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Conserved domains on  [gi|1370474309|ref|XP_024307109|]
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cytochrome P450 4F8 isoform X1 [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 74-417 0e+00

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


The actual alignment was detected with superfamily member cd20679:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 442  Bit Score: 723.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  74 LRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTP 153
Cdd:cd20679     1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAAVAPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 154 AFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVV 233
Cdd:cd20679    81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYIAAILELSALVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 234 KRNNQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKEL 313
Cdd:cd20679   161 KRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAKSKTLDFIDVLLLSKDEDGKEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 314 SDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLHP 393
Cdd:cd20679   241 SDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHP 320

                         330       340
                  ....*....|....*....|....
gi 1370474309 394 PIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:cd20679   321 PVTAISRCCTQDIVLPDGRVIPKG 344
 
Name Accession Description Interval E-value
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 74-417 0e+00

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: 723.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  74 LRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTP 153
Cdd:cd20679     1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAAVAPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 154 AFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVV 233
Cdd:cd20679    81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYIAAILELSALVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 234 KRNNQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKEL 313
Cdd:cd20679   161 KRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAKSKTLDFIDVLLLSKDEDGKEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 314 SDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLHP 393
Cdd:cd20679   241 SDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHP 320

                         330       340
                  ....*....|....*....|....
gi 1370474309 394 PIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:cd20679   321 PVTAISRCCTQDIVLPDGRVIPKG 344
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 52-417 3.87e-105

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: 318.84  E-value: 3.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  52 PQPRKQNWFLGHLGLVTPTEEGLRVLTQLVATYPQGFVRWLGPiTPIINLCHPDIVRSVINTSDAIT---DKDIVFYKTL 128
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGP-KPVVVLSGPEAVKEVLIKKGEEFsgrPDEPWFATSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 129 KPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTClDVFEHISLMTLDSLQKCIF 208
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVI-DITDLLFRAALNVICSILF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 209 --SFDSNCQEKPSEYITAIMELSALVVKRNNQ-FFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLtsqgvdd 285
Cdd:pfam00067 159 geRFGSLEDPKFLELVKAVQELSSLLSSPSPQlLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL------- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 286 flqAKAKSKTLDFIDVLLLSEDK-NGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKD 364
Cdd:pfam00067 232 ---DSAKKSPRDFLDALLLAKEEeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370474309 365 RepKEIEWDDLAQLPFLTMCLKESLRLHPPIPTF-ARGCTQDVVLPDsRVIPKG 417
Cdd:pfam00067 309 K--RSPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPG-YLIPKG 359
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 89-417 5.86e-38

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 141.57  E-value: 5.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  89 VRWLGPITPIINLCHPDIVRSVINTSDAITdKDIVFYKTLKP--WLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKI 166
Cdd:COG2124    35 FRVRLPGGGAWLVTRYEDVREVLRDPRTFS-SDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 167 FsksANIMHAKWQRLAMEGStcLDVFEHISLMTLDSLQKCIFSFdsncqekPSEYITAIMELSALVVKRnnqffrykdFL 246
Cdd:COG2124   114 I---REIADELLDRLAARGP--VDLVEEFARPLPVIVICELLGV-------PEEDRDRLRRWSDALLDA---------LG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 247 YFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSqgvddflqakaksktlDFIDVLLLSEDkNGKELSDEDIRAEADTFM 326
Cdd:COG2124   173 PLPPERRRRARRARAELDAYLRELIAERRAEPGD----------------DLLSALLAARD-DGERLSDEELRDELLLLL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 327 FGGHDTTASGLSWVLYNLARHPEYQERCRQEvqellkdrepkeiewddlaqLPFLTMCLKESLRLHPPIPTFARGCTQDV 406
Cdd:COG2124   236 LAGHETTANALAWALYALLRHPEQLARLRAE--------------------PELLPAAVEETLRLYPPVPLLPRTATEDV 295

                         330
                  ....*....|.
gi 1370474309 407 VLpDSRVIPKG 417
Cdd:COG2124   296 EL-GGVTIPAG 305
PLN02290 PLN02290
cytokinin trans-hydroxylase
 75-418 6.97e-30

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 121.07  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  75 RVLTQLVA---TYPQGFVRWLGPiTPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLL 151
Cdd:PLN02290   81 RLLPHYVAwskQYGKRFIYWNGT-EPRLCLTETELIKELLTKYNTVTGKSWLQQQGTKHFIGRGLLMANGADWYHQRHIA 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 152 TPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCifSFDSNCqEKPSEYITAIMELSAL 231
Cdd:PLN02290  160 APAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQTEVEIGEYMTRLTADIISRT--EFDSSY-EKGKQIFHLLTVLQRL 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 232 VVKRNNQFFrYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRrtltsqgvDDFLQAKAKSKTLDFIDVLLLSEDK--- 308
Cdd:PLN02290  237 CAQATRHLC-FPGSRFFPSKYNREIKSLKGEVERLLMEIIQSRR--------DCVEIGRSSSYGDDLLGMLLNEMEKkrs 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 309 NGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeiEWDDLAQLPFLTMCLKES 388
Cdd:PLN02290  308 NGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETP---SVDHLSKLTLLNMVINES 384

                         330       340       350
                  ....*....|....*....|....*....|
gi 1370474309 389 LRLHPPIPTFARGCTQDVVLPDSRvIPKGL 418
Cdd:PLN02290  385 LRLYPPATLLPRMAFEDIKLGDLH-IPKGL 413
 
Name Accession Description Interval E-value
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 74-417 0e+00

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: 723.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  74 LRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTP 153
Cdd:cd20679     1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAAVAPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 154 AFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVV 233
Cdd:cd20679    81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYIAAILELSALVV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 234 KRNNQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKEL 313
Cdd:cd20679   161 KRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAKSKTLDFIDVLLLSKDEDGKEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 314 SDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLHP 393
Cdd:cd20679   241 SDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHP 320

                         330       340
                  ....*....|....*....|....
gi 1370474309 394 PIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:cd20679   321 PVTAISRCCTQDIVLPDGRVIPKG 344
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 85-417 1.89e-171

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: 486.29  E-value: 1.89e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  85 PQGFVRWLGPITPIINLCHPDIVRSVINTSDAitdKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYI 164
Cdd:cd20659     1 PRAYVFWLGPFRPILVLNHPDTIKAVLKTSEP---KDRDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 165 KIFSKSANIMHAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIFSFDSNCQE--KPSEYITAIMELSALVVKRNNQFFRY 242
Cdd:cd20659    78 PVYNECTDILLEKWSKLAETGES-VEVFEDISLLTLDIILRCAFSYKSNCQQtgKNHPYVAAVHELSRLVMERFLNPLLH 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 243 KDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGvddfLQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEA 322
Cdd:cd20659   157 FDWIYYLTPEGRRFKKACDYVHKFAEEIIKKRRKELEDNK----DEALSKRKYLDFLDILLTARDEDGKGLTDEEIRDEV 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 323 DTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpkEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGC 402
Cdd:cd20659   233 DTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRD--DIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTL 310

                         330
                  ....*....|....*
gi 1370474309 403 TQDVVLpDSRVIPKG 417
Cdd:cd20659   311 TKPITI-DGVTLPAG 324
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 74-417 7.83e-153

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: 439.40  E-value: 7.83e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  74 LRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVINTSDAitdKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTP 153
Cdd:cd20678     1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDP---KAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 154 AFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSE--YITAIMELSAL 231
Cdd:cd20678    78 AFHYDILKPYVKLMADSVRVMLDKWEKLATQDSS-LEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSnsYIQAVSDLSNL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 232 VVKRNNQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQakaKSKTLDFIDVLLLSEDKNGK 311
Cdd:cd20678   157 IFQRLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIK---KKRHLDFLDILLFAKDENGK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 312 ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpkEIEWDDLAQLPFLTMCLKESLRL 391
Cdd:cd20678   234 SLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGD--SITWEHLDQMPYTTMCIKEALRL 311

                         330       340
                  ....*....|....*....|....*.
gi 1370474309 392 HPPIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:cd20678   312 YPPVPGISRELSKPVTFPDGRSLPAG 337
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 88-417 1.12e-115

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: 344.51  E-value: 1.12e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  88 FVRWLGPiTPIINLCHPDIVRSVINTSDAITDKDivFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIF 167
Cdd:cd20628     4 FRLWIGP-KPYVVVTNPEDIEVILSSSKLITKSF--LYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 168 SKSANIMHAKWQRLAmeGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKP-SEYITAIMELSALVVKRNNQFFRYKDFL 246
Cdd:cd20628    81 NENSKILVEKLKKKA--GGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEdSEYVKAVKRILEIILKRIFSPWLRFDFI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 247 YFLTPCGRRFHRACRLVHDFTDAVIQERRRTL--TSQGVDDFLQAKAKsKTLDFIDVLLLSEDKNGKeLSDEDIRAEADT 324
Cdd:cd20628   159 FRLTSLGKEQRKALKVLHDFTNKVIKERREELkaEKRNSEEDDEFGKK-KRKAFLDLLLEAHEDGGP-LTDEDIREEVDT 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 325 FMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDrEPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQ 404
Cdd:cd20628   237 FMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGD-DDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTE 315

                         330
                  ....*....|...
gi 1370474309 405 DVVLPDsRVIPKG 417
Cdd:cd20628   316 DIKLDG-YTIPKG 327
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 52-417 3.87e-105

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: 318.84  E-value: 3.87e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  52 PQPRKQNWFLGHLGLVTPTEEGLRVLTQLVATYPQGFVRWLGPiTPIINLCHPDIVRSVINTSDAIT---DKDIVFYKTL 128
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGP-KPVVVLSGPEAVKEVLIKKGEEFsgrPDEPWFATSR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 129 KPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTClDVFEHISLMTLDSLQKCIF 208
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVI-DITDLLFRAALNVICSILF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 209 --SFDSNCQEKPSEYITAIMELSALVVKRNNQ-FFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLtsqgvdd 285
Cdd:pfam00067 159 geRFGSLEDPKFLELVKAVQELSSLLSSPSPQlLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL------- 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 286 flqAKAKSKTLDFIDVLLLSEDK-NGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKD 364
Cdd:pfam00067 232 ---DSAKKSPRDFLDALLLAKEEeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370474309 365 RepKEIEWDDLAQLPFLTMCLKESLRLHPPIPTF-ARGCTQDVVLPDsRVIPKG 417
Cdd:pfam00067 309 K--RSPTYDDLQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPG-YLIPKG 359
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 91-417 5.52e-97

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: 296.87  E-value: 5.52e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  91 WLGPItPIINLCHPDIVRSVINTSDAITDKdiVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKS 170
Cdd:cd20660     7 WLGPK-PIVVLYSAETVEVILSSSKHIDKS--FEYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 171 ANIMHAKWQRLAmeGSTCLDVFEHISLMTLD-----SLQKCIfsfdsNCQ-EKPSEYITAIMELSALVVKRNNQFFRYKD 244
Cdd:cd20660    84 SEILVKKLKKEV--GKEEFDIFPYITLCALDiicetAMGKSV-----NAQqNSDSEYVKAVYRMSELVQKRQKNPWLWPD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 245 FLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTL-----TSQGVDDFLqAKAKSKTLDFIDvLLLSEDKNGKELSDEDIR 319
Cdd:cd20660   157 FIYSLTPDGREHKKCLKILHGFTNKVIQERKAELqksleEEEEDDEDA-DIGKRKRLAFLD-LLLEASEEGTKLSDEDIR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 320 AEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDrEPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFA 399
Cdd:cd20660   235 EEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGD-SDRPATMDDLKEMKYLECVIKEALRLFPSVPMFG 313

                         330
                  ....*....|....*...
gi 1370474309 400 RGCTQDVVLpDSRVIPKG 417
Cdd:cd20660   314 RTLSEDIEI-GGYTIPKG 330
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 91-417 1.44e-72

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: 234.27  E-value: 1.44e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  91 WLGPItPIINLCHPDIVRSVINTSDAItDKDIVfYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKS 170
Cdd:cd20680    18 WIGPV-PFVILYHAENVEVILSSSKHI-DKSYL-YKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMNEQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 171 ANIMHAKWQRLAMEGStcLDVFEHISLMTLDSLQKCIFSFDSNCQE-KPSEYITAIMELSALVVKRNNQFFRYKDFLYFL 249
Cdd:cd20680    95 SNILVEKLEKHVDGEA--FNCFFDITLCALDIICETAMGKKIGAQSnKDSEYVQAVYRMSDIIQRRQKMPWLWLDLWYLM 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 250 TPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFL---QAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFM 326
Cdd:cd20680   173 FKEGKEHNKNLKILHTFTDNVIAERAEEMKAEEDKTGDsdgESPSKKKRKAFLDMLLSVTDEEGNKLSHEDIREEVDTFM 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 327 FGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDV 406
Cdd:cd20680   253 FEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSD-RPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDC 331

                         330
                  ....*....|.
gi 1370474309 407 VLPDSRViPKG 417
Cdd:cd20680   332 EIRGFKV-PKG 341
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 88-417 5.11e-66

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: 216.70  E-value: 5.11e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  88 FVRWLGPiTPIINLCHPDIVrSVINTSDAITDKDiVFYKTLkpWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIF 167
Cdd:cd11057     4 FRAWLGP-RPFVITSDPEIV-QVVLNSPHCLNKS-FFYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 168 SKSANIMHAKWQRLAMEGStcLDVFEHISLMTLDSLQKCIFSFDSNCQ-EKPSEYITAIMELSALVVKRNNQFFRYKDFL 246
Cdd:cd11057    79 NEEAQKLVQRLDTYVGGGE--FDILPDLSRCTLEMICQTTLGSDVNDEsDGNEEYLESYERLFELIAKRVLNPWLHPEFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 247 YFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTS---QGVDDFLQAKAKSKTldFIDVLL-LSEdkNGKELSDEDIRAEA 322
Cdd:cd11057   157 YRLTGDYKEEQKARKILRAFSEKIIEKKLQEVELesnLDSEEDEENGRKPQI--FIDQLLeLAR--NGEEFTDEEIMDEI 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 323 DTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGC 402
Cdd:cd11057   233 DTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQ-FITYEDLQQLVYLEMVLKETMRLFPVGPLVGRET 311

                         330
                  ....*....|....*
gi 1370474309 403 TQDVVLPDSRVIPKG 417
Cdd:cd11057   312 TADIQLSNGVVIPKG 326
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 92-417 7.54e-63

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: 207.82  E-value: 7.54e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  92 LGPITPIInLCHPDIVRSVINTSDAITDKDiVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSA 171
Cdd:cd20620     8 LGPRRVYL-VTHPDHIQHVLVTNARNYVKG-GVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEAT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 172 NIMHAKWQRLAmeGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQ-EKPSEYITAIMELSAlvvKRNNQFFRYKdfLYFLT 250
Cdd:cd20620    86 AALLDRWEAGA--RRGPVDVHAEMMRLTLRIVAKTLFGTDVEGEaDEIGDALDVALEYAA---RRMLSPFLLP--LWLPT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 251 PCGRRFHRACRLVHDFTDAVIQERRRTLTSQGvddflqakaksktlDFIDVLLLSEDK-NGKELSDEDIRAEADTFMFGG 329
Cdd:cd20620   159 PANRRFRRARRRLDEVIYRLIAERRAAPADGG--------------DLLSMLLAARDEeTGEPMSDQQLRDEVMTLFLAG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 330 HDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEiewDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLP 409
Cdd:cd20620   225 HETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTA---EDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIG 301


                  ....*...
gi 1370474309 410 DSRvIPKG 417
Cdd:cd20620   302 GYR-IPAG 308
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 85-417 2.02e-60

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: 202.11  E-value: 2.02e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  85 PQGFVRWLGPI-TPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPY 163
Cdd:cd11069     1 YGGLIRYRGLFgSERLLVTDPKALKHILVTNSYDFEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 164 IKIFSKSANIMHAKWQRLAMEG---STCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIME-------LSALVV 233
Cdd:cd11069    81 YPIFWSKAEELVDKLEEEIEESgdeSISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYRrlfeptlLGSLLF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 234 KRNNQFFRyKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTsqgvddflqAKAKSKTLDFIDVLLLSEDKNGKE- 312
Cdd:cd11069   161 ILLLFLPR-WLVRILPWKANREIRRAKDVLRRLAREIIREKKAALL---------EGKDDSGKDILSILLRANDFADDEr 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 313 LSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLH 392
Cdd:cd11069   231 LSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDLDRLPYLNAVCRETLRLY 310

                         330       340
                  ....*....|....*....|....*
gi 1370474309 393 PPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11069   311 PPVPLTSREATKDTVI-KGVPIPKG 334
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 89-417 1.28e-54

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: 185.80  E-value: 1.28e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  89 VRWLGPITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFs 168
Cdd:cd00302     4 FRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVI- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 169 ksANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSfdsncqEKPSEYITAIMELSALVVKRNNQFFRykdfLYF 248
Cdd:cd00302    83 --REIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGG------PDLGEDLEELAELLEALLKLLGPRLL----RPL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 249 LTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGvddflqakaksktldfiDVLLLSEDKNGKELSDEDIRAEADTFMFG 328
Cdd:cd00302   151 PSPRLRRLRRARARLRDYLEELIARRRAEPADDL-----------------DLLLLADADDGGGLSDEEIVAELLTLLLA 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 329 GHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeiewDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVL 408
Cdd:cd00302   214 GHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTP-----EDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVEL 288


                  ....*....
gi 1370474309 409 PDsRVIPKG 417
Cdd:cd00302   289 GG-YTIPAG 296
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 83-418 2.81e-51

