARR--QAEgDISKMlqmvPLLKASIKETLRLHPISVT 354
Cdd:cd20646 237 SLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEvisVCPGDRipTAE-DIAKM----PLLKAVIKETLRLYPVVPG 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      355 LQRY-PESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLsKDKDLIH--FRNLGFGWGVRQCVGRRIAEL 431
Cdd:cd20646 312 NARViVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWL-RDGGLKHhpFGSIPFGYGVRACVGRRIAEL 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
3MZS_D      432 EMTLFLIHILENFKVEMQ-HIGDVDTIFNLILTPDKPIFL 470
Cdd:cd20646 391 EMYLALSRLIKRFEVRPDpSGGEVKAITRTLLVPNKPINL 430
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
45-470 2.11e-87

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: 274.32  E-value: 2.11e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       45 QKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAPE 124
Cdd:cd20648   3 AKYGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSSWKDYRQLRGHAYGLLTAEGEEWQRLRSLLAKHMLKPK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      125 AIKNFIPLLNPVSQDFVSLLhKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMFH 204
Cdd:cd20648  83 AVEAYAGVLNAVVTDLIRRL-RRQRSRSSPGVVKDIAGEFYKFGLEGISSVLFESRIGCLEANVPEETETFIQSINTMFV 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      205 TSVPLLNVPPELYRLFRtKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYC--LLKSEKMLLEDVKANIT 282
Cdd:cd20648 162 MTLLTMAMPKWLHRLFP-KPWQRFCRSWDQMFAFAKGHIDRRMAEVAAKLPRGEAIEGKYLtyFLAREKLPMKSIYGNVT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      283 EMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRY-PES 361
Cdd:cd20648 241 ELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARViPDR 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      362 DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDkDLIH-FRNLGFGWGVRQCVGRRIAELEMTLFLIHI 440
Cdd:cd20648 321 DIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKG-DTHHpYASLPFGFGKRSCIGRRIAELEVYLALARI 399
                       410       420       430
                ....*....|....*....|....*....|.
3MZS_D      441 LENFKVEMQHIGD-VDTIFNLILTPDKPIFL 470
Cdd:cd20648 400 LTHFEVRPEPGGSpVKPMTRTLLVPERSINL 430
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
45-466 9.88e-83

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: 262.05  E-value: 9.88e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       45 QKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAPE 124
Cdd:cd20645   2 KKFGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKPK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      125 AIKNFIPLLNPVSQDFVSLLHKRIKQQGSgkfVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMFH 204
Cdd:cd20645  82 EVMKLDGKINEVLADFMGRIDELCDETGR---VEDLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIKTMMS 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      205 TSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEifyqdlRRKTEFRNYPG------ILYCLLKSEKMLLedvk 278
Cdd:cd20645 159 TFGKMMVTPVELHKRLNTKVWQDHTEAWDNIFKTAKHCID------KRLQRYSQGPAndflcdIYHDNELSKKELY---- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      279 ANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRY 358
Cdd:cd20645 229 AAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRT 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      359 PESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLI 438
Cdd:cd20645 309 LDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHSINPFAHVPFGIGKRMCIGRRLAELQLQLALC 388
                       410       420
                ....*....|....*....|....*...
3MZS_D      439 HILENFKVEMQHIGDVDTIFNLILTPDK 466
Cdd:cd20645 389 WIIQKYQIVATDNEPVEMLHSGILVPSR 416
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
45-468 1.72e-73

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: 238.67  E-value: 1.72e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       45 QKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMAPE 124
Cdd:cd20647   2 REYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWQEYRDLRGRSTGLISAEGEQWLKMRSVLRQKILRPR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      125 AIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAV---YK 201
Cdd:cd20647  82 DVAVYSGGVNEVVADLIKRIKTLRSQEDDGETVTNVNDLFFKYSMEGVATILYECRLGCLENEIPKQTVEYIEALelmFS 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      202 MFHTSVPLLNVPPELyRLFRTKTWRDHVAAWDTIFNKAE-----KYTEIFYQdLRRKTEFRNypGILYCLLKSEKMLLED 276
Cdd:cd20647 162 MFKTTMYAGAIPKWL-RPFIPKPWEEFCRSWDGLFKFSQihvdnRLREIQKQ-MDRGEEVKG--GLLTYLLVSKELTLEE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      277 VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLN--ARRQAEG--DISKmlqmVPLLKASIKETLRLHPIS 352
Cdd:cd20647 238 IYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRnlGKRVVPTaeDVPK----LPLIRALLKETLRLFPVL 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      353 VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDkDLIHFRNLG---FGWGVRQCVGRRIA 429
Cdd:cd20647 314 PGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKD-ALDRVDNFGsipFGYGIRSCIGRRIA 392
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
3MZS_D      430 ELEMTLFLIHILENFKVEMQ-HIGDVDTIFNLILTPDKPI 468
Cdd:cd20647 393 ELEIHLALIQLLQNFEIKVSpQTTEVHAKTHGLLCPGGSI 432
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
48-467 5.20e-59

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: 199.28  E-value: 5.20e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYyqkPIGVLFKKSGTWKKDRVVLNTEvMAPEAIK 127
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFL---GDGLLTLDGPEHRRLRRLLAPA-FTPRALA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      128 NFIPLLNPVSQDFVsllhKRIKQQGSGKFvgDIKEDLFHFAFESITNVMFGERLgmleetvNPEAQKFIDAVYKMFHTSV 207
Cdd:cd00302  77 ALRPVIREIARELL----DRLAAGGEVGD--DVADLAQPLALDVIARLLGGPDL-------GEDLEELAELLEALLKLLG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      208 PLLNvppelyRLFRTKTWRDHVAAWDTIFnkaeKYTEIFYQDLRRKTEFRNYPGILYCLLKSEKMLLEDVKANITEMLAG 287
Cdd:cd00302 144 PRLL------RPLPSPRLRRLRRARARLR----DYLEELIARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLA 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      288 GVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA-RRQAEGDISKMlqmvPLLKASIKETLRLHPISVTLQRYPESDLVLQ 366
Cdd:cd00302 214 GHETTASLLAWALYLLARHPEVQERLRAEIDAVlGDGTPEDLSKL----PYLEAVVEETLRLYPPVPLLPRVATEDVELG 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      367 DYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLiHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKV 446
Cdd:cd00302 290 GYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEP-RYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDF 368
                       410       420
                ....*....|....*....|..
3MZS_D      447 EMQHIGDVDTIFN-LILTPDKP 467
Cdd:cd00302 369 ELVPDEELEWRPSlGTLGPASL 390
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
48-464 1.99e-50

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: 177.40  E-value: 1.99e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDVAHLFKFEG-SYPERYDIPPWlayhRYYQKPIGVLFKKSGTWKKDR-VVLNtevmapeA 125
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGdNFSDRPLLPSF----EIISGGKGILFSNGDYWKELRrFALS-------S 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      126 IKNF--IPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLgmlEETVNPEAQKFIDAVYKMF 203
Cdd:cd20617  70 LTKTklKKKMEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRF---PDEDDGEFLKLVKPIEEIF 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      204 HTS-----VPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKSEKMLlEDVK 278
Cdd:cd20617 147 KELgsgnpSDFIPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDD-DSII 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      279 ANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA----RRQAEGDISKMlqmvPLLKASIKETLRLHPIS-V 353
Cdd:cd20617 226 STCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVvgndRRVTLSDRSKL----PYLNAVIKEVLRLRPILpL 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      354 TLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLGFGWGVRQCVGRRIAELEM 433
Cdd:cd20617 302 GLPRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSEQFIPFGIGKRNCVGENLARDEL 381
                       410       420       430
                ....*....|....*....|....*....|...
3MZS_D      434 TLFLIHILENFKVE--MQHIGDVDTIFNLILTP 464
Cdd:cd20617 382 FLFFANLLLNFKFKssDGLPIDEKEVFGLTLKP 414
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
46-469 8.38e-46

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: 164.68  E-value: 8.38e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       46 KYGPIYREKLGNLESVYIIHPEDVAHLF-----KFEGSYPERYDIPPWLayhryyqkpIGVLFKKSGTWKKDRVVLNTeV 120
Cdd:cd11055   1 KYGKVFGLYFGTIPVIVVSDPEMIKEILvkefsNFTNRPLFILLDEPFD---------SSLLFLKGERWKRLRTTLSP-T 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      121 MAPEAIKNFIPLLNPVSQDFVSLLHKriKQQGSGKFvgDIKEDLFHFAFESITNVMFGerlgMLEETVNPEAQKFIDAVY 200
Cdd:cd11055  71 FSSGKLKLMVPIINDCCDELVEKLEK--AAETGKPV--DMKDLFQGFTLDVILSTAFG----IDVDSQNNPDDPFLKAAK 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      201 KMFHTSVPLLN----VPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEifyqdLRRKTEFRNYPGILYCLL--------- 267
Cdd:cd11055 143 KIFRNSIIRLFllllLFPLRLFLFLLFPFVFGFKSFSFLEDVVKKIIE-----QRRKNKSSRRKDLLQLMLdaqdsdedv 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEG----DISKM--LQMVpllkas 341
Cdd:cd11055 218 SKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSptydTVSKLkyLDMV------ 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      342 IKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRNLGFGWGV 420
Cdd:cd11055 292 INETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHpYAYLPFGAGP 371
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
3MZS_D      421 RQCVGRRIAELEMTLFLIHILENFKVEM--QHIGDVDTIFNLILTPDKPIF 469
Cdd:cd11055 372 RNCIGMRFALLEVKLALVKILQKFRFVPckETEIPLKLVGGATLSPKNGIY 422
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
47-448 2.61e-45

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: 163.98  E-value: 2.61e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       47 YGPIYREK-LGNLESVYIIHPEDVAHLFKfegsyPERYDIPPWLAYHRYYQKPIGvlfkkSGTW-------KKDRVVLNT 118
Cdd:cd11069   1 YGGLIRYRgLFGSERLLVTDPKALKHILV-----TNSYDFEKPPAFRRLLRRILG-----DGLLaaegeehKRQRKILNP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      119 eVMAPEAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPeaqkFIDA 198
Cdd:cd11069  71 -AFSYRHVKELYPIFWSKAEELVDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNE----LAEA 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      199 VYKMFHTS-------VPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKyteiFYQDLRRKTEFRNYPG---ILYCLLK 268
Cdd:cd11069 146 YRRLFEPTllgsllfILLLFLPRWLVRILPWKANREIRRAKDVLRRLARE----IIREKKAALLEGKDDSgkdILSILLR 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      269 S------EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQ------AEGDISKMlqmvP 336
Cdd:cd11069 222 AndfaddERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDppdgdlSYDDLDRL----P 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRWLSKDKD------LI 409
Cdd:cd11069 298 YLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAaspggaGS 377
                       410       420       430
                ....*....|....*....|....*....|....*....
3MZS_D      410 HFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:cd11069 378 NYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFEL 416
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
131-448 8.35e-45

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: 162.08  E-value: 8.35e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      131 PLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKmFHTSVPLl 210
Cdd:cd11059  74 AAMEPIIRERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSRERELLRRLL-ASLAPWL- 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      211 nvpPELYRLFRTKTWRDHVAAWDTIFNKAEKY-------TEIFYQDLRRKTEFRNYPGILYCLLKSEKMLLEDVKANITE 283
Cdd:cd11059 152 ---RWLPRYLPLATSRLIIGIYFRAFDEIEEWaldlcarAESSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALD 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDIS-KMLQMVPLLKASIKETLRLH-PISVTLQRY-PE 360
Cdd:cd11059 229 HIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPPDlEDLDKLPYLNAVIRETLRLYpPIPGSLPRVvPE 308
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      361 SDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRN---LGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd11059 309 GGATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMKrafWPFGSGSRMCIGMNLALMEMKLAL 388
                       330
                ....*....|.
3MZS_D      438 IHILENFKVEM 448
Cdd:cd11059 389 AAIYRNYRTST 399
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
109-468 6.51e-43

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: 157.33  E-value: 6.51e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      109 WKKDRVVLNTEVMAPEAIKNFipllNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETV 188
Cdd:cd20618  61 WRHLRKICTLELFSAKRLESF----QGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKE 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      189 NPEAQKFIDAVYKMFhTSVPLLNV---PPELYRLFRT---KTWRDHVAAWDTIFNKaekyteIFyQDLRRKTEFRNYPGI 262
Cdd:cd20618 137 SEEAREFKELIDEAF-ELAGAFNIgdyIPWLRWLDLQgyeKRMKKLHAKLDRFLQK------II-EEHREKRGESKKGGD 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      263 LYCLLKSEKMLLED-------VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNARRQAEGDISKM 331
Cdd:cd20618 209 DDDDLLLLLDLDGEgklsddnIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEEldsvVGRERLVEESDLPKL 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      332 lqmvPLLKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI- 409
Cdd:cd20618 289 ----PYLQAVVKETLRLHPPGpLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVk 364
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3MZS_D      410 --HFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENF--KVEMQHIGDVDT--IFNLILTPDKPI 468
Cdd:cd20618 365 gqDFELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFdwSLPGPKPEDIDMeeKFGLTVPRAVPL 429
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
122-450 1.73e-41

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: 153.15  E-value: 1.73e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      122 APEAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFvgDIKEDLFHFAFESITNVMFGERLGMLEetvNPEAQKFIDAVYK 201
Cdd:cd11061  66 SDKALRGYEPRILSHVEQLCEQLDDRAGKPVSWPV--DMSDWFNYLSFDVMGDLAFGKSFGMLE---SGKDRYILDLLEK 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      202 MFHTSVPLLNvPPELYRLFRTKT-WRDHVAAWdtifNKAEKYTEIFYQDlRRKTEFRNYPGILYCLLKS------EKMLL 274
Cdd:cd11061 141 SMVRLGVLGH-APWLRPLLLDLPlFPGATKAR----KRFLDFVRAQLKE-RLKAEEEKRPDIFSYLLEAkdpetgEGLDL 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      275 EDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDIS-KMLQMVPLLKASIKETLRLHP-IS 352
Cdd:cd11061 215 EELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLgPKLKSLPYLRACIDEALRLSPpVP 294
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      353 VTLQR-YPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRN--LGFGWGVRQCVGRRIA 429
Cdd:cd11061 295 SGLPReTPPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRARSafIPFSIGPRGCIGKNLA 374
                       330       340
                ....*....|....*....|.
3MZS_D      430 ELEMTLFLIHILENFKVEMQH 450
Cdd:cd11061 375 YMELRLVLARLLHRYDFRLAP 395
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
109-447 7.18e-41

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


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 151.54  E-value: 7.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      109 WKKDRVVLnTEVMAPEAIKNFIPLLNPVSQDFVSLLHKRIKQQGsgkfVGDIKEDLFHFAFESITNVMFGERLGMLEetv 188
Cdd:cd11056  61 WKELRQKL-TPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGK----ELEIKDLMARYTTDVIASCAFGLDANSLN--- 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      189 NPEAQkFIDAVYKMFHTSVP------LLNVPPELYRLFRTKTWrdhvaawdtifnkaEKYTEIFYQDLRRKT-EFRNYPG 261
Cdd:cd11056 133 DPENE-FREMGRRLFEPSRLrglkfmLLFFFPKLARLLRLKFF--------------PKEVEDFFRKLVRDTiEYREKNN 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      262 I--------LYCLLKSEKMLLEDVKANIT--EMLA-------GGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQA 324
Cdd:cd11056 198 IvrndfidlLLELKKKGKIEDDKSEKELTdeELAAqafvfflAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKH 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      325 EGDIS-KMLQMVPLLKASIKETLRLHPISVTLQRypesdLVLQDYLIPAK-------TLVQVAIYAMGRDPAFFSSPDKF 396
Cdd:cd11056 278 GGELTyEALQEMKYLDQVVNETLRKYPPLPFLDR-----VCTKDYTLPGTdvviekgTPVIIPVYALHHDPKYYPEPEKF 352
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
3MZS_D      397 DPTRWLSKDKDLIH-FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:cd11056 353 DPERFSPENKKKRHpYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVE 404
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
48-470 4.95e-40

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: 149.21  E-value: 4.95e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDV-------AHLFKFEGsyperYD-IPPWLAYhryyqkpiGVLFKKSGTWKKDRVVLNte 119
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEDIevilsssKLITKSFL-----YDfLKPWLGD--------GLLTSTGEKWRKRRKLLT-- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      120 vmaP----EAIKNFIPLLNPVSQDFVsllhKRIKQQGSGKFVgDIKEDLFHFAFESITNVMFGERLgmleETVNPEAQKF 195
Cdd:cd20628  66 ---PafhfKILESFVEVFNENSKILV----EKLKKKAGGGEF-DIFPYISLCTLDIICETAMGVKL----NAQSNEDSEY 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      196 IDAVYKMFHTSvpllnvppeLYRLFRTKTWrdhvaaWDTIFNKAEKYTEiFYQDLR------------RKTEFR-NYPGI 262
Cdd:cd20628 134 VKAVKRILEII---------LKRIFSPWLR------FDFIFRLTSLGKE-QRKALKvlhdftnkvikeRREELKaEKRNS 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      263 LYCLLKSEK-------MLLEDVK--ANITE---------MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVL-----N 319
Cdd:cd20628 198 EEDDEFGKKkrkafldLLLEAHEdgGPLTDedireevdtFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDeifgdD 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      320 ARRQAEGDISKM--LQMVpllkasIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFD 397
Cdd:cd20628 278 DRRPTLEDLNKMkyLERV------IKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFD 351
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3MZS_D      398 PTRWLSKDKDLIH-FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQH-IGDVDTIFNLILTPDKPIFL 470
Cdd:cd20628 352 PDRFLPENSAKRHpYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPpGEDLKLIAEIVLRSKNGIRV 426
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
48-449 5.83e-40

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: 149.01  E-value: 5.83e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDVAHLFKfegsypERYDippwlAYHRYyqKPIGVLFKKSG----------TWKKDRVVln 117
Cdd:cd11083   1 GSAYRFRLGRQPVLVISDPELIREVLR------RRPD-----EFRRI--SSLESVFREMGingvfsaegdAWRRQRRL-- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      118 teVMA---PEAIKNFIPLLNPVSQDFVSLLHKRIKQQGsgkfVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPeAQK 194
Cdd:cd11083  66 --VMPafsPKHLRYFFPTLRQITERLRERWERAAAEGE----AVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDP-LQE 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      195 FIDAVYKMFHTSVpllNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKSEKM-- 272
Cdd:cd11083 139 HLERVFPMLNRRV---NAPFPYWRYLRLPADRALDRALVEVRALVLDIIAAARARLAANPALAEAPETLLAMMLAEDDpd 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      273 -LL--EDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEG-DISKMLQMVPLLKASIKETLRL 348
Cdd:cd11083 216 aRLtdDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVpPLLEALDRLPYLEAVARETLRL 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      349 HPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKD-KDLIHFRN--LGFGWGVRQCVG 425
Cdd:cd11083 296 KPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGArAAEPHDPSslLPFGAGPRLCPG 375
                       410       420
                ....*....|....*....|....
3MZS_D      426 RRIAELEMTLFLIHILENFKVEMQ 449
Cdd:cd11083 376 RSLALMEMKLVFAMLCRNFDIELP 399
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
45-444 8.76e-38