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: 177.92  E-value: 2.81e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  83 TYPQGFVRWLGPiTPIINLCHPDIVRSVINTSDAITDKDIVfYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKP 162
Cdd:cd11052    10 QYGKNFLYWYGT-DPRLYVTEPELIKELLSKKEGYFGKSPL-QPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 163 YIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCifSFDSNCQEKPSEY--ITAIMELSAlvvkRNNQFF 240
Cdd:cd11052    88 MVPAMVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRT--AFGSSYEEGKEVFklLRELQKICA----QANRDV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 241 RYKDFLYFLTpcgRRFHRACRLVHDFTDA---VIQERRRTLTSQGVDDFLQakaksktlDFIDVLLLS--EDKNGKELSD 315
Cdd:cd11052   162 GIPGSRFLPT---KGNKKIKKLDKEIEDSlleIIKKREDSLKMGRGDDYGD--------DLLGLLLEAnqSDDQNKNMTV 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 316 EDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeiEWDDLAQLPFLTMCLKESLRLHPPI 395
Cdd:cd11052   231 QEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKP---PSDSLSKLKTVSMVINESLRLYPPA 307

                         330       340
                  ....*....|....*....|...
gi 1370474309 396 PTFARGCTQDVVLPDsRVIPKGL 418
Cdd:cd11052   308 VFLTRKAKEDIKLGG-LVIPKGT 329
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 96-417 2.93e-49

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: 172.38  E-value: 2.93e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  96 TPIINLCHPDIVRSV-INTSDAITDKDIVFyKTLKPWlGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIM 174
Cdd:cd11055    13 IPVIVVSDPEMIKEIlVKEFSNFTNRPLFI-LLDEPF-DSSLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 175 HAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIFSFDSNCQEKPS----EYITAIMELSALVVKRNNQFFRYKDFLYFLT 250
Cdd:cd11055    91 VEKLEKAAETGKP-VDMKDLFQGFTLDVILSTAFGIDVDSQNNPDdpflKAAKKIFRNSIIRLFLLLLLFPLRLFLFLLF 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 251 PCGRRFHRACRLVhDFTDAVIQERRRTLTSQGVDdFLQakaksktldfidvLLLS-----EDKNGKELSDEDIRAEADTF 325
Cdd:cd11055   170 PFVFGFKSFSFLE-DVVKKIIEQRRKNKSSRRKD-LLQ-------------LMLDaqdsdEDVSKKKLTDDEIVAQSFIF 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 326 MFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpkEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQD 405
Cdd:cd11055   235 LLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDG--SPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKED 312

                         330
                  ....*....|..
gi 1370474309 406 VVLPDSRvIPKG 417
Cdd:cd11055   313 CTINGVF-IPKG 323
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 104-417 4.61e-49

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: 172.55  E-value: 4.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 104 PDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAm 183
Cdd:cd11046    29 PAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRVFGRCSERLMEKLDAAA- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 184 EGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYI----TAIMELSalvvKRNNQFFRYKD--FLYFLTPCGRRFH 257
Cdd:cd11046   108 ETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTEESPVIkavyLPLVEAE----HRSVWEPPYWDipAALFIVPRQRKFL 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 258 RACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLlseDKNGKELSDEDIRAEADTFMFGGHDTTASGL 337
Cdd:cd11046   184 RDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLNEDDPSLLRFLV---DMRDEDVDSKQLRDDLMTMLIAGHETTAAVL 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 338 SWVLYNLARHPEYQERCRQEVQELLKDREPKEIewDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRV-IPK 416
Cdd:cd11046   261 TWTLYELSQNPELMAKVQAEVDAVLGDRLPPTY--EDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGGVkVPA 338


                  .
gi 1370474309 417 G 417
Cdd:cd11046   339 G 339
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 97-417 7.69e-49

cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, and similar cytochrome P450s; CYP46A1 is also called cholesterol 24-hydroxylase (EC 1.14.14.25), CH24H, cholesterol 24-monooxygenase, or cholesterol 24S-hydroxylase. It catalyzes the conversion of cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. CYP46A1 is associated with high-order brain functions; increased expression improves cognition while a reduction leads to a poor cognitive performance. It also plays a role in the pathogenesis or progression of neurodegenerative disorders. CYP46A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410706 [Multi-domain]  Cd Length: 429  Bit Score: 171.55  E-value: 7.69e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  97 PIINLCHPDIVRSVINTSDAItdKDIVFYKTLK-----PWLGDGLLLSVG-DKWRHHRRLLTPAFHFNILKPYIKIFSKS 170
Cdd:cd20613    23 PIVVVSDPEAVKEVLITLNLP--KPPRVYSRLAflfgeRFLGNGLVTEVDhEKWKKRRAILNPAFHRKYLKNLMDEFNES 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 171 ANIMHAKWQRLAmEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPS----EYITAIMElsALVVKRNNQFFRYKdfl 246
Cdd:cd20613   101 ADLLVEKLSKKA-DGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDspfpKAISLVLE--GIQESFRNPLLKYN--- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 247 yfltPCGRRFHR----ACRLVHDFTDAVIQERRrtltsqgvddflQAKAKSKTLDFiDVL--LLSEDKNGKELSDEDIRA 320
Cdd:cd20613   175 ----PSKRKYRRevreAIKFLRETGRECIEERL------------EALKRGEEVPN-DILthILKASEEEPDFDMEELLD 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 321 EADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRepKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFAR 400
Cdd:cd20613   238 DFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSK--QYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSR 315

                         330
                  ....*....|....*..
gi 1370474309 401 GCTQDVVLPDSRvIPKG 417
Cdd:cd20613   316 ELTKDIELGGYK-IPAG 331
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 96-417 1.32e-48

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: 170.80  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  96 TPIINLCHPDIVRSV-INTSDAITDKDIVFYKTLKPwLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIM 174
Cdd:cd11056    13 RPALLVRDPELIKQIlVKDFAHFHDRGLYSDEKDDP-LSANLFSLDGEKWKELRQKLTPAFTSGKLKNMFPLMVEVGDEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 175 HAKWQRLAMEGStCLDVFEHISLMTLDSLQKCIFSFDSNCQEKP-SEYITAIMELSalvvkRNNQFFRYKDFLYFLTPCG 253
Cdd:cd11056    92 VDYLKKQAEKGK-ELEIKDLMARYTTDVIASCAFGLDANSLNDPeNEFREMGRRLF-----EPSRLRGLKFMLLFFFPKL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 254 RRFHRACRL---VHDF----TDAVIQERRRTltsqgvddflqakaKSKTLDFIDVLL-------LSEDKNGKELSDEDIR 319
Cdd:cd11056   166 ARLLRLKFFpkeVEDFfrklVRDTIEYREKN--------------NIVRNDFIDLLLelkkkgkIEDDKSEKELTDEELA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 320 AEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFA 399
Cdd:cd11056   232 AQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHG-GELTYEALQEMKYLDQVVNETLRKYPPLPFLD 310

                         330
                  ....*....|....*....
gi 1370474309 400 RGCTQDVVLPDSR-VIPKG 417
Cdd:cd11056   311 RVCTKDYTLPGTDvVIEKG 329
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 92-417 4.20e-48

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: 169.36  E-value: 4.20e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  92 LGPiTPIINLCHPDIVRSVInTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSA 171
Cdd:cd11049    20 LGP-RPAYVVTSPELVRQVL-VNDRVFDKGGPLFDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 172 NIMHAKWQrlamEGSTcLDVFEHISLMTLDSLQKCIFSfdsncQEKPSEYITAIMELSALVVKRNNQFFRYKDFLYFL-T 250
Cdd:cd11049    98 EALAGSWR----PGRV-VDVDAEMHRLTLRVVARTLFS-----TDLGPEAAAELRQALPVVLAGMLRRAVPPKFLERLpT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 251 PCGRRFHRACRLVHDFTDAVIQERRRTLTSQGvddflqakaksktlDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGH 330
Cdd:cd11049   168 PGNRRFDRALARLRELVDEIIAEYRASGTDRD--------------DLLSLLLAARDEEGRPLSDEELRDQVITLLTAGT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 331 DTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKeieWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPD 410
Cdd:cd11049   234 ETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPAT---FEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGG 310


                  ....*..
gi 1370474309 411 SRvIPKG 417
Cdd:cd11049   311 HR-LPAG 316
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 74-417 7.00e-46

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: 163.14  E-value: 7.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  74 LRVLTQLVATYPQGFVRWLGPITPIINLCHPDIVRSVInTSDAITDKDIVFYKTLKPWLGD-GLLLSVGDKWRHHRRLLT 152
Cdd:cd11053     1 VGFLERLRARYGDVFTLRVPGLGPVVVLSDPEAIKQIF-TADPDVLHPGEGNSLLEPLLGPnSLLLLDGDRHRRRRKLLM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 153 PAFHFNILKPYIKIFsksANIMHAKWQRLAMEGStcLDVFEHISLMTLDSLQKCIFSF-DSNCQEKPSEYITAIMELSAL 231
Cdd:cd11053    80 PAFHGERLRAYGELI---AEITEREIDRWPPGQP--FDLRELMQEITLEVILRVVFGVdDGERLQELRRLLPRLLDLLSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 232 VVKRNNQFFRykdFLYFLTPcGRRFHRACRLVHDFTDAVIQERRRTLTSQGvDDFLqakaksktldfiDVLLLSEDKNGK 311
Cdd:cd11053   155 PLASFPALQR---DLGPWSP-WGRFLRARRRIDALIYAEIAERRAEPDAER-DDIL------------SLLLSARDEDGQ 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 312 ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeiewDDLAQLPFLTMCLKESLRL 391
Cdd:cd11053   218 PLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP-----EDIAKLPYLDAVIKETLRL 292

                         330       340
                  ....*....|....*....|....*.
gi 1370474309 392 HPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11053   293 YPVAPLVPRRVKEPVEL-GGYTLPAG 317
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 79-410 1.45e-44

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: 160.14  E-value: 1.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  79 QLVATYPQGFVRWLGPItPIINLCHPDIVRSVINTsdaITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFN 158
Cdd:cd20642     6 HTVKTYGKNSFTWFGPI-PRVIIMDPELIKEVLNK---VYDFQKPKTNPLTKLLATGLASYEGDKWAKHRKIINPAFHLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 159 ILKPYIKIFSKSANIMHAKWQRLAMEGSTC-LDVFEHISLMTLDSLQKCifSFDSNCQEKPSeyITAIM-ELSALVVKrN 236
Cdd:cd20642    82 KLKNMLPAFYLSCSEMISKWEKLVSSKGSCeLDVWPELQNLTSDVISRT--AFGSSYEEGKK--IFELQkEQGELIIQ-A 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 237 NQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSqgvddflqakAKSKTLDFIDVLLLSEDKNGKE---- 312
Cdd:cd20642   157 LRKVYIPGWRFLPTKRNRRMKEIEKEIRSSLRGIINKREKAMKA----------GEATNDDLLGILLESNHKEIKEqgnk 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 313 ---LSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeiEWDDLAQLPFLTMCLKESL 389
Cdd:cd20642   227 nggMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKP---DFEGLNHLKVVTMILYEVL 303

                         330       340
                  ....*....|....*....|.
gi 1370474309 390 RLHPPIPTFARGCTQDVVLPD 410
Cdd:cd20642   304 RLYPPVIQLTRAIHKDTKLGD 324
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 92-417 6.80e-44

cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410677 [Multi-domain]  Cd Length: 426  Bit Score: 158.07  E-value: 6.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  92 LGPI-------TPIINLCHPDIVRSVINTS---------DAItdkdiVFYKTLKPwLGDGLLLSVGDKWRHHRRLLTPAf 155
Cdd:cd11054     4 YGPIvreklggRDIVHLFDPDDIEKVFRNEgkypirpslEPL-----EKYRKKRG-KPLGLLNSNGEEWHRLRSAVQKP- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 156 hfnILKP-----YIKIFSKSANIMHAKWQRLAMEGSTCLDVFEH-ISLMTLDSLQKCIF-----SFDSNCQEKPSEYITA 224
Cdd:cd11054    77 ---LLRPksvasYLPAINEVADDFVERIRRLRDEDGEEVPDLEDeLYKWSLESIGTVLFgkrlgCLDDNPDSDAQKLIEA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 225 IMELSALVVKRNNQFFRYKdflYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDflqakakSKTLDFIDVLLL 304
Cdd:cd11054   154 VKDIFESSAKLMFGPPLWK---YFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEED-------EEEDSLLEYLLS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 305 SedkngKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeIEWDDLAQLPFLTMC 384
Cdd:cd11054   224 K-----PGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEP--ITAEDLKKMPYLKAC 296

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1370474309 385 LKESLRLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd11054   297 IKESLRLYPVAPGNGRILPKDIVLSGYH-IPKG 328
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 89-417 4.51e-41

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: 150.82  E-value: 4.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  89 VRWLGpITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYikifs 168
Cdd:cd11064     5 GPWPG-GPDGIVTADPANVEHILKTNFDNYPKGPEFRDLFFDLLGDGIFNVDGELWKFQRKTASHEFSSRALREF----- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 169 kSANIMHAKWQRLAM-------EGSTCLDVFEHISLMTLDSLQKCIFSFDSNC--QEKP-SEYITAIMELSALVVKRnnq 238
Cdd:cd11064    79 -MESVVREKVEKLLVplldhaaESGKVVDLQDVLQRFTFDVICKIAFGVDPGSlsPSLPeVPFAKAFDDASEAVAKR--- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 239 fFRYKDFLY----FLTPcG--RRFHRACRLVHDFTDAVIQERRRTLTSQGvddflqaKAKSKTLDFIDVLLLSEDKNGKE 312
Cdd:cd11064   155 -FIVPPWLWklkrWLNI-GseKKLREAIRVIDDFVYEVISRRREELNSRE-------EENNVREDLLSRFLASEEEEGEP 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 313 LSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIE---WDDLAQLPFLTMCLKESL 389
Cdd:cd11064   226 VSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESRvptYEELKKLVYLHAALSESL 305

                         330       340
                  ....*....|....*....|....*...
gi 1370474309 390 RLHPPIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:cd11064   306 RLYPPVPFDSKEAVNDDVLPDGTFVKKG 333
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 97-417 1.28e-40

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: 149.64  E-value: 1.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  97 PIINLCHPDIVRSVINTSDAITD--KDIVFYKTLKPWL-------GDGLLLSVGD--KWRHHRRLLTPAFHFNILKPYIK 165
Cdd:cd11068    14 PIFKLTLPGRRVVVVSSHDLIAElcDESRFDKKVSGPLeelrdfaGDGLFTAYTHepNWGKAHRILMPAFGPLAMRGYFP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 166 IFSKSANIMHAKWQRLAmeGSTCLDVFEHISLMTLDSLQKCIFSFDSNC--QEKPSEYITAImeLSALV-VKRNNQFFRY 242
Cdd:cd11068    94 MMLDIAEQLVLKWERLG--PDEPIDVPDDMTRLTLDTIALCGFGYRFNSfyRDEPHPFVEAM--VRALTeAGRRANRPPI 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 243 KDFLYFLTpcGRRFHRACRLVHDFTDAVIQERRRTlTSQGVDDFLqakaksktldfiDVLLLSED-KNGKELSDEDIRAE 321
Cdd:cd11068   170 LNKLRRRA--KRQFREDIALMRDLVDEIIAERRAN-PDGSPDDLL------------NLMLNGKDpETGEKLSDENIRYQ 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 322 ADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeiEWDDLAQLPFLTMCLKESLRLHPPIPTFARG 401
Cdd:cd11068   235 MITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPP---PYEQVAKLRYIRRVLDETLRLWPTAPAFARK 311

                         330
                  ....*....|....*.
gi 1370474309 402 CTQDVVLPDSRVIPKG 417
Cdd:cd11068   312 PKEDTVLGGKYPLKKG 327
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 96-417 2.78e-40

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: 148.56  E-value: 2.78e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  96 TPIINLCHPDIVRSV-INTSDAITDKDIVFYKTLkpwLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSksaNIM 174
Cdd:cd20621    13 KPLISLVDPEYIKEFlQNHHYYKKKFGPLGIDRL---FGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMIN---EIT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 175 HAKWQRLAMEGSTCLDVFEHIslmTLDSLQKCIFSFDSNCQ----EKPSEYITAIMELSALVVKrNNQF-------FRYK 243
Cdd:cd20621    87 KEKIKKLDNQNVNIIQFLQKI---TGEVVIRSFFGEEAKDLkingKEIQVELVEILIESFLYRF-SSPYfqlkrliFGRK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 244 DFLYFLTPCGRRFHRACRLVHDFTDAVIQERrrtltsqgVDDFLQAKAKSKTLDFIDVLLLSEDKNGK-ELSDEDIRAEA 322
Cdd:cd20621   163 SWKLFPTKKEKKLQKRVKELRQFIEKIIQNR--------IKQIKKNKDEIKDIIIDLDLYLLQKKKLEqEITKEEIIQQF 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 323 DTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpkEIEWDDLAQLPFLTMCLKESLRLHPPIP-TFARG 401
Cdd:cd20621   235 ITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDD--DITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRV 312

                         330
                  ....*....|....*.
gi 1370474309 402 CTQDVVLPDSRvIPKG 417
Cdd:cd20621   313 ATQDHQIGDLK-IKKG 327
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 82-417 7.04e-39

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: 144.90  E-value: 7.04e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  82 ATYPQGFVRWLGPiTPIINLCHPDIVRSVINTSdAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILK 161
Cdd:cd20639     9 KIYGKTFLYWFGP-TPRLTVADPELIREILLTR-ADHFDRYEAHPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 162 PYIKIFSKSANIMHAKWQRLAMEGSTC-LDVFEHISLMTLDSLQKCIF--SFDS-----NCQEKpseyitaIMELSALVV 233
Cdd:cd20639    87 RLVPHVVKSVADMLDKWEAMAEAGGEGeVDVAEWFQNLTEDVISRTAFgsSYEDgkavfRLQAQ-------QMLLAAEAF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 234 KRnnqfFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIqERRRTLTSQGVDDflqakaksktLDFIDVLLL----SEDKN 309
Cdd:cd20639   160 RK----VYIPGYRFLPTKKNRKSWRLDKEIRKSLLKLI-ERRQTAADDEKDD----------EDSKDLLGLmisaKNARN 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 310 GKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRE-PKEiewDDLAQLPFLTMCLKES 388
Cdd:cd20639   225 GEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDvPTK---DHLPKLKTLGMILNET 301

                         330       340
                  ....*....|....*....|....*....
gi 1370474309 389 LRLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd20639   302 LRLYPPAVATIRRAKKDVKLGGLD-IPAG 329
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 89-417 5.86e-38

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 141.57  E-value: 5.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  89 VRWLGPITPIINLCHPDIVRSVINTSDAITdKDIVFYKTLKP--WLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKI 166
Cdd:COG2124    35 FRVRLPGGGAWLVTRYEDVREVLRDPRTFS-SDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 167 FsksANIMHAKWQRLAMEGStcLDVFEHISLMTLDSLQKCIFSFdsncqekPSEYITAIMELSALVVKRnnqffrykdFL 246
Cdd:COG2124   114 I---REIADELLDRLAARGP--VDLVEEFARPLPVIVICELLGV-------PEEDRDRLRRWSDALLDA---------LG 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 247 YFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSqgvddflqakaksktlDFIDVLLLSEDkNGKELSDEDIRAEADTFM 326
Cdd:COG2124   173 PLPPERRRRARRARAELDAYLRELIAERRAEPGD----------------DLLSALLAARD-DGERLSDEELRDELLLLL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 327 FGGHDTTASGLSWVLYNLARHPEYQERCRQEvqellkdrepkeiewddlaqLPFLTMCLKESLRLHPPIPTFARGCTQDV 406
Cdd:COG2124   236 LAGHETTANALAWALYALLRHPEQLARLRAE--------------------PELLPAAVEETLRLYPPVPLLPRTATEDV 295

                         330
                  ....*....|.
gi 1370474309 407 VLpDSRVIPKG 417
Cdd:COG2124   296 EL-GGVTIPAG 305
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 96-417 9.79e-38

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: 141.54  E-value: 9.79e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  96 TPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAF------HFNILKPYIKIFSK 169
Cdd:cd11063    12 TRVIFTIEPENIKAVLATQFKDFGLGERRRDAFKPLLGDGIFTSDGEEWKHSRALLRPQFsrdqisDLELFERHVQNLIK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 170 sanimhakwqRLAMEGSTCLDVfEHISLMTLDS-----LQKCIFSFDSNCQEKP-SEYITAIMELSALVVKRnnqfFRYK 243
Cdd:cd11063    92 ----------LLPRDGSTVDLQ-DLFFRLTLDSateflFGESVDSLKPGGDSPPaARFAEAFDYAQKYLAKR----LRLG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 244 DFLYFLTPcgRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDflqakaKSKTLDFIDVLLlsedkngKELSD-EDIRAEA 322
Cdd:cd11063   157 KLLWLLRD--KKFREACKVVHRFVDPYVDKALARKEESKDEE------SSDRYVFLDELA-------KETRDpKELRDQL 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 323 DTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGC 402
Cdd:cd11063   222 LNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPT--PTYEDLKNMKYLRAVINETLRLYPPVPLNSRVA 299

                         330       340
                  ....*....|....*....|...
gi 1370474309 403 TQDVVLP-------DSRV-IPKG 417
Cdd:cd11063   300 VRDTTLPrgggpdgKSPIfVPKG 322
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 83-418 2.52e-36

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: 137.54  E-value: 2.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  83 TYPQGFVRWLGpITPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKP 162
Cdd:cd20640    10 QYGPIFTYSTG-NKQFLYVSRPEMVKEINLCVSLDLGKPSYLKKTLKPLFGGGILTSNGPHWAHQRKIIAPEFFLDKVKG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 163 YIKIFSKSANIMHAKWQ-RLAMEGSTCLDVF--EHISLMTLDSLQKCIFSFDSNcqeKPSEYITAIMELSaLVVKRNNQF 239
Cdd:cd20640    89 MVDLMVDSAQPLLSSWEeRIDRAGGMAADIVvdEDLRAFSADVISRACFGSSYS---KGKEIFSKLRELQ-KAVSKQSVL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 240 FRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGvdDFLQAkaksktldfidVLLLSEDKNGKELSDED-I 318
Cdd:cd20640   165 FSIPGLRHLPTKSNRKIWELEGEIRSLILEIVKEREEECDHEK--DLLQA-----------ILEGARSSCDKKAEAEDfI 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 319 RAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEiewDDLAQLPFLTMCLKESLRLHPPIPTF 398
Cdd:cd20640   232 VDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDA---DSLSRMKTVTMVIQETLRLYPPAAFV 308

                         330       340
                  ....*....|....*....|
gi 1370474309 399 ARGCTQDVVLPDSrVIPKGL 418
Cdd:cd20640   309 SREALRDMKLGGL-VVPKGV 327
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 133-417 5.12e-36

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: 136.68  E-value: 5.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 133 GDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIFSFDS 212
Cdd:cd11083    48 INGVFSAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWERAAAEGEA-VDVHKDLMRYTVDVTTSLAFGYDL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 213 NCQEKPSEYITAIME-LSALVVKRNNQFFRYkdFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGvddflQAKA 291
Cdd:cd11083   127 NTLERGGDPLQEHLErVFPMLNRRVNAPFPY--WRYLRLPADRALDRALVEVRALVLDIIAAARARLAANP-----ALAE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 292 KSKTLdfIDVLLLSEDKNGKeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEiE 371
Cdd:cd11083   200 APETL--LAMMLAEDDPDAR-LTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPP-L 275

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1370474309 372 WDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd11083   276 LEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIA-LPAG 320
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 91-417 1.15e-35

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


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 135.80  E-value: 1.15e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  91 WLGPItPIINLCHPDIVRSV-INTSDAITDK------DIVFYktlkpwlGDGLLLSVGDKWRHHRRLLTPAF-HFNILKP 162
Cdd:cd20617     7 WLGDV-PTVVLSDPEIIKEAfVKNGDNFSDRpllpsfEIISG-------GKGILFSNGDYWKELRRFALSSLtKTKLKKK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 163 YIKIFSKSANIMHAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIFS--FDSNCQEKPSEYITAIMELSALVVKRNNQ-F 239
Cdd:cd20617    79 MEELIEEEVNKLIESLKKHSKSGEP-FDPRPYFKKFVLNIINQFLFGkrFPDEDDGEFLKLVKPIEEIFKELGSGNPSdF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 240 FRYKDFLYFLTPcgRRFHRACRLVHDFTDAVIQERRRTLtsqgvdDFLQAKaksktlDFIDVLLLSEDKNGKE--LSDED 317
Cdd:cd20617   158 IPILLPFYFLYL--KKLKKSYDKIKDFIEKIIEEHLKTI------DPNNPR------DLIDDELLLLLKEGDSglFDDDS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 318 IRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeIEWDDLAQLPFLTMCLKESLRLHPPIP- 396
Cdd:cd20617   224 IISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRR--VTLSDRSKLPYLNAVIKEVLRLRPILPl 301

                         330       340
                  ....*....|....*....|.
gi 1370474309 397 TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20617   302 GLPRVTTEDTEI-GGYFIPKG 321
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 79-417 8.29e-35

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: 133.73  E-value: 8.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  79 QLVATYPQGFVRWLGPiTPIINLCHPDIVRSVIntsdaiTDKDIVFYKT-----LKPWLGDGLLLSVGDKWRHHRRLLTP 153
Cdd:cd20641     6 QWKSQYGETFLYWQGT-TPRICISDHELAKQVL------SDKFGFFGKSkarpeILKLSGKGLVFVNGDDWVRHRRVLNP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 154 AFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTC---LDVFEHISLMTLDSLqkCIFSFDSNCQEKpSEYITAIMELSA 230
Cdd:cd20641    79 AFSMDKLKSMTQVMADCTERMFQEWRKQRNNSETErieVEVSREFQDLTADII--ATTAFGSSYAEG-IEVFLSQLELQK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 231 LVVKRNNQFFrYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERrrtltsqgvddfLQAKAKSKTLDFIDVLLLSEDKNG 310
Cdd:cd20641   156 CAAASLTNLY-IPGTQYLPTPRNLRVWKLEKKVRNSIKRIIDSR------------LTSEGKGYGDDLLGLMLEAASSNE 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 311 ------KELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEV-QELLKDREPKEiewDDLAQLPFLTM 383
Cdd:cd20641   223 ggrrteRKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVfRECGKDKIPDA---DTLSKLKLMNM 299

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1370474309 384 CLKESLRLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd20641   300 VLMETLRLYGPVINIARRASEDMKLGGLE-IPKG 332
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 245-417 3.62e-33

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: 128.87  E-value: 3.62e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 245 FLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTltsqgvddflqakAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADT 324
Cdd:cd11042   153 FPPLPLPSFRRRDRARAKLKEIFSEIIQKRRKS-------------PDKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 325 FMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQ 404
Cdd:cd11042   220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDD-PLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARK 298

                         170
                  ....*....|....
gi 1370474309 405 DVVLPDSR-VIPKG 417
Cdd:cd11042   299 PFEVEGGGyVIPKG 312
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 134-417 5.09e-33

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: 128.07  E-value: 5.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 134 DGLLLSVGDKWRHHRRLLTPAFHFNILKP-YIKIFSKSANIMHAKWQRlameGSTClDVFEHISLMTLDSLQKCIFSFDs 212
Cdd:cd11043    53 SSLLTVSGEEHKRLRGLLLSFLGPEALKDrLLGDIDELVRQHLDSWWR----GKSV-VVLELAKKMTFELICKLLLGID- 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 213 ncqekPSEYITAIMELSALVVKRNNQFFrykdfLYFLtpcGRRFHR---ACRLVHDFTDAVIQERRRTLtsqgvddflqa 289
Cdd:cd11043   127 -----PEEVVEELRKEFQAFLEGLLSFP-----LNLP---GTTFHRalkARKRIRKELKKIIEERRAEL----------- 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 290 KAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKE 369
Cdd:cd11043   183 EKASPKGDLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKEEGE 262

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1370474309 370 -IEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11043   263 gLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEY-KGYTIPKG 310
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 120-417 9.25e-32

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: 125.13  E-value: 9.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 120 KDIVFYKTLKPwLGDGLLLSVGDKWRHHRRLLTPAFHFNILKpyiKIFSKS---ANIMHAKWQRLAMEGSTCL-DVFEHI 195
Cdd:cd11070    35 KPGNQYKIPAF-YGPNVISSEGEDWKRYRKIVAPAFNERNNA---LVWEESirqAQRLIRYLLEEQPSAKGGGvDVRDLL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 196 SLMTLDSLQKCIFSFDSNCQEKPSeyitAIMELSALVVKRN---NQFFRYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQ 272
Cdd:cd11070   111 QRLALNVIGEVGFGFDLPALDEEE----SSLHDTLNAIKLAifpPLFLNFPFLDRLPWVLFPSRKRAFKDVDEFLSELLD 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 273 ERRRTLTSQGVDDFLQAKAKSKTLdfidvlllSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQE 352
Cdd:cd11070   187 EVEAELSADSKGKQGTESVVASRL--------KRARRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQD 258

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370474309 353 RCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVV----LPDSRVIPKG 417
Cdd:cd11070   259 WLREEIDSVLGDEPDDWDYEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVvitgLGQEIVIPKG 327
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 88-417 1.24e-31

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: 124.72  E-value: 1.24e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  88 FVRwLGPITpiINLCHPDIVRSVINTSDAITDKDivFYKTLKPWLGDGLLlSVGDKWRH--HRRLLTPAFHfnilKPYIK 165
Cdd:cd11059     3 VVR-LGPNE--VSVNDLDAVREIYGGGFGKTKSY--WYFTLRGGGGPNLF-STLDPKEHsaRRRLLSGVYS----KSSLL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 166 ------IFSKSANIMHAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIF--SFDSNCQEKPSEYITAIMELSALvvkrnn 237
Cdd:cd11059    73 raamepIIRERVLPLIDRIAKEAGKSGS-VDVYPLFTALAMDVVSHLLFgeSFGTLLLGDKDSRERELLRRLLA------ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 238 qffrykDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKE--LSD 315
Cdd:cd11059   146 ------SLAPWLRWLPRYLPLATSRLIIGIYFRAFDEIEEWALDLCARAESSLAESSDSESLTVLLLEKLKGLKKqgLDD 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 316 EDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQEL-LKDREPkeIEWDDLAQLPFLTMCLKESLRLHPP 394
Cdd:cd11059   220 LEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLpGPFRGP--PDLEDLDKLPYLNAVIRETLRLYPP 297

                         330       340
                  ....*....|....*....|...
gi 1370474309 395 IPTfargctqdvvlPDSRVIPKG 417
Cdd:cd11059   298 IPG-----------SLPRVVPEG 309
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 77-417 2.52e-31

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: 123.58  E-value: 2.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  77 LTQLVATYpqGFVRWLGPI-TPIINLCHPDIVRSVIntsdaiTDKDIVFYKT------LKPWLGDGLLLSVGDKWRHHRR 149
Cdd:cd11045     3 ARQRYRRY--GPVSWTGMLgLRVVALLGPDANQLVL------RNRDKAFSSKqgwdpvIGPFFHRGLMLLDFDEHRAHRR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 150 LLTPAFHFNILKPYIKIFSKSANIMHAKWQrlameGSTCLDVFEHISLMTLDsLQKCIF---SFDSNCQEKPSEYITAIm 226
Cdd:cd11045    75 IMQQAFTRSALAGYLDRMTPGIERALARWP-----TGAGFQFYPAIKELTLD-LATRVFlgvDLGPEADKVNKAFIDTV- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 227 ELSALVVKRNNQFFRYkdflyfltpcgRRFHRACRLVHDFTDAVIQERRRTltsqGVDDFLQAkaksktldfidvLLLSE 306
Cdd:cd11045   148 RASTAIIRTPIPGTRW-----------WRGLRGRRYLEEYFRRRIPERRAG----GGDDLFSA------------LCRAE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 307 DKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRepkeIEWDDLAQLPFLTMCLK 386
Cdd:cd11045   201 DEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLALGKGT----LDYEDLGQLEVTDWVFK 276

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1370474309 387 ESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11045   277 EALRLVPPVPTLPRRAVKDTEV-LGYRIPAG 306
PLN02290 PLN02290
cytokinin trans-hydroxylase
 75-418 6.97e-30

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 121.07  E-value: 6.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  75 RVLTQLVA---TYPQGFVRWLGPiTPIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRLL 151
Cdd:PLN02290   81 RLLPHYVAwskQYGKRFIYWNGT-EPRLCLTETELIKELLTKYNTVTGKSWLQQQGTKHFIGRGLLMANGADWYHQRHIA 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 152 TPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCifSFDSNCqEKPSEYITAIMELSAL 231
Cdd:PLN02290  160 APAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQTEVEIGEYMTRLTADIISRT--EFDSSY-EKGKQIFHLLTVLQRL 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 232 VVKRNNQFFrYKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRrtltsqgvDDFLQAKAKSKTLDFIDVLLLSEDK--- 308
Cdd:PLN02290  237 CAQATRHLC-FPGSRFFPSKYNREIKSLKGEVERLLMEIIQSRR--------DCVEIGRSSSYGDDLLGMLLNEMEKkrs 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 309 NGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeiEWDDLAQLPFLTMCLKES 388
Cdd:PLN02290  308 NGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETP---SVDHLSKLTLLNMVINES 384

                         330       340       350
                  ....*....|....*....|....*....|
gi 1370474309 389 LRLHPPIPTFARGCTQDVVLPDSRvIPKGL 418
Cdd:PLN02290  385 LRLYPPATLLPRMAFEDIKLGDLH-IPKGL 413
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 105-417 1.31e-29

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: 118.86  E-value: 1.31e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 105 DIVRS-----VINTSDAItdKDI----------VFYKTLKPwlGDGLLLSVGDKWRH--HRRLLTPAFHFNILKPYI-KI 166
Cdd:cd11061     2 DVVRIgpnelSINDPDAL--KDIyghgsnclkgPFYDALSP--SASLTFTTRDKAEHarRRRVWSHAFSDKALRGYEpRI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 167 FSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQEKPS-EYITAIMELSALVVKrnnqFFRYKDF 245
Cdd:cd11061    78 LSHVEQLCEQLDDRAGKPVSWPVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKdRYILDLLEKSMVRLG----VLGHAPW 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 246 LYFLT---PCGRRFHRACRLVHDFTDAVIQERRRTlTSQGVDDFLQAkaksktldfidvllLSEDKN---GKELSDEDIR 319
Cdd:cd11061   154 LRPLLldlPLFPGATKARKRFLDFVRAQLKERLKA-EEEKRPDIFSY--------------LLEAKDpetGEGLDLEELV 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 320 AEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFa 399
Cdd:cd11061   219 GEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDD-EIRLGPKLKSLPYLRACIDEALRLSPPVPSG- 296