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: 143.44  E-value: 8.76e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       45 QKYGPIYREKLGNLESVYIIHPEDVAHLFK-----FEGSYPerYDIPPWLAYHRYyqkpIGVLFKKSGTWKKDRVVLNTE 119
Cdd:cd11073   2 KKYGPIMSLKLGSKTTVVVSSPEAAREVLKthdrvLSGRDV--PDAVRALGHHKS----SIVWPPYGPRWRMLRKICTTE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      120 VMAPEAIKNFIPLLNPVSQDFVSLLHKRikqQGSGKFVgDIKEDLFHFAFESITNVMFGERLGMLEETvnpEAQKFIDAV 199
Cdd:cd11073  76 LFSPKRLDATQPLRRRKVRELVRYVREK---AGSGEAV-DIGRAAFLTSLNLISNTLFSVDLVDPDSE---SGSEFKELV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      200 YKMfhtsVPLLNVP------PELYRL----FRTKTwRDHVAAWDTIFNK--AEKYTEIFyQDLRRKTEFRNYPGILYCLL 267
Cdd:cd11073 149 REI----MELAGKPnvadffPFLKFLdlqgLRRRM-AEHFGKLFDIFDGfiDERLAERE-AGGDKKKDDDLLLLLDLELD 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYE-------MARslnVQEMLREEVLNARRQAEGDISKMlqmvPLLKA 340
Cdd:cd11073 223 SESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAEllrnpekMAK---ARAELDEVIGKDKIVEESDISKL----PYLQA 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      341 SIKETLRLHP-ISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDL--IHFRNLGFG 417
Cdd:cd11073 296 VVKETLRLHPpAPLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFkgRDFELIPFG 375
                       410       420
                ....*....|....*....|....*..
3MZS_D      418 WGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd11073 376 SGRRICPGLPLAERMVHLVLASLLHSF 402
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
40-457 5.06e-35

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: 135.34  E-value: 5.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       40 HIENFQKYGPIYREKLGNLESVYIIHPEDVAHLFkFEGSYPErydiPPWLaYHRYyQKPIGVLFKKSG--------TWKK 111
Cdd:cd20613   4 LLEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVL-ITLNLPK----PPRV-YSRL-AFLFGERFLGNGlvtevdheKWKK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      112 DRVVLNtevmaP----EAIKNFIPLLNPVSQDFVsllhKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEET 187
Cdd:cd20613  77 RRAILN-----PafhrKYLKNLMDEFNESADLLV----EKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      188 VNPeaqkFIDAVYKMFHTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNypGILYCLL 267
Cdd:cd20613 148 DSP----FPKAISLVLEGIQESFRNPLLKYNPSKRKYRREVREAIKFLRETGRECIEERLEALKRGEEVPN--DILTHIL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KSEKmllEDVKANITEML-------AGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKM--LQM 334
Cdd:cd20613 222 KASE---EEPDFDMEELLddfvtffIAGQETTANLLSFTLLELGRHPEILKRLQAEvdeVLGSKQYVEyEDLGKLeyLSQ 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      335 VpllkasIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI-HFRN 413
Cdd:cd20613 299 V------LKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIpSYAY 372
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
3MZS_D      414 LGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM---QHIGDVDTI 457
Cdd:cd20613 373 FPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELvpgQSFGILEEV 419
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
46-445 7.14e-35

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: 135.06  E-value: 7.14e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       46 KYGPIYREKLGNLESVYIIHPEdVAH--LFKFEGSYPERydiPPwlayhryyQKPIGVLFK--KSG--------TWKKDR 113
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRE-LAHeaLVQKGSSFASR---PP--------ANPLRVLFSsnKHMvnsspygpLWRTLR 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      114 VVLNTEVMAPEAIKNFIPLLNPVSQDFVSLLHKRikQQGSGKFVgdIKEDLFHFAFESITNVM-FGERLGmlEETVnpea 192
Cdd:cd11075  69 RNLVSEVLSPSRLKQFRPARRRALDNLVERLREE--AKENPGPV--NVRDHFRHALFSLLLYMcFGERLD--EETV---- 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      193 qKFIDAVYKMF---HTSVPLLNVPPELYRLFRTKTWRDHVAawdTIFNKAEKYTE-IFYQDLRRKTEFRNYPGILYCLLK 268
Cdd:cd11075 139 -RELERVQRELllsFTDFDVRDFFPALTWLLNRRRWKKVLE---LRRRQEEVLLPlIRARRKRRASGEADKDYTDFLLLD 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      269 SEKMLLEDVKANIT---------EMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA----RRQAEGDISKMlqmv 335
Cdd:cd11075 215 LLDLKEEGGERKLTdeelvslcsEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVvgdeAVVTEEDLPKM---- 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      336 PLLKASIKETLRLH-PISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLS--KDKDLIH-- 410
Cdd:cd11075 291 PYLKAVVLETLRRHpPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAggEAADIDTgs 370
                       410       420       430
                ....*....|....*....|....*....|....*..
3MZS_D      411 --FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFK 445
Cdd:cd11075 371 keIKMMPFGAGRRICPGLGLATLHLELFVARLVQEFE 407
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
100-472 2.61e-33

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 130.84  E-value: 2.61e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      100 GVLFKKSGTWKKDRVVLNTeVMAPEAIKNFIPLLNPVSQDFVSLLHKRikqqgsgkfVGDIKEDLFHFAFESITNVMFGE 179
Cdd:cd20621  50 GLLFSEGEEWKKQRKLLSN-SFHFEKLKSRLPMINEITKEKIKKLDNQ---------NVNIIQFLQKITGEVVIRSFFGE 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      180 RL-------GMLEETVNPEAQKFIDAVYKMFHTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIF--------NKAEKYTE 244
Cdd:cd20621 120 EAkdlkingKEIQVELVEILIESFLYRFSSPYFQLKRLIFGRKSWKLFPTKKEKKLQKRVKELRqfiekiiqNRIKQIKK 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      245 IFYQDLRRKTEFRNYpgILYCLLKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQA 324
Cdd:cd20621 200 NKDEIKDIIIDLDLY--LLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGND 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      325 EGDISKMLQMVPLLKASIKETLRLHPISVTL-QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLS 403
Cdd:cd20621 278 DDITFEDLQKLNYLNAFIKEVLRLYNPAPFLfPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLN 357
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      404 KDKDLI-HFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDVDTIFNLILTPDKPIFLVF 472
Cdd:cd20621 358 QNNIEDnPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIPNPKLKLIFKLLYEPVNDLLLKL 427
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
108-437 9.64e-33

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: 128.85  E-value: 9.64e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      108 TWKKDRVVLNTeVMAPEAIKNFIPLlnpvsQDFVS--LLHKRIKQQGsgkfvgDIKEDLFHFAFESITNVMFGERLGMLE 185
Cdd:cd11065  61 RWRLHRRLFHQ-LLNPSAVRKYRPL-----QELESkqLLRDLLESPD------DFLDHIRRYAASIILRLAYGYRVPSYD 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      186 ETVNPEAQKFIDAVYKMFHTSVPLLNVPPELYRL--FRTKTWRDHVAAWdtiFNKAEKYTEIFYQDLRRKTEFRNYPGil 263
Cdd:cd11065 129 DPLLRDAEEAMEGFSEAGSPGAYLVDFFPFLRYLpsWLGAPWKRKAREL---RELTRRLYEGPFEAAKERMASGTATP-- 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      264 yCLLK--------SEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKM 331
Cdd:cd11065 204 -SFVKdlleeldkEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEEldrVVGPDRLPTfEDRPNL 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      332 lqmvPLLKASIKETLRLHPISVT-LQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDK---D 407
Cdd:cd11065 283 ----PYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKgtpD 358
                       330       340       350
                ....*....|....*....|....*....|
3MZS_D      408 LIHFRNLGFGWGVRQCVGRRIAelEMTLFL 437
Cdd:cd11065 359 PPDPPHFAFGFGRRICPGRHLA--ENSLFI 386
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
48-445 2.83e-31

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: 125.02  E-value: 2.83e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDVAHLFKFEGSYpERYDIppwlayHRYYQKPIGVLFKKSGTWKKDRVVLNTEvMAPEAIK 127
Cdd:cd11057   1 GSPFRAWLGPRPFVITSDPEIVQVVLNSPHCL-NKSFF------YDFFRLGRGLFSAPYPIWKLQRKALNPS-FNPKILL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      128 NFIPLLNPVSQDFVSLLHKRIKQQGSgkfvgDIKEDLFHFAFESITNVMFGERLGMleetVNPEAQKFIDAVYKMFHTSV 207
Cdd:cd11057  73 SFLPIFNEEAQKLVQRLDTYVGGGEF-----DILPDLSRCTLEMICQTTLGSDVND----ESDGNEEYLESYERLFELIA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      208 -----PLLNvpPE-LYRLF-------RTKTWRDHVAawDTIFNKAEKYTEIFYQDLR-RKTEFRNYPGILY-CLLK---- 268
Cdd:cd11057 144 krvlnPWLH--PEfIYRLTgdykeeqKARKILRAFS--EKIIEKKLQEVELESNLDSeEDEENGRKPQIFIdQLLElarn 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      269 SEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDIS-KMLQMVPLLKASIKETLR 347
Cdd:cd11057 220 GEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQFITyEDLQQLVYLEMVLKETMR 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      348 LHPISVTLQRYPESDLVL-QDYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRWLSKDKDLIH-FRNLGFGWGVRQCV 424
Cdd:cd11057 300 LFPVGPLVGRETTADIQLsNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQRHpYAFIPFSAGPRNCI 379
                       410       420
                ....*....|....*....|.
3MZS_D      425 GRRIAELEMTLFLIHILENFK 445
Cdd:cd11057 380 GWRYAMISMKIMLAKILRNYR 400
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
90-450 2.85e-31

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: 125.00  E-value: 2.85e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       90 AYHRYYQKPIGVLFkkSGTwkkdrvvlntevmapeAIKNFIPLLNPVSQDFVSLLhkrikqqgSGKFVGDIKEDLFH--- 166
Cdd:cd11060  55 KRHAALRRKVASGY--SMS----------------SLLSLEPFVDECIDLLVDLL--------DEKAVSGKEVDLGKwlq 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      167 -FAFESITNVMFGERLGMLEET--VNpeaqKFIDAVYKMFHTSVPLLNVPpELYRLFRTK---TWRDHVAAWDTIFNKAE 240
Cdd:cd11060 109 yFAFDVIGEITFGKPFGFLEAGtdVD----GYIASIDKLLPYFAVVGQIP-WLDRLLLKNplgPKRKDKTGFGPLMRFAL 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      241 KYTEIFYQDLRRKTEfrNYPGILYCLL-----KSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLRE 315
Cdd:cd11060 184 EAVAERLAEDAESAK--GRKDMLDSFLeaglkDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRA 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      316 EVLNArrQAEGDISKMLQMV-----PLLKASIKETLRLHP-ISVTLQRY-PESDLVLQDYLIPAKTLVQVAIYAMGRDPA 388
Cdd:cd11060 262 EIDAA--VAEGKLSSPITFAeaqklPYLQAVIKEALRLHPpVGLPLERVvPPGGATICGRFIPGGTIVGVNPWVIHRDKE 339
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
3MZS_D      389 FFSS-PDKFDPTRWL--SKDKDLIHFR-NLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQH 450
Cdd:cd11060 340 VFGEdADVFRPERWLeaDEEQRRMMDRaDLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVD 405
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
241-449 5.84e-31

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: 123.87  E-value: 5.84e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      241 KYTEIFYQ--DLRRKTEFRNYPGILYCLLKS-----EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEML 313
Cdd:cd11042 170 KLKEIFSEiiQKRRKSPDKDEDDMLQTLMDAkykdgRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEAL 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      314 REEVLNARRQAEGDISKM-LQMVPLLKASIKETLRLHPISVTLQRYPESDLVL--QDYLIPAKTLVQVAIYAMGRDPAFF 390
Cdd:cd11042 250 REEQKEVLGDGDDPLTYDvLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVegGGYVIPKGHIVLASPAVSHRDPEIF 329
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
3MZS_D      391 SSPDKFDPTRWL---SKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQ 449
Cdd:cd11042 330 KNPDEFDPERFLkgrAEDSKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELV 391
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
48-447 8.52e-31

cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of Mycobacterium tuberculosis cytochrome P450 132 (CYP132) and similar proteins. The function of CYP132 is as yet unknown. CYP132 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410713 [Multi-domain]  Cd Length: 406  Bit Score: 123.07  E-value: 8.52e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDVAHLFKFEgsyperydippwlayHRYYQKpiGVLFKKSG-------------TWKKDRv 114
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTN---------------ARNYVK--GGVYERLKlllgnglltsegdLWRRQR- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      115 vlntEVMAP----EAIKNFIPLLNPVSQDFVSLLHkrikqQGSGKFVGDIKEDLFHFAFESITNVMFGERlgmleetVNP 190
Cdd:cd20620  63 ----RLAQPafhrRRIAAYADAMVEATAALLDRWE-----AGARRGPVDVHAEMMRLTLRIVAKTLFGTD-------VEG 126
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      191 EAQKFIDAV-YKMFHTSVPLLNvPPELYRLFRTKTWRDHVAAWDTIFnkaekytEIFYqDL--RRKTEFRNYPGILYCLL 267
Cdd:cd20620 127 EADEIGDALdVALEYAARRMLS-PFLLPLWLPTPANRRFRRARRRLD-------EVIY-RLiaERRAAPADGGDLLSMLL 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KS------EKM----LLEDVkanITEMLAGGvNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMlqm 334
Cdd:cd20620 198 AArdeetgEPMsdqqLRDEV---MTLFLAGH-ETTANALSWTWYLLAQHPEVAARLRAEvdrVLGGRPPTAEDLPQL--- 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      335 vPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRN 413
Cdd:cd20620 271 -PYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPrYAY 349
                       410       420       430
                ....*....|....*....|....*....|....
3MZS_D      414 LGFGWGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:cd20620 350 FPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLR 383
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
47-448 2.40e-30

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: 122.32  E-value: 2.40e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       47 YGPIYREKLGN-----LESVYIIH------PEDVA---HLFKFEGSYPERYDIppwlAYHRYyqkpigvlfkkSGTWKKD 112
Cdd:cd11027   1 YGDVFSLYLGSrlvvvLNSGAAIKealvkkSADFAgrpKLFTFDLFSRGGKDI----AFGDY-----------SPTWKLH 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      113 RVVLNTevmapeAIKNFI---PLLNPVSQDFVSLLHKRIKQQGSGKFvgDIKEDLFHFAFESITNVMFGERLGMLeetvN 189
Cdd:cd11027  66 RKLAHS------ALRLYAsggPRLEEKIAEEAEKLLKRLASQEGQPF--DPKDELFLAVLNVICSITFGKRYKLD----D 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      190 PEAQKFIDAVYKMFH--TSVPLLNVPPELyRLFRTKTWRDHVAA---WDTIFNKaeKYTEifYQDLRRKTEFRNypgILY 264
Cdd:cd11027 134 PEFLRLLDLNDKFFEllGAGSLLDIFPFL-KYFPNKALRELKELmkeRDEILRK--KLEE--HKETFDPGNIRD---LTD 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      265 CLLKSEK-----------MLLED-VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDIS 329
Cdd:cd11027 206 ALIKAKKeaedegdedsgLLTDDhLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAElddVIGRDRLPTLSDR 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      330 KMLqmvPLLKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKD-KD 407
Cdd:cd11027 286 KRL---PYLEATIAEVLRLSSVVpLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENgKL 362
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
3MZS_D      408 LIHFRN-LGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:cd11027 363 VPKPESfLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSP 404
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
133-449 4.97e-30

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: 121.21  E-value: 4.97e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      133 LNPVSQDFVSLLHKRIKQQGSGKFVGDIKeDLFH-FAFESITNVMFGERLGMLEETV-NPEAQKFIDAVYKMFHTS---- 206
Cdd:cd11062  74 LEPLIQEKVDKLVSRLREAKGTGEPVNLD-DAFRaLTADVITEYAFGRSYGYLDEPDfGPEFLDALRALAEMIHLLrhfp 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      207 --VPLLNVPPElyrlFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKS----EKMLLEDVKAN 280
Cdd:cd11062 153 wlLKLLRSLPE----SLLKRLNPGLAVFLDFQESIAKQVDEVLRQVSAGDPPSIVTSLFHALLNSdlppSEKTLERLADE 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      281 ITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlnarRQAEGDIS-----KMLQMVPLLKASIKETLRL-HPISVT 354
Cdd:cd11062 229 AQTLIGAGTETTARTLSVATFHLLSNPEILERLREEL----KTAMPDPDsppslAELEKLPYLTAVIKEGLRLsYGVPTR 304
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      355 LQRY-PESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWL--SKDKDLIHFrNLGFGWGVRQCVGRRIAEL 431
Cdd:cd11062 305 LPRVvPDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLgaAEKGKLDRY-LVPFSKGSRSCLGINLAYA 383
                       330
                ....*....|....*...
3MZS_D      432 EMTLFLIHILENFKVEMQ 449
Cdd:cd11062 384 ELYLALAALFRRFDLELY 401
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
61-474 5.84e-30

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 121.00  E-value: 5.84e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       61 VYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNtEVMAPEAIKNFIPLL-NPVSQD 139
Cdd:COG2124  51 WVVSRPADVREVLRDPRFFSSALGAGLRPRLLRPVLGDGSLLTLDGPEHTRLRKLLA-PAFTPRALRGYRPLIrEIADRL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      140 FVSLLHKRIkqqgsgkfvgdikEDLFHFAFE---SITNVMFGERLGmleetvnpEAQKFIDAVYKMFHTSVPLLNVPPEl 216
Cdd:COG2124 130 LDDLWQGGA-------------DLVLDFAAEltlRVIAELLGVPLE--------DRPQLLRWSDALLLRLDPDLGPEEP- 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      217 yrlfrtktWRDHVAAWDTIFnkaekyteifyQDLRRK-TEFRNYPG--ILYCLLKSE-----KMLLEDVKANITEMLAGG 288
Cdd:COG2124 188 --------WRRARAARRELD-----------AYLRALiAERRAAPRddLLSLLLSAEddgggRLSDDEIRDELITLLVAG 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      289 VNTTSMTLQWHLYEMARSLNVQEMLREEvlnarrqaegdiskmlQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDY 368
Cdd:COG2124 249 HETTANALAWALYALLRHPDQLAKLRAE----------------PDRPLLEAVVEETLRLYPPVPLARRVATEDVELGGY 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      369 LIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdkdlihfRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVeM 448
Cdd:COG2124 313 RIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFNN--------AHLPFGGGPHRCLGAALARLELKVALAELLRRFPL-L 383
                       410       420
                ....*....|....*....|....*.
3MZS_D      449 QHIGDVDTIFNLILTPDKPIFLVFRP 474
Cdd:COG2124 384 LLAEPPPLVRRPTLVPRGGERLPVRR 409
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
48-453 1.43e-29

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: 119.70  E-value: 1.43e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDVAHLFKFEGSYPERYDIPPWLAYHRYYQKPIGVLfkkSGT-WKKDRVVLNTEVMAPeAI 126
Cdd:cd20615   1 GPIYRIWSGPTPEIVLTTPEHVKEFYRDSNKHHKAPNNNSGWLFGQLLGQCVGLL---SGTdWKRVRKVFDPAFSHS-AA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      127 KNFIPLLNPVSQDFVSLLHKriKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYKMFHTS 206
Cdd:cd20615  77 VYYIPQFSREARKWVQNLPT--NSGDGRRFVIDPAQALKFLPFRVIAEILYGELSPEEKEELWDLAPLREELFKYVIKGG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      207 VPLLNvppeLYRLFRTKTWR---DHVAAWdTIFNkaekyTEIFyqDLRRKTEFRNYPGILYCLLKSEKMLLEDVKANITE 283
Cdd:cd20615 155 LYRFK----ISRYLPTAANRrlrEFQTRW-RAFN-----LKIY--NRARQRGQSTPIVKLYEAVEKGDITFEELLQTLDE 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISK-MLQMVPLLKASIKETLRLHPISV-TLQRYPES 361
Cdd:cd20615 223 MLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDyILSTDTLLAYCVLESLRLRPLLAfSVPESSPT 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      362 DLVLQDYLIPAKTLVQVAIYAMG-RDPAFFSSPDKFDPTRWLSKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHI 440
Cdd:cd20615 303 DKIIGGYRIPANTPVVVDTYALNiNNPFWGPDGEAYRPERFLGISPTDLRYNFWRFGFGPRKCLGQHVADVILKALLAHL 382
                       410
                ....*....|...
3MZS_D      441 LENFKVEMQHIGD 453
Cdd:cd20615 383 LEQYELKLPDQGE 395
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
44-475 6.40e-29