                         330       340
                  ....*....|....*....|...
gi 1370474309 400 rgcTQDVVLP-----DSRVIPKG 417
Cdd:cd11061   297 ---LPRETPPggltiDGEYIPGG 316
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 122-417 4.45e-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: 108.91  E-value: 4.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 122 IVFYKTLkpwLGDG-LLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWqrlamEGSTCLDVFEHISLMTL 200
Cdd:cd11044    59 PRSVRRL---LGENsLSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRKW-----LKAGEVALYPELRRLTF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 201 DSLQKCIFSFDSNCQ-EKPSEYITAIME--LSALVVKRNNQFfrykdflyfltpcgRRFHRACRLVHDFTDAVIQERrrt 277
Cdd:cd11044   131 DVAARLLLGLDPEVEaEALSQDFETWTDglFSLPVPLPFTPF--------------GRAIRARNKLLARLEQAIRER--- 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 278 ltsqgvddflQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQE 357
Cdd:cd11044   194 ----------QEEENAEAKDALGLLLEAKDEDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQE 263

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 358 vQELLKDREPKEIEwdDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd11044   264 -QDALGLEEPLTLE--SLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQ-IPKG 319
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 132-417 1.08e-25

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 107.89  E-value: 1.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 132 LGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTClDVFEHISLMTLDSLQKCIFSFD 211
Cdd:cd20650    48 MKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVKNLRKEAEKGKPV-TLKDVFGAYSMDVITSTSFGVN 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 212 SNCQEKPSE-YITAIMELsaLVVKRNNQFFRYKDFLYFLTPCGRRFHrACRLVHDFTD----AV--IQERRRTLTSQGVD 284
Cdd:cd20650   127 IDSLNNPQDpFVENTKKL--LKFDFLDPLFLSITVFPFLTPILEKLN-ISVFPKDVTNffykSVkkIKESRLDSTQKHRV 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 285 DFLQAkaksktldFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKD 364
Cdd:cd20650   204 DFLQL--------MIDSQNSKETESHKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPN 275

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370474309 365 REPkeIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20650   276 KAP--PTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEI-NGVFIPKG 325
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 134-417 4.11e-25

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: 106.48  E-value: 4.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 134 DGLLLSVGDKWRHHRR-----LLTPafhfnilkpyiKIFSKSANIMHAKWQRL------AMEGSTCLDVFEHISLMTLDS 202
Cdd:cd20618    51 DIVFAPYGPHWRHLRKictleLFSA-----------KRLESFQGVRKEELSHLvkslleESESGKPVNLREHLSDLTLNN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 203 LQKCIFS-----FDSNCQEKPSEYITAIMELSALVVkrnnqFFRYKDFLYFLTP-----CGRRFHRACRLVHDFTDAVIQ 272
Cdd:cd20618   120 ITRMLFGkryfgESEKESEEAREFKELIDEAFELAG-----AFNIGDYIPWLRWldlqgYEKRMKKLHAKLDRFLQKIIE 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 273 ERRRtltsqgvddflQAKAKSKTLDFIDVLLLSEDKNGKE-LSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQ 351
Cdd:cd20618   195 EHRE-----------KRGESKKGGDDDDDLLLLLDLDGEGkLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVM 263

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474309 352 ERCRQEVQELL-KDREPKEiewDDLAQLPFLTMCLKESLRLHPPIP-TFARGCTQDVVLPDSRvIPKG 417
Cdd:cd20618   264 RKAQEELDSVVgRERLVEE---SDLPKLPYLQAVVKETLRLHPPGPlLLPHESTEDCKVAGYD-IPAG 327
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 97-401 6.74e-25

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: 105.41  E-value: 6.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  97 PIINLCHPDIVRSVinTSDAITDKDIVFYKTLKPWLGDGLLLSV-GDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMH 175
Cdd:cd11051    11 PLLVVTDPELAEQI--TQVTNLPKPPPLRKFLTPLTGGSSLISMeGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 176 AKWQRLAMEGS-TCLDvfEHISLMTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVVKRNNQFFRYKDFLYFltpcgr 254
Cdd:cd11051    89 AILRELAESGEvFSLE--ELTTNLTFDVIGRVTLDIDLHAQTGDNSLLTALRLLLALYRSLLNPFKRLNPLRPL------ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 255 rfhracrlvhdftdaviqeRRRTLTSQgVDDFLQAKAKSKtldfidvlllsedkngkeLSDEDIRAEADTFMFGGHDTTA 334
Cdd:cd11051   161 -------------------RRWRNGRR-LDRYLKPEVRKR------------------FELERAIDQIKTFLFAGHDTTS 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370474309 335 SGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKE--IEWDD--LAQLPFLTMCLKESLRLHPPIPTFARG 401
Cdd:cd11051   203 STLCWAFYLLSKHPEVLAKVRAEHDEVFgPDPSAAAelLREGPelLNQLPYTTAVIKETLRLFPPAGTARRG 274
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 145-417 1.14e-24

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: 104.97  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 145 RHHRRLLTPAF-------HFNILKPYIkifsksaNIMHAKWQRLAmEGSTCLDVFEHISLMTLDSLQKCIF--SFDSNCQ 215
Cdd:cd11058    59 ARLRRLLAHAFsekalreQEPIIQRYV-------DLLVSRLRERA-GSGTPVDMVKWFNFTTFDIIGDLAFgeSFGCLEN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 216 EKPSEYITAIMElsalvvkrnnqFFRYKDFLYFLtpcgRRFHRACRLVHDFTDAVIQERRRT---LTSQGVDDFLQAKAK 292
Cdd:cd11058   131 GEYHPWVALIFD-----------SIKALTIIQAL----RRYPWLLRLLRLLIPKSLRKKRKEhfqYTREKVDRRLAKGTD 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 293 SKtlDFIDVLLLSEDKnGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDrePKEIEW 372
Cdd:cd11058   196 RP--DFMSYILRNKDE-KKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSS--EDDITL 270

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1370474309 373 DDLAQLPFLTMCLKESLRLHPPIPTFargctqdvvLPdsRVIPKG 417
Cdd:cd11058   271 DSLAQLPYLNAVIQEALRLYPPVPAG---------LP--RVVPAG 304
PLN02936 PLN02936
epsilon-ring hydroxylase
 133-417 1.14e-23

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 102.56  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 133 GDGLLLSVGDKWRHHRRLLTPAFHFNILKPYI-KIFSKSANIMHAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIFSFD 211
Cdd:PLN02936   96 GSGFAIAEGELWTARRRAVVPSLHRRYLSVMVdRVFCKCAERLVEKLEPVALSGEA-VNMEAKFSQLTLDVIGLSVFNYN 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 212 SNCQEKPSEYITAIMELSALVVKRNNQFFRY--KDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQG----VDD 285
Cdd:PLN02936  175 FDSLTTDSPVIQAVYTALKEAETRSTDLLPYwkVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGevieGEE 254

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 286 FLQaKAKSKTLDFidvLLLSEDkngkELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDR 365
Cdd:PLN02936  255 YVN-DSDPSVLRF---LLASRE----EVSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGR 326

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370474309 366 EPKeieWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:PLN02936  327 PPT---YEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAG 375
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 265-417 1.65e-23

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: 101.50  E-value: 1.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 265 DFTDAVIQERRRTLtsqgvddflqAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNL 344
Cdd:cd11060   180 RFALEAVAERLAED----------AESAKGRKDMLDSFLEAGLKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYL 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474309 345 ARHPEYQERCRQEVQELLKDREPKE-IEWDDLAQLPFLTMCLKESLRLHPPIPtfargctqdvvLPDSRVIPKG 417
Cdd:cd11060   250 LKNPRVYAKLRAEIDAAVAEGKLSSpITFAEAQKLPYLQAVIKEALRLHPPVG-----------LPLERVVPPG 312
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 137-417 3.73e-23

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: 100.68  E-value: 3.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 137 LLSVGDKWRHHRRLLTpafhfnilkpyIKIFS-----KSANIMHAKWQRL-------AMEGStCLDVFEHISLMTLDSLQ 204
Cdd:cd11073    58 WPPYGPRWRMLRKICT-----------TELFSpkrldATQPLRRRKVRELvryvrekAGSGE-AVDIGRAAFLTSLNLIS 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 205 KCIFS-----FDSNCQEKPSEYITAIMELSAlvvKRN-NQFFrykDFLYFLTPCG--RRFHRACRLVHDFTDAVIQERRR 276
Cdd:cd11073   126 NTLFSvdlvdPDSESGSEFKELVREIMELAG---KPNvADFF---PFLKFLDLQGlrRRMAEHFGKLFDIFDGFIDERLA 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 277 TLTSQGvddflqakaKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQ 356
Cdd:cd11073   200 EREAGG---------DKKKDDDLLLLLDLELDSESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARA 270

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370474309 357 EVQELLKDRepKEIEWDDLAQLPFLTMCLKESLRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11073   271 ELDEVIGKD--KIVEESDISKLPYLQAVVKETLRLHPPAPlLLPRKAEEDVEV-MGYTIPKG 329
PLN02738 PLN02738
carotene beta-ring hydroxylase
 14-408 2.99e-22

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 99.22  E-value: 2.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  14 VAASPWLLLLVVGASWL--LARILAWTYAFYHNGRRLRCFPQPRkqnwflGHLGLVTpTEEGLRVLTQLVATYPQGFVRW 91
Cdd:PLN02738   99 VQKPGFPATLRNGLAKLgpPGELLAFLFTWVEAGEGYPKIPEAK------GSISAVR-GEAFFIPLYELFLTYGGIFRLT 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  92 LGPITPIInLCHPDIVRSVINTSDAITDKDIVfYKTLKPWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSA 171
Cdd:PLN02738  172 FGPKSFLI-VSDPSIAKHILRDNSKAYSKGIL-AEILEFVMGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQAS 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 172 NIMHAKWQRLAMEGSTcLDVFEHISLMTLDSLQKCIFSFDSNCQEkpseYITAIMELSALVVK----RNNQFFRYKDFLY 247
Cdd:PLN02738  250 DRLCQKLDAAASDGED-VEMESLFSRLTLDIIGKAVFNYDFDSLS----NDTGIVEAVYTVLReaedRSVSPIPVWEIPI 324

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 248 F--LTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGV---DDFLQAKAKSkTLDFidvLLLSedknGKELSDEDIRAEA 322
Cdd:PLN02738  325 WkdISPRQRKVAEALKLINDTLDDLIAICKRMVEEEELqfhEEYMNERDPS-ILHF---LLAS----GDDVSSKQLRDDL 396

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 323 DTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKeIEwdDLAQLPFLTMCLKESLRLHPPIPTFARGC 402
Cdd:PLN02738  397 MTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPT-IE--DMKKLKYTTRVINESLRLYPQPPVLIRRS 473


                  ....*.
gi 1370474309 403 TQDVVL 408
Cdd:PLN02738  474 LENDML 479
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 97-417 5.66e-22

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: 97.60  E-value: 5.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  97 PIINLCHPDIVRSVINTSDAITDKDIVFYKTLKPwLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHA 176
Cdd:cd20649    14 MFVVIAEPDMIKQVLVKDFNNFTNRMKANLITKP-MSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 177 KWQRLAMEGSTClDVFEHISLMTLDSLQKCIFSFDSNCQEKPSEYItaimelsalvVKRNNQFFRYK----------DFL 246
Cdd:cd20649    93 NLKSYAESGNAF-NIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPF----------VKNCKRFFEFSffrpililflAFP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 247 YFLTPCGRRFHRACR-LVHDFTDAVIQ------------ERRRtltsqgvdDFLQ------AKAKSKTLDFIDVL----- 302
Cdd:cd20649   162 FIMIPLARILPNKSRdELNSFFTQCIRnmiafrdqqspeERRR--------DFLQlmldarTSAKFLSVEHFDIVndade 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 303 -------------LLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELlkDREPKE 369
Cdd:cd20649   234 saydghpnspaneQTKPSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEF--FSKHEM 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1370474309 370 IEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd20649   312 VDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQR-IPAG 358
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 104-417 6.00e-22

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 97.93  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 104 PDIVRSVINTSDAITDKDIVFYKTLKPWLGDGLLLSVGDKWRHHRRllTPAFHF--NILKPYIKIFSKSANIMHAKWQRL 181
Cdd:PLN03195   83 PVNVEHVLKTNFANYPKGEVYHSYMEVLLGDGIFNVDGELWRKQRK--TASFEFasKNLRDFSTVVFREYSLKLSSILSQ 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 182 AMEGSTCLDVFEHISLMTLDSLQKCIFSFD---------SNCQEKPSEYITAIMELSALvvkrnNQFFRYKDFLYFLTPc 252
Cdd:PLN03195  161 ASFANQVVDMQDLFMRMTLDSICKVGFGVEigtlspslpENPFAQAFDTANIIVTLRFI-----DPLWKLKKFLNIGSE- 234

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 253 gRRFHRACRLVHDFTDAVIQERRRTLTSQGVDdflQAKAKSKTLD-FIdvlLLSEDKNGKeLSDEDIRAEADTFMFGGHD 331
Cdd:PLN03195  235 -ALLSKSIKVVDDFTYSVIRRRKAEMDEARKS---GKKVKHDILSrFI---ELGEDPDSN-FTDKSLRDIVLNFVIAGRD 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 332 TTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKE------------------IEWDDLAQLPFLTMCLKESLRLHP 393
Cdd:PLN03195  307 TTATTLSWFVYMIMMNPHVAEKLYSELKALEKERAKEEdpedsqsfnqrvtqfaglLTYDSLGKLQYLHAVITETLRLYP 386

                         330       340
                  ....*....|....*....|....
gi 1370474309 394 PIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:PLN03195  387 AVPQDPKGILEDDVLPDGTKVKAG 410
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 92-417 6.22e-22

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: 97.01  E-value: 6.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  92 LGPiTPIINLCHPDIVRSVINTSdAITD-------KDIVFYKTLKpwlgdglLLSVGDKWRHHRRLltPAFHfnilkpyi 164
Cdd:cd11076    10 LGE-TRVVITSHPETAREILNSP-AFADrpvkesaYELMFNRAIG-------FAPYGEYWRNLRRI--ASNH-------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 165 kIFSKSANIMHAKwQRLA------------MEGSTCLDVFEHISLMTLDSLQKCIF--SFDSNCQEKPSEyitaimELSA 230
Cdd:cd11076    71 -LFSPRRIAASEP-QRQAiaaqmvkaiakeMERSGEVAVRKHLQRASLNNIMGSVFgrRYDFEAGNEEAE------ELGE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 231 LVvkrNNQF-----FRYKDFLYFLT---PCGRRFhRACRL---VHDFTDAVIQERRRTLTSQGVDDFlqakaksktlDFI 299
Cdd:cd11076   143 MV---REGYellgaFNWSDHLPWLRwldLQGIRR-RCSALvprVNTFVGKIIEEHRAKRSNRARDDE----------DDV 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 300 DVLLlSEDKNGKeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKEiewDDLAQL 378
Cdd:cd11076   209 DVLL-SLQGEEK-LSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVgGSRRVAD---SDVAKL 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1370474309 379 PFLTMCLKESLRLHPPIP--TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11076   284 PYLQAVVKETLRLHPPGPllSWARLAIHDVTV-GGHVVPAG 323
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 141-417 2.49e-21

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


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 95.39  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 141 GDKWRHHRR-LLTPAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGS---TCLDVFEHislmTLDSLQKCIfSFDSNCQE 216
Cdd:cd11075    61 GPLWRTLRRnLVSEVLSPSRLKQFRPARRRALDNLVERLREEAKENPgpvNVRDHFRH----ALFSLLLYM-CFGERLDE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 217 KPSEYITAIMELSALVVKRnnqfFRYKDFLYFLTPCGRRfHRACRLVH------DFTDAVIQERRRTLTSQGVDdflqaK 290
Cdd:cd11075   136 ETVRELERVQRELLLSFTD----FDVRDFFPALTWLLNR-RRWKKVLElrrrqeEVLLPLIRARRKRRASGEAD-----K 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 291 AKSKTLDFIDVLLLSEDKnGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRepKEI 370
Cdd:cd11075   206 DYTDFLLLDLLDLKEEGG-ERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDE--AVV 282

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370474309 371 EWDDLAQLPFLTMCLKESLRLHPPIPTF-ARGCTQDVVLpDSRVIPKG 417
Cdd:cd11075   283 TEEDLPKMPYLKAVVLETLRRHPPGHFLlPHAVTEDTVL-GGYDIPAG 329
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 276-417 6.92e-21

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: 93.86  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 276 RTLTSQGVDDFLQAKAKSKTLDFIDV---LLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQE 352
Cdd:cd11062   180 QESIAKQVDEVLRQVSAGDPPSIVTSlfhALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILE 259

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370474309 353 RCRQEVQELLKDRePKEIEWDDLAQLPFLTMCLKESLRLHPPIPT-FARGCTQDVVLPDSRVIPKG 417
Cdd:cd11062   260 RLREELKTAMPDP-DSPPSLAELEKLPYLTAVIKEGLRLSYGVPTrLPRVVPDEGLYYKGWVIPPG 324
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 138-417 2.16e-20

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: 92.66  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 138 LSVGD---KWRHHRRLLTPAFHfNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLqkCIFSFDSNC 214
Cdd:cd11027    53 IAFGDyspTWKLHRKLAHSALR-LYASGGPRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVI--CSITFGKRY 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 215 QEKPSEYiTAIMELsalvvkrNNQFFRY------KDFLYFL----TPCGRRFHRACRLVHDFTDAVIQERRRTLTSQGVD 284
Cdd:cd11027   130 KLDDPEF-LRLLDL-------NDKFFELlgagslLDIFPFLkyfpNKALRELKELMKERDEILRKKLEEHKETFDPGNIR 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 285 DFLQAkaksktldFIDVLLLSEDKNGK---ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEV-QE 360
Cdd:cd11027   202 DLTDA--------LIKAKKEAEDEGDEdsgLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELdDV 273

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474309 361 LLKDREPkeiEWDDLAQLPFLTMCLKESLRLHPPIPT-FARGCTQDVVLPDSRvIPKG 417
Cdd:cd11027   274 IGRDRLP---TLSDRKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTLRGYT-IPKG 327
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 180-414 1.13e-19

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: 90.21  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 180 RLAMEGSTCLDVFEHISLMTLDSLQKCIF--SFDSNCQEKpseYITAIMELSALVVKRNNQ-FFRYKDFLYFLTPCGRRF 256
Cdd:cd11072    99 RESASSSSPVNLSELLFSLTNDIVCRAAFgrKYEGKDQDK---FKELVKEALELLGGFSVGdYFPSLGWIDLLTGLDRKL 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 257 HRACRLVHDFTDAVIQERRRTLTSQGVDDFLqakaksktLDFIDVLLLSEDKNGKELSDEDIRAE-ADTFmFGGHDTTAS 335
Cdd:cd11072   176 EKVFKELDAFLEKIIDEHLDKKRSKDEDDDD--------DDLLDLRLQKEGDLEFPLTRDNIKAIiLDMF-LAGTDTSAT 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 336 GLSWVLYNLARHPEYQERCRQEVQELLKDRepKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFA-RGCTQDVVL------ 408
Cdd:cd11072   247 TLEWAMTELIRNPRVMKKAQEEVREVVGGK--GKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLpRECREDCKIngydip 324


                  ....*.
gi 1370474309 409 PDSRVI 414
Cdd:cd11072   325 AKTRVI 330
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 303-417 3.30e-19

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: 88.79  E-value: 3.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 303 LLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKeieWDDLAQLPFL 381
Cdd:cd11065   209 LLEELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVgPDRLPT---FEDRPNLPYV 285

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370474309 382 TMCLKESLRLHPPIPT-FARGCTQDVVLpDSRVIPKG 417
Cdd:cd11065   286 NAIVKEVLRWRPVAPLgIPHALTEDDEY-EGYFIPKG 321
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 283-417 4.40e-19

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: 88.71  E-value: 4.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 283 VDDFLQAKAKSKTLDFidvllLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL 362
Cdd:cd20645   197 IDKRLQRYSQGPANDF-----LCDIYHDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVL 271

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370474309 363 KDREPKEIEwdDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDsRVIPKG 417
Cdd:cd20645   272 PANQTPRAE--DLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGD-YLLPKG 323
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 245-417 1.34e-18

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: 87.35  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 245 FLYFLTPCGRRFHRACRLVhdftDAVIQERRRtltsqgvdDFLQAKAKSKTLDFIDVL--LLSEDKNGKELSDEDIraeA 322
Cdd:cd11041   165 LVAPFLPEPRRLRRLLRRA----RPLIIPEIE--------RRRKLKKGPKEDKPNDLLqwLIEAAKGEGERTPYDL---A 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 323 DTFM---FGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDrepkEIEWDD--LAQLPFLTMCLKESLRLHPPIP- 396
Cdd:cd11041   230 DRQLalsFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAE----HGGWTKaaLNKLKKLDSFMKESQRLNPLSLv 305

                         170       180
                  ....*....|....*....|.
gi 1370474309 397 TFARGCTQDVVLPDSRVIPKG 417
Cdd:cd11041   306 SLRRKVLKDVTLSDGLTLPKG 326
PTZ00404 PTZ00404
cytochrome P450; Provisional
 75-417 5.29e-18

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 85.54  E-value: 5.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  75 RVLTQLVATYPQGFVRWLGPITPIInLCHPDIVRSV-INTSDAITDKdiVFYKTLK-PWLGDGLLLSVGDKWRHHRRLLT 152
Cdd:PTZ00404   52 RDLTKMSKKYGGIFRIWFADLYTVV-LSDPILIREMfVDNFDNFSDR--PKIPSIKhGTFYHGIVTSSGEYWKRNREIVG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 153 PAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTcldvFE---HISLMTLDSLQKCIFSFDSNCQEKPSEyitaiMELS 229
Cdd:PTZ00404  129 KAMRKTNLKHIYDLLDDQVDVLIESMKKIESSGET----FEpryYLTKFTMSAMFKYIFNEDISFDEDIHN-----GKLA 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 230 ALVVKRNNQFfryKDF----------------LYFLTPCGRRFHRacrlVHDFTDAVIQERRRTLTSQGVDDFLQakaks 293
Cdd:PTZ00404  200 ELMGPMEQVF---KDLgsgslfdvieitqplyYQYLEHTDKNFKK----IKKFIKEKYHEHLKTIDPEVPRDLLD----- 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 294 ktldfidvLLLSEDKNGkelSDEDIRAEADT---FMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpkEI 370
Cdd:PTZ00404  268 --------LLIKEYGTN---TDDDILSILATildFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRN--KV 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1370474309 371 EWDDLAQLPFLTMCLKESLRLHPPIP-TFARGCTQDVVLPDSRVIPKG 417
Cdd:PTZ00404  335 LLSDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDIIIGGGHFIPKD 382
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 20-396 6.61e-18

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 85.64  E-value: 6.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  20 LLLLVVGASWLLARIL-AWTYAFYHNGRRLrcfpQPRKQNW-FLGHLGLVTPTEEglRVLTQLVATY-PQGFVRwLGPIt 96
Cdd:PLN03112    4 FLLSLLFSVLIFNVLIwRWLNASMRKSLRL----PPGPPRWpIVGNLLQLGPLPH--RDLASLCKKYgPLVYLR-LGSV- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  97 PIINLCHPDIVRSVINTSDAI-------TDKDIVFYKTlkpwlGDGLLLSVGDKWRHHRR-----LLTPafhfNILKPYI 164
Cdd:PLN03112   76 DAITTDDPELIREILLRQDDVfasrprtLAAVHLAYGC-----GDVALAPLGPHWKRMRRicmehLLTT----KRLESFA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 165 KIFSKSANIM-HAKWQRLAMEGSTCL-DVFEHISL--MTLDSLQKCIFSFDSNCQEKPSEYITAIMELSALVvkrnnQFF 240
Cdd:PLN03112  147 KHRAEEARHLiQDVWEAAQTGKPVNLrEVLGAFSMnnVTRMLLGKQYFGAESAGPKEAMEFMHITHELFRLL-----GVI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 241 RYKDFLYF-----LTPCGRRFHRACRLVHDFTDAVIQERRRTLTSQgvddflqaKAKSKTLDFIDVLLLSEDKNGKE-LS 314
Cdd:PLN03112  222 YLGDYLPAwrwldPYGCEKKMREVEKRVDEFHDKIIDEHRRARSGK--------LPGGKDMDFVDVLLSLPGENGKEhMD 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 315 DEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKEiewDDLAQLPFLTMCLKESLRLHP 393
Cdd:PLN03112  294 DVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVgRNRMVQE---SDLVHLNYLRCVVRETFRMHP 370


                  ...
gi 1370474309 394 PIP 396
Cdd:PLN03112  371 AGP 373
PLN02183 PLN02183
ferulate 5-hydroxylase
 209-416 7.61e-18

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 85.29  E-value: 7.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 209 SFDSNCQEKPSEYITAIMELSALVVKrnnqfFRYKDFLYFL---TPCG--RRFHRACRLVHDFTDAVIQERRRTLTSQGV 283
Cdd:PLN02183  189 AFGSSSNEGQDEFIKILQEFSKLFGA-----FNVADFIPWLgwiDPQGlnKRLVKARKSLDGFIDDIIDDHIQKRKNQNA 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 284 DDFlqakAKSKTLDFIDVLL--LSED---------KNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQE 352
Cdd:PLN02183  264 DND----SEEAETDMVDDLLafYSEEakvnesddlQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLK 339

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370474309 353 RCRQEVQELLK-DREpkeIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPK 416
Cdd:PLN02183  340 RVQQELADVVGlNRR---VEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEV-AGYFIPK 400
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 210-417 2.00e-17

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 83.62  E-value: 2.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 210 FDSNCQEKPSEYITAIMELSALVvkrnnQFFRYKDF---LYFLTPCG--RRFHRACRLVHDFTDAVIQERRRTLTSQGVD 284
Cdd:cd20657   130 FAAKAGAKANEFKEMVVELMTVA-----GVFNIGDFipsLAWMDLQGveKKMKRLHKRFDALLTKILEEHKATAQERKGK 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 285 DflqakaksktlDFIDVLLLSEDKN--GKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL 362
Cdd:cd20657   205 P-----------DFLDFVLLENDDNgeGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVI 273

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370474309 363 -KDREPKEiewDDLAQLPFLTMCLKESLRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20657   274 gRDRRLLE---SDIPNLPYLQAICKETFRLHPSTPlNLPRIASEACEV-DGYYIPKG 326
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 297-417 3.99e-17

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: 82.65  E-value: 3.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 297 DFIDVLL-LSEDKNGK-ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKEIewd 373
Cdd:cd20655   206 DLLDILLdAYEDENAEyKITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVgKTRLVQES--- 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370474309 374 DLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20655   283 DLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKI-NGYDIPEK 325
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 135-400 6.52e-17

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: 82.02  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 135 GLLLSVGDKWRHHRRLLTPafhfNILKP-----YIKIFSKSANIMHAKWQRLAME---GSTCLDV--------FEHISLM 198
Cdd:cd20646    57 GPFTEEGEKWYRLRSVLNQ----RMLKPkevslYADAINEVVSDLMKRIEYLRERsgsGVMVSDLanelykfaFEGISSI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 199 TLDSLQKCIfsfDSNCQEKPSEYITAImelsalvvkrnNQFFRYKDFLYFLT-------PCGRRFHRACRLVHDFTDAVI 271
Cdd:cd20646   133 LFETRIGCL---EKEIPEETQKFIDSI-----------GEMFKLSEIVTLLPkwtrpylPFWKRYVDAWDTIFSFGKKLI 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 272 QERRRTLTSQGVDDflqAKAKSKTLDFidvlLLSEDKngkeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQ 351
Cdd:cd20646   199 DKKMEEIEERVDRG---EPVEGEYLTY----LLSSGK----LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQ 267

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370474309 352 ERCRQEVQELLK-DREPKEiewDDLAQLPFLTMCLKESLRLHPPIPTFAR 400
Cdd:cd20646   268 ERLYQEVISVCPgDRIPTA---EDIAKMPLLKAVIKETLRLYPVVPGNAR 314
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 261-417 1.43e-16

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: 81.14  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 261 RLVHDFTDAVIQERRRtltsqgvddfLQAKAKSKTL-DFIDVLLLSEDKNGKELSDEDIRAEAD--------TFMFGGHD 331
Cdd:cd11082   165 RIVKTLEKCAAKSKKR----------MAAGEEPTCLlDFWTHEILEEIKEAEEEGEPPPPHSSDeeiagtllDFLFASQD 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 332 TTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDS 411
Cdd:cd11082   235 ASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEP-PLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTED 313


                  ....*.
gi 1370474309 412 RVIPKG 417
Cdd:cd11082   314 YTVPKG 319
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 136-417 1.46e-16

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 81.19  E-value: 1.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 136 LLLSVGDKWRHHRRLL----TPAFHFNILKPyiKIFSKSANIMHAkWQ---RLAmEGSTcLDVFEHISLMTLDSLqkCIF 208
Cdd:cd20622    54 LVKSTGPAFRKHRSLVqdlmTPSFLHNVAAP--AIHSKFLDLIDL-WEakaRLA-KGRP-FSAKEDIHHAALDAI--WAF 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 209 SFDSNC-------------------------------QEKPSEYITAIMELS-ALVVKRNNQFFRYKDFLYFLTPcgrRF 256
Cdd:cd20622   127 AFGINFdasqtrpqlelleaedstilpagldepvefpEAPLPDELEAVLDLAdSVEKSIKSPFPKLSHWFYRNQP---SY 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 257 HRACRLVHDFTDAVIQERRRTLTSQGVDDflqaKAKSKtldfIDVLLLSED----KNGKE--LSDEDIRAEADTFMFGGH 330
Cdd:cd20622   204 RRAAKIKDDFLQREIQAIARSLERKGDEG----EVRSA----VDHMVRRELaaaeKEGRKpdYYSQVIHDELFGYLIAGH 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 331 DTTASGLSWVLYNLARHPEYQERCRQEVQELL-----KDREP--KEIEwddLAQLPFLTMCLKESLRLHPPIPTFARGCT 403
Cdd:cd20622   276 DTTSTALSWGLKYLTANQDVQSKLRKALYSAHpeavaEGRLPtaQEIA---QARIPYLDAVIEEILRCANTAPILSREAT 352

                         330
                  ....*....|....*
gi 1370474309 404 QD-VVLpdSRVIPKG 417
Cdd:cd20622   353 VDtQVL--GYSIPKG 365
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 141-396 1.62e-16

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 81.32  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 141 GDKWRHHRRLLT-PAFHFNILKPYIKIFSKSANIMHAKWQRLAMEGSTCLDVFEHISLMTLDSLQKCIFS--FDSncQEK 217
Cdd:PLN02394  121 GDHWRKMRRIMTvPFFTNKVVQQYRYGWEEEADLVVEDVRANPEAATEGVVIRRRLQLMMYNIMYRMMFDrrFES--EDD 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 218 PseyitAIMELSALVVKRNN--QFFRYK--DFLYFLTPCGRRFHRACRLVHD-----FTDAVIQERRRTLTSQGVDdflq 288
Cdd:PLN02394  199 P-----LFLKLKALNGERSRlaQSFEYNygDFIPILRPFLRGYLKICQDVKErrlalFKDYFVDERKKLMSAKGMD---- 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 289 aKAKSKTLdfIDVLLLSEDKNgkELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPk 368
Cdd:PLN02394  270 -KEGLKCA--IDHILEAQKKG--EINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQ- 343

                         250       260
                  ....*....|....*....|....*...
gi 1370474309 369 eIEWDDLAQLPFLTMCLKESLRLHPPIP 396
Cdd:PLN02394  344 -VTEPDTHKLPYLQAVVKETLRLHMAIP 370
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 132-417 3.09e-16

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


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 80.24  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 132 LGDGLLLSVGD-KWRHHRRLLTPAFHFNILKPYIKIFSKSANIMHAKWqrlaMEGSTCLDVFEHISLMTLDSLQKCIFSF 210
Cdd:cd20638    66 LGSGCLSNLHDsQHKHRKKVIMRAFSREALENYVPVIQEEVRSSVNQW----LQSGPCVLVYPEVKRLMFRIAMRILLGF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 211 DSNCQEKPSE--YITAIMELSalvvkrNNQFFRYKDF----LYfltpcgrRFHRACRLVHDFTDAVIQER-RRTLTSQGV 283
Cdd:cd20638   142 EPQQTDREQEqqLVEAFEEMI------RNLFSLPIDVpfsgLY-------RGLRARNLIHAKIEENIRAKiQREDTEQQC 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 284 DDFLQakaksktldfidVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQE--L 361
Cdd:cd20638   209 KDALQ------------LLIEHSRRNGEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEkgL 276

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474309 362 L--KDREPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20638   277 LstKPNENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFEL-NGYQIPKG 333
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 303-418 8.21e-16

cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain cleavage enzyme; Cytochrome P450 11A1 (CYP11A1, EC 1.14.15.6) is also called cholesterol side-chain cleavage enzyme, cholesterol desmolase, or cytochrome P450(scc). It catalyzes the side-chain cleavage reaction of cholesterol to form pregnenolone, the precursor of all steroid hormones. Missense or nonsense mutations of the CYP11A1 gene cause mild to severe early-onset adrenal failure depending on the severity of the enzyme dysfunction/deficiency. CYP11A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 78.60  E-value: 8.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 303 LLSEDKngkeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREpkeiewDDLAQL---- 378
Cdd:cd20643   224 LLLQDK----LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQ------GDMVKMlksv 293

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370474309 379 PFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRVIPKGL 418
Cdd:cd20643   294 PLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTL 333
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 311-417 1.88e-15

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: 77.65  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 311 KELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEwdDLAQLPFLTMCLKESLR 390
Cdd:cd20647   231 KELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAE--DVPKLPLIRALLKETLR 308

                          90       100
                  ....*....|....*....|....*..
gi 1370474309 391 LHPPIPTFARgCTQDVVLPDSRVIPKG 417
Cdd:cd20647   309 LFPVLPGNGR-VTQDDLIVGGYLIPKG 334
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 130-417 3.89e-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: 76.19  E-value: 3.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 130 PWLGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIK-IFSKsanIMHAKWQRLAMEGSTclDVFEHISLmtldslqkcif 208
Cdd:cd20629    42 PFLGHSILAMDGEEHRRRRRLLQPAFAPRAVARWEEpIVRP---IAEELVDDLADLGRA--DLVEDFAL----------- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 209 sfdsncqEKPSEYITAIMELSAlvvKRNNQFFR--YKDFLYFLTPCGRRFHRACRLVHDFTDAV---IQERRRTLTsqgv 283
Cdd:cd20629   106 -------ELPARVIYALLGLPE---EDLPEFTRlaLAMLRGLSDPPDPDVPAAEAAAAELYDYVlplIAERRRAPG---- 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 284 DDFLQAkaksktldfidvlLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQevqellk 363
Cdd:cd20629   172 DDLISR-------------LLRAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRR------- 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370474309 364 DRE--PKEIEwddlaqlpfltmclkESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20629   232 DRSliPAAIE---------------EGLRWEPPVASVPRMALRDVEL-DGVTIPAG 271
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 259-417 8.73e-15