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: 118.07  E-value: 6.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYII-HPEDVAHLFKfegsyperydIPPWLAYHRYYQKPIGVLFKKSGTW-------KKDRVV 115
Cdd:cd11053   8 RARYGDVFTLRVPGLGPVVVLsDPEAIKQIFT----------ADPDVLHPGEGNSLLEPLLGPNSLLlldgdrhRRRRKL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      116 LntevMAP---EAIKNFipllnpvSQDFVSLLHKRIKQQGSGKFVgDIKEDLFHFAFESITNVMFGERLGmleetvnPEA 192
Cdd:cd11053  78 L----MPAfhgERLRAY-------GELIAEITEREIDRWPPGQPF-DLRELMQEITLEVILRVVFGVDDG-------ERL 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      193 QKFIDAVYKMF-HTSVPLLNVPPELYRLFRTKTWRDHVAAwdtifnkAEKYTEIFYQDLRRKTEFRNYPG--ILYCLLKS 269
Cdd:cd11053 139 QELRRLLPRLLdLLSSPLASFPALQRDLGPWSPWGRFLRA-------RRRIDALIYAEIAERRAEPDAERddILSLLLSA 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      270 -----EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEV--LNARRQAEgDISKMlqmvPLLKASI 342
Cdd:cd11053 212 rdedgQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELdaLGGDPDPE-DIAKL----PYLDAVI 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      343 KETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFrnLGFGWGVRQ 422
Cdd:cd11053 287 KETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSPYEY--LPFGGGVRR 364
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
3MZS_D      423 CVGRRIAELEMTLFLIHILENFKVEmqhigdvdtifnliLTPDKPIFLVFRPF 475
Cdd:cd11053 365 CIGAAFALLEMKVVLATLLRRFRLE--------------LTDPRPERPVRRGV 403
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
111-444 1.47e-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: 117.20  E-value: 1.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      111 KDRVVLNTEVMAPEAIKNFIPLL-NPVSQDFVSLLHKRIKQQGSGKFVgDIKEDLFHFAFESITNVMFGERLGMLEETVN 189
Cdd:cd20656  64 KVRKLCTLELFTPKRLESLRPIReDEVTAMVESIFNDCMSPENEGKPV-VLRKYLSAVAFNNITRLAFGKRFVNAEGVMD 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      190 PEAQKFIDAVYK--MFHTSVPLLNVPPELYRLF--RTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFrnYPGILyc 265
Cdd:cd20656 143 EQGVEFKAIVSNglKLGASLTMAEHIPWLRWMFplSEKAFAKHGARRDRLTKAIMEEHTLARQKSGGGQQH--FVALL-- 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      266 LLKSEKMLLED-VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNARRQAEGDISKMlqmvPLLKA 340
Cdd:cd20656 219 TLKEQYDLSEDtVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEEldrvVGSDRVMTEADFPQL----PYLQC 294
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      341 SIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI--HFRNLGFG 417
Cdd:cd20656 295 VVKEALRLHPPTpLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKghDFRLLPFG 374
                       330       340
                ....*....|....*....|....*..
3MZS_D      418 WGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd20656 375 AGRRVCPGAQLGINLVTLMLGHLLHHF 401
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
38-469 1.90e-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: 117.08  E-value: 1.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       38 FRHIENFQKYGPIYREKLGNlESVYII-HPEDVAHLFKFegsyPERYDIPPWLAYHryYQKPIG---VLFKKSGTWKKDR 113
Cdd:cd11040   2 LRNGKKYFSGGPIFTIRLGG-QKIYVItDPELISAVFRN----PKTLSFDPIVIVV--VGRVFGspeSAKKKEGEPGGKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      114 VVLNTEVMAPEAIKNfIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESIT----NVMFGERLgmleetvN 189
Cdd:cd11040  75 LIRLLHDLHKKALSG-GEGLDRLNEAMLENLSKLLDELSLSGGTSTVEVDLYEWLRDVLTrattEALFGPKL-------P 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      190 PEAQKFIDAVYKmFHTSVPLLnvppeLYRLFRtKTWRDHVAAWDTIFNKAEKYteifYQDLRRKTE-----FRNYpgilY 264
Cdd:cd11040 147 ELDPDLVEDFWT-FDRGLPKL-----LLGLPR-LLARKAYAARDRLLKALEKY----YQAAREERDdgselIRAR----A 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      265 CLLKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEG-----DISKMLQMVPLLK 339
Cdd:cd11040 212 KVLREAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGtnailDLTDLLTSCPLLD 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      340 ASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSS-PDKFDPTRWLSKDKDLI------HFR 412
Cdd:cd11040 292 STYLETLRLHSSSTSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEIWGPdPEEFDPERFLKKDGDKKgrglpgAFR 371
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
3MZS_D      413 nlGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIGD-----VDTIFNL-ILTPDKPIF 469
Cdd:cd11040 372 --PFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDwkvpgMDESPGLgILPPKRDVR 432
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
46-470 1.99e-28

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


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 117.04  E-value: 1.99e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       46 KYGPIYREKLGNlESVYIIHPEDVAHLFKFEGSYP---ERYDIPpwlayhRYYqkpiG--VLFKKSGTWKKDRvvlntEV 120
Cdd:cd11070   1 KLGAVKILFVSR-WNILVTKPEYLTQIFRRRDDFPkpgNQYKIP------AFY----GpnVISSEGEDWKRYR-----KI 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      121 MAPeAIKNFIPLLNPV-----SQDFVSLLHKriKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQK- 194
Cdd:cd11070  65 VAP-AFNERNNALVWEesirqAQRLIRYLLE--EQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTl 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      195 --FIDAVYKMFHTSVPLLNVPPelYRLFRTktwrdhvaAWDTiFNKAEKYTEIFYQDLRRKTEfRNYPGILYCLLKSEKM 272
Cdd:cd11070 142 naIKLAIFPPLFLNFPFLDRLP--WVLFPS--------RKRA-FKDVDEFLSELLDEVEAELS-ADSKGKQGTESVVASR 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      273 LLED----------VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA--RRQAEGDISKMLQMVPLLKA 340
Cdd:cd11070 210 LKRArrsggltekeLLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVlgDEPDDWDYEEDFPKLPYLLA 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      341 SIKETLRLHPISVTLQRYPESDLVLQDYL-----IPAKTLVQVAIYAMGRDPAF-FSSPDKFDPTRWLSKDKDLI---HF 411
Cdd:cd11070 290 VIYETLRLYPPVQLLNRKTTEPVVVITGLgqeivIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWGSTSGEIGaatRF 369
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
3MZS_D      412 RN-----LGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMqHIGDVDTIFNLILTPDKPIFL 470
Cdd:cd11070 370 TPargafIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRV-DPEWEEGETPAGATRDSPAKL 432
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
287-465 2.64e-28

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: 116.62  E-value: 2.64e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      287 GGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQaEGDISK--MLQMvPLLKASIKETLRLHPIS-VTLQRYPESDL 363
Cdd:cd11041 238 AAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAE-HGGWTKaaLNKL-KKLDSFMKESQRLNPLSlVSLRRKVLKDV 315
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      364 VLQDYL-IPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWL---SKDKDLIHFR-------NLGFGWGVRQCVGRRIAELE 432
Cdd:cd11041 316 TLSDGLtLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYrlrEQPGQEKKHQfvstspdFLGFGHGRHACPGRFFASNE 395
                       170       180       190
                ....*....|....*....|....*....|....*
3MZS_D      433 MTLFLIHILENFKVEMQHIG--DVDTIFNLILTPD 465
Cdd:cd11041 396 IKLILAHLLLNYDFKLPEGGerPKNIWFGEFIMPD 430
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
135-428 1.08e-27

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: 114.48  E-value: 1.08e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      135 PVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEEtvnpeaQKFIDAVYKM------FHTS-- 206
Cdd:cd11072  85 SIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQ------DKFKELVKEAlellggFSVGdy 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      207 VPLLnvppELYRLFRTKTWR--DHVAAWDTIFNKAEKYTEifyQDLRRKTEFRNYPGILYCLLKSEKML-----LEDVKA 279
Cdd:cd11072 159 FPSL----GWIDLLTGLDRKleKVFKELDAFLEKIIDEHL---DKKRSKDEDDDDDDLLDLRLQKEGDLefpltRDNIKA 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      280 NITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlnaRRQA-------EGDISKMlqmvPLLKASIKETLRLHP-I 351
Cdd:cd11072 232 IILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEV---REVVggkgkvtEEDLEKL----KYLKAVIKETLRLHPpA 304
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
3MZS_D      352 SVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI--HFRNLGFGwgvrqcVGRRI 428
Cdd:cd11072 305 PLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDFKgqDFELIPFG------AGRRI 377
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
271-437 2.13e-27

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: 113.85  E-value: 2.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      271 KMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNARRQAEGDISKMlqmvPLLKASIKETL 346
Cdd:cd20655 223 KITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEidsvVGKTRLVQESDLPNL----PYLQAVVKETL 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      347 RLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWL--SKDKDLI-----HFRNLGFGWG 419
Cdd:cd20655 299 RLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLasSRSGQELdvrgqHFKLLPFGSG 378
                       170
                ....*....|....*...
3MZS_D      420 VRQCVGRRIAELEMTLFL 437
Cdd:cd20655 379 RRGCPGASLAYQVVGTAI 396
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
90-445 4.89e-27

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: 112.81  E-value: 4.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       90 AYHRYYQKPIGvlFKKSGT-WKKDRVVLNTEVMAPEAIKNFIPLLNPVSQDFVsllhKRIKQQGSGKFVGDIKeDLFHFA 168
Cdd:cd11076  42 AYELMFNRAIG--FAPYGEyWRNLRRIASNHLFSPRRIAASEPQRQAIAAQMV----KAIAKEMERSGEVAVR-KHLQRA 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      169 feSITNVM---FGERLGMLEEtvNPEAQKFIDAVykmfhtsvpllnvpPELYRLFRTKTWRDH--VAAWDTIFN------ 237
Cdd:cd11076 115 --SLNNIMgsvFGRRYDFEAG--NEEAEELGEMV--------------REGYELLGAFNWSDHlpWLRWLDLQGirrrcs 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      238 ----KAEKYTEIFYQDLRRKTEFR-----NYPGILYCLLKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLN 308
Cdd:cd11076 177 alvpRVNTFVGKIIEEHRAKRSNRarddeDDVDVLLSLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPD 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      309 VQEMLREEVLNA----RRQAEGDISKMlqmvPLLKASIKETLRLHPISVTLQ--RYPESDLVLQDYLIPAKTLVQVAIYA 382
Cdd:cd11076 257 IQSKAQAEIDAAvggsRRVADSDVAKL----PYLQAVVKETLRLHPPGPLLSwaRLAIHDVTVGGHVVPAGTTAMVNMWA 332
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3MZS_D      383 MGRDPAFFSSPDKFDPTRWLSKDK---------DLihfRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFK 445
Cdd:cd11076 333 ITHDPHVWEDPLEFKPERFVAAEGgadvsvlgsDL---RLAPFGAGRRVCPGKALGLATVHLWVAQLLHEFE 401
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
271-470 1.24e-26

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: 111.59  E-value: 1.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      271 KMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEV-----LNARRQAEGDISKMlqmvPLLKASIKET 345
Cdd:cd20660 227 KLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELdrifgDSDRPATMDDLKEM----KYLECVIKEA 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      346 LRLHPiSVTL-QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRNLGFGWGVRQC 423
Cdd:cd20660 303 LRLFP-SVPMfGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHpYAYIPFSAGPRNC 381
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
3MZS_D      424 VGRRIAELEMTLFLIHILENFKVE-MQHIGDVDTIFNLILTPDKPIFL 470
Cdd:cd20660 382 IGQKFALMEEKVVLSSILRNFRIEsVQKREDLKPAGELILRPVDGIRV 429
PTZ00404 PTZ00404
cytochrome P450; Provisional
45-466 2.92e-26

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 111.35  E-value: 2.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        45 QKYGPIYREKLGNLESVYIIHPEDVAHLF--KFEgSYPERYDIPPwLAYHRYYQkpiGVLFKKSGTWKKDRVVLNtEVMA 122
Cdd:PTZ00404  59 KKYGGIFRIWFADLYTVVLSDPILIREMFvdNFD-NFSDRPKIPS-IKHGTFYH---GIVTSSGEYWKRNREIVG-KAMR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       123 PEAIKNFIPLLNpvsqDFVSLLHKRIKQ-QGSGKfVGDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYK 201
Cdd:PTZ00404 133 KTNLKHIYDLLD----DQVDVLIESMKKiESSGE-TFEPRYYLTKFTMSAMFKYIFNEDISFDEDIHNGKLAELMGPMEQ 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       202 MFHT-----SVPLLNVPPELYRLFRTKTwrdhvaawDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKS------E 270
Cdd:PTZ00404 208 VFKDlgsgsLFDVIEITQPLYYQYLEHT--------DKNFKKIKKFIKEKYHEHLKTIDPEVPRDLLDLLIKEygtntdD 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       271 KMLleDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlnarRQAEGDISKML----QMVPLLKASIKETL 346
Cdd:PTZ00404 280 DIL--SILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEI----KSTVNGRNKVLlsdrQSTPYTVAIIKETL 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       347 RLHPISV-TLQRYPESDLVLQD-YLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRnlgFGWGVRQCV 424
Cdd:PTZ00404 354 RYKPVSPfGLPRSTSNDIIIGGgHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSNDAFMP---FSIGPRNCV 430
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
3MZS_D       425 GRRIAELEMTLFLIHILENFK---VEMQHIGDVDtIFNLILTPDK 466
Cdd:PTZ00404 431 GQQFAQDELYLAFSNIILNFKlksIDGKKIDETE-EYGLTLKPNK 474
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
135-449 3.55e-26

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: 109.98  E-value: 3.55e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      135 PVSQDFVSLLHKRIKQQ-GSGKFVgDIKeDLFHFA-FESITNVMFGERLGMLEETvnpEAQKFIDAVYKM--FHTSVPLL 210
Cdd:cd11058  79 PIIQRYVDLLVSRLRERaGSGTPV-DMV-KWFNFTtFDIIGDLAFGESFGCLENG---EYHPWVALIFDSikALTIIQAL 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      211 NVPPELYRLFRTKTwrdhvaAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKS----EKMLLEDVKANITEMLA 286
Cdd:cd11058 154 RRYPWLLRLLRLLI------PKSLRKKRKEHFQYTREKVDRRLAKGTDRPDFMSYILRNkdekKGLTREELEANASLLII 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      287 GGVNTTSMTLQWHLYEMARSLNVQEMLREEVlnarR---QAEGDIS--KMLQMvPLLKASIKETLRLHP-ISVTLQRY-P 359
Cdd:cd11058 228 AGSETTATALSGLTYYLLKNPEVLRKLVDEI----RsafSSEDDITldSLAQL-PYLNAVIQEALRLYPpVPAGLPRVvP 302
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      360 ESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLG----FGWGVRQCVGRRIAELEMTL 435
Cdd:cd11058 303 AGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNDKKEafqpFSVGPRNCIGKNLAYAEMRL 382
                       330
                ....*....|....
3MZS_D      436 FLIHILENFKVEMQ 449
Cdd:cd11058 383 ILAKLLWNFDLELD 396
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
44-477 4.13e-26

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: 110.07  E-value: 4.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEGSYpERYDIPpwlayhRYYQKPIG--VLFKKSGTWKKDRVVLNTEVM 121
Cdd:cd11044  18 YQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKL-VRYGWP------RSVRRLLGenSLSLQDGEEHRRRRKLLAPAF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      122 APEAIKNFIPLLNPVSQDFVSllhkriKQQGSGKFvgDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYk 201
Cdd:cd11044  91 SREALESYVPTIQAIVQSYLR------KWLKAGEV--ALYPELRRLTFDVAARLLLGLDPEVEAEALSQDFETWTDGLF- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      202 mfhtSVPLlNVPPELYRlfrtktwrDHVAAWDTIFNKAEKYTEifyqdLRRKTEFRNYPGILYCLLKSE-----KMLLED 276
Cdd:cd11044 162 ----SLPV-PLPFTPFG--------RAIRARNKLLARLEQAIR-----ERQEEENAEAKDALGLLLEAKdedgePLSMDE 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      277 VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMvPLLKASIKETLRLH-PISVTL 355
Cdd:cd11044 224 LKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKKM-PYLDQVIKEVLRLVpPVGGGF 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      356 QRYPEsDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWL---SKDKDLiHFRNLGFGWGVRQCVGRRIAELE 432
Cdd:cd11044 303 RKVLE-DFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSparSEDKKK-PFSLIPFGGGPRECLGKEFAQLE 380
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
3MZS_D      433 MTLFLIHILENFKVEmqhigdvdtifnliLTPDKPIFLVFRPFNQ 477
Cdd:cd11044 381 MKILASELLRNYDWE--------------LLPNQDLEPVVVPTPR 411
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
141-464 4.24e-26

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: 109.95  E-value: 4.24e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      141 VSLLHKRIKQQGSgkfVGDIKEDLFHFAFESITNVMFGERLGML-EETVNPEAQKFIDAVYKMFHTSVPLLNVPPeLYRL 219
Cdd:cd11063  86 VQNLIKLLPRDGS---TVDLQDLFFRLTLDSATEFLFGESVDSLkPGGDSPPAARFAEAFDYAQKYLAKRLRLGK-LLWL 161
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      220 FRTKTWRDHVAAWDTIFNkaekytEIFYQDLRRKTEFRNYPG-----ILYCLLKS--EKMLLEDVKANIteMLAGgVNTT 292
Cdd:cd11063 162 LRDKKFREACKVVHRFVD------PYVDKALARKEESKDEESsdryvFLDELAKEtrDPKELRDQLLNI--LLAG-RDTT 232
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      293 SMTLQWHLYEMARSLNVQEMLREEVLN----ARRQAEGDISKMlqmvPLLKASIKETLRLHPISVTLQRYPESDLVL--- 365
Cdd:cd11063 233 ASLLSFLFYELARHPEVWAKLREEVLSlfgpEPTPTYEDLKNM----KYLRAVINETLRLYPPVPLNSRVAVRDTTLprg 308
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      366 ------QDYLIPAKTLVQVAIYAMGRDPA-FFSSPDKFDPTRWLSKDKDLIHFrnLGFGWGVRQCVGRRIAELEMTLFLI 438
Cdd:cd11063 309 ggpdgkSPIFVPKGTRVLYSVYAMHRRKDiWGPDAEEFRPERWEDLKRPGWEY--LPFNGGPRICLGQQFALTEASYVLV 386
                       330       340
                ....*....|....*....|....*..
3MZS_D      439 HILENF-KVEMQHIGDVDTIFNLILTP 464
Cdd:cd11063 387 RLLQTFdRIESRDVRPPEERLTLTLSN 413
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
284-447 4.75e-26

cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 109.66  E-value: 4.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMlqmvPLLKASIKETLRLHPISVTLQRYPE 360
Cdd:cd11049 228 LLTAGTETTASTLAWAFHLLARHPEVERRLHAEldaVLGGRPATFEDLPRL----TYTRRVVTEALRLYPPVWLLTRRTT 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      361 SDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWL---SKDKDLIHFrnLGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd11049 304 ADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLpgrAAAVPRGAF--IPFGAGARKCIGDTFALTELTLAL 381
                       170
                ....*....|
3MZS_D      438 IHILENFKVE 447
Cdd:cd11049 382 ATIASRWRLR 391
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
47-474 5.00e-26

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: 110.10  E-value: 5.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       47 YGPIYREKLGNlESVYIIHPEDVAH-LFKFE----GSYPERYdippwlAYHryyqkpiGVLFKKSGT------W----KK 111
Cdd:cd11066   1 NGPVFQIRLGN-KRIVVVNSFASVRdLWIKNssalNSRPTFY------TFH-------KVVSSTQGFtigtspWdescKR 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      112 DRVVLNTEVMAPeAIKNFIPLLNPVSQDFVSLLHKRIKQqgsGKFVGDIKEDLFHFAFESITNVMFGERL------GMLE 185
Cdd:cd11066  67 RRKAAASALNRP-AVQSYAPIIDLESKSFIRELLRDSAE---GKGDIDPLIYFQRFSLNLSLTLNYGIRLdcvdddSLLL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      186 ETVNPEaqkfiDAVYKMFHTSVPLLNVPPeLYRLFRTKTWRDHVAawDTIFNKAEKYTEIFYQDLRRKTEFRN-YPGILY 264
Cdd:cd11066 143 EIIEVE-----SAISKFRSTSSNLQDYIP-ILRYFPKMSKFRERA--DEYRNRRDKYLKKLLAKLKEEIEDGTdKPCIVG 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      265 CLLK--SEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARS--LNVQEMLREEVLNARRQAEGDISKML--QMVPLL 338
Cdd:cd11066 215 NILKdkESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPpgQEIQEKAYEEILEAYGNDEDAWEDCAaeEKCPYV 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      339 KASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI----HFrn 413
Cdd:cd11066 295 VALVKETLRYFTVLpLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIpgppHF-- 372
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
3MZS_D      414 lGFGWGVRQCVGRRIAELEMTLFLIHILENFKvemqhIGDVDTIFNLILTPDK----PIFLVFRP 474
Cdd:cd11066 373 -SFGAGSRMCAGSHLANRELYTAICRLILLFR-----IGPKDEEEPMELDPFEynacPTALVAEP 431
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
162-448 9.50e-26

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: 109.22  E-value: 9.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      162 EDLFH-FAFESITNVMFGERLGML--EETVNPEAQKFIDA---VYKMFHTSVPL------LNVPPElyRLFR--TKTWRD 227
Cdd:cd11064 108 QDVLQrFTFDVICKIAFGVDPGSLspSLPEVPFAKAFDDAseaVAKRFIVPPWLwklkrwLNIGSE--KKLReaIRVIDD 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      228 HVAawDTIFNKAEKYTEIFYQDLRRK---TEFRNYPGILYCLLKSEkmLLEDVKANIteMLAGGvNTTSMTLQWHLYEMA 304
Cdd:cd11064 186 FVY--EVISRRREELNSREEENNVREdllSRFLASEEEEGEPVSDK--FLRDIVLNF--ILAGR-DTTAAALTWFFWLLS 258
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      305 RSLNVQEMLREEVLNARRQAEGDISKMLQM-----VPLLKASIKETLRLHPiSVTLQ-RYPESDLVLQD-YLIPAKTLVQ 377
Cdd:cd11064 259 KNPRVEEKIREELKSKLPKLTTDESRVPTYeelkkLVYLHAALSESLRLYP-PVPFDsKEAVNDDVLPDgTFVKKGTRIV 337
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      378 VAIYAMGR-------DPAffsspdKFDPTRWLSKDKDLIH---FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:cd11064 338 YSIYAMGRmesiwgeDAL------EFKPERWLDEDGGLRPespYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFK 411

                .
3MZS_D      448 M 448
Cdd:cd11064 412 V 412
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
46-447 3.45e-24

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: 104.92  E-value: 3.45e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       46 KYGPIYREKLGNLESVYIIHPEDVAH-LFKFEGSYPERydIPPWLAYhryyqKPI--GVLFKKSGTWKKDRVVLnTEVMA 122
Cdd:cd20649   1 KYGPICGYYIGRRMFVVIAEPDMIKQvLVKDFNNFTNR--MKANLIT-----KPMsdSLLCLRDERWKRVRSIL-TPAFS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      123 PEAIKNFIPLLNPVSQdfvsLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLgmlEETVNPEaQKFIDAVYKM 202
Cdd:cd20649  73 AAKMKEMVPLINQACD----VLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQV---DSQKNPD-DPFVKNCKRF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      203 FHTSVP------LLNVP----PELYRL----------FRTKTWRDHVAAWDTifNKAEKYTEIFYQ---DLRRKTEF--- 256
Cdd:cd20649 145 FEFSFFrpililFLAFPfimiPLARILpnksrdelnsFFTQCIRNMIAFRDQ--QSPEERRRDFLQlmlDARTSAKFlsv 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      257 --------------RNYPGILYC----LLKSEKMLLED-VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEV 317
Cdd:cd20649 223 ehfdivndadesayDGHPNSPANeqtkPSKQKRMLTEDeIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREV 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      318 LNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFD 397
Cdd:cd20649 303 DEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFI 382
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
3MZS_D      398 PTRWLSKDKDLIH-FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:cd20649 383 PERFTAEAKQRRHpFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
159-470 4.44e-24

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: 103.80  E-value: 4.44e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      159 DIKEDLFHFAFESITNVMFGErlgMLEETVNPEAQKFIDAVYKMFhtSVPLlNVPP-ELYRLFRTKTwrdhvaawdtifN 237
Cdd:cd11043 105 VVLELAKKMTFELICKLLLGI---DPEEVVEELRKEFQAFLEGLL--SFPL-NLPGtTFHRALKARK------------R 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      238 KAEKYTEIFYQDLRRKTEFRNYPGILYCLLK-----SEKMLLEDVKANITEMLAGGVNTTSMTLQW---HLYEMARSLnv 309
Cdd:cd11043 167 IRKELKKIIEERRAELEKASPKGDLLDVLLEekdedGDSLTDEEILDNILTLLFAGHETTSTTLTLavkFLAENPKVL-- 244
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      310 QEMLRE--EVLNARRQAEG----DISKM--LQMVpllkasIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIY 381
Cdd:cd11043 245 QELLEEheEIAKRKEEGEGltweDYKSMkyTWQV------INETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSAR 318
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      382 AMGRDPAFFSSPDKFDPTRWLSKDKD-LIHFrnLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMqhIGDVDTIFNL 460
Cdd:cd11043 319 ATHLDPEYFPDPLKFNPWRWEGKGKGvPYTF--LPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEV--VPDEKISRFP 394
                       330
                ....*....|..
3MZS_D      461 ILTPDK--PIFL 470
Cdd:cd11043 395 LPRPPKglPIRL 406
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
45-450 1.21e-23

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: 103.03  E-value: 1.21e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       45 QKYGPIYREKLGNLESVYIIHPEDVAHLF---KFEgsypeRYDIPPwLAYHRYYqkpIGV-LFKKSGT---WKKDRVVLn 117
Cdd:cd11068  10 DELGPIFKLTLPGRRVVVVSSHDLIAELCdesRFD-----KKVSGP-LEELRDF---AGDgLFTAYTHepnWGKAHRIL- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      118 TEVMAPEAIKNFIP-LLNPVSQdfvslLHKRIKQQGSGKFVgDIKEDLFHFAFESITNVMFGERLGMLEEtvnPEAQKFI 196
Cdd:cd11068  80 MPAFGPLAMRGYFPmMLDIAEQ-----LVLKWERLGPDEPI-DVPDDMTRLTLDTIALCGFGYRFNSFYR---DEPHPFV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      197 DAVYKMFHTSVPLLNVPPE---LYRLFRTKTWRDHVAAWDTIfnkaekyTEIFYQdlRRKTEFRNYPGILYCLLKS---- 269
Cdd:cd11068 151 EAMVRALTEAGRRANRPPIlnkLRRRAKRQFREDIALMRDLV-------DEIIAE--RRANPDGSPDDLLNLMLNGkdpe 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      270 --EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMlqmvPLLKASIKE 344
Cdd:cd11068 222 tgEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEvdeVLGDDPPPYEQVAKL----RYIRRVLDE 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      345 TLRLHPISVTLQRYPESDLVLQD-YLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRWLSKdkdliHFRNLG------F 416
Cdd:cd11068 298 TLRLWPTAPAFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPE-----EFRKLPpnawkpF 372
                       410       420       430
                ....*....|....*....|....*....|....
3MZS_D      417 GWGVRQCVGRRIAELEMTLFLIHILENFKVEMQH 450
Cdd:cd11068 373 GNGQRACIGRQFALQEATLVLAMLLQRFDFEDDP 406
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
179-464 3.58e-23

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: 101.53  E-value: 3.58e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      179 ERLGMLEETVNpEAQKFIDaVYKMFHTSVPLLN-VPPEL--YRLFRT----------KTWRDHVAAWDTifNKAEKYTEI 245
Cdd:cd20651 131 QKLRKLLELVH-LLFRNFD-MSGGLLNQFPWLRfIAPEFsgYNLLVElnqklieflkEEIKEHKKTYDE--DNPRDLIDA 206
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      246 FYQDLRRKTEfrnypgilycllKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNAR 321
Cdd:cd20651 207 YLREMKKKEP------------PSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEidevVGRDR 274
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      322 RQAEGDISKMlqmvPLLKASIKETLRLHPI-SVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTR 400
Cdd:cd20651 275 LPTLDDRSKL----PYTEAVILEVLRIFTLvPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPER 350
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
3MZS_D      401 WLSKDKDLI-HFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDVDT---IFNLILTP 464
Cdd:cd20651 351 FLDEDGKLLkDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDLegiPGGITLSP 418
PLN02183 PLN02183
ferulate 5-hydroxylase
266-450 4.06e-23

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 102.24  E-value: 4.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       266 LLKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLN----VQEMLREEVLNARRQAEGDISKMLqmvpLLKAS 341
Cdd:PLN02183 294 LQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEdlkrVQQELADVVGLNRRVEESDLEKLT----YLKCT 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       342 IKETLRLH-PISVTLQRYPEsDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSK---DKDLIHFRNLGFG 417
Cdd:PLN02183 370 LKETLRLHpPIPLLLHETAE-DAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPgvpDFKGSHFEFIPFG 448
                        170       180       190
                 ....*....|....*....|....*....|...
3MZS_D       418 WGVRQCVGRRIAELEMTLFLIHILENFKVEMQH 450
Cdd:PLN02183 449 SGRRSCPGMQLGLYALDLAVAHLLHCFTWELPD 481
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
287-470 4.18e-23

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: 101.34  E-value: 4.18e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      287 GGVNTTSMTLQWHLYEMARSLNVQEMLREEV-LNARRQAEGDISKMLQMvPLLKASIKETLRLHPISVTLQRYPESDLVL 365
Cdd:cd20650 239 AGYETTSSTLSFLLYELATHPDVQQKLQEEIdAVLPNKAPPTYDTVMQM-EYLDMVVNETLRLFPIAGRLERVCKKDVEI 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      366 QDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd20650 318 NGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDpYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNF 397
                       170       180       190
                ....*....|....*....|....*....|....*.
3MZS_D      445 KV----------EMQHIGdvdtifnlILTPDKPIFL 470
Cdd:cd20650 398 SFkpcketqiplKLSLQG--------LLQPEKPIVL 425
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
169-464 1.22e-22

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: 100.06  E-value: 1.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      169 FESITNVMFGERLGMLEETVNPEAQKFI----------------DAVYKMFHTSVPLLNVPPELYRLFRtktwrdhvaaw 232
Cdd:cd11028 116 YLSVGNVICAICFGKRYSRDDPEFLELVksnddfgafvgagnpvDVMPWLRYLTRRKLQKFKELLNRLN----------- 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      233 DTIFNKAEKYTEIFYQDLRRKtefrnypgILYCLLK-SEKMLLEDVKAN----------ITEMLAGGVNTTSMTLQWHLY 301
Cdd:cd11028 185 SFILKKVKEHLDTYDKGHIRD--------ITDALIKaSEEKPEEEKPEVgltdehiistVQDLFGAGFDTISTTLQWSLL 256
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      302 EMARSLNVQEMLREE---VLNARRQAEGDISKMLqmvPLLKASIKETLRLHPI-SVTLQRYPESDLVLQDYLIPAKTLVQ 377
Cdd:cd11028 257 YMIRYPEIQEKVQAEldrVIGRERLPRLSDRPNL---PYTEAFILETMRHSSFvPFTIPHATTRDTTLNGYFIPKGTVVF 333
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      378 VAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI---HFRNLGFGWGVRQCVGRRIAELEMTLF---LIHILEnFKVEMQHI 451
Cdd:cd11028 334 VNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDktkVDKFLPFGAGRRRCLGEELARMELFLFfatLLQQCE-FSVKPGEK 412
                       330
                ....*....|...
3MZS_D      452 GDVDTIFNLILTP 464
Cdd:cd11028 413 LDLTPIYGLTMKP 425
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
225-455 2.63e-22

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


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 99.02  E-value: 2.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      225 WRDHVAAWDTIFNK---AEKYTEIFYQDL---RRKTEFRNYP----GILYCLLKSEKMLLEDVKAN------------IT 282
Cdd:cd20652 161 FLRHLPSYKKAIEFlvqGQAKTHAIYQKIideHKRRLKPENPrdaeDFELCELEKAKKEGEDRDLFdgfytdeqlhhlLA 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      283 EMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPI-SVTLQRYPES 361
Cdd:cd20652 241 DLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVvPLGIPHGCTE 320
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      362 DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI---HFrnLGFGWGVRQCVGRRIAELEMTLFLI 438
Cdd:cd20652 321 DAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLkpeAF--IPFQTGKRMCLGDELARMILFLFTA 398
                       250
                ....*....|....*..
3MZS_D      439 HILENFKVEMQHIGDVD 455
Cdd:cd20652 399 RILRKFRIALPDGQPVD 415
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
48-439 3.21e-22

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: 98.65  E-value: 3.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       48 GPIYREKLGNLESVYIIHPEDVAHLFK-FEGSYPERydiPP-----WLAYHryYQKpigVLFKKSGT-WKKDRVVLNTEV 120
Cdd:cd20657   1 GPIMYLKVGSCGVVVASSPPVAKAFLKtHDANFSNR---PPnagatHMAYN--AQD---MVFAPYGPrWRLLRKLCNLHL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      121 MAPEAIKNFipllNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLgmLEETVNPEAQKFIDAVY 200
Cdd:cd20657  73 FGGKALEDW----AHVRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSKRV--FAAKAGAKANEFKEMVV 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      201 KMFhTSVPLLNVP---PELyrlfrtkTWRD--HVAA--------WDTIFNKAEKYTEIFYQDlrRKTEfrnyPGILYCLL 267
Cdd:cd20657 147 ELM-TVAGVFNIGdfiPSL-------AWMDlqGVEKkmkrlhkrFDALLTKILEEHKATAQE--RKGK----PDFLDFVL 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KS-------EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNV----QEMLREEVLNARRQAEGDISKMlqmvP 336
Cdd:cd20657 213 LEnddngegERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDIlkkaQEEMDQVIGRDRRLLESDIPNL----P 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI-----H 410
Cdd:cd20657 289 YLQAICKETFRLHPSTpLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKVdvrgnD 368
                       410       420       430
                ....*....|....*....|....*....|..
3MZS_D      411 FRNLGFGWGVRQCVGRR--IAELEMTL-FLIH 439
Cdd:cd20657 369 FELIPFGAGRRICAGTRmgIRMVEYILaTLVH 400
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
46-446 1.13e-21

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: 96.62  E-value: 1.13e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       46 KYGPIYREKLGNLESVYIIHPE-------DVAHLFKFEGSYPerYDIPPWlaYHRyyqkpiGVLFKKSGTWKKDRVVLnT 118
Cdd:cd11045   9 RYGPVSWTGMLGLRVVALLGPDanqlvlrNRDKAFSSKQGWD--PVIGPF--FHR------GLMLLDFDEHRAHRRIM-Q 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      119 EVMAPEAIKNFIPLLNPVSQDFVSllhkRIKQQGSGKFVGDIKEDLFHFAfesiTNVMFGERLGmleetvnPEAQKFIDA 198
Cdd:cd11045  78 QAFTRSALAGYLDRMTPGIERALA----RWPTGAGFQFYPAIKELTLDLA----TRVFLGVDLG-------PEADKVNKA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      199 VYKMFHTSVPLLNVPpelyrLFRTKTWRDHvaawdtifnKAEKYTEIFYqdLRRKTEFRNYPG----ILYCLLKSE---K 271
Cdd:cd11045 143 FIDTVRASTAIIRTP-----IPGTRWWRGL---------RGRRYLEEYF--RRRIPERRAGGGddlfSALCRAEDEdgdR 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      272 MLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLnARRQAEGDISKMLQMvPLLKASIKETLRLHPI 351
Cdd:cd11045 207 FSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESL-ALGKGTLDYEDLGQL-EVTDWVFKEALRLVPP 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      352 SVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWL-SKDKDLIH-FRNLGFGWGVRQCVGRRIA 429
Cdd:cd11045 285 VPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSpERAEDKVHrYAWAPFGGGAHKCIGLHFA 364
                       410
                ....*....|....*..
3MZS_D      430 ELEMTLFLIHILENFKV 446
Cdd:cd11045 365 GMEVKAILHQMLRRFRW 381
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
60-447 1.39e-21

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: 96.86  E-value: 1.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       60 SVYIIHPEDVAHLFKFEGSYPERYD--IPPWLAYhryyqkpiGVLFKKSGTWKKDRVVLNtevmaP----EAIKNFIPLL 133
Cdd:cd20659  14 ILVLNHPDTIKAVLKTSEPKDRDSYrfLKPWLGD--------GLLLSNGKKWKRNRRLLT-----PafhfDILKPYVPVY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      134 NPVSQDfvsLLHKRIKQQGSGKFVgDIKEDLFHFAFESITNVMFGERLGMLEETVNPEaqkFIDAVYKMFHTSV-----P 208
Cdd:cd20659  81 NECTDI---LLEKWSKLAETGESV-EVFEDISLLTLDIILRCAFSYKSNCQQTGKNHP---YVAAVHELSRLVMerflnP 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      209 LLNVPPeLYRLfrTKTWRDhvaawdtiFNKAEKYTEIFYQDL---RRKT---------EFRNYPGILYCLLKS-----EK 271
Cdd:cd20659 154 LLHFDW-IYYL--TPEGRR--------FKKACDYVHKFAEEIikkRRKElednkdealSKRKYLDFLDILLTArdedgKG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      272 MLLEDVKAN-ITEMLAGGvNTTSMTLQWHLYEMARSLNVQEMLREEV---LNARRQAE-GDISKMlqmvPLLKASIKETL 346
Cdd:cd20659 223 LTDEEIRDEvDTFLFAGH-DTTASGISWTLYSLAKHPEHQQKCREEVdevLGDRDDIEwDDLSKL----PYLTMCIKESL 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      347 RLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRNLGFGWGVRQCVG 425
Cdd:cd20659 298 RLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDpFAFIPFSAGPRNCIG 377
                       410       420
                ....*....|....*....|..
3MZS_D      426 RRIAELEMTLFLIHILENFKVE 447
Cdd:cd20659 378 QNFAMNEMKVVLARILRRFELS 399
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
44-454 2.75e-21

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: 95.89  E-value: 2.75e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       44 FQKYGPIYREKLGNLESVYIIHPEDVAHLFKfegSYPERYDIPPWLAYHryyQKPI---GVLFKKSGTWKKDRvvlntEV 120
Cdd:cd11046   7 FLEYGPIYKLAFGPKSFLVISDPAIAKHVLR---SNAFSYDKKGLLAEI---LEPImgkGLIPADGEIWKKRR-----RA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      121 MAPEAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETvnpeaQKFIDAVY 200
Cdd:cd11046  76 LVPALHKDYLEMMVRVFGRCSERLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTEE-----SPVIKAVY 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      201 KMF----HTSV---PLLNVPPELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFRNY-----PGILYCLL- 267
Cdd:cd11046 151 LPLveaeHRSVwepPYWDIPAALFIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYlneddPSLLRFLVd 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 -----KSEKMLLEDVKAniteMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMLQMVPLLk 339
Cdd:cd11046 231 mrdedVDSKQLRDDLMT----MLIAGHETTAAVLTWTLYELSQNPELMAKVQAEvdaVLGDRLPPTYEDLKKLKYTRRV- 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      340 asIKETLRLHPISVTLQRYPESDLVLQD--YLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-----FR 412
Cdd:cd11046 306 --LNESLRLYPQPPVLIRRAVEDDKLPGggVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNeviddFA 383
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
3MZS_D      413 NLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM----QHIGDV 454
Cdd:cd11046 384 FLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELdvgpRHVGMT 429
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
46-474 3.26e-21