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 75.87  E-value: 8.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 259 ACRLVHDFTDAVIQERRRtltsqgvddflQAKAKSKTL--DFIDVLLLSEDKNGKEL-SDEDIRAEADTFMFGGHDTTAS 335
Cdd:cd20658   187 AMRIIRKYHDPIIDERIK-----------QWREGKKKEeeDWLDVFITLKDENGNPLlTPDEIKAQIKELMIAAIDNPSN 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 336 GLSWVLYNLARHPEYQERCRQEVQELL-KDREPKEiewDDLAQLPFLTMCLKESLRLHPPIPTF-ARGCTQDVVLPDSRv 413
Cdd:cd20658   256 AVEWALAEMLNQPEILRKATEELDRVVgKERLVQE---SDIPNLNYVKACAREAFRLHPVAPFNvPHVAMSDTTVGGYF- 331


                  ....
gi 1370474309 414 IPKG 417
Cdd:cd20658   332 IPKG 335
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 274-417 2.33e-14

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: 74.40  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 274 RRRTLTSQG-VDDFLQ-----AKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARH 347
Cdd:cd20614   159 ARRSRRARAwIDARLSqlvatARANGARTGLVAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEH 238

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 348 PEYQERCRQEVQELlkDREPKEIEwdDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20614   239 PAVWDALCDEAAAA--GDVPRTPA--ELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIEL-GGRRIPAG 303
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 133-417 2.53e-14

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: 74.37  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 133 GDGLLLSVGDKWRHHRRLLTpafhfNILKPY-IKIFSKSANIMHAkwqRLAMEGSTCLDVFEHISLMTLDSLQKCIFSFd 211
Cdd:cd20652    46 GNGIICAEGDLWRDQRRFVH-----DWLRQFgMTKFGNGRAKMEK---RIATGVHELIKHLKAESGQPVDPSPVLMHSL- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 212 sncqekpSEYITAIMelSALVVKRNNQFFRYKDFLY--------------FLtPCGRRFHRACRLV----------HDFT 267
Cdd:cd20652   117 -------GNVINDLV--FGFRYKEDDPTWRWLRFLQeegtkligvagpvnFL-PFLRHLPSYKKAIeflvqgqaktHAIY 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 268 DAVIQERRRTLTSQGVDDflQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIR-AEADtfMFG-GHDTTASGLSWVLYNLA 345
Cdd:cd20652   187 QKIIDEHKRRLKPENPRD--AEDFELCELEKAKKEGEDRDLFDGFYTDEQLHhLLAD--LFGaGVDTTITTLRWFLLYMA 262

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370474309 346 RHPEYQERCRQEVQELLKDrePKEIEWDDLAQLPFLTMCLKESLRLHPPIPT-FARGCTQDVVLPDSRvIPKG 417
Cdd:cd20652   263 LFPKEQRRIQRELDEVVGR--PDLVTLEDLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVLAGYR-IPKG 332
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 132-417 3.51e-14

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 73.96  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 132 LGDGLLLSVGDKWRHHRRLLT--------PAFHFNILKPYIKifSKSANIMHAkwqrLAMEGSTCL----DVFEHISLmt 199
Cdd:PLN02426  119 LGRGIFNVDGDSWRFQRKMASlelgsvsiRSYAFEIVASEIE--SRLLPLLSS----AADDGEGAVldlqDVFRRFSF-- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 200 lDSLQKCIFSFDSNCQEKP---SEYITAIMELSALVVKR----NNQFFRYKDFLYFLTPcgRRFHRACRLVHDFTDAVIQ 272
Cdd:PLN02426  191 -DNICKFSFGLDPGCLELSlpiSEFADAFDTASKLSAERamaaSPLLWKIKRLLNIGSE--RKLKEAIKLVDELAAEVIR 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 273 ERRRTLTSqGVDDFLqakakSKTLDFIDvlllsedkngkelSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQE 352
Cdd:PLN02426  268 QRRKLGFS-ASKDLL-----SRFMASIN-------------DDKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVAS 328

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370474309 353 RCRQEVQELLKDREpKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSRVIPKG 417
Cdd:PLN02426  329 AIREEADRVMGPNQ-EAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTFVAKG 392
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 139-396 8.54e-14

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: 72.64  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 139 SVGDKWRHHRRLLTpafhfnilkpyIKIFS-----KSANIMHAKWQRL-------AMEGSTCLDVFEHISLMTLDSLQ-- 204
Cdd:cd20653    56 PYGDHWRNLRRITT-----------LEIFSshrlnSFSSIRRDEIRRLlkrlardSKGGFAKVELKPLFSELTFNNIMrm 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 205 ---KCIFSFDSNCQEKPS---EYITAIMELSALvvkrNNQ-----FFRYKDFLYFLtpcgRRFHRACRLVHDFTDAVIQE 273
Cdd:cd20653   125 vagKRYYGEDVSDAEEAKlfrELVSEIFELSGA----GNPadflpILRWFDFQGLE----KRVKKLAKRRDAFLQGLIDE 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 274 RRRTLTSqgvddflqakaKSKTLdfIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQER 353
Cdd:cd20653   197 HRKNKES-----------GKNTM--IDHLLSLQESQPEYYTDEIIKGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKK 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370474309 354 CRQEVQELLKdrEPKEIEWDDLAQLPFLTMCLKESLRLHPPIP 396
Cdd:cd20653   264 AREEIDTQVG--QDRLIEESDLPKLPYLQNIISETLRLYPAAP 304
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 254-417 2.18e-13

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 71.40  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 254 RRFHRACRLVHDFTDAVIQERrrtltsqgvddfLQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTT 333
Cdd:cd20636   176 RKGIKARDILHEYMEKAIEEK------------LQRQQAAEYCDALDYMIHSARENGKELTMQELKESAVELIFAAFSTT 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 334 ASGLSWVLYNLARHPEYQERCRQEV--QELLKDRE--PKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLp 409
Cdd:cd20636   244 ASASTSLVLLLLQHPSAIEKIRQELvsHGLIDQCQccPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFEL- 322


                  ....*...
gi 1370474309 410 DSRVIPKG 417
Cdd:cd20636   323 DGYQIPKG 330
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 273-396 3.66e-13

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


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 70.59  E-value: 3.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 273 ERRRTLTSQGVDDFLQAKAKSKT-LDFIDVLLLSEDKngKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQ 351
Cdd:cd20656   187 ARRDRLTKAIMEEHTLARQKSGGgQQHFVALLTLKEQ--YDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQ 264

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370474309 352 ERCRQEVQELL-KDREPKEIewdDLAQLPFLTMCLKESLRLHPPIP 396
Cdd:cd20656   265 EKAQEELDRVVgSDRVMTEA---DFPQLPYLQCVVKEALRLHPPTP 307
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 312-417 5.49e-13

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: 70.09  E-value: 5.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 312 ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEWDD---LAQLPFLTMCLKES 388
Cdd:cd11040   218 GLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDLtdlLTSCPLLDSTYLET 297

                          90       100
                  ....*....|....*....|....*....
gi 1370474309 389 LRLHPPIPTfARGCTQDVVLPDSRVIPKG 417
Cdd:cd11040   298 LRLHSSSTS-VRLVTEDTVLGGGYLLRKG 325
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 229-417 6.78e-13

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: 69.70  E-value: 6.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 229 SALVVKRNNQFFRYKDFL-----YFLTP-CGRRFHRACRLVHDFTDAVIQERRRTLTsqgvddflQAKAKSKTLDFIDVL 302
Cdd:cd20616   140 KAIVLKIQGYFDAWQALLikpdiFFKISwLYKKYEKAVKDLKDAIEILIEQKRRRIS--------TAEKLEDHMDFATEL 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 303 LLSEdkNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEiewDDLAQLPFLT 382
Cdd:cd20616   212 IFAQ--KRGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQN---DDLQKLKVLE 286

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370474309 383 MCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20616   287 NFINESMRYQPVVDFVMRKALEDDVI-DGYPVKKG 320
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 220-396 8.61e-13

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 69.84  E-value: 8.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 220 EYITAIMELSALvvkrnnqfFRYKDF---LYFLTPCG-----RRFHRAcrlVHDFTDAVIQERRRTltsqgvddflQAKA 291
Cdd:PLN02687  208 EMVVELMQLAGV--------FNVGDFvpaLRWLDLQGvvgkmKRLHRR---FDAMMNGIIEEHKAA----------GQTG 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 292 KSKTLDFIDVLLL-----SEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDR 365
Cdd:PLN02687  267 SEEHKDLLSTLLAlkreqQADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVgRDR 346

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370474309 366 EPKEIewdDLAQLPFLTMCLKESLRLHPPIP 396
Cdd:PLN02687  347 LVSES---DLPQLTYLQAVIKETFRLHPSTP 374
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 253-417 1.05e-12

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 69.36  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 253 GRRFHRACR----LVHDFTDaVIQERRrtltsqgvddFLQAK-AKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMF 327
Cdd:PLN02302  229 GFAYHRALKarkkLVALFQS-IVDERR----------NSRKQnISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLN 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 328 GGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREP--KEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQD 405
Cdd:PLN02302  298 AGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKRPPgqKGLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTD 377

                         170
                  ....*....|..
gi 1370474309 406 VVLpDSRVIPKG 417
Cdd:PLN02302  378 VEV-NGYTIPKG 388
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 312-416 1.17e-12

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: 69.01  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 312 ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEwdDLAQLPFLTMCLKESLRL 391
Cdd:cd20648   229 KLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAA--DVARMPLLKAVVKEVLRL 306

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370474309 392 HPPIPTFARgctqdvVLPDSR------VIPK 416
Cdd:cd20648   307 YPVIPGNAR------VIPDRDiqvgeyIIPK 331
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 312-417 2.05e-12

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: 68.33  E-value: 2.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 312 ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKD--REPKEIewddLAQLPFLTMCLKESL 389
Cdd:cd20644   227 ELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQisEHPQKA----LTELPLLKAALKETL 302

                          90       100
                  ....*....|....*....|....*...
gi 1370474309 390 RLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd20644   303 RLYPVGITVQRVPSSDLVLQNYH-IPAG 329
PLN03018 PLN03018
homomethionine N-hydroxylase
 260-417 3.01e-12

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 68.11  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 260 CRLVHDFTDAVIQERRRTLTSQGvddflqakAKSKTLDFIDVLLLSEDKNGKEL-SDEDIRAEADTFMFGGHDTTASGLS 338
Cdd:PLN03018  264 VNLVRSYNNPIIDERVELWREKG--------GKAAVEDWLDTFITLKDQNGKYLvTPDEIKAQCVEFCIAAIDNPANNME 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 339 WVLYNLARHPEYQERCRQEVQELL-KDREPKEiewDDLAQLPFLTMCLKESLRLHPPI----PTFARgctQDVVLpDSRV 413
Cdd:PLN03018  336 WTLGEMLKNPEILRKALKELDEVVgKDRLVQE---SDIPNLNYLKACCRETFRIHPSAhyvpPHVAR---QDTTL-GGYF 408


                  ....
gi 1370474309 414 IPKG 417
Cdd:PLN03018  409 IPKG 412
PLN02655 PLN02655
ent-kaurene oxidase
 267-396 3.39e-12

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 67.84  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 267 TDAVIQERRRTLTSqgvddflqAKAKSKTLDFidvlLLSEDKNgkeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLAR 346
Cdd:PLN02655  227 MKALIKQQKKRIAR--------GEERDCYLDF----LLSEATH---LTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAK 291

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370474309 347 HPEYQERCRQEVQELLKDREPKEiewDDLAQLPFLTMCLKESLRLHPPIP 396
Cdd:PLN02655  292 NPDKQERLYREIREVCGDERVTE---EDLPNLPYLNAVFHETLRKYSPVP 338
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 141-396 4.41e-12

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 67.50  E-value: 4.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 141 GDKWRHHRRLLT-PAFHFNILKPYIKIF-SKSANIMH-AKWQRLAMEGSTCLDvfEHISLMTLDSLQKCIFSFDSNCQEK 217
Cdd:cd11074    61 GEHWRKMRRIMTvPFFTNKVVQQYRYGWeEEAARVVEdVKKNPEAATEGIVIR--RRLQLMMYNNMYRIMFDRRFESEDD 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 218 PseyitAIMELSALVVKRNN--QFFRYK--DFLYFLTPCGRRFHRACRLVHD-----FTDAVIQERRRTLTSQGVDDFLQ 288
Cdd:cd11074   139 P-----LFVKLKALNGERSRlaQSFEYNygDFIPILRPFLRGYLKICKEVKErrlqlFKDYFVDERKKLGSTKSTKNEGL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 289 AKAksktldfIDVLLLSEDKNgkELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKdREPK 368
Cdd:cd11074   214 KCA-------IDHILDAQKKG--EINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLG-PGVQ 283

                         250       260
                  ....*....|....*....|....*...
gi 1370474309 369 EIEwDDLAQLPFLTMCLKESLRLHPPIP 396
Cdd:cd11074   284 ITE-PDLHKLPYLQAVVKETLRLRMAIP 310
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 284-417 7.48e-12

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: 66.47  E-value: 7.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 284 DDFLQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERcrqevqeLLK 363
Cdd:cd11078   176 ADLVAERRREPRDDLISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRR-------LRA 248

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370474309 364 DRE--PKEIEwddlaqlpfltmclkESLRLHPPIPTFARGCTQDVVLPDSRvIPKG 417
Cdd:cd11078   249 DPSliPNAVE---------------ETLRYDSPVQGLRRTATRDVEIGGVT-IPAG 288
PLN02966 PLN02966
cytochrome P450 83A1
 273-405 7.90e-12

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 66.69  E-value: 7.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 273 ERRRTLTSQGVDDFLQAK-AKSKTLDFIDVLL--LSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPE 349
Cdd:PLN02966  242 ERQDTYIQEVVNETLDPKrVKPETESMIDLLMeiYKEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQ 321

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370474309 350 YQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTF-ARGCTQD 405
Cdd:PLN02966  322 VLKKAQAEVREYMKEKGSTFVTEDDVKNLPYFRALVKETLRIEPVIPLLiPRACIQD 378
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 132-393 1.04e-11

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: 66.16  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 132 LGDGLLLSVGDKWRHHRRLLTPAFHFNILKPYIKIFSKSAnimhAKWQRLAMEGSTCLDVFehislmTLDSLQKC-IFSF 210
Cdd:cd20615    48 LGQCVGLLSGTDWKRVRKVFDPAFSHSAAVYYIPQFSREA----RKWVQNLPTNSGDGRRF------VIDPAQALkFLPF 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 211 dsncqekpseYITAIM-----------ELSALVVKRNNQF--------FRYKDFLYFLTPCGRR---FHRACRlvhDFTD 268
Cdd:cd20615   118 ----------RVIAEIlygelspeekeELWDLAPLREELFkyvikgglYRFKISRYLPTAANRRlreFQTRWR---AFNL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 269 AVIQERRRTLTSQGVDDFLQAKAKSKT-----LDFIDVLLlsedkngkelsdediraeadtfmFGGHDTTASGLSWVLYN 343
Cdd:cd20615   185 KIYNRARQRGQSTPIVKLYEAVEKGDItfeelLQTLDEML-----------------------FANLDVTTGVLSWNLVF 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370474309 344 LARHPEYQERCRQEVQELLKDREPkeiEWDD--LAQLPFLTMCLKESLRLHP 393
Cdd:cd20615   242 LAANPAVQEKLREEISAAREQSGY---PMEDyiLSTDTLLAYCVLESLRLRP 290
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 306-417 1.51e-11

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: 65.78  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 306 EDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIewDDLAQLPFLTMCL 385
Cdd:cd11028   220 EEKPEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRL--SDRPNLPYTEAFI 297

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370474309 386 KESLRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11028   298 LETMRHSSFVPfTIPHATTRDTTL-NGYFIPKG 329
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 101-417 3.21e-11

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: 64.42  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 101 LCHPDiVRSVINTSDAITDKDIVFYKtlKPWLGDGLLLSVGDKwRH--HRRLLTPAFHFNILKPYIKIFSKSANIMhakW 178
Cdd:cd11080    15 SRYED-VRRILKDPDGFTTKSLAERA--EPVMRGPVLAQMTGK-EHaaKRAIVVRAFRGDALDHLLPLIKENAEEL---I 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 179 QRLAMEGStcLDVFEHISL-----MTLDSLqkcifSFDSNCQEKPSEYITAIMELSALVVkrnnqffrykdflyfLTPCG 253
Cdd:cd11080    88 APFLERGR--VDLVNDFGKpfavnVTMDML-----GLDKRDHEKIHEWHSSVAAFITSLS---------------QDPEA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 254 RRFHRACR-LVHDFTDAVIQERRRTLTSqgvddflqakaksktlDFIDVLLLSEdKNGKELSDEDIRAEADTFMFGGHDT 332
Cdd:cd11080   146 RAHGLRCAeQLSQYLLPVIEERRVNPGS----------------DLISILCTAE-YEGEALSDEDIKALILNVLLAATEP 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 333 TASGLSWVLYNLARHPEYQERCRQevqellkDREpkeiewddlaqlpFLTMCLKESLRLHPPIPTFARGCTQDVVLPDSR 412
Cdd:cd11080   209 ADKTLALMIYHLLNNPEQLAAVRA-------DRS-------------LVPRAIAETLRYHPPVQLIPRQASQDVVVSGME 268


                  ....*
gi 1370474309 413 vIPKG 417
Cdd:cd11080   269 -IKKG 272
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 237-417 3.55e-11

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: 64.55  E-value: 3.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 237 NQFFrykdFLYFLTP--CG-RRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFlqakaksktldfIDVLLlSEDKNGKEL 313
Cdd:cd20651   155 NQFP----WLRFIAPefSGyNLLVELNQKLIEFLKEEIKEHKKTYDEDNPRDL------------IDAYL-REMKKKEPP 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 314 S----DEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPkeiEWDDLAQLPFLTMCLKES 388
Cdd:cd20651   218 SssftDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVgRDRLP---TLDDRSKLPYTEAVILEV 294