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 96.43  E-value: 3.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        46 KYGPIYREKLGNLESVYIIHPEDVAHLFKFE----GSYPeRYDIPPWLAY--HRYYQKPIGvlfkksGTWKKDRVVLNTE 119
Cdd:PLN03112  63 KYGPLVYLRLGSVDAITTDDPELIREILLRQddvfASRP-RTLAAVHLAYgcGDVALAPLG------PHWKRMRRICMEH 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       120 VMAPEAIKNFIpllNPVSQDFVSLLHKRIKQQGSGKFVgDIKEDLFHFAFESITNVMFGERLGMLEETVNPEAQKFidav 199
Cdd:PLN03112 136 LLTTKRLESFA---KHRAEEARHLIQDVWEAAQTGKPV-NLREVLGAFSMNNVTRMLLGKQYFGAESAGPKEAMEF---- 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       200 ykmfhtsvplLNVPPELYRLFRTKTWRDHVAAWDTI--------FNKAEKYTEIFYQ-------DLRRKTEFRNYPGILY 264
Cdd:PLN03112 208 ----------MHITHELFRLLGVIYLGDYLPAWRWLdpygcekkMREVEKRVDEFHDkiidehrRARSGKLPGGKDMDFV 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       265 CLLKS-------EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA----RRQAEGDISKMlq 333
Cdd:PLN03112 278 DVLLSlpgengkEHMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVvgrnRMVQESDLVHL-- 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       334 mvPLLKASIKETLRLHPISVTL-QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDK---DLI 409
Cdd:PLN03112 356 --NYLRCVVRETFRMHPAGPFLiPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGsrvEIS 433
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3MZS_D       410 H---FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFK------VEMQHIgDVDTIFNLILTPDKPIFLVFRP 474
Cdd:PLN03112 434 HgpdFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDwsppdgLRPEDI-DTQEVYGMTMPKAKPLRAVATP 506
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
109-474 2.19e-20

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  Cd Length: 444  Bit Score: 93.20  E-value: 2.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      109 WKKDRVVLNTEVMAPEAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVgDIKEDLFHFAFESITNVMFGERL---GMLE 185
Cdd:cd20658  61 WKKMRKVLTTELMSPKRHQWLHGKRTEEADNLVAYVYNMCKKSNGGGLV-NVRDAARHYCGNVIRKLMFGTRYfgkGMED 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      186 ETVNPEAQKFIDAVYKM--FHTSVPLLNVPPELYRLFRTKTWRDHVAAWDTIfnkaEKYTEIFYQDLRR------KTEFR 257
Cdd:cd20658 140 GGPGLEEVEHMDAIFTAlkCLYAFSISDYLPFLRGLDLDGHEKIVREAMRII----RKYHDPIIDERIKqwregkKKEEE 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      258 NYPGILYCLLKSEKMLL---EDVKANITEMLAGGVNTTSMTLQWHLYEMarsLNVQEMLR---EE----VLNARRQAEGD 327
Cdd:cd20658 216 DWLDVFITLKDENGNPLltpDEIKAQIKELMIAAIDNPSNAVEWALAEM---LNQPEILRkatEEldrvVGKERLVQESD 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      328 ISKmLQMVpllKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDK 406
Cdd:cd20658 293 IPN-LNYV---KACAREAFRLHPVApFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDS 368
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
3MZS_D      407 DLI----HFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQhiGDVDTIfNLI-----LTPDKPIFLVFRP 474
Cdd:cd20658 369 EVTltepDLRFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLP--PNVSSV-DLSeskddLFMAKPLVLVAKP 442
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
279-438 2.33e-20

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: 92.89  E-value: 2.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      279 ANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlnarrQAEGDI---SKMLQMVPLLKASIKETLRLHPISVTL 355
Cdd:cd20614 211 DNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEA-----AAAGDVprtPAELRRFPLAEALFRETLRLHPPVPFV 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      356 QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTL 435
Cdd:cd20614 286 FRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPNPVELLQFGGGPHFCLGYHVACVELVQ 365

                ...
3MZS_D      436 FLI 438
Cdd:cd20614 366 FIV 368
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
83-447 2.53e-20

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: 93.52  E-value: 2.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       83 YDIPPWlaYHRYyqKPIGVLFKKSGTWKKDRVVLN--TEVMAPEAIKNFipllnpvsQDFVSLLHKRIKQQGSGKFvgDI 160
Cdd:cd20622  46 GGIGPH--HHLV--KSTGPAFRKHRSLVQDLMTPSflHNVAAPAIHSKF--------LDLIDLWEAKARLAKGRPF--SA 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      161 KEDLFHFAFESITNVMFG------------ERLGMLEETVN----------PEAQK---------FIDAVYKMFHTSVPL 209
Cdd:cd20622 112 KEDIHHAALDAIWAFAFGinfdasqtrpqlELLEAEDSTILpagldepvefPEAPLpdeleavldLADSVEKSIKSPFPK 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      210 L------NVPPeLYRLFRTKTwrdhvaawDTIFNKAEKYTEIFyQDLRRKTEFRNypGILYcLLKSEKMLLE----DVKA 279
Cdd:cd20622 192 LshwfyrNQPS-YRRAAKIKD--------DFLQREIQAIARSL-ERKGDEGEVRS--AVDH-MVRRELAAAEkegrKPDY 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      280 NITEM-------LAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQA--EG---DISKMLQM-VPLLKASIKETL 346
Cdd:cd20622 259 YSQVIhdelfgyLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEAvaEGrlpTAQEIAQArIPYLDAVIEEIL 338
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      347 RLHPISVTLQRYPESDLVLQDYLIPAKTLVqvaiYAMGRDPAFFSSP---------------------------DKFDPT 399
Cdd:cd20622 339 RCANTAPILSREATVDTQVLGYSIPKGTNV----FLLNNGPSYLSPPieidesrrssssaakgkkagvwdskdiADFDPE 414
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
3MZS_D      400 RWLSKDK-------DLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:cd20622 415 RWLVTDEetgetvfDPSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELL 469
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
270-474 3.45e-20

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 92.99  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       270 EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNARRQAEGDISKMlqmvPLLKASIKET 345
Cdd:PLN00110 283 EKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEmdqvIGRNRRLVESDLPKL----PYLQAICKES 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       346 LRLHP-ISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-----FRNLGFGWG 419
Cdd:PLN00110 359 FRKHPsTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDprgndFELIPFGAG 438
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
3MZS_D       420 VRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDV--DTIFNLILTPDKPIFLVFRP 474
Cdd:PLN00110 439 RRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELnmDEAFGLALQKAVPLSAMVTP 495
PLN02655 PLN02655
ent-kaurene oxidase
225-425 5.01e-20

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 92.50  E-value: 5.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       225 WRDHVAAWDTIFNKAEKyTEIFYQDLRRKT---------EFRNYPG---ILYC--LLKSEKMLLED-VKANITEMLAGGV 289
Cdd:PLN02655 197 WRDFFPYLSWIPNKSFE-TRVQTTEFRRTAvmkalikqqKKRIARGeerDCYLdfLLSEATHLTDEqLMMLVWEPIIEAA 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       290 NTTSMTLQWHLYEMARSLNVQEMLREEVLNA---RRQAEGDISKMlqmvPLLKASIKETLRLH-PISVTLQRYPESDLVL 365
Cdd:PLN02655 276 DTTLVTTEWAMYELAKNPDKQERLYREIREVcgdERVTEEDLPNL----PYLNAVFHETLRKYsPVPLLPPRFVHEDTTL 351
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
3MZS_D       366 QDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRNLGFGWGVRQCVG 425
Cdd:PLN02655 352 GGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADmYKTMAFGAGKRVCAG 412
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
277-455 7.09e-20

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


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 91.91  E-value: 7.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      277 VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNARRQAEGDISKMlqmvPLLKASIKETLRLHPIS 352
Cdd:cd20654 242 IKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEEldthVGKDRWVEESDIKNL----VYLQAIVKETLRLYPPG 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      353 VTL-QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLS--KDKDLI--HFRNLGFGWGVRQCVGRR 427
Cdd:cd20654 318 PLLgPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTthKDIDVRgqNFELIPFGSGRRSCPGVS 397
                       170       180
                ....*....|....*....|....*...
3MZS_D      428 IAELEMTLFLIHILENFKVEMQHIGDVD 455
Cdd:cd20654 398 FGLQVMHLTLARLLHGFDIKTPSNEPVD 425
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
270-458 1.22e-19

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: 90.78  E-value: 1.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      270 EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISK----MLQMVPLLKASI 342
Cdd:cd11051 179 KRFELERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEhdeVFGPDPSAAAELLRegpeLLNQLPYTTAVI 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      343 KETLRLHPISVTLqRYPESDLVLQD----YLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLG--- 415
Cdd:cd11051 259 KETLRLFPPAGTA-RRGPPGVGLTDrdgkEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYPPKSAwrp 337
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
3MZS_D      416 FGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIgDVDTIF 458
Cdd:cd11051 338 FERGPRNCIGQELAMLELKIILAMTVRRFDFEKAYD-EWDAKG 379
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
47-423 8.50e-19

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 88.98  E-value: 8.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        47 YGPIYREKLGNLESVYIIHPEDVAHLFKFEGSypeRYDIPPWLAYHR---YYQKPIGvLFKKSGTWKKDRVVLNTEVMAP 123
Cdd:PLN03234  61 YGPIFTMKIGGRRLAVISSAELAKELLKTQDL---NFTARPLLKGQQtmsYQGRELG-FGQYTAYYREMRKMCMVNLFSP 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       124 EAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGkfvgDIKEDLFHFAFESITNVMFGERLgmleETVNPEAQKFIDAVYKMF 203
Cdd:PLN03234 137 NRVASFRPVREEECQRMMDKIYKAADQSGTV----DLSELLLSFTNCVVCRQAFGKRY----NEYGTEMKRFIDILYETQ 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       204 HTSVPLLnvppeLYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDL--------RRKTEFRNYPGILYCLLKSE----K 271
Cdd:PLN03234 209 ALLGTLF-----FSDLFPYFGFLDNLTGLSARLKKAFKELDTYLQELldetldpnRPKQETESFIDLLMQIYKDQpfsiK 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       272 MLLEDVKANITEMLAGGVNTTSMTLQW---HLYEMARSLN-VQEMLREEVLNARRQAEGDISKMlqmvPLLKASIKETLR 347
Cdd:PLN03234 284 FTHENVKAMILDIVVPGTDTAAAVVVWamtYLIKYPEAMKkAQDEVRNVIGDKGYVSEEDIPNL----PYLKAVIKESLR 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       348 LHP-ISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRWLSKDKDL----IHFRNLGFGWGVR 421
Cdd:PLN03234 360 LEPvIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMKEHKGVdfkgQDFELLPFGSGRR 439

                 ..
3MZS_D       422 QC 423
Cdd:PLN03234 440 MC 441
PLN00168 PLN00168
Cytochrome P450; Provisional
13-445 2.03e-18

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 87.70  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        13 IPSPGDNGWLNLYHFWREKGSQRIHFRhienfqkYGPIYREKLGNLESVYIIhPEDVAHLFKFEGSypERYDIPPWLAYH 92
Cdd:PLN00168  43 VPLLGSLVWLTNSSADVEPLLRRLIAR-------YGPVVSLRVGSRLSVFVA-DRRLAHAALVERG--AALADRPAVASS 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        93 RYYQKPIGVLFKKS--GTWKKDRVVLNTEVMAPEAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVgdikeDLFHFA-F 169
Cdd:PLN00168 113 RLLGESDNTITRSSygPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVV-----ETFQYAmF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       170 ESITNVMFGERLGmlEETVNPEAQKFIDAVYKMFHTSVPLLNVPPELYRLFRTKTwrdhvaawDTIFNKAEKYTEIFYQD 249
Cdd:PLN00168 188 CLLVLMCFGERLD--EPAVRAIAAAQRDWLLYVSKKMSVFAFFPAVTKHLFRGRL--------QKALALRRRQKELFVPL 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       250 LRRKTEFRNYPGILYCLLKSEKML-------LEDVKAN---------------ITEMLAGGVNTTSMTLQWHLYEMARSL 307
Cdd:PLN00168 258 IDARREYKNHLGQGGEPPKKETTFehsyvdtLLDIRLPedgdraltddeivnlCSEFLNAGTDTTSTALQWIMAELVKNP 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       308 NVQEMLREEVLNA-----RRQAEGDISKMlqmvPLLKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIY 381
Cdd:PLN00168 338 SIQSKLHDEIKAKtgddqEEVSEEDVHKM----PYLKAVVLEGLRKHPPAhFVLPHKAAEDMEVGGYLIPKGATVNFMVA 413
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3MZS_D       382 AMGRDPAFFSSPDKFDPTRWLS----KDKDLI---HFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFK 445
Cdd:PLN00168 414 EMGRDEREWERPMEFVPERFLAggdgEGVDVTgsrEIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFE 484
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
269-466 6.43e-18

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: 85.84  E-value: 6.43e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      269 SEKMLLedvkANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEV-----------LNARRQaegdiskmlqmVPL 337
Cdd:cd20673 229 SDDHIL----MTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIdqnigfsrtptLSDRNH-----------LPL 293
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      338 LKASIKETLRLHPISVTLqrYPE---SDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRN- 413
Cdd:cd20673 294 LEATIREVLRIRPVAPLL--IPHvalQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQLISPSl 371
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
3MZS_D      414 --LGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM---QHIGDVDTIFNLILTPDK 466
Cdd:cd20673 372 syLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVpdgGQLPSLEGKFGVVLQIDP 429
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
159-475 6.58e-18

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: 85.54  E-value: 6.58e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      159 DIKEDLFHFAFESITNVMFGErlgmlEETVNPEAQKFIDAVYKMFHT----------SVPLLNVPPE--LYRLFRTKTWR 226
Cdd:cd20674 105 DIQEEFSLLTCSIICCLTFGD-----KEDKDTLVQAFHDCVQELLKTwghwsiqaldSIPFLRFFPNpgLRRLKQAVENR 179
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      227 DHVAawdtifnkaEKYTEiFYQDLRRKTEFRNYpgILYCLL--------KSEKMLLED-VKANITEMLAGGVNTTSMTLQ 297
Cdd:cd20674 180 DHIV---------ESQLR-QHKESLVAGQWRDM--TDYMLQglgqprgeKGMGQLLEGhVHMAVVDLFIGGTETTASTLS 247
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      298 WHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPA 372
Cdd:cd20674 248 WAVAFLLHHPEIQDRLQEEldrVLGPGASPSyKDRARL----PLLNATIAEVLRLRPVVpLALPHRTTRDSSIAGYDIPK 323
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      373 KTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDliHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIG 452
Cdd:cd20674 324 GTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAA--NRALLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDG 401
                       330       340
                ....*....|....*....|...
3MZS_D      453 DVDTifnliLTPDKPIFLVFRPF 475
Cdd:cd20674 402 ALPS-----LQPVAGINLKVQPF 419
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
275-446 7.67e-18

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: 85.51  E-value: 7.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      275 EDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEV---LNARRQAEGDISKMLQMvPLLKASIKETLRLHPI 351
Cdd:cd20679 243 EDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVqelLKDREPEEIEWDDLAQL-PFLTMCIKESLRLHPP 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      352 SVTLQRYPESDLVLQD-YLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRW---LSKDKDLIHFrnLGFGWGVRQCVGRR 427
Cdd:cd20679 322 VTAISRCCTQDIVLPDgRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFdpeNSQGRSPLAF--IPFSAGPRNCIGQT 399
                       170
                ....*....|....*....
3MZS_D      428 IAELEMTLFLIHILENFKV 446
Cdd:cd20679 400 FAMAEMKVVLALTLLRFRV 418
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
109-437 1.30e-17

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: 84.58  E-value: 1.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      109 WKKDRVVLNTEVMAPEAIKNFIPllnpVSQDFVSLLHKRIKQQGSGKFVG-DIKEDLFHFAFESITNVMFGERLGMLEET 187
Cdd:cd20653  61 WRNLRRITTLEIFSSHRLNSFSS----IRRDEIRRLLKRLARDSKGGFAKvELKPLFSELTFNNIMRMVAGKRYYGEDVS 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      188 VNPEAQKFIDAVYKMFHTS--------VPLLnvppelyRLFRTKTWRDHVAawdtifNKAEKYTEiFYQDL---RRKTEF 256
Cdd:cd20653 137 DAEEAKLFRELVSEIFELSgagnpadfLPIL-------RWFDFQGLEKRVK------KLAKRRDA-FLQGLideHRKNKE 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      257 RNYPGILYCLLKsekmLLED---------VKANITEMLAGGVNTTSMTLQWhlyEMARSLN---VQEMLREE----VLNA 320
Cdd:cd20653 203 SGKNTMIDHLLS----LQESqpeyytdeiIKGLILVMLLAGTDTSAVTLEW---AMSNLLNhpeVLKKAREEidtqVGQD 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      321 RRQAEGDISKMlqmvPLLKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPT 399
Cdd:cd20653 276 RLIEESDLPKL----PYLQNIISETLRLYPAApLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPE 351
                       330       340       350
                ....*....|....*....|....*....|....*...
3MZS_D      400 RWLSKDKDLihFRNLGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd20653 352 RFEGEEREG--YKLIPFGLGRRACPGAGLAQRVVGLAL 387
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
279-444 1.36e-17

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: 84.53  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      279 ANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLKASIKETLRLH---PI 351
Cdd:cd11026 229 MTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEidrVIGRNRTPSlEDRAKM----PYTDAVIHEVQRFGdivPL 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      352 SVTlqRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKdliHFRN----LGFGWGVRQCVGRR 427
Cdd:cd11026 305 GVP--HAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQG---KFKKneafMPFSAGKRVCLGEG 379
                       170
                ....*....|....*..
3MZS_D      428 IAELEMTLFLIHILENF 444
Cdd:cd11026 380 LARMELFLFFTSLLQRF 396
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
281-444 1.93e-17

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: 84.44  E-value: 1.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      281 ITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLKASIKETLRLHPI-SVTL 355
Cdd:cd20666 233 IGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEidtVIGPDRAPSlTDKAQM----PFTEATIMEVQRMTVVvPLSI 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      356 QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNL-GFGWGVRQCVGRRIAELEMT 434
Cdd:cd20666 309 PHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFiPFGIGRRVCMGEQLAKMELF 388
                       170
                ....*....|
3MZS_D      435 LFLIHILENF 444
Cdd:cd20666 389 LMFVSLMQSF 398
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
288-445 2.71e-17

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


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 83.93  E-value: 2.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      288 GVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA--RRQAEGD-ISKM--LQMVpllkasIKETLRLHPISVTLQRYPESD 362
Cdd:cd11052 244 GHETTALLLTWTTMLLAIHPEWQEKAREEVLEVcgKDKPPSDsLSKLktVSMV------INESLRLYPPAVFLTRKAKED 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      363 LVLQDYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRW---LSK-DKDLIHFrnLGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd11052 318 IKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFadgVAKaAKHPMAF--LPFGLGPRNCIGQNFATMEAKIVL 395

                ....*...
3MZS_D      438 IHILENFK 445
Cdd:cd11052 396 AMILQRFS 403
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
287-445 8.57e-17

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: 82.50  E-value: 8.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      287 GGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQ 366
Cdd:cd20641 246 AGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLG 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      367 DYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRwlskdkdlihFRN------------LGFGWGVRQCVGRRIAELEM 433
Cdd:cd20641 326 GLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLR----------FANgvsraathpnalLSFSLGPRACIGQNFAMIEA 395
                       170
                ....*....|..
3MZS_D      434 TLFLIHILENFK 445
Cdd:cd20641 396 KTVLAMILQRFS 407
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
38-444 8.87e-17

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: 82.07  E-value: 8.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       38 FRHIENFQK-YGPIYREKLGNLESVYIIHPE---DVAHLFKFEGSYPerydippwlAYHRYYQKPI--GVLFKKSG-TWK 110
Cdd:cd20640   1 FPYFDKWRKqYGPIFTYSTGNKQFLYVSRPEmvkEINLCVSLDLGKP---------SYLKKTLKPLfgGGILTSNGpHWA 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      111 KDRVVLNTEVMaPEAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGkfVGDIK--EDLFHFAFESITNVMFGERLGMLEETV 188
Cdd:cd20640  72 HQRKIIAPEFF-LDKVKGMVDLMVDSAQPLLSSWEERIDRAGGM--AADIVvdEDLRAFSADVISRACFGSSYSKGKEIF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      189 NP--EAQKFIDavykmfHTSVpLLNVPpeLYRLFRTKT----WRDHVAAWDTIFNKAEKYTEifYQDLRRKtefrnypgI 262
Cdd:cd20640 149 SKlrELQKAVS------KQSV-LFSIP--GLRHLPTKSnrkiWELEGEIRSLILEIVKEREE--ECDHEKD--------L 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      263 LYCLLKS------EKMLLED-VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDiSKMLQMV 335
Cdd:cd20640 210 LQAILEGarsscdKKAEAEDfIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPD-ADSLSRM 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      336 PLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRW---LSKDKDLIHF 411
Cdd:cd20640 289 KTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFsngVAAACKPPHS 368
                       410       420       430
                ....*....|....*....|....*....|...
3MZS_D      412 RnLGFGWGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd20640 369 Y-MPFGAGARTCLGQNFAMAELKVLVSLILSKF 400
PLN02687 PLN02687
flavonoid 3'-monooxygenase
276-442 2.52e-16

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 81.40  E-value: 2.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       276 DVKANITEMLAGGVNTTSMTLQWHLYEMARSLNV----QEMLREEVLNARRQAEGDISKMlqmvPLLKASIKETLRLHPI 351
Cdd:PLN02687 297 EIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDIlkkaQEELDAVVGRDRLVSESDLPQL----TYLQAVIKETFRLHPS 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       352 S-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLS---------KDKDlihFRNLGFGWGVR 421
Cdd:PLN02687 373 TpLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPggehagvdvKGSD---FELIPFGAGRR 449
                        170       180
                 ....*....|....*....|....*
3MZS_D       422 QCVGR----RIAELeMTLFLIHILE 442
Cdd:PLN02687 450 ICAGLswglRMVTL-LTATLVHAFD 473
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
268-467 2.82e-16

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: 80.91  E-value: 2.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEV---LNARRQAEGDISKMLqmvPLLKASIKE 344
Cdd:cd20677 228 KSAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIdekIGLSRLPRFEDRKSL---HYTEAFINE 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      345 TLRlHPISV--TLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSK----DKDLIHfRNLGFGW 418
Cdd:cd20677 305 VFR-HSSFVpfTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDEngqlNKSLVE-KVLIFGM 382
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
3MZS_D      419 GVRQCVGRRIAELEMTLFLIHILENFKVE--MQHIGDVDTIFNLILTPdKP 467
Cdd:cd20677 383 GVRKCLGEDVARNEIFVFLTTILQQLKLEkpPGQKLDLTPVYGLTMKP-KP 432
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
2-449 9.34e-16

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 79.21  E-value: 9.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D         2 ASTKTPRPyseipsPGDNGW------LNLYhfwrekgSQRIHFRHIENFQKYGPIYREKLGNLESVYIIHPEDV------ 69
Cdd:PLN02196  30 SSTKLPLP------PGTMGWpyvgetFQLY-------SQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAkfvlvt 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        70 -AHLFKfegsyperydiPPWLAYHRYYQKPIGVLFKKSGTWKKDRVVLNTEVMaPEAIKNFIPLLNPVSQDFVsllhkri 148
Cdd:PLN02196  97 kSHLFK-----------PTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFM-PDAIRNMVPDIESIAQESL------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       149 kQQGSGKFVG---DIKEDLFHFAFESItnvmFGErlgmlEETVNPEAQKFIDAVYKMFHTSVPLlNVPpelyrlfrtktw 225
Cdd:PLN02196 158 -NSWEGTQINtyqEMKTYTFNVALLSI----FGK-----DEVLYREDLKRCYYILEKGYNSMPI-NLP------------ 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       226 rdhvaawDTIFNKAEKYTEIFYQDLRRK-TEFRNYPGILYCLLKS-----EKMLLEDVKANITEMLAGGVNTTSMTLQWH 299
Cdd:PLN02196 215 -------GTLFHKSMKARKELAQILAKIlSKRRQNGSSHNDLLGSfmgdkEGLTDEQIADNIIGVIFAARDTTASVLTWI 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       300 LYEMARSLNVQEMLREEVLNARRQAE-------GDISKMlqmvPLLKASIKETLRLHPI-SVTLQRYPEsDLVLQDYLIP 371
Cdd:PLN02196 288 LKYLAENPSVLEAVTEEQMAIRKDKEegesltwEDTKKM----PLTSRVIQETLRVASIlSFTFREAVE-DVEYEGYLIP 362
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
3MZS_D       372 AKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHfrnLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQ 449
Cdd:PLN02196 363 KGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNTF---MPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIV 437
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
275-467 1.06e-15

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: 78.94  E-value: 1.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      275 EDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQE-MLRE--EVLNARRQAEGDISKMLqmvpLLKASIKETLRLHPI 351
Cdd:cd20616 223 ENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEaILKEiqTVLGERDIQNDDLQKLK----VLENFINESMRYQPV 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      352 SVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPaFFSSPDKFDPTrwlskdkdliHFRN-------LGFGWGVRQCV 424
Cdd:cd20616 299 VDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLE----------NFEKnvpsryfQPFGFGPRSCV 367
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
3MZS_D      425 GRRIAELEMTLFLIHILENFKVEMQHIGDVDTI---FNLILTPDKP 467
Cdd:cd20616 368 GKYIAMVMMKAILVTLLRRFQVCTLQGRCVENIqktNDLSLHPDET 413
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
270-444 1.46e-15

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: 78.65  E-value: 1.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      270 EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLH 349
Cdd:cd20639 226 EKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLY 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      350 PISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFsSPD--KFDPTRWlSKDKDLIHFRNLG---FGWGVRQCV 424
Cdd:cd20639 306 PPAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELW-GNDaaEFNPARF-ADGVARAAKHPLAfipFGLGPRTCV 383
                       170       180
                ....*....|....*....|
3MZS_D      425 GRRIAELEMTLFLIHILENF 444
Cdd:cd20639 384 GQNLAILEAKLTLAVILQRF 403
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
274-439 1.73e-15

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  Cd Length: 434  Bit Score: 78.12  E-value: 1.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      274 LEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA----RRQAEGDISKMlqmvPLLKASIKETLRLH 349
Cdd:cd20675 233 KEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVvgrdRLPCIEDQPNL----PYVMAFLYEAMRFS 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      350 P-ISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSK----DKDLIhFRNLGFGWGVRQCV 424
Cdd:cd20675 309 SfVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDEngflNKDLA-SSVMIFSVGKRRCI 387
                       170
                ....*....|....*...
3MZS_D      425 GRRIAELEMTLF---LIH 439
Cdd:cd20675 388 GEELSKMQLFLFtsiLAH 405
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
271-470 2.48e-15

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: 77.88  E-value: 2.48e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      271 KMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVL----NARRQAEGDISKMLQMvplLKASIKETL 346
Cdd:cd20680 238 KLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDevfgKSDRPVTMEDLKKLRY---LECVIKESL 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      347 RLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRNLGFGWGVRQCVG 425
Cdd:cd20680 315 RLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHpYAYIPFSAGPRNCIG 394
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
3MZS_D      426 RRIAELEMTLFLIHILENFKVEM-QHIGDVDTIFNLILTPDKPIFL 470
Cdd:cd20680 395 QRFALMEEKVVLSCILRHFWVEAnQKREELGLVGELILRPQNGIWI 440
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
291-437 2.82e-15

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: 77.67  E-value: 2.82e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      291 TTSMTlqWHLYEMARSLNVQEMLREEVLNARRQAEGDIS-KMLQMVPLLKASIKETLRLHPISVTLQRYPESDLVL-QDY 368
Cdd:cd11082 237 TSSLV--WALQLLADHPDVLAKVREEQARLRPNDEPPLTlDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLtEDY 314
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3MZS_D      369 LIPAKTLVQVAIYAMGRDPafFSSPDKFDPTRWLSKDK-DLIHFRN-LGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd11082 315 TVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQeDRKYKKNfLVFGAGPHQCVGQEYAINHLMLFL 383
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
275-446 3.39e-15

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 77.32  E-value: 3.39e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      275 EDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlnarRQAEGDISKM----LQMVPLLKASIKETLRLHP 350
Cdd:cd20678 238 EDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEI----REILGDGDSItwehLDQMPYTTMCIKEALRLYP 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      351 ISVTLQRYPESDLVLQD-YLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH-FRNLGFGWGVRQCVGRRI 428
Cdd:cd20678 314 PVPGISRELSKPVTFPDgRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHsHAFLPFSAGPRNCIGQQF 393
                       170
                ....*....|....*...
3MZS_D      429 AELEMTLFLIHILENFKV 446
Cdd:cd20678 394 AMNEMKVAVALTLLRFEL 411
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
284-467 3.78e-15

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: 76.57  E-value: 3.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLqwhlyemarsLNVQEML--REEVLNARRQAEGdiskmlqmvpLLKASIKETLRLHPISVTLQRYPES 361
Cdd:cd20629 200 LLPAGSDTTYRAL----------ANLLTLLlqHPEQLERVRRDRS----------LIPAAIEEGLRWEPPVASVPRMALR 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      362 DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlskdKDLIHFrnlGFGWGVRQCVGRRIAELEMTLFLIHIL 441
Cdd:cd20629 260 DVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR-----KPKPHL---VFGGGAHRCLGEHLARVELREALNALL 331
                       170       180
                ....*....|....*....|....*.
3MZS_D      442 ENFKvemqhigdvdtifNLILTPDKP 467
Cdd:cd20629 332 DRLP-------------NLRLDPDAP 344
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
289-444 5.19e-15

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221  Cd Length: 503  Bit Score: 77.08  E-value: 5.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       289 VNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQ-AEGDISKMlqmvPLLKASIKETLRLH-PISVTLQRYPESDL 363
Cdd:PLN02394 306 IETTLWSIEWGIAELVNHPEIQKKLRDEldtVLGPGNQvTEPDTHKL----PYLQAVVKETLRLHmAIPLLVPHMNLEDA 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       364 VLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDL----IHFRNLGFGWGVRQCVGRRIAELEMTLFLIH 439
Cdd:PLN02394 382 KLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKVeangNDFRFLPFGVGRRSCPGIILALPILGIVLGR 461

                 ....*
3MZS_D       440 ILENF 444
Cdd:PLN02394 462 LVQNF 466
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
337-436 5.20e-15

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: 76.42  E-value: 5.20e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLH-PISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlsKDKdlihfRNLG 415
Cdd:cd11029 254 LWPAAVEELLRYDgPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR---DAN-----GHLA 325
                        90       100
                ....*....|....*....|....*.
3MZS_D      416 FGWGVRQCVGRRIAELEM-----TLF 436
Cdd:cd11029 326 FGHGIHYCLGAPLARLEAeialgALL 351
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
268-448 1.39e-14

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: 75.39  E-value: 1.39e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVL----NARRQAEGdISKmLQMVPLLkasIK 343
Cdd:cd20642 226 KNGGMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLqvfgNNKPDFEG-LNH-LKVVTMI---LY 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      344 ETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDK-FDPTRW---LSK-DKDLIHFrnLGFGW 418
Cdd:cd20642 301 EVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWGDDAKeFNPERFaegISKaTKGQVSY--FPFGW 378
                       170       180       190
                ....*....|....*....|....*....|
3MZS_D      419 GVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:cd20642 379 GPRICIGQNFALLEAKMALALILQRFSFEL 408
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
308-448 1.96e-14

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 75.04  E-value: 1.96e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      308 NVQEMLREEVLNARRQ----AEGDISKMlqmvPLLKASIKETLRLHPISVtLQRYPESDLVLQDYLIPAKTLVQVAIYAM 383
Cdd:cd20635 246 KVMEEISSVLGKAGKDkikiSEDDLKKM----PYIKRCVLEAIRLRSPGA-ITRKVVKPIKIKNYTIPAGDMLMLSPYWA 320
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3MZS_D      384 GRDPAFFSSPDKFDPTRWLSKDKDlihfRNL------GFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:cd20635 321 HRNPKYFPDPELFKPERWKKADLE----KNVflegfvAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTL 387
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
284-437 9.31e-14

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: 72.60  E-value: 9.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLqwhlyemarSLNVQEMLREEVLNARRQAEGDiskmlqmvpLLKASIKETLRLHPIS--VTLQRYPES 361
Cdd:cd11031 214 LLVAGHETTASQI---------GNGVLLLLRHPEQLARLRADPE---------LVPAAVEELLRYIPLGagGGFPRYATE 275
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
3MZS_D      362 DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlskdKDLIHfrnLGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd11031 276 DVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR-----EPNPH---LAFGHGPHHCLGAPLARLELQVAL 343
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
47-445 1.67e-13

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: 72.15  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       47 YGPIYREKLGNLESVYIIHPEDVAH-LFKFEGSYPERYDIPPWLAYHRYYqkpiGVLFKKSGTWKKDRVVLNTEV----M 121
Cdd:cd20664   1 YGSIFTVQMGTKKVVVLAGYKTVKEaLVNHAEAFGGRPIIPIFEDFNKGY----GILFSNGENWKEMRRFTLTTLrdfgM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      122 APEAIKNFIpllnpvSQDFVSLLhKRIKQQGSGKFvgdikeDLFHFAFESITNVMFGERLGMLEETVNPEAQKFIDAVYK 201
Cdd:cd20664  77 GKKTSEDKI------LEEIPYLI-EVFEKHKGKPF------ETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      202 MFH----TSVPLLNVPPELyRLFRtktwRDHVAAWDTIFNKAEKYTEIFYQDLRRKTEFrNYPGILYCLL-------KSE 270
Cdd:cd20664 144 NMKltgsPSVQLYNMFPWL-GPFP----GDINKLLRNTKELNDFLMETFMKHLDVLEPN-DQRGFIDAFLvkqqeeeESS 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      271 KMLLEDvkANITEMLA----GGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMlqmvPLLKASIK 343
Cdd:cd20664 218 DSFFHD--DNLTCSVGnlfgAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEidrVIGSRQPQVEHRKNM----PYTDAVIH 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      344 ETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIH---FrnLGFGWG 419
Cdd:cd20664 292 EIQRFANIVpMNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKrdaF--MPFSAG 369
                       410       420
                ....*....|....*....|....*.
3MZS_D      420 VRQCVGRRIAELEMTLFLIHILENFK 445
Cdd:cd20664 370 RRVCIGETLAKMELFLFFTSLLQRFR 395
PLN02936 PLN02936
epsilon-ring hydroxylase
260-448 2.07e-13

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 72.13  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       260 PGILYCLLKS-EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMlqmv 335
Cdd:PLN02936 261 PSVLRFLLASrEEVSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEEldrVLQGRPPTYEDIKEL---- 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       336 PLLKASIKETLRLHP-ISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRW---------LSKD 405
Cdd:PLN02936 337 KYLTRCINESMRLYPhPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdldgpvpneTNTD 416
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
3MZS_D       406 kdlihFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:PLN02936 417 -----FRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLEL 454
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
281-464 2.73e-13

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: 71.41  E-value: 2.73e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      281 ITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMLqmvPLLKASIKETLRLHPI-SVTLQ 356
Cdd:cd20667 230 VIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQEldeVLGASQLICYEDRKRL---PYTNAVIHEVQRLSNVvSVGAV 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      357 RYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDlihFRN----LGFGWGVRQCVGRRIAELE 432
Cdd:cd20667 307 RQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGN---FVMneafLPFSAGHRVCLGEQLARME 383
                       170       180       190
                ....*....|....*....|....*....|....*
3MZS_D      433 MTLFLIHILENFKVEM-QHIGDVDT--IFNLILTP 464
Cdd:cd20667 384 LFIFFTTLLRTFNFQLpEGVQELNLeyVFGGTLQP 418
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
208-441 2.99e-13

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: 70.83  E-value: 2.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      208 PLLNVPPELYRLFRTKTWRDH--------VAAWDTIFNKAEKYTEifyqdlRRKTEFRNypGILYCLLKSE----KMLLE 275
Cdd:cd11034 118 RLLGLPDEDGERLRDWVHAILhdedpeegAAAFAELFGHLRDLIA------ERRANPRD--DLISRLIEGEidgkPLSDG 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      276 DVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLnarrqaegdiskmlqmvpLLKASIKETLRLHPISVTL 355
Cdd:cd11034 190 EVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLIADPS------------------LIPNAVEEFLRFYSPVAGL 251
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      356 QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdkdlihfRNLGFGWGVRQCVGRRIAELEMTL 435
Cdd:cd11034 252 ARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTPN--------RHLAFGSGVHRCLGSHLARVEARV 323

                ....*.
3MZS_D      436 FLIHIL 441
Cdd:cd11034 324 ALTEVL 329
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
274-456 3.17e-13

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: 71.14  E-value: 3.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      274 LEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA----RRQAEGDISKMlqmvPLLKASIKETLR-- 347
Cdd:cd20665 224 LENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVigrhRSPCMQDRSHM----PYTDAVIHEIQRyi 299
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      348 -LHPISVtlqryPES---DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKD---KDLIHFrnLGFGWGV 420
Cdd:cd20665 300 dLVPNNL-----PHAvtcDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENgnfKKSDYF--MPFSAGK 372
                       170       180       190
                ....*....|....*....|....*....|....*..
3MZS_D      421 RQCVGRRIAELEMTLFLIHILENFKVE-MQHIGDVDT 456
Cdd:cd20665 373 RICAGEGLARMELFLFLTTILQNFNLKsLVDPKDIDT 409
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
270-433 3.74e-13

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


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 70.58  E-value: 3.74e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      270 EKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSlnvqemlrEEVLNARRQaegDISkmlqmvpLLKASIKETLRLH 349
Cdd:cd11080 187 EALSDEDIKALILNVLLAATEPADKTLALMIYHLLNN--------PEQLAAVRA---DRS-------LVPRAIAETLRYH 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      350 PISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlskdKDLI---HF----RNLGFGWGVRQ 422
Cdd:cd11080 249 PPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHR-----EDLGirsAFsgaaDHLAFGSGRHF 323
                       170
                ....*....|.
3MZS_D      423 CVGRRIAELEM 433
Cdd:cd11080 324 CVGAALAKREI 334
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
121-445 5.22e-13

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 70.75  E-value: 5.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      121 MAPEAIKNFIPLLNPVSQDFVSLLHKRIkqQGSGKFvgDIKEDLFHFAFESITNVMFGERL-GMLEETVNPE-AQKFIDA 198
Cdd:cd11071  89 LLKSRSSRFIPEFRSALSELFDKWEAEL--AKKGKA--SFNDDLEKLAFDFLFRLLFGADPsETKLGSDGPDaLDKWLAL 164
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      199 VYKMFHTSVPLLNVPPELYRLFRTKTwrdhvaawdtiFNKAEKYTEIFyqdlrrkTEFRNYPgiLYCLLKSEKMLL--ED 276
Cdd:cd11071 165 QLAPTLSLGLPKILEELLLHTFPLPF-----------FLVKPDYQKLY-------KFFANAG--LEVLDEAEKLGLsrEE 224
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      277 VKANITEMLA----GGVNTTSMTLQWHLYEMarSLNVQEMLREEVLNARRQAEGDISKMLQMVPLLKASIKETLRLHPiS 352
Cdd:cd11071 225 AVHNLLFMLGfnafGGFSALLPSLLARLGLA--GEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHP-P 301
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      353 VTLQ-RYPESDLVLQD----YLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIhfRNLGFGWGV------- 420
Cdd:cd11071 302 VPLQyGRARKDFVIEShdasYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGEEGKLL--KHLIWSNGPeteeptp 379
                       330       340
                ....*....|....*....|....*..
3MZS_D      421 --RQCVGRRIAELEMTLFLIHILENFK 445
Cdd:cd11071 380 dnKQCPGKDLVVLLARLFVAELFLRYD 406
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
274-450 6.02e-13