                         170       180       190
                  ....*....|....*....|....*....|
gi 1370474309 389 LRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20651   295 LRIFTLVPiGIPHRALKDTTL-GGYRIPKD 323
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 263-417 5.45e-11

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: 63.73  E-value: 5.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 263 VHDFTDAVIQERRRTLTSqgvddflqakakSKTLDFIDVLLL--SEDKN--GKELSDEDIRAEADTFMFGGHDTTASGLS 338
Cdd:cd11026   180 IKSFIRELVEEHRETLDP------------SSPRDFIDCFLLkmEKEKDnpNSEFHEENLVMTVLDLFFAGTETTSTTLR 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 339 WVLYNLARHPEYQERCRQEVQELL-KDREPkeiEWDDLAQLPFLTMCLKESLRLHPPIPT-FARGCTQDVVLPDSRvIPK 416
Cdd:cd11026   248 WALLLLMKYPHIQEKVQEEIDRVIgRNRTP---SLEDRAKMPYTDAVIHEVQRFGDIVPLgVPHAVTRDTKFRGYT-IPK 323


                  .
gi 1370474309 417 G 417
Cdd:cd11026   324 G 324
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 306-417 1.51e-10

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 62.65  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 306 EDKNGkeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKE-IEWDDLAQLPFLTMC 384
Cdd:PLN02196  255 GDKEG--LTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGEsLTWEDTKKMPLTSRV 332

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370474309 385 LKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:PLN02196  333 IQETLRVASILSFTFREAVEDVEY-EGYLIPKG 364
PLN00168 PLN00168
Cytochrome P450; Provisional
 271-394 1.59e-10

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 62.66  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 271 IQERRRTLTSQGVDDFLQAKAKSKTLDFIDVLL---LSEDKNgKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARH 347
Cdd:PLN00168  258 IDARREYKNHLGQGGEPPKKETTFEHSYVDTLLdirLPEDGD-RALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKN 336

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370474309 348 PEYQERCRQEVQELLKDrEPKEIEWDDLAQLPFLTMCLKESLRLHPP 394
Cdd:PLN00168  337 PSIQSKLHDEIKAKTGD-DQEEVSEEDVHKMPYLKAVVLEGLRKHPP 382
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 297-415 4.00e-10

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: 60.81  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 297 DFIDVLLLSEdKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEvQELLkdrePKEIEwddla 376
Cdd:cd11034   171 DLISRLIEGE-IDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRLIAD-PSLI----PNAVE----- 239

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370474309 377 qlpfltmclkESLRLHPPIPTFARGCTQDVVLPDSRVIP 415
Cdd:cd11034   240 ----------EFLRFYSPVAGLARTVTQEVEVGGCRLKP 268
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 258-406 4.62e-10

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: 60.68  E-value: 4.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 258 RACRLVHDFTDAVIQERRRtltsQGVDDFLQAkaksktldfidvlLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGL 337
Cdd:cd11035   148 AAAQAVLDYLTPLIAERRA----NPGDDLISA-------------ILNAEIDGRPLTDDELLGLCFLLFLAGLDTVASAL 210

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370474309 338 SWVLYNLARHPEYQERCRQEvqellKDREPKEIEwddlaqlpfltmclkESLRLHPPiPTFARGCTQDV 406
Cdd:cd11035   211 GFIFRHLARHPEDRRRLRED-----PELIPAAVE---------------ELLRRYPL-VNVARIVTRDV 258
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 271-417 5.23e-10

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: 61.09  E-value: 5.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 271 IQERRRTLTSQGVDDFLQakaksktlDFIDVLLLSEdKNGKELSDED----IRAEADTFMFGGHDTTASGLSWVLYNLAR 346
Cdd:cd20654   200 LEEHRQKRSSSGKSKNDE--------DDDDVMMLSI-LEDSQISGYDadtvIKATCLELILGGSDTTAVTLTWALSLLLN 270

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370474309 347 HPEYQERCRQEVQELL-KDREpkeIEWDDLAQLPFLTMCLKESLRLHPPIPTFA-RGCTQDVVLPDSRViPKG 417
Cdd:cd20654   271 NPHVLKKAQEELDTHVgKDRW---VEESDIKNLVYLQAIVKETLRLYPPGPLLGpREATEDCTVGGYHV-PKG 339
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 237-396 7.85e-10

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 60.48  E-value: 7.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 237 NQFFRYKDFLYFLTPCGRRFHRACRLVhdftDAVIQErrrtLTSQGVDdflQAKAKSKTLDFIDVLL--LSEDKNGKELS 314
Cdd:PLN03234  217 SDLFPYFGFLDNLTGLSARLKKAFKEL----DTYLQE----LLDETLD---PNRPKQETESFIDLLMqiYKDQPFSIKFT 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 315 DEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDRepKEIEWDDLAQLPFLTMCLKESLRLHPP 394
Cdd:PLN03234  286 HENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDK--GYVSEEDIPNLPYLKAVIKESLRLEPV 363


                  ..
gi 1370474309 395 IP 396
Cdd:PLN03234  364 IP 365
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 287-417 9.51e-10

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 60.25  E-value: 9.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 287 LQAKAKSKTLDFIDVLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEV--QELLKD 364
Cdd:cd20637   196 LQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrsNGILHN 275

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370474309 365 --REPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20637   276 gcLCEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFEL-DGFQIPKG 329
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 297-396 9.80e-10

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: 60.12  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 297 DFIDVLLL-----SEDKNGKELSDEDIR-AEADTFMfGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKei 370
Cdd:cd20674   201 DMTDYMLQglgqpRGEKGMGQLLEGHVHmAVVDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASP-- 277

                          90       100
                  ....*....|....*....|....*.
gi 1370474309 371 EWDDLAQLPFLTMCLKESLRLHPPIP 396
Cdd:cd20674   278 SYKDRARLPLLNATIAEVLRLRPVVP 303
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 184-417 1.51e-09

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: 59.64  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 184 EGSTCLDVFEHISLMTLDSLQKCIFSFDSNCQeKPSEYITAIMELSALVVKrnnqfFR-----YKDFL----YFLTPCGR 254
Cdd:cd11066   104 EGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCV-DDDSLLLEIIEVESAISK-----FRstssnLQDYIpilrYFPKMSKF 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 255 RFHRacrlvhdftDAVIQERRRTLtsqgvDDFLQaKAKSKTLDFID----VLLLSEDKNGKeLSDEDIRAEADTFMFGGH 330
Cdd:cd11066   178 RERA---------DEYRNRRDKYL-----KKLLA-KLKEEIEDGTDkpciVGNILKDKESK-LTDAELQSICLTMVSAGL 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 331 DTTASGLSWVLYNLARHP--EYQERCRQEVQELLKDREPkeiEWDDLA---QLPFLTMCLKESLRLHPPIPT-FARGCTQ 404
Cdd:cd11066   242 DTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDED---AWEDCAaeeKCPYVVALVKETLRYFTVLPLgLPRKTTK 318

                         250
                  ....*....|...
gi 1370474309 405 DVVLpDSRVIPKG 417
Cdd:cd11066   319 DIVY-NGAVIPAG 330
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 255-417 1.56e-09

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: 59.30  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 255 RFHRACRLVHDFTDAVIQERRRTLTsqgvDDFLQAkaksktldfidvlLLSEDKNGKELSDEDIRAEADTFMFGGHDTTA 334
Cdd:cd11038   169 RIEAAVEELYDYADALIEARRAEPG----DDLIST-------------LVAAEQDGDRLSDEELRNLIVALLFAGVDTTR 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 335 SGLSWVLYNLARHPEyqercrqevqellkdrepkeiEWDDLAQLPFLTM-CLKESLRLHPPIPTFARGCTQDVVLPDSRv 413
Cdd:cd11038   232 NQLGLAMLTFAEHPD---------------------QWRALREDPELAPaAVEEVLRWCPTTTWATREAVEDVEYNGVT- 289


                  ....
gi 1370474309 414 IPKG 417
Cdd:cd11038   290 IPAG 293
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 297-396 6.22e-09

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 57.55  E-value: 6.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 297 DFIDVLLLS-EDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKEiewDD 374
Cdd:PLN00110  268 DFLDVVMANqENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIgRNRRLVE---SD 344

                          90       100
                  ....*....|....*....|..
gi 1370474309 375 LAQLPFLTMCLKESLRLHPPIP 396
Cdd:PLN00110  345 LPKLPYLQAICKESFRKHPSTP 366
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 206-417 7.50e-09

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: 57.09  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 206 CIFSFDSNCQEKPSEYITAIMELS-ALVVKRNNQFFRYK--DFLYFLtPCG--RRFHRACRLVHDFTDAVIQERRRTLTs 280
Cdd:cd20666   120 CSMSFGRRFDYQDVEFKTMLGLMSrGLEISVNSAAILVNicPWLYYL-PFGpfRELRQIEKDITAFLKKIIADHRETLD- 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 281 qgvddflqakaKSKTLDFIDVLLL---SEDKNGKELS-DED--IRAEADTFmFGGHDTTASGLSWVLYNLARHPEYQERC 354
Cdd:cd20666   198 -----------PANPRDFIDMYLLhieEEQKNNAESSfNEDylFYIIGDLF-IAGTDTTTNTLLWCLLYMSLYPEVQEKV 265

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370474309 355 RQEVQELL-KDREPkeiEWDDLAQLPFLTMCLKESLRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20666   266 QAEIDTVIgPDRAP---SLTDKAQMPFTEATIMEVQRMTVVVPlSIPHMASENTVL-QGYTIPKG 326
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 265-417 1.44e-08

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: 56.38  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 265 DFTDAVIQERRRTLTsqgvDDFLQakaksktldfidvLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNL 344
Cdd:cd11033   174 AYFRELAEERRANPG----DDLIS-------------VLANAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLAL 236

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474309 345 ARHPEyqercrqevQ-ELLKdrepkeiewDDLAQLPflTMcLKESLRLHPPIPTFARGCTQDVVLPDsRVIPKG 417
Cdd:cd11033   237 AEHPD---------QwERLR---------ADPSLLP--TA-VEEILRWASPVIHFRRTATRDTELGG-QRIRAG 288
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 254-409 2.16e-08

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 56.17  E-value: 2.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 254 RRFHRACRLVHDFTDAVIQERRRTLTSQGVDDFLQAKAKSKTLDfIDVlllSEDKNGKELSDEDIRAEADTFMFGGHDTT 333
Cdd:PLN02169  242 RKMRTALATVNRMFAKIISSRRKEEISRAETEPYSKDALTYYMN-VDT---SKYKLLKPKKDKFIRDVIFSLVLAGRDTT 317

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370474309 334 ASGLSWVLYNLARHPEYQERCRQEVQellkdrepKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLP 409
Cdd:PLN02169  318 SSALTWFFWLLSKHPQVMAKIRHEIN--------TKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLP 385
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 274-417 2.20e-08

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 55.44  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 274 RRRTLTSQGVDDF-------LQAKAKSKTLDFIDV--LLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNL 344
Cdd:cd11079   131 GDRAATAEVAEEFdgiirdlLADRRAAPRDADDDVtaRLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYL 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370474309 345 ARHPEYQERCRQEVQELlkdrePKEIEwddlaqlpfltmclkESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd11079   211 ARHPELQARLRANPALL-----PAAID---------------EILRLDDPFVANRRITTRDVEL-GGRTIPAG 262
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 254-417 2.60e-08

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


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 55.78  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 254 RRFHRACRLVHDFTDAVIQERRRTLtsqgvddflqakAKSKTLDFIDVLLLSEDK-----NGKELSDEDIRAEAdTFMFG 328
Cdd:cd20675   179 RNFKQLNREFYNFVLDKVLQHRETL------------RGGAPRDMMDAFILALEKgksgdSGVGLDKEYVPSTV-TDIFG 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 329 -GHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKeIEwdDLAQLPFLTMCLKESLRLHPPIP-TFARGCTQD 405
Cdd:cd20675   246 aSQDTLSTALQWILLLLVRYPDVQARLQEELDRVVgRDRLPC-IE--DQPNLPYVMAFLYEAMRFSSFVPvTIPHATTAD 322

                         170
                  ....*....|..
gi 1370474309 406 VVLPDSRvIPKG 417
Cdd:cd20675   323 TSILGYH-IPKD 333
PLN02774 PLN02774
brassinosteroid-6-oxidase
 270-417 4.68e-08

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 54.78  E-value: 4.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 270 VIQERRRTLTSQgvDDFLQAkaksktldfidvlLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPE 349
Cdd:PLN02774  232 LIQERRASGETH--TDMLGY-------------LMRKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPK 296

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370474309 350 YQERCRQEVQELLKDREPKE-IEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:PLN02774  297 ALQELRKEHLAIRERKRPEDpIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMEL-NGYVIPKG 364
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 255-417 6.34e-08

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: 54.11  E-value: 6.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 255 RFHRACRLVHDFTDAVIQERRRTLTS--QGVDDFLQAKAKSKTLDFIDVLLLSEDKNGKeLSDEDIRAEADTFMFGGHDT 332
Cdd:cd11031   143 RFRAWSDALLSTSALTPEEAEAARQElrGYMAELVAARRAEPGDDLLSALVAARDDDDR-LSEEELVTLAVGLLVAGHET 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 333 TASGLSWVLYNLARHPEyqercrqEVQELLKDRE--PKEIEwddlaqlpfltmclkESLRLHPPIPT--FARGCTQDVVL 408
Cdd:cd11031   222 TASQIGNGVLLLLRHPE-------QLARLRADPElvPAAVE---------------ELLRYIPLGAGggFPRYATEDVEL 279


                  ....*....
gi 1370474309 409 PDsRVIPKG 417
Cdd:cd11031   280 GG-VTIRAG 287
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 191-417 8.21e-08

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 54.21  E-value: 8.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 191 VFEHISLMTLDSLQKCIFSFDsncqekPSEYITAIMELSALVVKrnnQFFRYKdfLYFLTPCGRRFHRACRLVHDFTDAV 270
Cdd:PLN02987  166 LMEEAKKITFELTVKQLMSFD------PGEWTESLRKEYVLVIE---GFFSVP--LPLFSTTYRRAIQARTKVAEALTLV 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 271 IQERRRTltsqgvddflQAKAKSKTLDFIDVLLLSEDKngkeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEY 350
Cdd:PLN02987  235 VMKRRKE----------EEEGAEKKKDMLAALLASDDG----FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLA 300

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474309 351 QERCRQEVQEL-LKDREPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:PLN02987  301 LAQLKEEHEKIrAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEV-KGYTIPKG 367
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 328-417 2.24e-07

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: 52.59  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 328 GGHDTTASGLSWVLYNLARHPEyqercrqevqellkdrepkeiEWDDLAQLPFL-TMCLKESLRLHPPIPTFARGCTQDV 406
Cdd:cd11037   213 AGLDTTISAIGNALWLLARHPD---------------------QWERLRADPSLaPNAFEEAVRLESPVQTFSRTTTRDT 271

                          90
                  ....*....|.
gi 1370474309 407 VLpDSRVIPKG 417
Cdd:cd11037   272 EL-AGVTIPAG 281
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 285-417 3.42e-07

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: 51.83  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 285 DFLQAKAKSKTLDFIDVLLLSEDKnGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEvQELLkd 364
Cdd:cd11032   167 EHLEERRRNPRDDLISRLVEAEVD-GERLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRAD-PSLI-- 242

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370474309 365 rePKEIEwddlaqlpfltmclkESLRLHPPIPTFARGCTQDVVLPDsRVIPKG 417
Cdd:cd11032   243 --PGAIE---------------EVLRYRPPVQRTARVTTEDVELGG-VTIPAG 277
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 88-417 5.53e-07

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: 51.35  E-value: 5.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  88 FVRWLGPITPIInLCHPDIVR-SVINTSDAITDKDI--VFYKTLKpwlGDGLLLSVGDKWRHHRRL-LTPAFHFNILKPY 163
Cdd:cd20664     5 FTVQMGTKKVVV-LAGYKTVKeALVNHAEAFGGRPIipIFEDFNK---GYGILFSNGENWKEMRRFtLTTLRDFGMGKKT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 164 IkifsksanimhakwQRLAMEGSTCL-DVFEHISLMTLDSLQKCIFSFdsncqekpSEYITAIM-------ELSAL--VV 233
Cdd:cd20664    81 S--------------EDKILEEIPYLiEVFEKHKGKPFETTLSMNVAV--------SNIIASIVlghrfeyTDPTLlrMV 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 234 KRNNQFFRYKD----FLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSqgvddFLQAKAKSKTLDFIDVLLLSEDKN 309
Cdd:cd20664   139 DRINENMKLTGspsvQLYNMFPWLGPFPGDINKLLRNTKELNDFLMETFMK-----HLDVLEPNDQRGFIDAFLVKQQEE 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 310 gKELSDEDIRAEADTF----MFG-GHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKeieWDDLAQLPFLTMC 384
Cdd:cd20664   214 -EESSDSFFHDDNLTCsvgnLFGaGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQ---VEHRKNMPYTDAV 289

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1370474309 385 LKESLRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20664   290 IHEIQRFANIVPmNLPHATTRDVTF-RGYFIPKG 322
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 297-391 5.69e-07

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: 51.38  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 297 DFIDVLLLSEDKNGKE----LSDED-IRAEADTFMfGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPkeIE 371
Cdd:cd20667   201 DFIDCYLAQITKTKDDpvstFSEENmIQVVIDLFL-GGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQL--IC 277

                          90       100
                  ....*....|....*....|
gi 1370474309 372 WDDLAQLPFLTMCLKESLRL 391
Cdd:cd20667   278 YEDRKRLPYTNAVIHEVQRL 297
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 297-417 7.44e-07