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: 70.61  E-value: 6.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      274 LEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLKASIKETLRLH 349
Cdd:cd20661 236 MENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEidlVVGPNGMPSfEDKCKM----PYTEAVLHEVLRFC 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      350 PIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI-HFRNLGFGWGVRQCVGRR 427
Cdd:cd20661 312 NIVpLGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAkKEAFVPFSLGRRHCLGEQ 391
                       170       180
                ....*....|....*....|...
3MZS_D      428 IAELEMTLFLIHILENFKVEMQH 450
Cdd:cd20661 392 LARMEMFLFFTALLQRFHLHFPH 414
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
209-452 7.22e-13

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: 69.94  E-value: 7.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      209 LLNVPPELYRLFRTktWRDHVAAWDTIFNKAEKYTEI---------FYQDL---RRKTEFRNYPGiLYCLLKS---EKML 273
Cdd:cd11078 130 LLGVPEEDMERFRR--WADAFALVTWGRPSEEEQVEAaaavgelwaYFADLvaeRRREPRDDLIS-DLLAAADgdgERLT 206
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      274 LEDVKANITEMLAGGVNTTSMTLQWHLYEMARslnvQEMLREEVLNARRqaegdiskmlqmvpLLKASIKETLRLHPISV 353
Cdd:cd11078 207 DEELVAFLFLLLVAGHETTTNLLGNAVKLLLE----HPDQWRRLRADPS--------------LIPNAVEETLRYDSPVQ 268
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      354 TLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlSKDKdlihfRNLGFGWGVRQCVGRRIAELEM 433
Cdd:cd11078 269 GLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR--PNAR-----KHLTFGHGIHFCLGAALARMEA 341
                       250       260
                ....*....|....*....|..
3MZS_D      434 TLFLIHIL---ENFKVEMQHIG 452
Cdd:cd11078 342 RIALEELLrrlPGMRVPGQEVV 363
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
289-446 7.50e-13

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: 70.19  E-value: 7.50e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      289 VNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQ-AEGDISKMlqmvPLLKASIKETLRLH-PISVTLQRYPESDL 363
Cdd:cd11074 246 IETTLWSIEWGIAELVNHPEIQKKLRDEldtVLGPGVQiTEPDLHKL----PYLQAVVKETLRLRmAIPLLVPHMNLHDA 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      364 VLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDL----IHFRNLGFGWGVRQCVGRRIAELEMTLFLIH 439
Cdd:cd11074 322 KLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVeangNDFRYLPFGVGRRSCPGIILALPILGITIGR 401

                ....*..
3MZS_D      440 ILENFKV 446
Cdd:cd11074 402 LVQNFEL 408
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
268-445 1.27e-12

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: 69.44  E-value: 1.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      268 KSEKMLLED-VKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAEGDISKMLqmvPLLKASIK 343
Cdd:cd20671 214 PKETLFHDAnVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEidrVLGPGCLPNYEDRKAL---PYTSAVIH 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      344 ETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRN-LGFGWGVRQ 422
Cdd:cd20671 291 EVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAfLPFSAGRRV 370
                       170       180
                ....*....|....*....|...
3MZS_D      423 CVGRRIAELEMTLFLIHILENFK 445
Cdd:cd20671 371 CVGESLARTELFIFFTGLLQKFT 393
PLN02500 PLN02500
cytochrome P450 90B1
234-448 1.28e-12

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 69.51  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       234 TIFNKAEKYTEIFYQDLRRKTEFRNYPGILYCLLKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEML 313
Cdd:PLN02500 237 TILKFIERKMEERIEKLKEEDESVEEDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQEL 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       314 REEVLN-ARRQAEGDISKM----LQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPA 388
Cdd:PLN02500 317 REEHLEiARAKKQSGESELnwedYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSS 396
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       389 FFSSPDKFDPTRWL----------SKDKDLIHFrnLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:PLN02500 397 LYDQPQLFNPWRWQqnnnrggssgSSSATTNNF--MPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWEL 464
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
34-443 1.29e-12

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: 69.46  E-value: 1.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       34 QRIHFRHIENfQKYGPIYREKLGNLESVYIIHPEDVAHLFKFEgsypERYDIPPWLAYHRYYQKPiGVLFKKSGTWKKDR 113
Cdd:cd20638   9 QRRKFLQMKR-QKYGYIYKTHLFGRPTVRVMGAENVRQILLGE----HKLVSVQWPASVRTILGS-GCLSNLHDSQHKHR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      114 VVLNTEVMAPEAIKNFIPllnpVSQDFVSLLHKRIKQQGSGKFV-GDIKEDLFHFAFESItnvmfgerLGMLEETVNPEA 192
Cdd:cd20638  83 KKVIMRAFSREALENYVP----VIQEEVRSSVNQWLQSGPCVLVyPEVKRLMFRIAMRIL--------LGFEPQQTDREQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      193 -QKFIDAVYKMFHT--SVPLlNVP-PELYRLFRtktwrdhvaAWDTIFNKAEKYTEIFYQDLRRKTEFRNYPGIL--YCL 266
Cdd:cd20638 151 eQQLVEAFEEMIRNlfSLPI-DVPfSGLYRGLR---------ARNLIHAKIEENIRAKIQREDTEQQCKDALQLLieHSR 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      267 LKSEKMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEV-----LNARRQAEGDIS-KMLQMVPLLKA 340
Cdd:cd20638 221 RNGEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELqekglLSTKPNENKELSmEVLEQLKYTGC 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      341 SIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKD-KDLIHFRNLGFGWG 419
Cdd:cd20638 301 VIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLpEDSSRFSFIPFGGG 380
                       410       420
                ....*....|....*....|....
3MZS_D      420 VRQCVGRRIAELEMTLFLIHILEN 443
Cdd:cd20638 381 SRSCVGKEFAKVLLKIFTVELARH 404
PLN02302 PLN02302
ent-kaurenoic acid oxidase
327-447 1.55e-12

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 69.36  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       327 DISKMlqmvPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWlsKDK 406
Cdd:PLN02302 346 DVRKM----EYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW--DNY 419
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
3MZS_D       407 DLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:PLN02302 420 TPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLE 460
PLN02738 PLN02738
carotene beta-ring hydroxylase
248-448 1.67e-12

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 69.56  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       248 QDLRRKTEFRNY--PGILYCLLK-----SEKMLLEDvkanITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlna 320
Cdd:PLN02738 360 EELQFHEEYMNErdPSILHFLLAsgddvSSKQLRDD----LMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEV--- 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       321 rRQAEGDISKMLQMVPLLKAS---IKETLRLHPIS-VTLQRYPESDlVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKF 396
Cdd:PLN02738 433 -DSVLGDRFPTIEDMKKLKYTtrvINESLRLYPQPpVLIRRSLEND-MLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKF 510
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
3MZS_D       397 DPTRW----LSKDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:PLN02738 511 NPERWpldgPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQL 566
PLN02966 PLN02966
cytochrome P450 83A1
45-448 2.63e-12

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 68.62  E-value: 2.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        45 QKYGPIYREKLGNLESVYIIHPEDVAHLFKFEG-SYPERydiPPWLAyHRY--YQKPIGVLFKKSGTWKKDRVVLNTEVM 121
Cdd:PLN02966  60 KKYGPILSYRIGSRTMVVISSAELAKELLKTQDvNFADR---PPHRG-HEFisYGRRDMALNHYTPYYREIRKMGMNHLF 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       122 APEAIKNFipllNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEEtvnpEAQKFIDAVYK 201
Cdd:PLN02966 136 SPTRVATF----KHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGE----EMKRFIKILYG 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       202 mfhTSVPLLNVppELYRLFRTKTWRDHVAAWDTIFNKAEKYTEIFYQDL--------RRKTEFRNYPGILYCLLKSE--- 270
Cdd:PLN02966 208 ---TQSVLGKI--FFSDFFPYCGFLDDLSGLTAYMKECFERQDTYIQEVvnetldpkRVKPETESMIDLLMEIYKEQpfa 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       271 -KMLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLNARRQ------AEGDISKMlqmvPLLKASIK 343
Cdd:PLN02966 283 sEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEkgstfvTEDDVKNL----PYFRALVK 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       344 ETLRLHP-ISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFS-SPDKFDPTRWLSKDKDL--IHFRNLGFGWG 419
Cdd:PLN02966 359 ETLRIEPvIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWGpNPDEFRPERFLEKEVDFkgTDYEFIPFGSG 438
                        410       420
                 ....*....|....*....|....*....
3MZS_D       420 VRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:PLN02966 439 RRMCPGMRLGAAMLEVPYANLLLNFNFKL 467
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
284-437 3.71e-12

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: 67.62  E-value: 3.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVLnarrqaegdiskmlqmvpLLKASIKETLRLHPIsVTLQRYPESDL 363
Cdd:cd11035 198 LFLAGLDTVASALGFIFRHLARHPEDRRRLREDPE------------------LIPAAVEELLRRYPL-VNVARIVTRDV 258
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
3MZS_D      364 VLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlskdKDLIHFrnlGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd11035 259 EFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR-----KPNRHL---AFGAGPHRCLGSHLARLELRIAL 324
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
275-441 3.80e-12

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 67.75  E-value: 3.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      275 EDVKANITEMLAGGVNTTSMTLqwhlyemarSLNVQEMLREEvlnaRRQAEGDISKMLQMVP----LLKASIKETLRLHP 350
Cdd:cd20612 186 DEVRDNVLGTAVGGVPTQSQAF---------AQILDFYLRRP----GAAHLAEIQALARENDeadaTLRGYVLEALRLNP 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      351 ISVTLQRYPESDLVLQDYL-----IPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDkdlIHfrnlgFGWGVRQCVG 425
Cdd:cd20612 253 IAPGLYRRATTDTTVADGGgrtvsIKAGDRVFVSLASAMRDPRAFPDPERFRLDRPLESY---IH-----FGHGPHQCLG 324
                       170
                ....*....|....*.
3MZS_D      426 RRIAELEMTLFLIHIL 441
Cdd:cd20612 325 EEIARAALTEMLRVVL 340
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
209-446 3.82e-12

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: 67.62  E-value: 3.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      209 LLNVPPELYRLFrtKTWRDHVAA--------WDTIFNKAEKYTEI---FYQDLRRKtefRNYPG--ILYCLLKSE---KM 272
Cdd:cd11032 119 LLGVPAEDRELF--KKWSDALVSglgddsfeEEEVEEMAEALRELnayLLEHLEER---RRNPRddLISRLVEAEvdgER 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      273 LLEDVKANITE-MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREevlnarrqaegDISkmlqmvpLLKASIKETLRLHPI 351
Cdd:cd11032 194 LTDEEIVGFAIlLLIAGHETTTNLLGNAVLCLDEDPEVAARLRA-----------DPS-------LIPGAIEEVLRYRPP 255
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      352 SVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKdkdliHfrnLGFGWGVRQCVGRRIAEL 431
Cdd:cd11032 256 VQRTARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDRNPNP-----H---LSFGHGIHFCLGAPLARL 327
                       250
                ....*....|....*
3MZS_D      432 EMTLFLIHILENFKV 446
Cdd:cd11032 328 EARIALEALLDRFPR 342
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
284-437 4.00e-12

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: 67.61  E-value: 4.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEvlnarrqaegdiskmlqmvP-LLKASIKETLRLHPISVTLQRYPESD 362
Cdd:cd11037 210 YLSAGLDTTISAIGNALWLLARHPDQWERLRAD-------------------PsLAPNAFEEAVRLESPVQTFSRTTTRD 270
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
3MZS_D      363 LVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdkdlihfRNLGFGWGVRQCVGRRIAELEMTLFL 437
Cdd:cd11037 271 TELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITRNPS--------GHVGFGHGVHACVGQHLARLEGEALL 337
PLN02971 PLN02971
tryptophan N-hydroxylase
275-445 4.13e-12

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 68.14  E-value: 4.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       275 EDVKANITEMLAGGVNTTSMTLQWHLYEMarsLNVQEMLR---EE----VLNARRQAEGDISKMlqmvPLLKASIKETLR 347
Cdd:PLN02971 326 DEIKPTIKELVMAAPDNPSNAVEWAMAEM---INKPEILHkamEEidrvVGKERFVQESDIPKL----NYVKAIIREAFR 398
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       348 LHPISV-TLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI----HFRNLGFGWGVRQ 422
Cdd:PLN02971 399 LHPVAAfNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTltenDLRFISFSTGKRG 478
                        170       180
                 ....*....|....*....|...
3MZS_D       423 CVGRRIAELEMTLFLIHILENFK 445
Cdd:PLN02971 479 CAAPALGTAITTMMLARLLQGFK 501
PLN03018 PLN03018
homomethionine N-hydroxylase
275-444 4.29e-12

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 68.11  E-value: 4.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       275 EDVKANITEMLAGGVNTTSMTLQWHLYEMARSlnvQEMLR------EEVLNARRQA-EGDISKMlqmvPLLKASIKETLR 347
Cdd:PLN03018 313 DEIKAQCVEFCIAAIDNPANNMEWTLGEMLKN---PEILRkalkelDEVVGKDRLVqESDIPNL----NYLKACCRETFR 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       348 LHPISVTLQRY-PESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWL-----SKDKDLI--HFRNLGFGWG 419
Cdd:PLN03018 386 IHPSAHYVPPHvARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLqgdgiTKEVTLVetEMRFVSFSTG 465
                        170       180
                 ....*....|....*....|....*
3MZS_D       420 VRQCVGRRIAELEMTLFLIHILENF 444
Cdd:PLN03018 466 RRGCVGVKVGTIMMVMMLARFLQGF 490
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
284-434 8.38e-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: 66.62  E-value: 8.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEvlnarrqaegdiskmlqmvP-LLKASIKETLRLHPISVTLQRYPESD 362
Cdd:cd11038 222 LLFAGVDTTRNQLGLAMLTFAEHPDQWRALRED-------------------PeLAPAAVEEVLRWCPTTTWATREAVED 282
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
3MZS_D      363 LVLQDYLIPAKTLVQVAIYAMGRDPAFFsSPDKFDPTRwlskDKDlihfRNLGFGWGVRQCVGRRIAELEMT 434
Cdd:cd11038 283 VEYNGVTIPAGTVVHLCSHAANRDPRVF-DADRFDITA----KRA----PHLGFGGGVHHCLGAFLARAELA 345
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
287-455 9.75e-12

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: 66.74  E-value: 9.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      287 GGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLKASIKETLRL-HPISVTLQRYPES 361
Cdd:cd20668 237 AGTETVSTTLRYGFLLLMKHPEVEAKVHEEidrVIGRNRQPKfEDRAKM----PYTEAVIHEIQRFgDVIPMGLARRVTK 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      362 DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKD---KDLIHFrnLGFGWGVRQCVGRRIAELEMTLFLI 438
Cdd:cd20668 313 DTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKgqfKKSDAF--VPFSIGKRYCFGEGLARMELFLFFT 390
                       170
                ....*....|....*...
3MZS_D      439 HILENFKVEM-QHIGDVD 455
Cdd:cd20668 391 TIMQNFRFKSpQSPEDID 408
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
254-462 1.74e-11

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 66.18  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       254 TEFRNYPGILYCLLKSEK-MLLEDVkanITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREEVlNARRQAEgDISKML 332
Cdd:PLN02169 281 TYYMNVDTSKYKLLKPKKdKFIRDV---IFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI-NTKFDNE-DLEKLV 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       333 qmvpLLKASIKETLRLHPISVTLQRYP-ESDLVLQDYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRWLSKDKDLIH 410
Cdd:PLN02169 356 ----YLHAALSESMRLYPPLPFNHKAPaKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRH 431
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
3MZS_D       411 ---FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDVDTIFNLIL 462
Cdd:PLN02169 432 epsYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKVIEGHKIEAIPSILL 486
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
284-444 2.47e-11

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: 65.55  E-value: 2.47e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      284 MLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNARRQAEGDISKMlqmvPLLKASIKETLRLHP-ISVTLQRY 358
Cdd:cd20669 234 LLFGGTETVSTTLRYGFLILMKYPKVAARVQEEidrvVGRNRLPTLEDRARM----PYTDAVIHEIQRFADiIPMSLPHA 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      359 PESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDlihFRN----LGFGWGVRQCVGRRIAELEMT 434
Cdd:cd20669 310 VTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGS---FKKndafMPFSAGKRICLGESLARMELF 386
                       170
                ....*....|
3MZS_D      435 LFLIHILENF 444
Cdd:cd20669 387 LYLTAILQNF 396
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
209-449 2.58e-11

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 65.14  E-value: 2.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      209 LLNVP---PELYRLFRTKTWRDHVAAWD-----TIFNKAEKYTEIFYQDLrrkTEFRNYPG---ILYCLLKSEKmllEDV 277
Cdd:cd20630 124 MLGVPaewDEQFRRFGTATIRLLPPGLDpeeleTAAPDVTEGLALIEEVI---AERRQAPVeddLLTTLLRAEE---DGE 197
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      278 KANITEMLA-------GGVNTTSMTLQWHLYEMARslnvqemlREEVLnARRQAEGDiskmlqmvpLLKASIKETLRLHP 350
Cdd:cd20630 198 RLSEDELMAlvaalivAGTDTTVHLITFAVYNLLK--------HPEAL-RKVKAEPE---------LLRNALEEVLRWDN 259
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      351 IS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlskdkdliHFR-NLGFGWGVRQCVGRRI 428
Cdd:cd20630 260 FGkMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR---------DPNaNIAFGYGPHFCIGAAL 330
                       250       260
                ....*....|....*....|.
3MZS_D      429 AELEMTLFLIHILENFKvEMQ 449
Cdd:cd20630 331 ARLELELAVSTLLRRFP-EME 350
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
337-444 2.74e-11

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


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 64.88  E-value: 2.74e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLHPiSVTL-QRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlsKDKdlihfRNLG 415
Cdd:cd20625 244 LIPAAVEELLRYDS-PVQLtARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR---APN-----RHLA 314
                        90       100
                ....*....|....*....|....*....
3MZS_D      416 FGWGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd20625 315 FGAGIHFCLGAPLARLEAEIALRALLRRF 343
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
34-448 4.90e-11

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 64.80  E-value: 4.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D        34 QRIHFRHIENFQKyGPIYREKLGNLESVYIIHPEDVAHLFKFEGSyperyDIPPWLAYHRYYQKPIGV-LFKKSG-TWKK 111
Cdd:PLN03195  52 DRMHDWLVEYLSK-DRTVVVKMPFTTYTYIADPVNVEHVLKTNFA-----NYPKGEVYHSYMEVLLGDgIFNVDGeLWRK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       112 DRVVLNTEVmapeAIKNFIPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKEDLFHFAFESITNVMFGERLGMLEETV--N 189
Cdd:PLN03195 126 QRKTASFEF----ASKNLRDFSTVVFREYSLKLSSILSQASFANQVVDMQDLFMRMTLDSICKVGFGVEIGTLSPSLpeN 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       190 PEAQ-----------KFIDAVYKMFHtsvpLLNVPPElyrlfrtktwrdhvaawdTIFNKAEKYTEIFYQDL--RRKTEF 256
Cdd:PLN03195 202 PFAQafdtaniivtlRFIDPLWKLKK----FLNIGSE------------------ALLSKSIKVVDDFTYSVirRRKAEM 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       257 RNYPGILYCL---LKSEKMLL-EDVKANITE---------MLAGGVNTTSMTLQWHLYEMARSLNVQEMLR------EEV 317
Cdd:PLN03195 260 DEARKSGKKVkhdILSRFIELgEDPDSNFTDkslrdivlnFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYselkalEKE 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       318 LNARRQAEGDIS---KMLQMVPLLK-----------ASIKETLRLHPISVTLQRYPESDLVLQD-YLIPAKTLVQVAIYA 382
Cdd:PLN03195 340 RAKEEDPEDSQSfnqRVTQFAGLLTydslgklqylhAVITETLRLYPAVPQDPKGILEDDVLPDgTKVKAGGMVTYVPYS 419
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
3MZS_D       383 MGRDPAFFsSPD--KFDPTRWLsKD---KDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:PLN03195 420 MGRMEYNW-GPDaaSFKPERWI-KDgvfQNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQL 488
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
47-444 5.02e-11

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 64.43  E-value: 5.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       47 YGPIYREKLGNLESVYIIHPEDVAHLFKFEG-SYPERydiPPWLAYHRYYQKpIGVLFKKSGTWKKDRVvlntevMAPEA 125
Cdd:cd20662   1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEqNFMNR---PETPLRERIFNK-NGLIFSSGQTWKEQRR------FALMT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      126 IKNF---IPLLNPVSQDFVSLLHKRIKQQGSGKFVGDIKedlFHFAFES-ITNVMFGER-----------LGMLEETVNP 190
Cdd:cd20662  71 LRNFglgKKSLEERIQEECRHLVEAIREEKGNPFNPHFK---INNAVSNiICSVTFGERfeyhdewfqelLRLLDETVYL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      191 EAQKfIDAVYKMFHTSVPLLNVPP-------ELYRLFRTKTWRDHVAAWDTifNKAEKYTEIFYQDLRRKTEfrnyPGIL 263
Cdd:cd20662 148 EGSP-MSQLYNAFPWIMKYLPGSHqtvfsnwKKLKLFVSDMIDKHREDWNP--DEPRDFIDAYLKEMAKYPD----PTTS 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      264 YCLlksekmllEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLK 339
Cdd:cd20662 221 FNE--------ENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEidrVIGQKRQPSlADRESM----PYTN 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      340 ASIKETLRL-HPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKdlihFRN----L 414
Cdd:cd20662 289 AVIHEVQRMgNIIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQ----FKKreafL 364
                       410       420       430
                ....*....|....*....|....*....|
3MZS_D      415 GFGWGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd20662 365 PFSMGKRACLGEQLARSELFIFFTSLLQKF 394
PLN02774 PLN02774
brassinosteroid-6-oxidase
262-447 6.84e-11

brassinosteroid-6-oxidase


Pssm-ID: 178373  Cd Length: 463  Bit Score: 64.03  E-value: 6.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       262 ILYCLLKSE----KMLLEDVKANITEMLAGG---VNTTSMTLQWHLYEMARSLnvqEMLREEVL--NARRQAEGDIS-KM 331
Cdd:PLN02774 246 MLGYLMRKEgnryKLTDEEIIDQIITILYSGyetVSTTSMMAVKYLHDHPKAL---QELRKEHLaiRERKRPEDPIDwND 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       332 LQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLskDKDL-IH 410
Cdd:PLN02774 323 YKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWL--DKSLeSH 400
                        170       180       190
                 ....*....|....*....|....*....|....*..
3MZS_D       411 FRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:PLN02774 401 NYFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWE 437
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
337-436 8.01e-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: 63.70  E-value: 8.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLHPIS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlskdkdlIHFRNLG 415
Cdd:cd11030 251 LVPGAVEELLRYLSIVqDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR--------PARRHLA 322
                        90       100
                ....*....|....*....|....*.
3MZS_D      416 FGWGVRQCVGRRIAELEM-----TLF 436
Cdd:cd11030 323 FGHGVHQCLGQNLARLELeialpTLF 348
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
288-446 2.63e-10

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: 62.10  E-value: 2.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      288 GVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLKASIKETLR---LHPISVtlqryPE 360
Cdd:cd20672 238 GTETTSTTLRYGFLLMLKYPHVAEKVQKEidqVIGSHRLPTlDDRAKM----PYTDAVIHEIQRfsdLIPIGV-----PH 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      361 ---SDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRN-LGFGWGVRQCVGRRIAELEMTLF 436
Cdd:cd20672 309 rvtKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAfMPFSTGKRICLGEGIARNELFLF 388
                       170
                ....*....|
3MZS_D      437 LIHILENFKV 446
Cdd:cd20672 389 FTTILQNFSV 398
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
269-459 1.22e-09

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


Pssm-ID: 215600  Cd Length: 452  Bit Score: 60.14  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       269 SEKMLLEDVKANITEMLAGGVNT--TSMTLQW-HLYEMARSLNvqeMLREEVLNARRQAEgDISKMLQ-----MVPLLKA 340
Cdd:PLN03141 244 SDELTDDLISDNMIDMMIPGEDSvpVLMTLAVkFLSDCPVALQ---QLTEENMKLKRLKA-DTGEPLYwtdymSLPFTQN 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       341 SIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNlgFGWGV 420
Cdd:PLN03141 320 VITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDMNNSSFTP--FGGGQ 397
                        170       180       190
                 ....*....|....*....|....*....|....*....
3MZS_D       421 RQCVGRRIAELEMTLFLIHILENFKvemqHIGDVDTIFN 459
Cdd:PLN03141 398 RLCPGLDLARLEASIFLHHLVTRFR----WVAEEDTIVN 432
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
337-441 1.30e-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: 59.68  E-value: 1.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRwlskDKDlihfRNLGF 416
Cdd:cd11079 226 LLPAAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR----HAA----DNLVY 297
                        90       100
                ....*....|....*....|....*
3MZS_D      417 GWGVRQCVGRRIAELEMTLFLIHIL 441
Cdd:cd11079 298 GRGIHVCPGAPLARLELRILLEELL 322
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
337-444 1.65e-09

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: 59.46  E-value: 1.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVqVAIYAMG-RDPAFFSSPDKFDPTRWLSKdkdliHfrnLG 415
Cdd:cd11033 252 LLPTAVEEILRWASPVIHFRRTATRDTELGGQRIRAGDKV-VLWYASAnRDEEVFDDPDRFDITRSPNP-----H---LA 322
                        90       100
                ....*....|....*....|....*....
3MZS_D      416 FGWGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd11033 323 FGGGPHFCLGAHLARLELRVLFEELLDRV 351
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
288-455 1.54e-08

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 56.47  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      288 GVNTTSMTLQWHLYEMARSLNVQEMLREEVLNA----RRQAEGDISKMlqmvPLLKASIKETLRLH---PISVtlqryPE 360
Cdd:cd20670 238 GTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVigphRLPSVDDRVKM----PYTDAVIHEIQRLTdivPLGV-----PH 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      361 S---DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKdliHFRN----LGFGWGVRQCVGRRIAELEM 433
Cdd:cd20670 309 NvirDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQG---RFKKneafVPFSSGKRVCLGEAMARMEL 385
                       170       180
                ....*....|....*....|...
3MZS_D      434 TLFLIHILENFKVE-MQHIGDVD 455
Cdd:cd20670 386 FLYFTSILQNFSLRsLVPPADID 408
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
280-466 2.12e-08

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: 56.18  E-value: 2.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      280 NITEMLAG-GVNTTSMTLQWHLYEMARSLNVQEMLREE----VLNARRQAEGDISkmlqMVPLLKASIKETLRlHPISV- 353
Cdd:cd20676 240 NIVNDLFGaGFDTVTTALSWSLMYLVTYPEIQKKIQEEldevIGRERRPRLSDRP----QLPYLEAFILETFR-HSSFVp 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      354 -TLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHfRNLG-----FGWGVRQCVGRR 427
Cdd:cd20676 315 fTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEIN-KTESekvmlFGLGKRRCIGES 393
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
3MZS_D      428 IAELEMTLFLIHILENFKVEMQHIGDVDT--IFNLILTPDK 466
Cdd:cd20676 394 IARWEVFLFLAILLQQLEFSVPPGVKVDMtpEYGLTMKHKR 434
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
269-464 3.29e-08

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: 55.59  E-value: 3.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      269 SEKMLLEDvkaNITEMLAGGVNTTSMTLqWHLYEMARSLNVQEMLREEVlnarRQAEGDISKMLQMVPLLK---ASIKET 345
Cdd:cd20627 199 SEQQVLED---SMIFSLAGCVITANLCT-WAIYFLTTSEEVQKKLYKEV----DQVLGKGPITLEKIEQLRycqQVLCET 270
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      346 LR---LHPISVTLQrypESDLVLQDYLIPAKTLVqvaIYAMG---RDPAFFSSPDKFDPTRWlSKDKDLIHFRNLGFGwG 419
Cdd:cd20627 271 VRtakLTPVSARLQ---ELEGKVDQHIIPKETLV---LYALGvvlQDNTTWPLPYRFDPDRF-DDESVMKSFSLLGFS-G 342
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
3MZS_D      420 VRQCVGRRIAELEMTLFLIHILENFKVEMQHIGDVDTIFNLILTP 464
Cdd:cd20627 343 SQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSP 387
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
275-444 4.01e-08

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: 55.47  E-value: 4.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      275 EDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE---VLNARRQAE-GDISKMlqmvPLLKASIKETLRLHP 350
Cdd:cd20663 229 ENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEideVIGQVRRPEmADQARM----PYTNAVIHEVQRFGD 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      351 IS-VTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLI-HFRNLGFGWGVRQCVGRRI 428
Cdd:cd20663 305 IVpLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVkPEAFMPFSAGRRACLGEPL 384
                       170
                ....*....|....*.
3MZS_D      429 AELEMTLFLIHILENF 444
Cdd:cd20663 385 ARMELFLFFTCLLQRF 400
PLN02290 PLN02290
cytokinin trans-hydroxylase
288-445 6.08e-08

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 54.82  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       288 GVNTTSMTLQWHLYEMARSLNVQEMLREEV---LNARRQAEGDISKM--LQMVpllkasIKETLRLHPISVTLQRYPESD 362
Cdd:PLN02290 328 GHETTALLLTWTLMLLASNPTWQDKVRAEVaevCGGETPSVDHLSKLtlLNMV------INESLRLYPPATLLPRMAFED 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       363 LVLQDYLIPAKTLVQVAIYAMGRDPAFF-SSPDKFDPTRWLSKD-KDLIHFrnLGFGWGVRQCVGRRIAELEMTLFLIHI 440
Cdd:PLN02290 402 IKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPfAPGRHF--IPFAAGPRNCIGQAFAMMEAKIILAML 479

                 ....*
3MZS_D       441 LENFK 445
Cdd:PLN02290 480 ISKFS 484
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
298-453 6.27e-07

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 51.53  E-value: 6.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      298 WHLYEMARSLNVQEMLREE---VLNARRQAEG---DIS----KMLQMVpLLKASIKETLRLHPISVTLqRYPESDLVLQ- 366
Cdd:cd20632 237 WAMYYLLRHPEALAAVRDEidhVLQSTGQELGpdfDIHltreQLDSLV-YLESAINESLRLSSASMNI-RVVQEDFTLKl 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      367 --DYLIPAKTLVQVAIY--AMGRDPAFFSSPD--KFD--------PTRWLSKDKDLIHFRnLGFGWGVRQCVGRRIAELE 432
Cdd:cd20632 315 esDGSVNLRKGDIVALYpqSLHMDPEIYEDPEvfKFDrfvedgkkKTTFYKRGQKLKYYL-MPFGSGSSKCPGRFFAVNE 393
                       170       180
                ....*....|....*....|.
3MZS_D      433 MTLFLIHILENFkvEMQHIGD 453
Cdd:cd20632 394 IKQFLSLLLLYF--DLELLEE 412
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
118-448 9.00e-07

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: 51.00  E-value: 9.00e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      118 TEVMAPEAIKNFIPLLNPVSQDfvsllhkRIKQQGSGKFVGDIKEDLFHFAFESITNVMFG-----ERLGMLEETVnpea 192
Cdd:cd20637  87 SKLFSHEALESYLPKIQQVIQD-------TLRVWSSNPEPINVYQEAQKLTFRMAIRVLLGfrvseEELSHLFSVF---- 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      193 QKFIDAVYkmfhtSVPLlNVPPELYRlfRTKTWRDHVaawdtifnkaEKYTEIFYQDLRRKTEFRNYPGILYCLLKSEK- 271
Cdd:cd20637 156 QQFVENVF-----SLPL-DLPFSGYR--RGIRARDSL----------QKSLEKAIREKLQGTQGKDYADALDILIESAKe 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      272 ----MLLEDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE-----VLNARRQAEGDIS-KMLQMVPLLKAS 341
Cdd:cd20637 218 hgkeLTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREElrsngILHNGCLCEGTLRlDTISSLKYLDCV 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      342 IKETLRLH-PIS----VTLQRYPesdlvLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRW---LSKDKDLiHFRN 413
Cdd:cd20637 298 IKEVLRLFtPVSggyrTALQTFE-----LDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFgqeRSEDKDG-RFHY 371
                       330       340       350
                ....*....|....*....|....*....|....*
3MZS_D      414 LGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:cd20637 372 LPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFEL 406
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
275-444 1.05e-06

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 51.13  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       275 EDVKANITEMLAGGVNTTSMTLQWHLYEMARSLNVQEMLREE--VLNARRQAEGDIS-KMLQMVPLLKASIKETLRLHPI 351
Cdd:PLN02987 266 EEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEheKIRAMKSDSYSLEwSDYKSMPFTQCVVNETLRVANI 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       352 SVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHFRNLG-FGWGVRQCVGRRIAE 430
Cdd:PLN02987 346 IGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTpFGGGPRLCPGYELAR 425
                        170
                 ....*....|....
3MZS_D       431 LEMTLFLIHILENF 444
Cdd:PLN02987 426 VALSVFLHRLVTRF 439
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
119-447 1.39e-06

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 50.46  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       119 EVMAPEAIKNFIPLLNPVSQDfvsllhkrikqqGSGKFVgDIKEDLFHFAFESITNVMFGERLGMLEETVnpEAQKFIDA 198
Cdd:PLN02426 153 EIVASEIESRLLPLLSSAADD------------GEGAVL-DLQDVFRRFSFDNICKFSFGLDPGCLELSL--PISEFADA 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       199 vykmFHTSVPL-----LNVPPELY---RLFRTKTWRDhvaawdtiFNKAEKYTEIFYQDL---RRKTEFRNYPGIL---Y 264
Cdd:PLN02426 218 ----FDTASKLsaeraMAASPLLWkikRLLNIGSERK--------LKEAIKLVDELAAEVirqRRKLGFSASKDLLsrfM 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       265 CLLKSEKMLLEDVkanITEMLAGGvNTTSMTLQWHLYEMARSLNVQEMLREEV--LNARRQAEGDISKMLQMvPLLKASI 342
Cdd:PLN02426 286 ASINDDKYLRDIV---VSFLLAGR-DTVASALTSFFWLLSKHPEVASAIREEAdrVMGPNQEAASFEEMKEM-HYLHAAL 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       343 KETLRLHPISVTLQRYPESDLVLQD-YLIPAKTLVQVAIYAMGRDPAFFSsPD--KFDPTRWLSKDKDLIH--FRNLGFG 417
Cdd:PLN02426 361 YESMRLFPPVQFDSKFAAEDDVLPDgTFVAKGTRVTYHPYAMGRMERIWG-PDclEFKPERWLKNGVFVPEnpFKYPVFQ 439
                        330       340       350
                 ....*....|....*....|....*....|
3MZS_D       418 WGVRQCVGRRIAELEMTLFLIHILENFKVE 447
Cdd:PLN02426 440 AGLRVCLGKEMALMEMKSVAVAVVRRFDIE 469
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
337-444 3.06e-06

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 49.03  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      337 LLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSkdkdlihfRNLGF 416
Cdd:cd11036 220 LAAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTA--------RSAHF 291
                        90       100
                ....*....|....*....|....*...
3MZS_D      417 GWGVRQCVGRRIAELEMTLFLIHILENF 444
Cdd:cd11036 292 GLGRHACLGAALARAAAAAALRALAARF 319
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
340-429 3.77e-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: 48.97  E-value: 3.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      340 ASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDkdlihfRNLGFGWG 419
Cdd:cd20619 236 AIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPPAAS------RNLSFGLG 309
                        90
                ....*....|
3MZS_D      420 VRQCVGRRIA 429
Cdd:cd20619 310 PHSCAGQIIS 319
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
320-450 3.13e-05

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 45.91  E-value: 3.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      320 ARRQAEGDISKMLQMVPLLKASIKETLRLHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPT 399
Cdd:cd20624 226 ARAREEAAVPPGPLARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPE 305
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
3MZS_D      400 RWLskDKDLIHFRNL-GFGWGVRQCVGRRIAELEMTLFLIHILENFKVEMQH 450
Cdd:cd20624 306 IWL--DGRAQPDEGLvPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLE 355
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
329-448 4.02e-05

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  Cd Length: 449  Bit Score: 45.82  E-value: 4.02e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      329 SKMLQMVPLLKASIKETLRLHPISVtLQRYPESDLVL-----QDYLIPAKTLVQVAIY-AMGRDPAFFSSPDKFDPTRWL 402
Cdd:cd20633 287 RDMLLKTPVLDSAVEETLRLTAAPV-LIRAVVQDMTLkmangREYALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFL 365
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
3MZS_D      403 S----------KDKDLIHFRNLGFGWGVRQCVGRRIAELEMTLFLIHILENFKVEM 448
Cdd:cd20633 366 NpdggkkkdfyKNGKKLKYYNMPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLEL 421
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
235-448 6.13e-05

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: 45.45  E-value: 6.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      235 IFNKAEKYTEIFYQDLRRKTEFRNYpgilyCL--LKSEKMLLEDVKANITEM----------LAGGVNTTSMTLqWHLYE 302
Cdd:cd20631 180 MFKTAKSAREALAERLLHENLQKRE-----NIseLISLRMLLNDTLSTLDEMekarthvamlWASQANTLPATF-WSLFY 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      303 MARSLNVQEMLREEV---LNARRQAEGDISK-------MLQMVPLLKASIKETLRLHPISVTLqRYPESDLVLQdyLIPA 372
Cdd:cd20631 254 LLRCPEAMKAATKEVkrtLEKTGQKVSDGGNpivltreQLDDMPVLGSIIKEALRLSSASLNI-RVAKEDFTLH--LDSG 330
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      373 KTLV-----QVAIYA--MGRDPAFFSSPDKFDPTRWLSKDKD--LIHFRN--------LGFGWGVRQCVGRRIAELEMTL 435
Cdd:cd20631 331 ESYAirkddIIALYPqlLHLDPEIYEDPLTFKYDRYLDENGKekTTFYKNgrklkyyyMPFGSGTSKCPGRFFAINEIKQ 410
                       250
                ....*....|...
3MZS_D      436 FLIHILENFKVEM 448
Cdd:cd20631 411 FLSLMLCYFDMEL 423
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
274-448 6.19e-05

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: 45.21  E-value: 6.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      274 LEDVKANITEMLAGGVNTT-----SMTLQWHLYEMARSLNVQEMLREEVLNARRQAEGDIS-KMLQMVPLLKASIKETLR 347
Cdd:cd20636 225 MQELKESAVELIFAAFSTTasastSLVLLLLQHPSAIEKIRQELVSHGLIDQCQCCPGALSlEKLSRLRYLDCVVKEVLR 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D      348 LHPISVTLQRYPESDLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSK--DKDLIHFRNLGFGWGVRQCVG 425
Cdd:cd20636 305 LLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEreESKSGRFNYIPFGGGVRSCIG 384
                       170       180
                ....*....|....*....|...
3MZS_D      426 RRIAELEMTLFLIHILENFKVEM 448
Cdd:cd20636 385 KELAQVILKTLAVELVTTARWEL 407
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
362-411 8.02e-05

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: 44.83  E-value: 8.02e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
3MZS_D      362 DLVLQDYLIPAKTLVQVAIYAMGRDPAFFSSPDKFDPTRWLSKDKDLIHF 411
Cdd:cd11067 289 DFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGDPFDF 338
PLN02648 PLN02648
allene oxide synthase
309-405 2.91e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 43.00  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
3MZS_D       309 VQEMLREEVLNARRQAEGDIS-KMLQMVPLLKASIKETLRLHPiSVTLQrY--PESDLVLQ--DYLIPAKT---LVQVAI 380
Cdd:PLN02648 306 LQARLAEEVRSAVKAGGGGVTfAALEKMPLVKSVVYEALRIEP-PVPFQ-YgrAREDFVIEshDAAFEIKKgemLFGYQP 383
                         90       100
                 ....*....|....*....|....*
3MZS_D       381 YAMgRDPAFFSSPDKFDPTRWLSKD 405
Cdd:PLN02648 384 LVT-RDPKVFDRPEEFVPDRFMGEE 407
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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