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: 51.17  E-value: 7.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 297 DFIDVLLL----SEDKNGKELSDEDIRAEADTFM-----FG-GHDTTASGLSWVLYNLARHPEYQERCRQEV-QELLKDR 365
Cdd:cd20673   202 DLLDALLQakmnAENNNAGPDQDSVGLSDDHILMtvgdiFGaGVETTTTVLKWIIAFLLHNPEVQKKIQEEIdQNIGFSR 281

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370474309 366 EPKeieWDDLAQLPFLTMCLKESLRLHPPIPTFargcTQDVVLPDSRV----IPKG 417
Cdd:cd20673   282 TPT---LSDRNHLPLLEATIREVLRIRPVAPLL----IPHVALQDSSIgeftIPKG 330
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 218-392 1.55e-06

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: 49.73  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 218 PSEYITAIMELSAlvvKRNNQFFRYKDFLYFLTPCG---RRFHRACRLVH---DFTDAVIQERRRTLtsqGVDDFLQaka 291
Cdd:cd20630   117 PFRVISAMLGVPA---EWDEQFRRFGTATIRLLPPGldpEELETAAPDVTeglALIEEVIAERRQAP---VEDDLLT--- 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 292 ksktldfidvLLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEvQELLKDREPKEIE 371
Cdd:cd20630   188 ----------TLLRAEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE-PELLRNALEEVLR 256

                         170       180
                  ....*....|....*....|.
gi 1370474309 372 WDDLAQLPFLTMCLkESLRLH 392
Cdd:cd20630   257 WDNFGKMGTARYAT-EDVELC 276
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 84-396 2.80e-06

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: 49.15  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  84 YPQGFVRWLGPiTPIINLC-HPDIVRSVINTSDAITDKDIVfyKTL-KPWLGDGLLLSVGDKWRHHRRL-LTPAFHFNIL 160
Cdd:cd20670     1 YGPVFTVYMGP-RPVVVLCgHEAVKEALVDQADEFSGRGEL--ATIeRNFQGHGVALANGERWRILRRFsLTILRNFGMG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 161 KPYIKifsksanimhakwQRLAMEGSTCLDVFEHISLMTLDslqkcifsfdsncqekPSEYITAIME--LSALVVKRNnq 238
Cdd:cd20670    78 KRSIE-------------ERIQEEAGYLLEEFRKTKGAPID----------------PTFFLSRTVSnvISSVVFGSR-- 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 239 fFRYKD--FLYFLTPCGRRF---HRACRLVHDFTDAVIQ-----ERRRTLTSQGVDDFLQAKAK--------SKTLDFID 300
Cdd:cd20670   127 -FDYEDkqFLSLLRMINESFiemSTPWAQLYDMYSGIMQylpgrHNRIYYLIEELKDFIASRVKineasldpQNPRDFID 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 301 VLLLS--EDKNG--KELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKEiewDDL 375
Cdd:cd20670   206 CFLIKmhQDKNNphTEFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIgPHRLPSV---DDR 282

                         330       340
                  ....*....|....*....|.
gi 1370474309 376 AQLPFLTMCLKESLRLHPPIP 396
Cdd:cd20670   283 VKMPYTDAVIHEIQRLTDIVP 303
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 293-417 4.88e-06

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: 48.26  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 293 SKTLDFIDVLLLSEDK---NGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPK 368
Cdd:cd20662   198 DEPRDFIDAYLKEMAKypdPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIgQKRQPS 277

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370474309 369 eieWDDLAQLPFLTMCLKESLRLHPPIP-TFARGCTQDVVLPDSRvIPKG 417
Cdd:cd20662   278 ---LADRESMPYTNAVIHEVQRMGNIIPlNVPREVAVDTKLAGFH-LPKG 323
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 258-417 5.93e-06

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: 47.91  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 258 RACRLVHDFTDAVIQERRRTLTSQGVDDFLQ----AKAKSKTLDFIDVLLLSEDkNGKELSDEDIRAEADTFMFGGHDTT 333
Cdd:cd11029   149 RFRRWSDALVDTDPPPEEAAAALRELVDYLAelvaRKRAEPGDDLLSALVAARD-EGDRLSEEELVSTVFLLLVAGHETT 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 334 ASGLSWVLYNLARHPEYQERcrqevqeLLKDREPkeieWDDLAQlpfltmclkESLRLHPPIPTFA-RGCTQDVVLPDsR 412
Cdd:cd11029   228 VNLIGNGVLALLTHPDQLAL-------LRADPEL----WPAAVE---------ELLRYDGPVALATlRFATEDVEVGG-V 286


                  ....*
gi 1370474309 413 VIPKG 417
Cdd:cd11029   287 TIPAG 291
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 298-417 6.60e-06

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: 47.87  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 298 FIDVLLL--SEDKNGKEL-SDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIEwdD 374
Cdd:cd20671   201 YIEALIQkqEEDDPKETLfHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYE--D 278

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370474309 375 LAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20671   279 RKALPYTSAVIHEVQRFITLLPHVPRCTAADTQF-KGYLIPKG 320
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 270-417 7.06e-06

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 47.81  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 270 VIQERRRTLTSQGVDDFLQAKaksktlDFIDVLLlsedKNGKE-LSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHP 348
Cdd:PLN03141  213 IIEEKRRAMKNKEEDETGIPK------DVVDVLL----RDGSDeLTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCP 282

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370474309 349 EYQERCRQEVQEL--LKDREPKEIEWDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLPDsRVIPKG 417
Cdd:PLN03141  283 VALQQLTEENMKLkrLKADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKG-YLIPKG 352
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 280-417 8.12e-06

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: 47.87  E-value: 8.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 280 SQGVDDFLQAKAKS--KTLD------FIDVLLL---SEDKNGK-ELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARH 347
Cdd:cd20668   177 LQGLEDFIAKKVEHnqRTLDpnsprdFIDSFLIrmqEEKKNPNtEFYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKH 256

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370474309 348 PEYQERCRQEVQELL-KDREPKeieWDDLAQLPFLTMCLKESLRLHPPIPT-FARGCTQDVVLPDSrVIPKG 417
Cdd:cd20668   257 PEVEAKVHEEIDRVIgRNRQPK---FEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKDTKFRDF-FLPKG 324
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 305-418 9.88e-06

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: 47.32  E-value: 9.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 305 SEDK-----NGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKeieWDDLAQL 378
Cdd:cd20676   220 CQDKkldenANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIgRERRPR---LSDRPQL 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370474309 379 PFLTMCLKESLRLHPPIP-TFARGCTQDVVLpDSRVIPKGL 418
Cdd:cd20676   297 PYLEAFILETFRHSSFVPfTIPHCTTRDTSL-NGYYIPKDT 336
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 254-417 1.52e-05

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: 46.78  E-value: 1.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 254 RRFHRACRLVHDFTDAVIQERRRtltsQGVDDFLQAkaksktldfidvlLLSEDKNGKELSDEDIRAEADTFMFGGHDTT 333
Cdd:cd20625   155 ARANAAAAELAAYFRDLIARRRA----DPGDDLISA-------------LVAAEEDGDRLSEDELVANCILLLVAGHETT 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 334 ASGLSWVLYNLARHPEYQERCRQEvQELLkdrePKEIEwddlaqlpfltmclkESLRLHPPIPTFARGCTQDVVLPDsRV 413
Cdd:cd20625   218 VNLIGNGLLALLRHPEQLALLRAD-PELI----PAAVE---------------ELLRYDSPVQLTARVALEDVEIGG-QT 276


                  ....
gi 1370474309 414 IPKG 417
Cdd:cd20625   277 IPAG 280
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 88-417 2.17e-05

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


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 46.29  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  88 FVRWLGPItPIINLCHPDIVR-SVINTSDAITDKDI--VFYKTLKpwlGDGLLLSVGDKWRHHRRL-LTPAFHFNILKPY 163
Cdd:cd20669     5 YTVYLGPR-PVVVLCGYQAVKeALVDQAEEFSGRGDypVFFNFTK---GNGIAFSNGERWKILRRFaLQTLRNFGMGKRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 164 IKifsksanimhakwQRLAMEGSTCLDVFEHISLMTLDSLQK---------CIFSFDSNCQEKPSEYITAIMELSalvvk 234
Cdd:cd20669    81 IE-------------ERILEEAQFLLEELRKTKGAPFDPTFLlsravsniiCSVVFGSRFDYDDKRLLTILNLIN----- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 235 rnnqffryKDFLYFLTPCGRRF-------------HRacRLVHDFtdaviqERRRTLTSQGVDDFLQAKAKSKTLDFIDV 301
Cdd:cd20669   143 --------DNFQIMSSPWGELYnifpsvmdwlpgpHQ--RIFQNF------EKLRDFIAESVREHQESLDPNSPRDFIDC 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 302 LLLSEDKNGKELS----DEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKeieWDDLA 376
Cdd:cd20669   207 FLTKMAEEKQDPLshfnMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVgRNRLPT---LEDRA 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1370474309 377 QLPFLTMCLKESLRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20669   284 RMPYTDAVIHEIQRFADIIPmSLPHAVTRDTNF-RGFLIPKG 324
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 297-417 4.41e-05

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


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 45.46  E-value: 4.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 297 DFIDVLL--LSEDKNGKELS--DEDIR-AEADTFMfGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPkei 370
Cdd:cd20663   206 DLTDAFLaeMEKAKGNPESSfnDENLRlVVADLFS-AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIgQVRRP--- 281

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1370474309 371 EWDDLAQLPFLTMCLKESLRLHPPIPT-FARGCTQDVVLPDSrVIPKG 417
Cdd:cd20663   282 EMADQARMPYTNAVIHEVQRFGDIVPLgVPHMTSRDIEVQGF-LIPKG 328
PLN02971 PLN02971
tryptophan N-hydroxylase
 292-417 6.03e-05

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 45.03  E-value: 6.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 292 KSKTLDFIDVLLLSEDKNGKEL-SDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL-KDREPKE 369
Cdd:PLN02971  301 RTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVgKERFVQE 380

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370474309 370 iewDDLAQLPFLTMCLKESLRLHpPIPTFArgcTQDVVLPDSRV----IPKG 417
Cdd:PLN02971  381 ---SDIPKLNYVKAIIREAFRLH-PVAAFN---LPHVALSDTTVagyhIPKG 425
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 344-417 6.75e-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: 44.76  E-value: 6.75e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370474309 344 LARHPEYQERCRQEVQELlkdrepkeiewDDLAQLPFLTMCLKESLRLHPPIPTFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20624   218 LAAHPEQAARAREEAAVP-----------PGPLARPYLRACVLDAVRLWPTTPAVLRESTEDTVW-GGRTVPAG 279
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 305-417 7.20e-05

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: 44.70  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 305 SEDKNGKeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKeiEWDDLAQLPFLTMC 384
Cdd:cd20677   225 AEDKSAV-LSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLP--RFEDRKSLHYTEAF 301

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370474309 385 LKESLRLHPPIP-TFARGCTQDVVLpDSRVIPKG 417
Cdd:cd20677   302 INEVFRHSSFVPfTIPHCTTADTTL-NGYFIPKD 334
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 258-362 4.05e-04

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: 42.12  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 258 RACRLVHDFTDAVIQERRRTLTsqgvDDFLQAkaksktldfidvlLLSEDKNGKELSDEDIRAEADTFMFGGHDTTASGL 337
Cdd:cd11030   166 AAGAELRAYLDELVARKRREPG----DDLLSR-------------LVAEHGAPGELTDEELVGIAVLLLVAGHETTANMI 228

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370474309 338 SWVLYNLARHPEYQERCRQE-------VQELL 362
Cdd:cd11030   229 ALGTLALLEHPEQLAALRADpslvpgaVEELL 260
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 339-408 4.18e-04

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 42.35  E-value: 4.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474309 339 WVLYNLARHPEYQERCRQEVQELLKD--REPK------EIEWDDLAQLPFLTMCLKESLRLHPPiPTFARGCTQDVVL 408
Cdd:cd20633   246 WLLLYLLKHPEAMKAVREEVEQVLKEtgQEVKpggpliNLTRDMLLKTPVLDSAVEETLRLTAA-PVLIRAVVQDMTL 322
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 298-417 5.54e-04

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 42.11  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 298 FIDVLLLSEDKNGKEL----SDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKeiEWD 373
Cdd:cd20661   215 FIDAYLDEMDQNKNDPestfSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMP--SFE 292

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370474309 374 DLAQLPFLTMCLKESLRLHPPIPT-FARGCTQDVVLpDSRVIPKG 417
Cdd:cd20661   293 DKCKMPYTEAVLHEVLRFCNIVPLgIFHATSKDAVV-RGYSIPKG 336
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 311-391 7.51e-04

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: 41.52  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 311 KELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDR-EPKEIEWD------DLAQLPFLTM 383
Cdd:cd20632   209 DVLQDYDKAAHHFAFLWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQSTgQELGPDFDihltreQLDSLVYLES 288


                  ....*...
gi 1370474309 384 CLKESLRL 391
Cdd:cd20632   289 AINESLRL 296
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 339-417 1.11e-03

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: 41.14  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 339 WVLYNLARHPEYQERCRQEVQELLKD--REPKEIEWDDLAQLPFLTMCLKESLRLHPP--IPtfaRGCTQDVVLPDSrVI 414
Cdd:cd20635   232 WTLAFILSHPSVYKKVMEEISSVLGKagKDKIKISEDDLKKMPYIKRCVLEAIRLRSPgaIT---RKVVKPIKIKNY-TI 307


                  ...
gi 1370474309 415 PKG 417
Cdd:cd20635   308 PAG 310
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 119-408 1.82e-03

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 40.32  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 119 DKDIVFYKTLKP----WLGDGLLLSVGDKWRHHRRLltPAFHFNILKPY----IKIFSKSANIMHAKWQrLAMEGSTCLD 190
Cdd:cd11071    47 EKEDVFGGTYMPstsfTGGYRVLPYLDTSEPKHAKL--KAFLFELLKSRssrfIPEFRSALSELFDKWE-AELAKKGKAS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 191 VfehislmtLDSLQKCIFSF--DSNCQEKPSEyitAIMELSALVVKRNNQFFRykdfLYFLTPCGRRFHRACRLVHDFTD 268
Cdd:cd11071   124 F--------NDDLEKLAFDFlfRLLFGADPSE---TKLGSDGPDALDKWLALQ----LAPTLSLGLPKILEELLLHTFPL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 269 AviqerrRTLTSQGVDDFLQ--AKAKSKTLDFIDVLLLSEDKNGKELsdediraeadTFM-----FGGhdtTASGLSWVL 341
Cdd:cd11071   189 P------FFLVKPDYQKLYKffANAGLEVLDEAEKLGLSREEAVHNL----------LFMlgfnaFGG---FSALLPSLL 249

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370474309 342 YNLARH-PEYQERCRQEVQELLKDREPKEIEwdDLAQLPFLTMCLKESLRLHPPIP-TFARGcTQDVVL 408
Cdd:cd11071   250 ARLGLAgEELHARLAEEIRSALGSEGGLTLA--ALEKMPLLKSVVYETLRLHPPVPlQYGRA-RKDFVI 315
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 88-397 2.69e-03

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: 39.76  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309  88 FVRWLGPiTPIINLCHPDIVR-SVINTSDAITDKDIVfyKTLKPWLGD-GLLLSVGDKWRHHRRL-LTPAFHFNILKPYI 164
Cdd:cd20672     5 FTVHLGP-RPVVMLCGTDAIReALVDQAEAFSGRGTI--AVVDPIFQGyGVIFANGERWKTLRRFsLATMRDFGMGKRSV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 165 KifsksanimhakwQRLAMEGSTCLDVFEHISLMTLD--SLQKCIFS-------FDSNCQEKPSEYITaIMEL----SAL 231
Cdd:cd20672    82 E-------------ERIQEEAQCLVEELRKSKGALLDptFLFQSITAniicsivFGERFDYKDPQFLR-LLDLfyqtFSL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 232 VVKRNNQFFR-YKDFLYFLTPCGRRFHRACRLVHDFTDAVIQERRRTLTSqgvddflqakakSKTLDFIDVLLLSEDK-- 308
Cdd:cd20672   148 ISSFSSQVFElFSGFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDP------------SAPRDFIDTYLLRMEKek 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 309 --NGKELSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELLKDREPKEIewDDLAQLPFLTMCLK 386
Cdd:cd20672   216 snHHTEFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTL--DDRAKMPYTDAVIH 293

                         330
                  ....*....|.
gi 1370474309 387 ESLRLHPPIPT 397
Cdd:cd20672   294 EIQRFSDLIPI 304
PLN02500 PLN02500
cytochrome P450 90B1
 313-406 4.83e-03

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 39.08  E-value: 4.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 313 LSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPEYQERCRQEVQELL---KDREPKEIEWDDLAQLPFLTMCLKESL 389
Cdd:PLN02500  275 LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIArakKQSGESELNWEDYKKMEFTQCVINETL 354

                          90
                  ....*....|....*..
gi 1370474309 390 RLHPPIPTFARGCTQDV 406
Cdd:PLN02500  355 RLGNVVRFLHRKALKDV 371
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 270-416 5.83e-03

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: 38.65  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370474309 270 VIQERRRTLTSQGVddflqakaksktldFIDVLLLSEdkngkeLSDEDIRAEADTFMFGGHDTTASGLSWVLYNLARHPE 349
Cdd:cd20627   175 VIKERKGKNFSQHV--------------FIDSLLQGN------LSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEE 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370474309 350 YQERCRQEVQELLKDrEPkeIEWDDLAQLPFLTMCLKESLRLHPPIPTFARgcTQDVV-LPDSRVIPK 416
Cdd:cd20627   235 VQKKLYKEVDQVLGK-GP--ITLEKIEQLRYCQQVLCETVRTAKLTPVSAR--LQELEgKVDQHIIPK 297
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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